Bjorkman, Pamela J.

Combined from CaltechAUTHORS

• Kubinski, Hannah C. and Despres, Hannah W., et el. (2024) Variant mutation in SARS-CoV-2 nucleocapsid enhances viral infection via altered genomic encapsidation; bioRxiv; 53; PMCID PMC10979914; 10.1101/2024.03.08.584120
• Dam, Kim-Marie A. and Fan, Chengcheng, et el. (2024) Publisher Correction: Intermediate conformations of CD4-bound HIV-1 Env heterotrimers; Nature; Vol. 627; E7; 10.1038/s41586-024-07082-z
• Cohen, Alexander A. and van Doremalen, Neeltje, et el. (2023) Mosaic RBD nanoparticles protect against multiple sarbecovirus challenges in animal models; PMCID PMC8978945; 10.1101/2022.03.25.485875
• Horns, Felix and Martinez, Joe A., et el. (2023) Engineering RNA export for measurement and manipulation of living cells; Cell; Vol. 186; No. 17; 3642-3658.e32; PMCID PMC10528933; 10.1016/j.cell.2023.06.013
• Hoffmann, Magnus A. G. and Yang, Zhi, et el. (2023) ESCRT recruitment to SARS-CoV-2 spike induces virus-like particles that improve mRNA vaccines; Cell; Vol. 186; No. 11; 2380-2391; PMCID PMC10121106; 10.1016/j.cell.2023.04.024
• Shrock, Ellen L. and Timms, Richard T., et el. (2023) Germline-encoded amino acid–binding motifs drive immunodominant public antibody responses; Science; Vol. 380; No. 6640; Art. No. eadc9498; PMCID PMC10273302; 10.1126/science.adc9498
• Gristick, Harry B. and Hartweger, Harald, et el. (2023) CD4-binding site immunogens elicit heterologous anti-HIV-1 neutralizing antibodies in transgenic and wildtype animals; 10.1101/2022.09.08.507086
• Braet, Sean M. and Buckley, Theresa S. C., et el. (2023) Timeline of changes in spike conformational dynamics in emergent SARS-CoV-2 variants reveal progressive stabilization of trimer stalk and enhanced NTD dynamics; 10.1101/2022.08.26.505369
• Hills, Rory A. and Tan, Tiong Kit, et el. (2023) Multiviral Quartet Nanocages Elicit Broad Anti-Coronavirus Responses for Proactive Vaccinology; PMCID PMC9980174; 10.1101/2023.02.24.529520
• Dam, Kim-Marie A. and Fan, Chengcheng, et el. (2023) Structural characterization of HIV-1 Env heterotrimers bound to one or two CD4 receptors reveals intermediate Env conformations; 10.1101/2023.01.27.525985
• Hoffmann, Magnus A. G. and Yang, Zhi, et el. (2023) ESCRT recruitment to mRNA-encoded SARS-CoV-2 spike induces virus-like particles and enhanced antibody responses; PMCID PMC9810232; 10.1101/2022.12.26.521940
• Braet, Sean M. and Buckley, Theresa S. C., et el. (2023) Timeline of changes in spike conformational dynamics in emergent SARS-CoV-2 variants reveal progressive stabilization of trimer stalk with altered NTD dynamics; eLife; Vol. 12; Art. No. e82584; PMCID PMC10049203; 10.7554/elife.82584
• Cable, Jennifer and Balachandran, Siddharth, et el. (2023) Viral immunity: Basic mechanisms and therapeutic applications—a Keystone Symposia report; Annals of the New York Academy of Sciences; Vol. 1521; No. 1; 32-45; 10.1111/nyas.14960
• Gristick, Harry B. and Hartweger, Harald, et el. (2023) CD4 binding site immunogens elicit heterologous anti–HIV-1 neutralizing antibodies in transgenic and wild-type animals; Science Immunology; Vol. 8; No. 80; eade6364; PMCID PMC10202037; 10.1126/sciimmunol.ade6364
• Huang, Kuan-Ying A. and Chen, Xiaorui, et el. (2023) Structural basis for a conserved neutralization epitope on the receptor-binding domain of SARS-CoV-2; Nature Communications; Vol. 14; Art. No. 311; PMCID PMC9852238; 10.1038/s41467-023-35949-8
• Yang, Zhi and Dam, Kim-Marie A., et el. (2022) Antibody Recognition of CD4-Induced Open HIV-1 Env Trimers; Journal of Virology; Vol. 96; No. 24; e0108222; PMCID PMC9769388; 10.1128/jvi.01082-22
• Fan, Chengcheng and Cohen, Alexander A., et el. (2022) Neutralizing monoclonal antibodies elicited by mosaic RBD nanoparticles bind conserved sarbecovirus epitopes; Immunity; Vol. 55; No. 12; 2419-2435.e10; PMCID PMC9606073; 10.1016/j.immuni.2022.10.019
• Dam, Kim-Marie A. and Barnes, Christopher O., et el. (2022) HIV-1 CD4-binding site germline antibody-Env structures inform vaccine design; Nature Communications; Vol. 13; Art. No. 6123; PMCID PMC9576718; 10.1038/s41467-022-33860-2
• Barnes, Christopher O. and Schoofs, Till, et el. (2022) A naturally arising broad and potent CD4-binding site antibody with low somatic mutation; Science Advances; Vol. 8; No. 32; Art. No. eabp8155; 10.1126/sciadv.abp8155
• Cohen, Alexander A. and van Doremalen, Neeltje, et el. (2022) Mosaic RBD nanoparticles protect against challenge by diverse sarbecoviruses in animal models; Science; Vol. 377; No. 6606; Art. No. eabq0839; PMCID PMC9273039; 10.1126/science.abq0839
• Yang, Zhi and Dam, Kim-Marie A., et el. (2022) Antibody recognition of CD4-induced open HIV-1 Env trimers; 10.1101/2022.07.27.501785
• Fan, Chengcheng and Cohen, Alexander A., et el. (2022) Neutralizing monoclonal antibodies elicited by mosaic RBD nanoparticles bind conserved sarbecovirus epitopes; 10.1101/2022.06.28.497989
• Dam, Kim-Marie A. and Mutia, Patricia S., et el. (2022) Comparing methods for immobilizing HIV-1 SOSIPs in ELISAs that evaluate antibody binding; Scientific Reports; Vol. 12; Art. No. 11172; PMCID PMC9247892; 10.1038/s41598-022-15506-x
• Bozhanova, Nina G. and Flyak, Andrew I., et el. (2022) Computational identification of HCV neutralizing antibodies with a common HCDR3 disulfide bond motif in the antibody repertoires of infected individuals; Nature Communications; Vol. 13; Art. No. 3178; PMCID PMC9177688; 10.1038/s41467-022-30865-9
• Jacobs, Jana L. and Bain, William, et el. (2022) Severe Acute Respiratory Syndrome Coronavirus 2 Viremia Is Associated With Coronavirus Disease 2019 Severity and Predicts Clinical Outcome; Clinical Infectious Diseases; Vol. 74; No. 9; 1525-1533; PMCID PMC9070832; 10.1093/cid/ciab686
• Cable, Jennifer and Rappuoli, Rino, et el. (2022) Innovative vaccine approaches—a Keystone Symposia report; Annals of the New York Academy of Sciences; Vol. 1511; No. 1; 59-86; 10.1111/nyas.14739
• Dam, Kim-Marie A. and Barnes, Christopher O., et el. (2022) HIV-1 CD4-binding site germline antibody-Env structures inform vaccine design; 10.1101/2022.03.25.485873
• Needham, Brittany D. and Funabashi, Masanori, et el. (2022) A gut-derived metabolite alters brain activity and anxiety behaviour in mice; Nature; Vol. 602; No. 7899; 647-653; PMCID PMC9170029; 10.1038/s41586-022-04396-8
• Tanaka, Shiho and Olson, C. Anders, et el. (2022) Rapid identification of neutralizing antibodies against SARS-CoV-2 variants by mRNA display; Cell Reports; Vol. 38; No. 6; Art. No. 110348; PMCID PMC8769934; 10.1016/j.celrep.2022.110348
• Yang, Zhi and Dam, Kim-Marie A., et el. (2022) Neutralizing antibodies induced in immunized macaques recognize the CD4-binding site on an occluded-open HIV-1 envelope trimer; Nature Communications; Vol. 13; Art. No. 732; PMCID PMC8826976; 10.1038/s41467-022-28424-3
• Weber, Timm and Potthoff, Julian, et el. (2022) Analysis of antibodies from HCV elite neutralizers identifies genetic determinants of broad neutralization; Immunity; Vol. 55; No. 2; 341-354; PMCID PMC10089621; 10.1016/j.immuni.2021.12.003
• Vanshylla, Kanika and Fan, Chengcheng, et el. (2022) Discovery of ultrapotent broadly neutralizing antibodies from SARS-CoV-2 elite neutralizers; Cell Host and Microbe; Vol. 30; No. 1; 69-82; PMCID PMC8683262; 10.1016/j.chom.2021.12.010
• Ogega, Clinton O. and Skinner, Nicole E., et el. (2022) B cell overexpression of FCRL5 and PD-1 is associated with low antibody titers in HCV infection; PLOS Pathogens; Vol. 18; No. 1; Art. No. e1010179; PMCID PMC8769295; 10.1371/journal.ppat.1010179
• Barnes, Christopher and Scheid, Johannes F., et el. (2021) Structural insights into antibody-mediated neutralization of SARS-CoV-2; Glycobiology; Vol. 31; No. 12; 1696-1697; 10.1093/glycob/cwab121
• Escolano, Amelia and Gristick, Harry B., et el. (2021) Sequential immunization of macaques elicits heterologous neutralizing antibodies targeting the V3-glycan patch of HIV-1 Env; Science Translational Medicine; Vol. 13; No. 621; Art. No. abk1533; PMCID PMC8932345; 10.1126/scitranslmed.abk1533
• Brune, Karl D. and Liekniņa, Ilva, et el. (2021) N-Terminal Modification of Gly-His-Tagged Proteins with Azidogluconolactone; ChemBioChem; Vol. 22; No. 22; 3199-3207; 10.1002/cbic.202100381
• Woodward, Denise and Ricks, Ernest, Jr., et el. (2021) The Path of Science in Future Tibetan Buddhist Education; Frontiers in Communication; Vol. 6; Art. No. 731604; 10.3389/fcomm.2021.731604
• Abernathy, Morgan E. and Gristick, Harry B., et el. (2021) Antibody elicited by HIV-1 immunogen vaccination in macaques displaces Env fusion peptide and destroys a neutralizing epitope; npj Vaccines; Vol. 6; Art. No. 126; PMCID PMC8545924; 10.1038/s41541-021-00387-4
• Abernathy, Morgan E. and Dam, Kim-Marie A., et el. (2021) How Antibodies Recognize Pathogenic Viruses: Structural Correlates of Antibody Neutralization of HIV-1, SARS-CoV-2, and Zika; Viruses; Vol. 13; No. 10; Art. No. 2106; PMCID PMC8537525; 10.3390/v13102106
• Jette, Claudia A. and Cohen, Alexander A., et el. (2021) Broad cross-reactivity across sarbecoviruses exhibited by a subset of COVID-19 donor-derived neutralizing antibodies; Cell Reports; Vol. 36; No. 13; Art. No. 109760; PMCID PMC8423902; 10.1016/j.celrep.2021.109760
• Ullah, Irfan and Prévost, Jérémie, et el. (2021) Live imaging of SARS-CoV-2 infection in mice reveals that neutralizing antibodies require Fc function for optimal efficacy; Immunity; Vol. 54; No. 9; 2143-2158; PMCID PMC8372518; 10.1016/j.immuni.2021.08.015
• Muecksch, Frauke and Weisblum, Yiska, et el. (2021) Affinity maturation of SARS-CoV-2 neutralizing antibodies confers potency, breadth, and resilience to viral escape mutations; Immunity; Vol. 54; No. 8; 1853-1868; PMCID PMC8323339; 10.1016/j.immuni.2021.07.008
• West, Anthony P., Jr. and Wertheim, Joel O., et el. (2021) Detection and characterization of the SARS-CoV-2 lineage B.1.526 in New York; Nature Communications; Vol. 12; Art. No. 4886; PMCID PMC8352861; 10.1038/s41467-021-25168-4
• Hensley, Matthew K. and Bain, William G., et el. (2021) Intractable Coronavirus Disease 2019 (COVID-19) and Prolonged Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) Replication in a Chimeric Antigen Receptor-Modified T-Cell Therapy Recipient: A Case Study; Clinical Infectious Diseases; Vol. 73; No. 3; e815-e821; PMCID PMC7929077; 10.1093/cid/ciab072
• Garber, Arkadiy I. and Kupper, Maria, et el. (2021) The Evolution of Interdependence in a Four-Way Mealybug Symbiosis; Genome Biology and Evolution; Vol. 13; No. 8; Art. No. evab123; PMCID PMC8331144; 10.1093/gbe/evab123
• Bjorkman, Pamela J. (2021) Neutralizing antibodies against coronaviruses
• Bjorkman, Pamela (2021) Neutralizing antibodies against coronaviruses; Microscopy and Microanalysis; Vol. 27; No. S1; 1112-1113; 10.1017/s1431927621004177
• Greaney, Allison J. and Starr, Tyler N., et el. (2021) Mapping mutations to the SARS-CoV-2 RBD that escape binding by different classes of antibodies; Nature Communications; Vol. 12; Art. No. 4196; PMCID PMC8263750; 10.1038/s41467-021-24435-8
• Haugh, Kelsey A. and Ladinsky, Mark S., et el. (2021) In vivo imaging of retrovirus infection reveals a role for Siglec-1/CD169 in multiple routes of transmission; eLife; Vol. 10; Art. No. e64179; PMCID PMC8298093; 10.7554/eLife.64179
• Hoffmann, Magnus A. G. and Kieffer, Collin, et el. (2021) In vitro characterization of engineered red blood cells as viral traps against HIV-1 and SARS-CoV-2; Molecular Therapy - Methods and Clinical Development; Vol. 21; 161-170; PMCID PMC7944778; 10.1016/j.omtm.2021.03.003
• Scheid, Johannes F. and Barnes, Christopher O., et el. (2021) B cell genomics behind cross-neutralization of SARS-CoV-2 variants and SARS-CoV; Cell; Vol. 184; No. 12; 3205-3221; PMCID PMC8064835; 10.1016/j.cell.2021.04.032
• Livanos, Alexandra E. and Jha, Divya, et el. (2021) Intestinal Host Response to SARS-CoV-2 Infection and COVID-19 Outcomes in Patients With Gastrointestinal Symptoms; Gastroenterology; Vol. 160; No. 7; 2435-2450; PMCID PMC7931673; 10.1053/j.gastro.2021.02.056
• De Gasparo, Raoul and Pedotti, Mattia, et el. (2021) Bispecific IgG neutralizes SARS-CoV-2 variants and prevents escape in mice; Nature; Vol. 593; No. 7859; 424-428; PMCID PMC8330819; 10.1038/s41586-021-03461-y
• Bloom, Jesse D. and Chan, Yujia Alina, et el. (2021) Investigate the origins of COVID-19; Science; Vol. 372; No. 6543; 694; PMCID PMC9520851; 10.1126/science.abj0016
• Agudelo, Marianna and Palus, Martin, et el. (2021) Broad and potent neutralizing human antibodies to tick-borne flaviviruses protect mice from disease; Journal of Experimental Medicine; Vol. 218; No. 5; Art. No. e20210236; PMCID PMC8040517; 10.1084/jem.20210236
• Wang, Zijun and Schmidt, Fabian, et el. (2021) mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants; Nature; Vol. 592; No. 7855; 616-622; PMCID PMC7836122; 10.1038/s41586-021-03324-6
• Jette, Claudia A. and Barnes, Christopher O., et el. (2021) Cryo-EM structures of HIV-1 trimer bound to CD4-mimetics BNM-III-170 and M48U1 adopt a CD4-bound open conformation; Nature Communications; Vol. 12; Art. No. 1950; PMCID PMC8007822; 10.1038/s41467-021-21816-x
• Gaebler, Christian and Wang, Zijun, et el. (2021) Evolution of antibody immunity to SARS-CoV-2; Nature; Vol. 591; No. 7851; 639-644; PMCID PMC8221082; 10.1038/s41586-021-03207-w
• Muecksch, Frauke and Weisblum, Yiska, et el. (2021) Development of potency, breadth and resilience to viral escape mutations in SARS-CoV-2 neutralizing antibodies; PMCID PMC7987023; 10.1101/2021.03.07.434227
• Cohen, Alexander A. and Yang, Zhi, et el. (2021) Construction, characterization, and immunization of nanoparticles that display a diverse array of influenza HA trimers; PLoS ONE; Vol. 16; No. 3; Art. No. e0247963; PMCID PMC7932532; 10.1371/journal.pone.0247963
• Bain, William G. and Peñaloza, Hernán F., et el. (2021) Lower Respiratory Tract Myeloid Cells Harbor SARS-Cov-2 and Display an Inflammatory Phenotype; CHEST; Vol. 159; No. 3; 963-966; PMCID PMC7671922; 10.1016/j.chest.2020.10.083
• Esswein, Shannon R. and Bjorkman, Pamela J. (2021) Structural Basis for Germline Antibody Binding to Zika Virus Envelope Domain III; Biophysical Journal; Vol. 120; No. 3; 276A-277A; 10.1016/j.bpj.2020.11.1760
• Cohen, Alexander A. and Gnanapragasam, Priyanthi N. P., et el. (2021) Mosaic nanoparticles elicit cross-reactive immune responses to zoonotic coronaviruses in mice; Science; Vol. 371; No. 6530; 735-741; PMCID PMC7928838; 10.1126/science.abf6840
• Bárcena, Montserrat and Barnes, Christopher O., et el. (2021) Structural biology in the fight against COVID-19; Nature Structural & Molecular Biology; Vol. 28; No. 1; 2-7; 10.1038/s41594-020-00544-8
• Barnes, Christopher O. and Jette, Claudia A., et el. (2020) SARS-CoV-2 neutralizing antibody structures inform therapeutic strategies; Nature; Vol. 588; No. 7839; 682-687; PMCID PMC8092461; 10.1038/s41586-020-2852-1
• Linsky, Thomas W. and Vergara, Renan, et el. (2020) De novo design of potent and resilient hACE2 decoys to neutralize SARS-CoV-2; Science; Vol. 370; No. 6521; 1208-1214; PMCID PMC7920261; 10.1126/science.abe0075
• Wang, Zijun and Barnes, Christopher O., et el. (2020) A broadly neutralizing macaque monoclonal antibody against the HIV-1 V3-Glycan patch; eLife; Vol. 9; Art. No. e61991; PMCID PMC7577740; 10.7554/eLife.61991
• Barnes, Christopher O. and Jette, Claudia A., et el. (2020) Structural classification of neutralizing antibodies against the SARS-CoV-2 spike receptor-binding domain suggests vaccine and therapeutic strategies; 10.1101/2020.08.30.273920
• Barnes, Christopher O. and West, Anthony P., Jr., et el. (2020) Structures of Human Antibodies Bound to SARS-CoV-2 Spike Reveal Common Epitopes and Recurrent Features of Antibodies; Cell; Vol. 182; No. 4; 828-842; PMCID PMC7311918; 10.1016/j.cell.2020.06.025
• Robbiani, Davide F. and Gaebler, Christian, et el. (2020) Convergent Antibody Responses to SARS-CoV-2 Infection in Convalescent Individuals; Nature; Vol. 584; No. 7821; 437-442; PMCID PMC7263513; 10.1038/s41586-020-2456-9
• Hoffmann, Magnus A. G. and Bar-On, Yotam, et el. (2020) Nanoparticles presenting clusters of CD4 expose a universal vulnerability of HIV-1 by mimicking target cells; Proceedings of the National Academy of Sciences of the United States of America; Vol. 117; No. 31; 18719-18728; PMCID PMC7414181; 10.1073/pnas.2010320117
• Ladinsky, Mark S. and Gnanapragasam, Priyanthi N. P., et el. (2020) Electron tomography visualization of HIV-1 fusion with target cells using fusion inhibitors to trap the pre-hairpin intermediate; eLife; Vol. 9; Art. No. e58411; PMCID PMC7394545; 10.7554/eLife.58411
• Esswein, Shannon R. and Gristick, Harry B., et el. (2020) Structural basis for Zika envelope domain III recognition by a germline version of a recurrent neutralizing antibody; Proceedings of the National Academy of Sciences of the United States of America; Vol. 117; No. 18; 9865-9875; PMCID PMC7211955; 10.1073/pnas.1919269117
• Li, Shirley and Kujawski, Maciej, et el. (2020) Use of Click-Chemistry to Make Bivalent Antibodies for Redirection of T Cells: Proof of Concept in an In Vitro HIV Model; Molecular Therapy; Vol. 28; No. 4; 369; 10.1016/j.ymthe.2020.04.019
• Van Rompay, Koen K. A. and Coffey, Lark L., et el. (2020) A Combination of Two Human Monoclonal Antibodies Limits Fetal Damage by Zika Virus in Macaques; Proceedings of the National Academy of Sciences of the United States of America; Vol. 117; No. 14; 7981-7989; PMCID PMC7149495; 10.1073/pnas.2000414117
• Flyak, Andrew I. and Ruiz, Stormy E., et el. (2020) An ultralong CDRH2 in HCV neutralizing antibody demonstrates structural plasticity of antibodies against E2 glycoprotein; eLife; Vol. 9; Art. No. e53169; PMCID PMC7064334; 10.7554/elife.53169
• Schommers, Philipp and Gruell, Henning, et el. (2020) Restriction of HIV-1 Escape by a Highly Broad and Potent Neutralizing Antibody; Cell; Vol. 180; No. 3; 471-489; PMCID PMC7042716; 10.1016/j.cell.2020.01.010
• Bjorkman, Pamela J. (2020) Can we use structural knowledge to design a protective vaccine against HIV-1?; HLA; Vol. 95; No. 2; 95-103; 10.1111/tan.13759
• Einav, Tal and Yazdi, Shahrzad, et el. (2020) Harnessing Avidity: Quantifying Entropic and Energetic Effects of Linker Length and Rigidity Required for Multivalent Binding of Antibodies to HIV-1 Spikes; 10.1101/406454
• Yang, Zhi and Wang, Haoqing, et el. (2019) Asymmetric opening of HIV-1 Env bound to CD4 and a coreceptor-mimicking antibody; Nature Structural & Molecular Biology; Vol. 26; No. 12; 1167-1175; 10.1038/s41594-019-0344-5
• Einav, Tal and Yazdi, Shahrzad, et el. (2019) Harnessing Avidity: Quantifying the Entropic and Energetic Effects of Linker Length and Rigidity for Multivalent Binding of Antibodies to HIV-1; Cell Systems; Vol. 9; No. 5; 466-474; PMCID PMC6892280; 10.1016/j.cels.2019.09.007
• Schommers, P. and Gruell, H., et el. (2019) Novel highly potent CD4bs bNAb with restricted pathway to HIV-1 escape; HIV Medicine; Vol. 20; No. S9; 50; 10.1111/hiv.12814
• Ladinsky, Mark S. and Khamaikawin, Wannisa, et el. (2019) Mechanisms of virus dissemination in bone marrow of HIV-1-infected humanized BLT mice; eLife; Vol. 8; Art. No. e46916; PMCID PMC6839903; 10.7554/elife.46916
• Bublitz, DeAnna C. and Chadwick, Grayson L., et el. (2019) Peptidoglycan Production by an Insect-Bacterial Mosaic; Cell; Vol. 179; No. 3; 703-712; PMCID PMC6838666; 10.1016/j.cell.2019.08.054
• Escolano, Amelia and West, Anthony P., Jr., et el. (2019) Immunization expands B cells specific to HIV-1 V3 glycan in mice and macaques; Nature; Vol. 570; No. 7762; 468-473; PMCID PMC6657810; 10.1038/s41586-019-1250-z
• Schoofs, Till and Barnes, Christopher O., et el. (2019) Broad and Potent Neutralizing Antibodies Recognize the Silent Face of the HIV Envelope; Immunity; Vol. 50; No. 6; 1513-1529; PMCID PMC6591006; 10.1016/j.immuni.2019.04.014
• Ladinsky, Mark S. and Araujo, Leandro P., et el. (2019) Endocytosis of commensal antigens by intestinal epithelial cells regulates mucosal T cell homeostasis; Science; Vol. 363; No. 6431; Art. No. eaat4042; PMCID PMC6708280; 10.1126/science.aat4042
• Uchil, Pradeep D. and Pi, Ruoxi, et el. (2019) A Protective Role for the Lectin CD169/Siglec-1 against a Pathogenic Murine Retrovirus; Cell Host & Microbe; Vol. 25; No. 1; 87-100; PMCID PMC6331384; 10.1016/j.chom.2018.11.011
• Einav, Tal and Gnanapragasam, Priyanthi N. P., et el. (2018) Modeling Entropic and Energetic Effects of Linker Length and Rigidity within Synthetic HIV-1 Antibodies designed to Bind Bivalently to Env Spikes; 10.1101/406454
• Kinchen, Valerie J. and Zahid, Muhammad N., et el. (2018) Broadly Neutralizing Antibody Mediated Clearance of Human Hepatitis C Virus Infection; Cell Host & Microbe; Vol. 24; No. 5; 717-730; PMCID PMC6250073; 10.1016/j.chom.2018.10.012
• Flyak, Andrew I. and Ruiz, Stormy, et el. (2018) HCV Broadly Neutralizing Antibodies Use a CDRH3 Disulfide Motif to Recognize an E2 Glycoprotein Site that Can Be Targeted for Vaccine Design; Cell Host & Microbe; Vol. 24; No. 5; 703-716; PMCID PMC6258177; 10.1016/j.chom.2018.10.009
• Keeffe, Jennifer R. and Van Rompay, Koen K. A., et el. (2018) A Combination of Two Human Monoclonal Antibodies Prevents Zika Virus Escape Mutations in Non-human Primates; Cell Reports; Vol. 25; No. 6; 1385-1394; PMCID PMC6268006; 10.1016/j.celrep.2018.10.031
• Chuang, Gwo-Yu and Zhou, Jing, et el. (2018) Structural survey of HIV-1-neutralizing antibodies targeting Env trimer delineates epitope categories and suggests vaccine templates; 10.1101/312579
• Wang, Haoqing and Barnes, Christopher O., et el. (2018) Partially Open HIV-1 Envelope Structures Exhibit Conformational Changes Relevant for Coreceptor Binding and Fusion; Cell Host & Microbe; Vol. 24; No. 4; 579-592; PMCID PMC6185872; 10.1016/j.chom.2018.09.003
• Gristick, Harry and van Schooten, Jelle, et el. (2018) Engineering HIV Immunogens to Elicit IOMA-like Antibodies Targeting the CD4 Binding Site; AIDS Research and Human Retroviruses; Vol. 34; No. S1; 59; 10.1089/aid.2018.5000.abstracts
• Barnes, Christopher O. and Wang, Haoqing, et el. (2018) A Co-receptor-mimicking Antibody Stabilizes the Displaced V1V2 Loops in a Partially Open sCD4-bound HIV-1 Envelope Complex; AIDS Research and Human Retroviruses; Vol. 34; No. S1; 131; 10.1089/aid.2018.5000.abstracts
• Escolano, Amelia and Gristick, Harry B., et el. (2018) Sequential Immunization Strategies to Elicit HIV-1 bNAbs in Animal Models With a Polyclonal B Cell Repertoire; AIDS Research and Human Retroviruses; Vol. 34; No. S1; 331; 10.1089/aid.2018.5000.abstracts
• Galimidi, Rachel P. and Einav, Tal, et el. (2018) Quantifying the Entropic and Energetic Effects of Linker Length and Rigidity within Synthetic HIV-1 Antibodies designed to Bind Bivalently to Env Spikes; 10.1101/406454
• Mendoza, Pilar and West, Anthony P., Jr., et el. (2018) Combination therapy with anti-HIV-1 antibodies maintains viral suppression; Nature; Vol. 561; No. 7724; 479-484; PMCID PMC6166473; 10.1038/s41586-018-0531-2
• Stadtmueller, Beth M. and Bridges, Michael D., et el. (2018) DEER Spectroscopy Measurements Reveal Multiple Conformations of HIV-1 SOSIP Envelopes that Show Similarities with Envelopes on Native Virions; Immunity; Vol. 49; No. 2; 235-246; PMCID PMC6104740; 10.1016/j.immuni.2018.06.017
• Donaldson, G. P. and Ladinsky, M. S., et el. (2018) Gut microbiota utilize immunoglobulin A for mucosal colonization; Science; Vol. 360; No. 6390; 795-800; PMCID PMC5973787; 10.1126/science.aaq0926
• Barnes, Christopher O. and Gristick, Harry B., et el. (2018) Structural characterization of a highly-potent V3-glycan broadly neutralizing antibody bound to natively-glycosylated HIV-1 envelope; Nature Communications; Vol. 9; Art. No. 1251; PMCID PMC5871869; 10.1038/s41467-018-03632-y
• Kieffer, Collin and Ladinsky, Mark S., et el. (2017) Multiscale imaging of HIV-1 transmission in humanized mice; AIDS Research and Human Retroviruses; Vol. 33; No. S1; S6-S7; PMCID PMC5685215; 10.1089/AID.2017.0142
• Scheid, Johannes and Nussenzweig, Michel, et el. (2017) Human immunodeficiency virus neutralizing antibodies and methods of use thereof [APPLICATION]
• Gristick, Harry B. and Wang, Haoqing, et el. (2017) X-ray and EM structures of a natively glycosylated HIV-1 envelope trimer; Acta Crystallographica Section D Structural Biology; Vol. 73; No. 10; 822-828; PMCID PMC5633907; 10.1107/S2059798317013353
• Greider, Carol and Bjorkman, Pamela (2017) Not just Salk; Science; Vol. 357; No. 6356; 1105-1106; 10.1126/science.aao6221
• Chiuppesi, Flavia and Wussow, Felix, et el. (2017) Comparison of homologous and heterologous prime-boost vaccine approaches using Modified Vaccinia Ankara and soluble protein to induce neutralizing antibodies by the human cytomegalovirus pentamer complex in mice; PLoS ONE; Vol. 12; No. 8; Art. No. e0183377; PMCID PMC5558987; 10.1371/journal.pone.0183377
• Wang, Haoqing and Gristick, Harry B., et el. (2017) Asymmetric recognition of HIV-1 Envelope trimer by V1V2 loop-targeting antibodies; eLife; Vol. 6; Art. No. e27389; PMCID PMC5472438; 10.7554/eLife.27389.001
• Robbiani, Davide F. and Khouri, Ricardo, et el. (2017) Recurrent Potent Human Neutralizing Antibodies to Zika Virus in Brazil and Mexico; Cell; Vol. 169; No. 4; 597-609; PMCID PMC5492969; 10.1016/j.cell.2017.04.024
• Gu, Mingyu and Lajoie, Dollie, et el. (2017) LEM2 recruits CHMP7 for ESCRT-mediated nuclear envelope closure in fission yeast and human cells; Proceedings of the National Academy of Sciences of the United States of America; Vol. 114; No. 11; E2166-E2175; PMCID PMC5358359; 10.1073/pnas.1613916114
• Kieffer, Collin and Ladinsky, Mark S., et el. (2017) Longitudinal imaging of HIV-1 spread in humanized mice with parallel 3D immunofluorescence and electron tomography; eLife; Vol. 6; Art. No. e23282; PMCID PMC5338924; 10.7554/eLife.23282
• Caskey, Marina and West, Anthony P., Jr., et el. (2017) Antibody 10-1074 suppresses viremia in HIV-1-infected individuals; Nature Medicine; Vol. 23; No. 2; 185-191; PMCID PMC5467219; 10.1038/nm.4268
• Freund, Natalia T. and Wang, Haoqing, et el. (2017) Coexistence of potent HIV-1 broadly neutralizing antibodies and antibody-sensitive viruses in a viremic controller; Science Translational Medicine; Vol. 9; No. 373; Art. No. aal2144; PMCID PMC5467220; 10.1126/scitranslmed.aal2144
• Gu, M. and Chen, O. S., et el. (2016) Lem2p (LEM2) and Cmp7p (CHMP7) function in ESCRT-dependent nuclear envelope remodeling in fission yeast; Molecular Biology of the Cell; Vol. 27; Art. No. P498
• Gu, M. and LaJoie, D., et el. (2016) Non-Canonical ESCRT Structures and Functions; Molecular Biology of the Cell; Vol. 27; No. 25; M191; 10.1091/mbc.E16-10-0736
• Wang, Haoqing and Cohen, Alexander A., et el. (2016) Cryo-EM structure of a CD4-bound open HIV-1 envelope trimer reveals structural rearrangements of the gp120 V1V2 loop; Proceedings of the National Academy of Sciences of the United States of America; Vol. 113; No. 46; E7151-E7158; PMCID PMC5135367; 10.1073/pnas.1615939113
• Diskin, Ron and Bjorkman, Pamela J., et el. (2016) Antibodies directed toward the HIV-1 GP120 CD4 binding site with increased potency and breadth
• Owens, Gwen E. and New, Danielle M., et el. (2016) Comparative analysis of anti-polyglutamine Fab crystals grown on Earth and in microgravity; Acta Crystallographica Section F: Structural Biology and Crystallization Communications; Vol. 72; No. 10; 762-771; PMCID PMC5053161; 10.1107/S2053230X16014011
• Gristick, Harry B. and von Boehmer, Lotta, et el. (2016) Natively glycosylated HIV-1 Env structure reveals new mode for antibody recognition of the CD4-binding site; Nature Structural & Molecular Biology; Vol. 23; No. 10; 906-915; PMCID PMC5127623; 10.1038/nsmb.3291
• Gristick, Harry and von Boehmer, Lotta, et el. (2016) Structure of a Natively-glycosylated HIV-1 Env Reveals a New Mode for VH1-2 Antibody Recognition of the CD4 Binding Site Relevant to Vaccine Design; AIDS Research and Human Retroviruses; Vol. 32; No. Suppl. 1; 62
• Stadtmueller, Beth M. and Yang, Zhongyu, et el. (2016) Biophysical and Biochemical Characterization of Avian Secretory Component Provides Structural Insights into the Evolution of the Polymeric Ig Receptor; Journal of Immunology; Vol. 197; No. 4; 1408-1414; PMCID PMC4976031; 10.4049/jimmunol.1600463
• Scheid, Johannes F. and West, Anthony P., Jr., et el. (2016) HIV-1 antibody 3BNC117 suppresses viral rebound in humans during treatment interruption; Nature; Vol. 535; No. 7613; 556-560; PMCID PMC5034582; 10.1038/nature18929
• Schoofs, Till and Klein, Florian, et el. (2016) HIV-1 therapy with monoclonal antibody 3BNC117 elicits host immune responses against HIV-1; Science; Vol. 352; No. 6288; 997-1001; PMCID PMC5151174; 10.1126/science.aaf0972
• Ahmed, Alysia A. and Keremane, Sravya R., et el. (2016) Structural characterization of GASDALIE Fc bound to the activating Fc receptor FcγRIIIa; Journal of Structural Biology; Vol. 194; No. 1; 78-89; PMCID PMC4769027; 10.1016/j.jsb.2016.02.001
• Scharf, Louise and West, Anthony P. , Jr., et el. (2016) Structural basis for germline antibody recognition of HIV-1 immunogens; eLife; Vol. 5; Art. No. e13783; PMCID PMC4811768; 10.7554/eLife.13783
• Stadtmueller, Beth M. and Huey-Tubman, Kathryn E., et el. (2016) The structure and dynamics of secretory component and its interactions with polymeric immunoglobulins; eLife; Vol. 5; Art. No. e10640; PMCID PMC4786434; 10.7554/eLife.10640
• Morgand, Marion and Bouvin-Pley, Mélanie, et el. (2016) V1/V2 Neutralizing Epitope is Conserved in Divergent Non-M Groups of HIV-1; Journal of Acquired Immune Deficiency Syndromes; Vol. 71; No. 3; 237-245; PMCID PMC4770367; 10.1097/QAI.0000000000000854
• Ndjamen, Blaise and Joshi, Devashish S., et el. (2016) Characterization of Antibody Bipolar Bridging Mediated by the Human Cytomegalovirus Fc receptor gp68; Journal of Virology; Vol. 90; No. 6; 3262-3567; PMCID PMC4810659; 10.1128/JVI.02855-15
• Ding, Shilei and Veillete, Maxime, et el. (2016) A Highly-Conserved Residue of the HIV-1-gp120 Inner Domain is Important for ADCC Responses Mediated by Anti-Cluster A Antibodies; Journal of Virology; Vol. 90; No. 4; 2127-2134; PMCID PMC4733974; 10.1128/JVI.02779-15
• Davenport, Yunji W. and West, Anthony P., et el. (2016) Structure of an HIV-2 gp120 in complex with CD4; Journal of Virology; Vol. 90; No. 4; 2112-2118; PMCID PMC4733984; 10.1128/JVI.02678-15
• Treweek, Jennifer B. and Chan, Ken Y., et el. (2015) Whole-body tissue stabilization and selective extractions via tissue-hydrogel hybrids for high-resolution intact circuit mapping and phenotyping; Nature Protocols; Vol. 10; No. 11; 1860-1896; PMCID PMC4917295; 10.1038/nprot.2015.122
• Sewald, Xaver and Ladinsky, Mark S., et el. (2015) Retroviruses use CD169-mediated trans-infection of permissive lymphocytes to establish infection; Science; Vol. 350; No. 6260; 563-567; PMCID PMC4651917; 10.1126/science.aab2749
• Freund, Natalia T. and Horwitz, Joshua A., et el. (2015) A New Glycan-Dependent CD4-Binding Site Neutralizing Antibody Exerts Pressure on HIV-1 In Vivo; PLoS Pathogens; Vol. 11; No. 10; Art. No. e1005238; PMCID PMC4627763; 10.1371/journal.ppat.1005238
• Scharf, Louise and Wang, Haoqing, et el. (2015) Broadly Neutralizing Antibody 8ANC195 Recognizes Closed and Open States of HIV-1 Env; Cell; Vol. 162; No. 6; 1379-1390; PMCID PMC4587768; 10.1016/j.cell.2015.08.035
• Owens, Gwen E. and New, Danielle M., et el. (2015) Anti-polyQ antibodies recognize a short polyQ stretch in both normal and mutant huntingtin exon 1; Journal of Molecular Biology; Vol. 427; No. 15; 2507-2519; PMCID PMC4520773; 10.1016/j.jmb.2015.05.023
• Yoon, Hyejin and Macke, Jennifer, et el. (2015) CATNAP: a tool to compile, analyze and tally neutralizing antibody panels; Nucleic Acids Research; Vol. 43; No. W1; W213-W219; PMCID PMC4489231; 10.1093/nar/gkv404
• Dosenovic, Pia and von Boehmer, Lotta, et el. (2015) Immunization for HIV-1 Broadly Neutralizing Antibodies in Human Ig Knockin Mice; Cell; Vol. 161; No. 7; 1505-1515; PMCID PMC4604566; 10.1016/j.cell.2015.06.003
• Zhou, Tongqing and West, Anthony P., Jr., et el. (2015) Structural Repertoire of HIV-1-Neutralizing Antibodies Targeting the CD4 Supersite in 14 Donors; Cell; Vol. 161; No. 6; 1280-1292; PMCID PMC4683157; 10.1016/j.cell.2015.05.007
• Sievers, Stuart A. and Scharf, Louise, et el. (2015) Antibody engineering for increased potency, breadth and half-life; Current Opinion in HIV and AIDS; Vol. 10; No. 3; 151-159; PMCID PMC4465343; 10.1097/COH.0000000000000148
• Ndjamen, Blaise and Bjorkman, Pamela (2015) Distinct Intracellular Trafficking Patterns of Host IgG by Herpes Virus Fc-Receptors; FASEB Journal; Vol. 29; No. S1; Art. No. 574.30
• Barbian, Hannah J. and Galimidi, Rachel P., et el. (2015) Neutralization Properties of Simian Immunodeficiency Viruses Infecting Chimpanzees and Gorillas; mBio; Vol. 6; No. 2; Art. No. e00296; PMCID PMC4453581; 10.1128/mBio.00296-15
• Galimidi, Rachel P. and Klein, Joshua S., et el. (2015) Intra-Spike Crosslinking Overcomes Antibody Evasion by HIV-1; Cell; Vol. 160; No. 3; 433-446; PMCID PMC4401576; 10.1016/j.cell.2015.01.016
• Wu, Yunji and Bjorkman, Pamela J. (2015) Structural Basis for Enhanced Hiv-1 Neutralization by a Dimeric Immunoglobulin G Form of the Glycan-Recognizing Antibody 2G12; Biophysical Journal; Vol. 108; No. 2; 374A; 10.1016/j.bpj.2014.11.2053
• Bjorkman, Pamela J. (2015) Not Second Class: The First Class II MHC Crystal Structure; Journal of Immunology; Vol. 194; No. 1; 3-4; 10.4049/jimmunol.1402828
• Ndjamen, B. and Fraser, S. E., et el. (2014) Distinct Intracellular Trafficking Patterns of Host IgG by Herpes Virus Fc-Receptors
• Bouvin-Pley, M. and Morgand, M., et el. (2014) Drift of the HIV-1 envelope glycoprotein gp120 toward increased neutralization resistance over the course of the epidemic: a comprehensive study using the most potent and broadly neutralizing monoclonal antibodies; Journal of Virology; Vol. 88; No. 23; 13910-13917; PMCID PMC4248973; 10.1128/JVI.02083-14
• Klein, Florian and Nogueira, Lilian, et el. (2014) Enhanced HIV-1 immunotherapy by commonly arising antibodies that target virus escape variants; Journal of Experimental Medicine; Vol. 211; No. 12; 2361-2372; PMCID PMC4235636; 10.1084/jem.20141050
• Sievers, Stuart A. and Patel, Sonal N., et el. (2014) Engineering Antibodies to Enhance Activity and Increase Half-life; AIDS Research and Human Retroviruses; Vol. 30; No. S1; A210; 10.1089/aid.2014.5456.abstract
• Bouvin-Pley, Mélanie and Morgand, Marion, et el. (2014) Adaptation of HIV-1 Envelope Glycoprotein gp120 to Humoral Immunity over the Course of the Epidemic; AIDS Research and Human Retroviruses; Vol. 30; No. S1; A224; 10.1089/aid.2014.5490.abstract
• Nishimura, Yoshiaki and Shingai, Masashi, et el. (2014) Preexposure passive transfer predicts plasma antibody levels prevent HIV-I aquisition; Journal of Medical Primatology; Vol. 43; No. 5; 378; 10.1111/jmp.12150
• Klein, Joshua S. and Jiang, Siduo, et el. (2014) Design and characterization of structured protein linkers with differing flexibilities; Protein Engineering, Design and Selection; Vol. 27; No. 10; 325-330; PMCID PMC4191447; 10.1093/protein/gzu043
• Shingai, Masashi and Bjorkman, Pamela J. (2014) Passive transfer of modest titers of potent and broadly neutralizing anti-HIV monoclonal antibodies block SHIV infection in macaques; Journal of Experimental Medicine; Vol. 211; No. 10; 2061-2074; PMCID PMC4172223; 10.1084/jem.20132494
• Ahmed, Alysia A. and Giddens, John, et el. (2014) Structural characterization of anti-inflammatory Immunoglobulin G Fc proteins; Journal of Molecular Biology; Vol. 426; No. 18; 3166-3179; PMCID PMC4159253; 10.1016/j.jmb.2014.07.006
• Bjorkman, Pamela (2014) Engineering Improved Antibodies Against HIV; Protein Science; Vol. 23; No. S1; 62-63; 10.1002/pro.2504
• Scharf, Louise and Scheid, Johannes F., et el. (2014) Antibody 8ANC195 Reveals a Site of Broad Vulnerability on the HIV-1 Envelope Spike; Cell Reports; Vol. 7; No. 3; 785-795; PMCID PMC4109818; 10.1016/j.celrep.2014.04.001
• Ndjamen, Blaise and Farley, Alexander H., et el. (2014) The Herpes Virus Fc Receptor gE-gI Mediates Antibody Bipolar Bridging to Clear Viral Antigens from the Cell Surface; PLoS Pathogens; Vol. 10; No. 3; Art. No. e1003961; PMCID PMC3946383; 10.1371/journal.ppat.1003961
• West, Anthony P., Jr. and Scharf, Louise, et el. (2014) Structural Insights on the Role of Antibodies in HIV-1 Vaccine and Therapy; Cell; Vol. 156; No. 4; 633-648; PMCID PMC4041625; 10.1016/j.cell.2014.01.052
• Ladinsky, Mark S. and Kieffer, Collin, et el. (2014) Electron Tomography of HIV-1 Infection in Gut-Associated Lymphoid Tissue; PLoS Pathogens; Vol. 10; No. 1; Art. No. e1003899; PMCID PMC3907528; 10.1371/journal.ppat.1003899
• Wu, Yunji and West, Anthony P., Jr., et el. (2013) Structural Basis for Enhanced HIV-1 Neutralization by a Dimeric Immunoglobulin G Form of the Glycan-Recognizing Antibody 2G12; Cell Reports; Vol. 5; No. 5; 1443-1455; PMCID PMC3919625; 10.1016/j.celrep.2013.11.015
• West, A. P., Jr. and Scharf, L., et el. (2013) Computational Analysis of Anti-HIV-1 Antibody Neutralization Panel Data to Identify Potential Functional Epitope Residues; AIDS Research and Human Retroviruses; Vol. 29; No. 11; A170; 10.1089/aid.2013.1500
• Galimidi, R. P. and West, A. P., et el. (2013) Thwarting HIV Evasion of Antibody Avidity with Novel Antibody Architectures; AIDS Research and Human Retroviruses; Vol. 29; No. 11; A140-A141; 10.1089/aid.2013.1500
• Scharf, L. and West, A. P., et el. (2013) Structural Basis for HIV-1 gp120 Recognition by a Germ-line Version of a Broadly Neutralizing Antibody; AIDS Research and Human Retroviruses; Vol. 29; No. 11; A11-A12; 10.1089/aid.2013.1500
• Horwitz, Joshua A. and Halper-Stromberg, Ariel, et el. (2013) HIV-1 suppression and durable control by combining single broadly neutralizing antibodies and antiretroviral drugs in humanized mice; Proceedings of the National Academy of Sciences of the United States of America; Vol. 110; No. 41; 16538-16543; PMCID PMC3799352; 10.1073/pnas.1315295110
• West, Anthony P., Jr. and Scharf, Louise, et el. (2013) Computational analysis of anti-HIV-1 antibody neutralization panel data to identify potential functional epitope residues; Proceedings of the National Academy of Sciences of the United States of America; Vol. 110; No. 26; 10598-10603; PMCID PMC3696754; 10.1073/pnas.1309215110
• Diskin, Ron and Klein, Florian, et el. (2013) Restricting HIV-1 pathways for escape using rationally designed anti–HIV-1 antibodies; Journal of Experimental Medicine; Vol. 210; No. 6; 1235-1249; PMCID PMC3674693; 10.1084/jem.20130221
• Galimidi, Rachel and West, Anthony, et el. (2013) Thwarting HIV evasion of antibody avidity with novel antibody architectures; Journal of Immunology; Vol. 190; 179.7
• Parrish, Nicholas F. and Galimidi, Rachel P., et el. (2013) Phenotypic properties of transmitted founder HIV-1; Proceedings of the National Academy of Sciences of the United States of America; Vol. 110; No. 17; 6626-6633; PMCID PMC3637789; 10.1073/pnas.1304288110
• Scharf, Louise and West, Anthony P., Jr., et el. (2013) Structural basis for HIV-1 gp120 recognition by a germ-line version of a broadly neutralizing antibody; Proceedings of the National Academy of Sciences of the United States of America; Vol. 110; No. 15; 6049-6054; PMCID PMC3625305; 10.1073/pnas.1303682110
• Ndjamen, Blaise and Farley, Alexander, et el. (2013) Intracellular Trafficking of an Antibody Bipolar Bridged Complex of HSV-1 gE-gI, IgG, and a Viral Antigen; FASEB Journal; Vol. 27; Art. No. 767.3
• Diskin, Ron and Sather, D. Noah, et el. (2013) Overcoming HIV pathways for escape using rationally-designed anti-HIV antibodies; Journal of Acquired Immune Deficiency Syndromes; Vol. 62; No. S1; 49-49; 10.1097/01.qai.0000429234.07501.af
• Klein, Florian and Diskin, Ron, et el. (2013) Somatic Mutations of the Immunoglobulin Framework Are Generally Required for Broad and Potent HIV-1 Neutralization; Cell; Vol. 153; No. 1; 126-138; PMCID PMC3792590; 10.1016/j.cell.2013.03.018
• Klein, Florian and Halper-Stromberg, Ariel, et el. (2012) HIV therapy by a combination of broadly neutralizing antibodies in humanized mice; Nature; Vol. 492; No. 7427; 118-122; PMCID PMC3809838; 10.1038/nature11604
• Mouquet, Hugo and Scharf, Louise, et el. (2012) Complex-type N-glycan recognition by potent broadly neutralizing HIV antibodies; Proceedings of the National Academy of Sciences of the United States of America; Vol. 109; No. 47; E3268-E3277; PMCID PMC3511153; 10.1073/pnas.1217207109
• Pietzsch, John and Gruell, Henning, et el. (2012) A mouse model for HIV-1 entry; Proceedings of the National Academy of Sciences of the United States of America; Vol. 109; No. 39; 15859-15864; PMCID PMC3465400; 10.1073/pnas.1213409109
• West, A. P., Jr. and Diskin, R., et el. (2012) Structural basis for germline gene usage of a potent class of antibodies targeting the CD4 binding site of HIV-1 gp120; Retrovirology; Vol. 9; No. S2; Art. No. O33; PMCID PMC3441645; 10.1186/1742-4690-9-S2-O33
• West, Anthony P., Jr. and Diskin, Ron, et el. (2012) Structural basis for germ-line gene usage of a potent class of antibodies targeting the CD4-binding site of HIV-1 gp120; Proceedings of the National Academy of Sciences of the United States of America; Vol. 109; No. 30; E2983-E2090; PMCID PMC3409792; 10.1073/pnas.1208984109
• Ladinsky, Mark S. and Huey-Tubman, Kathryn E., et el. (2012) Electron tomography of late stages of FcRn-mediated antibody transcytosis in neonatal rat small intestine; Molecular Biology of the Cell; Vol. 23; No. 13; 2537-2545; PMCID PMC3386217; 10.1091/mbc.E12-02-0093
• Ndjamen, Blaise and Farley, Alexander, et el. (2012) A Model System to Investigate Antibody Bipolar Bridging Mediated by gE-gI, a Herpes Virus Fc Receptor; FASEB Journal; Vol. 26; Art. No. 605.8
• West, Anthony P., Jr. and Galimidi, Rachel P., et el. (2012) Single-Chain Fv-Based Anti-HIV Proteins: Potential and Limitations; Journal of Virology; Vol. 86; No. 1; 195-202; PMCID PMC3255864; 10.1128/JVI.05848-11
• Diskin, Ron and Scheid, Johannes F., et el. (2011) Increasing the Potency and Breadth of an HIV Antibody by Using Structure-Based Rational Design; Science; Vol. 334; No. 6060; 1289-1293; PMCID PMC3232316; 10.1126/science.1213782
• Bai, Yu and Ye, Lilin, et el. (2011) Intracellular neutralization of viral infection in polarized epithelial cells by neonatal Fc receptor (FcRn)-mediated IgG transport; Proceedings of the National Academy of Sciences of the United States of America; Vol. 108; No. 45; 18406-18411; PMCID PMC3215070; 10.1073/pnas.1115348108
• Scheid, Johannes F. and Mouquet, Hugo, et el. (2011) Sequence and Structural Convergence of Broad and Potent HIV Antibodies That Mimic CD4 Binding; Science; Vol. 333; No. 6049; 1633-1637; PMCID PMC3351836; 10.1126/science.1207227
• Keeffe, Jennifer R. and Gnanapragasam, Priyanthi N. P., et el. (2011) Designed oligomers of cyanovirin-N show enhanced HIV neutralization; Proceedings of the National Academy of Sciences of the United States of America; Vol. 108; No. 34; 14079-14084; PMCID PMC3161612; 10.1073/pnas.1108777108
• He, Yongning and Bjorkman, Pamela J. (2011) Structure of FcRY, an avian immunoglobulin receptor related to mammalian mannose receptors, and its complex with IgY; Proceedings of the National Academy of Sciences of the United States of America; Vol. 108; No. 30; 12431-12436; PMCID PMC3145690; 10.1073/pnas.1106925108
• Yang, Fan and West, Anthony P., Jr., et el. (2011) Crystal structure of a hemojuvelin-binding fragment of neogenin at 1.8 Å; Journal of Structural Biology; Vol. 174; No. 1; 239-244; PMCID PMC3074981; 10.1016/j.jsb.2010.10.005
• Luo, Xin M. and Lei, Margarida Y. Y., et el. (2010) Dimeric 2G12 as a Potent Protection against HIV-1; PLoS Pathogens; Vol. 6; No. 12; Art. No. e1001225; PMCID PMC3002980; 10.1371/journal.ppat.1001225
• Jerdeva, Galina V. and Tesar, Devin B., et el. (2010) Comparison of FcRn- and pIgR-Mediated Transport in MDCK Cells by Fluorescence Confocal Microscopy; Traffic; Vol. 11; No. 9; 1205-1220; PMCID PMC2975666; 10.1111/j.1600-0854.2010.01083.x
• Klein, Joshua S. and Webster, Alexandre, et el. (2010) A dimeric form of the HIV-1 antibody 2G12 elicits potent antibody-dependent cellular cytotoxicity; AIDS; Vol. 24; No. 11; 1633-1640; PMCID PMC2898891; 10.1097/QAD.0b013e32833ad8c8
• Gleick, P. H. and Anderson, D. J., et el. (2010) Climate Change and the Integrity of Science; Science; Vol. 328; No. 5979; 689-690; PMCID PMC5125622; 10.1126/science.328.5979.689
• Klein, Joshua S. and Bjorkman, Pamela J. (2010) Few and Far Between: How HIV May Be Evading Antibody Avidity; PLoS Pathogens; Vol. 6; No. 5; Art. No. e1000908; PMCID PMC2877745; 10.1371/journal.ppat.1000908
• Diskin, Ron and Marcovecchio, Paola M., et el. (2010) Structure of a clade C HIV-1 gp120 bound to CD4 and CD4-induced antibody reveals anti-CD4 polyreactivity; Nature Structural & Molecular Biology; Vol. 17; No. 5; 608-614; PMCID PMC2949298; 10.1038/nsmb.1796
• Tesar, Devin B. and Bjorkman, Pamela J. (2010) An intracellular traffic jam: Fc receptor-mediated transport of immunoglobulin G; Current Opinion in Structural Biology; Vol. 20; No. 2; 226-233; PMCID PMC2865255; 10.1016/j.sbi.2010.01.010
• Li, Li and Fang, Celia J., et el. (2010) Binding and uptake of H-ferritin are mediated by human transferrin receptor-1; Proceedings of the National Academy of Sciences of the United States of America; Vol. 107; No. 8; 3505-3510; PMCID PMC2840523; 10.1073/pnas.0913192107
• West, Anthony P., Jr. and Galimidi, Rachel P., et el. (2010) Evaluation of CD4-CD4i Antibody Architectures Yields Potent, Broadly Cross-Reactive Anti-Human Immunodeficiency Virus Reagents; Journal of Virology; Vol. 84; No. 1; 261-269; PMCID PMC2798438; 10.1128/JVI.01528-09
• Yang, Zhiru and West, Anthony P., Jr., et el. (2009) Crystal structure of TNFα complexed with a poxvirus MHC-related TNF binding protein; Nature Structural & Molecular Biology; Vol. 16; No. 11; 1189-1191; PMCID PMC2819277; 10.1038/nsmb.1683
• He, Yongning and Jensen, Grant J., et el. (2009) Nanogold as a specific marker for electron cryotomography; Microscopy and Microanalysis; Vol. 15; No. 3; 183-188; PMCID PMC2785728; 10.1017/S1431927609090424
• Klein, Joshua S. and Gnanapragasam, Priyanthi N. P., et el. (2009) Examination of the contributions of size and avidity to the neutralization mechanisms of the anti-HIV antibodies b12 and 4E10; Proceedings of the National Academy of Sciences of the United States of America; Vol. 106; No. 18; 7385-7390; PMCID PMC2678646; 10.1073/pnas.0811427106
• He, Yongning and Jensen, Grant J., et el. (2009) Cryo-electron tomography of homophilic adhesion mediated by the neural cell adhesion molecule L1; Structure; Vol. 17; No. 3; 460-471; PMCID PMC2744468; 10.1016/j.str.2009.01.009
• Rice, Adrian E. and Mendez, Michael J., et el. (2009) Investigation of the biophysical and cell biological properties of ferroportin, a multipass integral membrane protein iron exporter; Journal of Molecular Biology; Vol. 386; No. 3; 717-732; PMCID PMC2677177; 10.1016/j.jmb.2008.12.063
• West, Anthony P., Jr. and Galimidi, Rachel P., et el. (2009) Design and Expression of a Dimeric Form of the Human Immunodeficiency Virus Type 1 Antibody 2G12 with Increased Neutralization Potency; Journal of Virology; Vol. 83; No. 1; 98-104; PMCID PMC2612297; 10.1128/JVI.01564-08
• He, Wanzhong and Ladinsky, Mark S., et el. (2008) FcRn-mediated antibody transport across epithelial cells revealed by electron tomography; Nature; Vol. 455; No. 7212; 542-546; PMCID PMC2773227; 10.1038/nature07255
• Arnon, Tal I. and Kaiser, Jens T., et el. (2008) The Crystal Structure of CHIR-AB1: A Primordial Avian Classical Fc Receptor; Journal of Molecular Biology; Vol. 381; No. 4; 1012-1024; PMCID PMC2603183; 10.1016/j.jmb.2008.06.082
• Yang, Zhiru and Bjorkman, Pamela J. (2008) Structure of UL18, a peptide-binding viral MHC mimic, bound to a host inhibitory receptor; Proceedings of the National Academy of Sciences of the United States of America; Vol. 105; No. 29; 10095-10100; PMCID PMC2465803; 10.1073/pnas.0804551105
• Zhang, An-Sheng and Yang, Fan, et el. (2008) Neogenin-mediated hemojuvelin shedding occurs after hemojuvelin traffics to the plamsa membrane; Journal of Biological Chemistry; Vol. 283; No. 25; 17494-17502; PMCID PMC2427329; 10.1074/jbc.M710527200
• Morphew, M. and He, W., et el. (2008) Silver enhancement of Nanogold particles during freeze substitution for electron microscopy; Journal of Microscopy; Vol. 230; No. 2; 263-267; PMCID PMC2722379; 10.1111/j.1365-2818.2008.01983.x
• Yang, Fan and West, Anthony P., et el. (2008) Neogenin Interacts with Hemojuvelin through Its Two Membrane-Proximal Fibronectin Type III Domains; Biochemistry; Vol. 47; No. 14; 4237-4245; PMCID PMC2819367; 10.1021/bi800036h
• Sprague, Elizabeth R. and Reinhard, Henrike, et el. (2008) The Human Cytomegalovirus Fc Receptor gp68 Binds the Fc CH2-CH3 Interface of Immunoglobulin G; Journal of Virology; Vol. 82; No. 7; 3490-3499; PMCID PMC2268481; 10.1128/JVI.01476-07
• Tesar, Devin B. and Cheung, Evelyn J., et el. (2008) The Chicken Yolk Sac IgY Receptor, a Mammalian Mannose Receptor Family Member, Transcytoses IgY across Polarized Epithelial Cells; Molecular Biology of the Cell; Vol. 19; No. 4; 1587-1593; PMCID PMC2291411; 10.1091/mbc.E07-09-0972
• Schmidt, Paul J. and Toran, Paul T., et el. (2008) The Transferrin Receptor Modulates Hfe-Dependent Regulation of Hepcidin Expression; Cell Metabolism; Vol. 7; No. 3; 205-214; PMCID PMC2292811; 10.1016/j.cmet.2007.11.016
• He, Wanzhong and Kivork, Christine, et el. (2007) A freeze substitution fixation-based gold enlarging technique for EM studies of endocytosed nanogold-labeled molecules; Journal of Structural Biology; Vol. 160; No. 1; 103-113; PMCID PMC2076746; 10.1016/j.jsb.2007.07.004
• Ja, William W. and West, Anthony P., Jr., et el. (2007) Extension of Drosophila melanogaster life span with a GPCR peptide inhibitor; Nature Chemical Biology; Vol. 3; No. 7; 415-419; PMCID PMC2803097; 10.1038/nchembio.2007.2
• Li, Pingwei and Huey-Tubman, Kathryn E., et el. (2007) The structure of a polyQ–anti-polyQ complex reveals binding according to a linear lattice model; Nature Structural & Molecular Biology; Vol. 14; No. 5; 381-387; 10.1038/nsmb1234
• Tesar, Devin B. and Tiangco, Noreen E., et el. (2006) Ligand Valency Affects Transcytosis, Recycling and Intracellular Trafficking Mediated by the Neonatal Fc Receptor; Traffic; Vol. 7; No. 9; 1127-1142; PMCID PMC1618808; 10.1111/j.1600-0854.2006.00457.x
• Bjorkman, Pamela J. (2006) Finding the groove; Nature Immunology; Vol. 7; No. 8; 787-789; 10.1038/ni0806-787
• Olson, Rich and Dulac, Catherine, et el. (2006) MHC homologs in the nervous system — they haven't lost their groove; Current Opinion in Neurobiology; Vol. 16; No. 3; 351-357; 10.1016/j.conb.2006.05.007
• Sprague, Elizabeth R. and Wang, Chu, et el. (2006) Crystal Structure of the HSV-1 Fc Receptor Bound to Fc Reveals a Mechanism for Antibody Bipolar Bridging; PLoS Biology; Vol. 4; No. 6; Art. No. e148; PMCID PMC1450327; 10.1371/journal.pbio.0040148
• McDermott, Lindsay C. and Freel, June A., et el. (2006) Zn-α_2-glycoprotein, an MHC Class I-Related Glycoprotein Regulator of Adipose Tissues: Modification or Abrogation of Ligand Binding by Site-Directed Mutagenesis; Biochemistry; Vol. 45; No. 7; 2035-2041; 10.1021/bi051881v
• Hamburger, A. E. and Bjorkman, P. J., et el. (2006) Structural Insights into Antibody-Mediated Mucosal Immunity; ISBN 978-3-540-30656-6; Gut-Associated Lymphoid Tissues; 173-204; 10.1007/3-540-30657-9_8
• Halbrooks, Peter J. and Giannetti, Anthony M., et el. (2005) Composition of pH-Sensitive Triad in C-Lobe of Human Serum Transferrin. Comparison to Sequences of Ovotransferrin and Lactoferrin Provides Insight into Functional Differences in Iron Release; Biochemistry; Vol. 44; No. 47; 15451-15460; 10.1021/bi0518693
• Giannetti, Anthony M. and Halbrooks, Peter J., et el. (2005) The Molecular Mechanism for Receptor-Stimulated Iron Release from the Plasma Iron Transport Protein Transferrin; Structure; Vol. 13; No. 11; 1613-1623; 10.1016/j.str.2005.07.016
• Zhang, An-Sheng and West, Anthony P., Jr., et el. (2005) Interaction of hemojuvelin with neogenin results in iron accumulation in human embryonic kidney 293 cells; Journal of Biological Chemistry; Vol. 280; No. 40; 33885-33894; 10.1074/jbc.M506207200
• Olson, Rich and Huey-Tubman, Kathryn E., et el. (2005) Structure of a Pheromone Receptor-Associated MHC Molecule with an Open and Empty Groove; PLoS Biology; Vol. 3; No. 8; 1436-1448; PMCID PMC1174912; 10.1371/journal.pbio.0030257
• Hamburger, Agnes E. and West, Anthony P., Jr., et el. (2005) Crystal Structure of a Secreted Insect Ferritin Reveals a Symmetrical Arrangement of Heavy and Light Chains; Journal of Molecular Biology; Vol. 349; No. 3; 558-569; 10.1016/j.jmb.2005.03.074
• Davis, Mindy I. and Bennett, Melanie J., et el. (2005) Crystal structure of prostate-specific membrane antigen, a tumor marker and peptidase; Proceedings of the National Academy of Sciences of the United States of America; Vol. 102; No. 17; 5981-5986; PMCID PMC556220; 10.1073/pnas.0502101102
• Luo, Rensheng and Mann, Beth, et el. (2005) Solution structure of choline binding protein A, the major adhesin of Streptococcus pneumoniae; EMBO Journal; Vol. 24; No. 1; 34-43; PMCID PMC544903; 10.1038/sj.emboj.7600490
• Bjorkman, P. J. and Saper, M. A., et el. (2005) Pillars Article: Structure of the human class I histocompatibility antigen, HLA-A2; Journal of Immunology; Vol. 174; No. 1; 6-12
• Hamburger, Agnes E. and West, Anthony P., Jr., et el. (2004) Crystal Structure of a Polymeric Immunoglobulin Binding Fragment of the Human Polymeric Immunoglobulin Receptor; Structure; Vol. 12; No. 11; 1925-1935; 10.1016/j.str.2004.09.006
• Delker, Silvia L. and West, Anthony P., Jr., et el. (2004) Crystallographic studies of ligand binding by Zn-α_2-glycoprotein; Journal of Structural Biology; Vol. 148; No. 2; 205-213; 10.1016/j.jsb.2004.04.009
• Giannetti, Anthony M. and Bjorkman, Pamela J. (2004) HFE and transferrin directly compete for transferrin receptor in solution and at the cell surface; Journal of Biological Chemistry; Vol. 279; No. 24; 25866-25875; 10.1074/jbc.M401467200
• West, Anthony P., Jr. and Herr, Andrew B., et el. (2004) The Chicken Yolk Sac IgY Receptor, a Functional Equivalent of the Mammalian MHC-Related Fc Receptor, Is a Phospholipase A_2 Receptor Homolog; Immunity; Vol. 20; No. 5; 601-610; 10.1016/S1074-7613(04)00113-X
• Sprague, Elizabeth R. and Martin, W. Lance, et el. (2004) pH Dependence and Stoichiometry of Binding to the Fc Region of IgG by the Herpes Simplex Virus Fc Receptor gE-gI; Journal of Biological Chemistry; Vol. 279; No. 14; 14184-14193; 10.1074/jbc.M313281200
• Giannetti, Anthony M. and Snow, Peter M., et el. (2003) Mechanism for Multiple Ligand Recognition by the Human Transferrin Receptor; PLoS Biology; Vol. 1; No. 3; 341-350; PMCID PMC300677; 10.1371/journal.pbio.0000051
• Willcox, Benjamin E. and Thomas, Leonard M., et el. (2003) Crystal structure of HLA-A2 bound to LIR-1, a host and viral major histocompatibility complex receptor; Nature Immunology; Vol. 4; No. 9; 913-919; 10.1038/ni961
• Herr, Andrew B. and Ballister, Edward R., et el. (2003) Insights into IgA-mediated immune responses from the crystal structures of human FcαRI and its complex with IgA1-Fc; Nature; Vol. 423; No. 6940; 614-620; 10.1038/nature01685
• Herr, Andrew B. and White, Clinton L., et el. (2003) Bivalent Binding of IgA1 to FcαRI Suggests a Mechanism for Cytokine Activation of IgA Phagocytosis; Journal of Molecular Biology; Vol. 327; No. 3; 645-657; 10.1016/S0022-2836(03)00149-9
• Vogt, Todd M. and Blackwell, Aaron D., et el. (2003) Heterotypic interactions between transferrin receptor and transferrin receptor 2; Blood; Vol. 101; No. 5; 2008-2014; 10.1182/blood-2002-09-2742
• Willcox, Benjamin E. and Thomas, Leonard M., et el. (2002) Crystal structure of LIR-2 (ILT4) at 1.8 Å: differences from LIR-1 (ILT2) in regions implicated in the binding of the Human Cytomegalovirus class I MHC homolog UL18; BMC Structural Biology; Vol. 2; Art. No. 6; PMCID PMC130215; 10.1186/1472-6807-2-6
• Bennett, Melanie J. and Huey-Tubman, Kathryn E., et el. (2002) A linear lattice model for polyglutamine in CAG-expansion diseases; Proceedings of the National Academy of Sciences of the United States of America; Vol. 99; No. 18; 11634-11639; PMCID PMC129321; 10.1073/pnas.182393899
• West, Anthony P., Jr. and Giannetti, Anthony M., et el. (2001) Mutational analysis of the transferrin receptor reveals overlapping HFE and transferrin binding sites; Journal of Molecular Biology; Vol. 313; No. 2; 385-397; 10.1006/jmbi.2001.5048
• Kennedy, Malcolm W. and Heikema, Astrid P., et el. (2001) Hydrophobic Ligand Binding by Zn-α_2-glycoprotein, a Soluble Fat-depleting Factor Related to Major Histocompatibility Complex Proteins; Journal of Biological Chemistry; Vol. 276; No. 37; 35008-35013; 10.1074/jbc.C100301200
• O'Callaghan, Christopher A. and Cerwenka, Adelheid, et el. (2001) Molecular Competition for NKG2D: H60 and RAE1 Compete Unequally for NKG2D with Dominance of H60; Immunity; Vol. 15; No. 2; 201-211; 10.1016/S1074-7613(01)00187-X
• Martin, W. Lance and West, Anthony P., Jr., et el. (2001) Crystal Structure at 2.8 Å of an FcRn/Heterodimeric Fc Complex: Mechanism of pH-Dependent Binding; Molecular Cell; Vol. 7; No. 4; 867-877; 10.1016/S1097-2765(01)00230-1
• West, Anthony P., Jr. and Llamas, Lynda L., et el. (2001) Crystal structure of the ectodomain of Methuselah, a Drosophila G protein-coupled receptor associated with extended lifespan; Proceedings of the National Academy of Sciences of the United States of America; Vol. 98; No. 7; 3744-3749; PMCID PMC31123; 10.1073/pnas.051625298
• Liu, Yang and Misulovin, Ziva, et el. (2001) The molecular mechanism of sulfated carbohydrate recognition by the cysteine-rich domain of mannose receptor; Journal of Molecular Biology; Vol. 305; No. 3; 481-490; 10.1006/jmbi.2000.4326
• West, Anthony P., Jr. and Bennett, Melanie J., et el. (2000) Comparison of the Interactions of Transferrin Receptor and Transferrin Receptor 2 with Transferrin and the Hereditary Hemochromatosis Protein HFE; Journal of Biological Chemistry; Vol. 275; No. 49; 38135-38138; 10.1074/jbc.C000664200
• Chapman, Tara L. and Heikema, Astrid P., et el. (2000) Crystal Structure and Ligand Binding Properties of the D1D2 Region of the Inhibitory Receptor LIR-1 (ILT2); Immunity; Vol. 13; No. 5; 727-736; 10.1016/S1074-7613(00)00071-6
• West, Anthony P., Jr. and Bjorkman, Pamela J. (2000) Crystal Structure and Immunoglobulin G Binding Properties of the Human Major Histocompatibility Complex-Related Fc Receptor; Biochemistry; Vol. 39; No. 32; 9698-9708; 10.1021/bi000749m
• Liu, Yang and Chirino, Arthur J., et el. (2000) Crystal Structure of the Cysteine-Rich Domain of Mannose Receptor Complexed with a Sulfated Carbohydrate Ligand; Journal of Experimental Medicine; Vol. 191; No. 7; 1105-1115; PMCID PMC2193177; 10.1084/jem.191.7.1105
• Bennett, Melanie J. and Lebrón, José A., et el. (2000) Crystal structure of the hereditary haemochromatosis protein HFE complexed with transferrin receptor; Nature; Vol. 403; No. 6765; 46-53; 10.1038/47417
• Lebrón, José A. and West, Anthony P., Jr., et el. (1999) The hemochromatosis protein HFE competes with transferrin for binding to the transferrin receptor; Journal of Molecular Biology; Vol. 294; No. 1; 239-245; 10.1006/jmbi.1999.3252
• Chapman, Tara L. and Heikema, Astrid P., et el. (1999) The Inhibitory Receptor LIR-1 Uses a Common Binding Interaction to Recognize Class I MHC Molecules and the Viral Homolog UL18; Immunity; Vol. 11; No. 5; 603-613; 10.1016/S1074-7613(00)80135-1
• Hamburger, Zsuzsa A. and Brown, Michele S., et el. (1999) Crystal Structure of Invasin: A Bacterial Integrin-Binding Protein; Science; Vol. 286; No. 5438; 291-295; 10.1126/science.286.5438.291
• Martin, W. Lance and Bjorkman, Pamela J. (1999) Characterization of the 2:1 Complex between the Class I MHC-Related Fc Receptor and Its Fc Ligand in Solution; Biochemistry; Vol. 38; No. 39; 12639-12647; 10.1021/bi9913505
• Sánchez, Luis M. and Penny, David M., et el. (1999) Stoichiometry of the Interaction between the Major Histocompatibility Complex-Related Fc Receptor and Its Fc Ligand; Biochemistry; Vol. 38; No. 29; 9471-9476; 10.1021/bi9907330
• Hanke, Thomas and Takizawa, Hisao, et el. (1999) Direct Assessment of MHC Class I Binding by Seven Ly49 Inhibitory NK Cell Receptors; Immunity; Vol. 11; No. 1; 67-77; 10.1016/S1074-7613(00)80082-5
• Lebrón, José A. and Bjorkman, Pamela J. (1999) The Transferrin Receptor Binding Site on HFE, the Class I MHC-related Protein Mutated in Hereditary Hemochromatosis; Journal of Molecular Biology; Vol. 289; No. 4; 1109-1118; 10.1006/jmbi.1999.2842
• Sánchez, Luis M. and Chirino, Arthur J., et el. (1999) Crystal Structure of Human ZAG, a Fat-Depleting Factor Related to MHC Molecules; Science; Vol. 283; No. 5409; 1914-1919; 10.1126/science.283.5409.1914
• Chapman, Tara L. and You, Il, et el. (1999) Characterization of the Interaction between the Herpes Simplex Virus Type I Fc Receptor and Immunoglobulin G; Journal of Biological Chemistry; Vol. 274; No. 11; 6911-6999; 10.1074/jbc.274.11.6911
• Lebrón, José A. and Shen, Huazhang, et el. (1999) Tolerization of adult mice to immunodominant proteins before monoclonal antibody production; Journal of Immunological Methods; Vol. 222; No. 1-2; 59-63; 10.1016/S0022-1759(98)00179-3
• Weng, Zhiping and Gulukota, Kamalakar, et el. (1998) Computational determination of the structure of rat Fc bound to the neonatal Fc receptor; Journal of Molecular Biology; Vol. 282; No. 2; 217-225; 10.1006/jmbi.1998.2020
• Su, Xiao-Dong and Gastinel, Louis N., et el. (1998) Crystal Structure of Hemolin: A Horseshoe Shape with Implications for Homophilic Adhesion; Science; Vol. 281; No. 5379; 991-995; 10.1126/science.281.5379.991
• Leong, Clement C. and Chapman, Tara L., et el. (1998) Modulation of Natural Killer Cell Cytotoxicity in Human Cytomegalovirus Infection: The Role of Endogenous Class I Major Histocompatibility Complex and a Viral Class I Homolog; Journal of Experimental Medicine; Vol. 187; No. 10; 1681-1687; PMCID PMC2212284; 10.1084/jem.187.10.1681
• Lebrón, José A. and Bennett, Melanie J., et el. (1998) Crystal Structure of the Hemochromatosis Protein HFE and Characterization of Its Interaction with Transferrin Receptor; Cell; Vol. 93; No. 1; 111-123; 10.1016/S0092-8674(00)81151-4
• Feder, John N. and Penny, David M., et el. (1998) The hemochromatosis gene product complexes with the transferrin receptor and lowers its affinity for ligand binding; Proceedings of the National Academy of Sciences of the United States of America; Vol. 95; No. 4; 1472-1477; PMCID PMC19050; 10.1073/pnas.95.4.1472
• Wilson, Ian A. and Bjorkman, Pamela J. (1998) Unusual MHC-like molecules; CD1, Fc receptor, the hemochromatosis gene product, and viral homologs; Current Opinion in Immunology; Vol. 10; No. 1; 67-73; 10.1016/S0952-7915(98)80034-4
• Vaughn, Daniel E. and Bjorkman, Pamela J. (1998) Structural basis of pH-dependent antibody binding by the neonatal Fc receptor; Structure; Vol. 6; No. 1; 63-73; 10.1016/S0969-2126(98)00008-2
• Chapman, Tara L. and Bjorkman, Pamela J. (1998) Characterization of a murine cytomegalovirus class I major histocompati L.bility complex (MHC) homolog: comparison to MHC molecules and to the human cytomegalovirus MHC homolog; Journal of Virology; Vol. 72; No. 1; 460-466; PMCID PMC109395
• Vaughn, Daniel E. and Milburn, Christina M., et el. (1997) Identification of critical IgG binding epitopes on the neonatal Fc receptor; Journal of Molecular Biology; Vol. 274; No. 4; 597-607; 10.1006/jmbi.1997.1388
• West, Anthony P., Jr. and Bjorkman, Pamela J., et el. (1997) Expression and Circular Dichroism Studies of the Extracellular Domain of the alpha Subunit of the Nicotinic Acetylcholine Receptor; Journal of Biological Chemistry; Vol. 272; No. 41; 25468-25473; 10.1074/jbc.272.41.25468
• Vaughn, Daniel E. and Bjorkman, Pamela J. (1997) High-Affinity Binding of the Neonatal Fc Receptor to Its IgG Ligand Requires Receptor Immobilization; Biochemistry; Vol. 36; No. 31; 9374-9380; 10.1021/bi970841r
• Morgan, Chantal S. and Holton, James M., et el. (1997) Circular dichroism determination of class I MHC-peptide equilibrium dissociation constants; Protein Science; Vol. 6; No. 8; 1771-1773; PMCID PMC2143769; 10.1002/pro.5560060819
• Sánchez, Luis M. and López-Otín, Carlos, et el. (1997) Biochemical characterization and crystalization of human Zn-α2-glycoprotein, a soluble class I major histocompatibility complex homolog; Proceedings of the National Academy of Sciences of the United States of America; Vol. 94; No. 9; 4626-4630; PMCID PMC20774; 10.1073/pnas.94.9.4626
• Bjorkman, Pamela J. (1997) MHC Restriction in Three Dimensions: A View of T Cell Receptor/Ligand Interactions; Cell; Vol. 89; No. 2; 167-170; 10.1016/S0092-8674(00)80195-6
• Gakamsky, Dmitry M. and Bjorkman, Pamela J., et el. (1996) Peptide Interaction with a Class I Major Histocompatibility Complex-Encoded Molecule: Allosteric Control of the Ternary Complex Stability; Biochemistry; Vol. 35; No. 47; 14841-14848; 10.1021/bi961707u
• Raghavan, Malini and Bjorkman, Pamela J. (1996) Fc receptors and their interactions with immunoglobulins; Annual Review of Cell and Developmental Biology; Vol. 12; 181-220; 10.1146/annurev.cellbio.12.1.181
• Raghavan, Malini and Lebrón, José A., et el. (1996) Extended repertoire of permissible peptide ligands for HLA-B*2702; Protein Science; Vol. 5; No. 10; 2080-2088; PMCID PMC2143273; 10.1002/pro.5560051014
• Vaughn, Daniel E. and Bjorkman, Pamela J. (1996) The (Greek) Key to Structures of Neural Adhesion Molecules; Neuron; Vol. 16; No. 2; 261-273; 10.1016/S0896-6273(00)80045-8
• Raghavan, Malini and Wang, Yongping, et el. (1995) Effects of receptor dimerization on the interaction between the class I major histocompatibility complex-related Fc receptor and IgG; Proceedings of the National Academy of Sciences of the United States of America; Vol. 92; No. 24; 11200-11204; PMCID PMC40599; 10.1073/pnas.92.24.11200
• Raghavan, Malini and Bonagura, Vincent R., et el. (1995) Analysis of the pH Dependence of the Neonatal Fc Receptor/Immunoglobulin G Interaction Using Antibody and Receptor Variants; Biochemistry; Vol. 34; No. 45; 14649-14657; 10.1021/bi00045a005
• Fahnestock, Margaret L. and Johnson, Jennifer L., et el. (1995) The MHC class I homolog encoded by human cytomegalovirus binds endogenous peptides; Immunity; Vol. 3; No. 5; 583-590; 10.1016/1074-7613(95)90129-9
• Raghavan, Malini and Bjorkman, Pamela J. (1995) BIAcore: a microchip-based system for analyzing the formation of macromolecular complexes; Structure; Vol. 3; No. 4; 331-333; 10.1016/S0969-2126(01)00164-2.
• Bjorkman, Pamela J. and Burmeister, Wilhelm P. (1994) Structures of two classes of MHC molecules elucidated: crucial differences and similarities; Current Opinion in Structural Biology; Vol. 4; No. 6; 852-856; 10.1016/0959-440X(94)90266-6
• Burmeister, Wilhelm P. and Huber, Andrew H., et el. (1994) Crystal structure of the complex of rat neonatal Fc receptor with Fc; Nature; Vol. 372; No. 6504; 379-383; 10.1038/372379a0
• Burmeister, Wilhelm P. and Gastinel, Louis N., et el. (1994) Crystal structure at 2.2 Å resolution of the MHC-related neonatal Fc receptor; Nature; Vol. 372; No. 6504; 336-343; 10.1038/372336a0
• Strong, Roland K. and Penny, David M., et el. (1994) Engineering and expression of a secreted murine TCR with reduced N-linked glycosylation; Journal of Immunology; Vol. 153; No. 9; 4111-4121
• Strong, Roland K. and Vaughn, Daniel E., et el. (1994) Expression and Crystallization of a Soluble Form of Drosophila Fasciclin III; Journal of Molecular Biology; Vol. 241; No. 3; 483-487; 10.1006/jmbi.1994.1523
• Fahnestock, Margaret L. and Johnson, Jennifer L., et el. (1994) Effects of Peptide Length and Composition on Binding to an Empty Class I MHC Heterodimer; Biochemistry; Vol. 33; No. 26; 8149-8158; 10.1021/bi00192a020
• Raghavan, Malini and Chen, Marcus Y., et el. (1994) Investigation of the interaction between the class I MHC-related Fc receptor and its immunoglobulin G ligand; Immunity; Vol. 1; No. 4; 303-315; 10.1016/1074-7613(94)90082-5
• Huber, Andrew H. and Wang, Yu-mei Eureka, et el. (1994) Crystal structure of tandem type III fiibronectin domains from drosophila neuroglian at 2.0 Å; Neuron; Vol. 12; No. 4; 717-731; 10.1016/0896-6273(94)90326-3
• Fahnestock, Margaret L. and Dadgari, Joseph M., et el. (1994) Phosphatidyl inositol-linked forms of a murine class I MHC molecule expressed on Chinese hamster ovary cells retain peptide binding capability and alloreactivity; International Immunology; Vol. 6; No. 2; 307-314; 10.1093/intimm/6.2.307
• Raghavan, Malini and Gastinel, Louis N., et el. (1993) The class I major histocompatibility complex related Fc receptor shows pH-dependent stability differences correlating with immunoglobulin binding and release; Biochemistry; Vol. 32; No. 33; 8654-8660; 10.1021/bi00084a037
• Huber, Andrew H. and Kelley, Robert F., et el. (1993) Crystallization and Stoichiometry of Binding of a Complex between a Rat Intestinal Fc Receptor and Fc; Journal of Molecular Biology; Vol. 230; No. 3; 1077-1083; 10.1006/jmbi.1993.1220
• Wang, Wen-Ching and Zinn, Kai, et el. (1993) Expression and Structural Studies of Fasciclin I, an Insect Cell Adhesion Molecule; Journal of Biological Chemistry; Vol. 268; No. 2; 1448-1455
• Fahnestock, Margaret L. and Tamir, Ilana, et el. (1992) Thermal stability comparison of purified empty and peptide-filled forms of a class I MHC molecule; Science; Vol. 258; No. 5088; 1658-1662; 10.1126/science.1360705
• Gastinel, Louis N. and Simister, Neil E., et el. (1992) Expression and crystallization of a soluble and functional form of an Fc receptor related to class I histocompatibility molecules; Proceedings of the National Academy of Sciences of the United States of America; Vol. 89; No. 2; 638-642; PMCID PMC48294; 10.1073/pnas.89.2.638
• Devaux, Brigitte and Bjorkman, Pamela J., et el. (1991) Generation of monoclonal antibodies against soluble human T cell receptor polypeptides; European Journal of Immunology; Vol. 21; No. 9; 2111-2119; 10.1002/eji.1830210920
• Saper, M. A. and Bjorkman, P. J., et el. (1991) Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 Å resolution; Journal of Molecular Biology; Vol. 219; No. 2; 277-319; 10.1016/0022-2836(91)90567-P
• Chamow, Steven M. and Peers, David H., et el. (1990) Enzymatic Cleavage of a CD4 Immunoadhesin Generates Crystallizable, Biologically Active Fd-like Fragments; Biochemistry; Vol. 29; No. 42; 9885-9891; 10.1021/bi00494a019
• Bjorkman, Pamela J. and Parham, Peter (1990) Structure, Function, and Diversity of Class I Major Histocompatibility Complex Molecules; Annual Review of Biochemistry; Vol. 59; 253-288; 10.1146/annurev.bi.59.070190.001345
• Garrett, T. P. J. and Saper, M. A., et el. (1989) Specificity pockets for the side chains of peptide antigens in HLA-Aw68; Nature; Vol. 342; No. 6250; 692-696; 10.1038/342692a0
• Davis, M. M. and Chien, Yueh-Hsiu, et el. (1989) A Possible Basis for Major Histocompatibility Complex-Restricted T-Cell Recognition; Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences; Vol. 323; No. 1217; 521-524; 10.1098/rstb.1989.0030
• Davis, Mark M. and Bjorkman, Pamela J. (1989) A Model for T Cell Receptor and MHC/Peptide Interaction; ISBN 978-1-4757-5805-4; Mechanisms of Lymphocyte Activation and Immune Regulation II; 13-16; 10.1007/978-1-4757-5803-0_1
• Davis, M. M. and Berg, L. J., et el. (1989) TCR Recognition and Selection In Vivo; Cold Spring Harbor Symposia on Quantitative Biology; Vol. 54; No. 0; 119-128; 10.1101/SQB.1989.054.01.015
• Bjorkman, Pamela J. and Bennett, William S., et el. (1989) Data Collection from Very Thin HLA Crystals Using Synchrotron Radiation; ISBN 978-1-4684-8043-6; Synchrotron Radiation in Structural Biology; 123-131; 10.1007/978-1-4684-8041-2_15
• Bjorkman, P. J. and Davis, M. M. (1989) Model for the Interaction of T-cell Receptors with Peptide/MHC Complexes; Cold Spring Harbor Symposia on Quantitative Biology; Vol. 54; 365-373; 10.1101/SQB.1989.054.01.045