Varshavsky, Alexander J.

Combined from CaltechAUTHORS

• Varshavsky, Alexander and Lewis, Kim, et el. (2023) Deletions of DNA in cancer and their possible uses for therapy; Bioessays; Vol. 45; No. 7; e2300051; PMCID PMC11102808; 10.1002/bies.202300051
• Varshavsky, Alexander and Finley, Daniel, et el. (2023) Dieter Wolf (1941–2023): a life dedicated to understanding protein quality control and the ubiquitin‐proteasome system; EMBO Journal; Vol. 42; No. 11; Art. No. e114222; 10.15252/embj.2023114222
• Kim, Bong Heon and Kim, Min Kyung, et el. (2022) Crystal structure of the Ate1 arginyl-tRNA-protein transferase and arginylation of N-degron substrates; Proceedings of the National Academy of Sciences of the United States of America; Vol. 119; No. 31; Art. No. e2209597119; PMCID PMC9351520; 10.1073/pnas.2209597119
• Chen, Shun-Jia and Kim, Leehyeon, et el. (2021) Aminopeptidases trim Xaa-Pro proteins, initiating their degradation by the Pro/N-degron pathway; Proceedings of the National Academy of Sciences of the United States of America; Vol. 118; No. 43; Art. No. e2115430118; PMCID PMC8639330; 10.1073/pnas.2115430118
• Vu, Tri T. M. and Mitchell, Dylan C., et el. (2020) The Arg/N-degron pathway targets transcription factors and regulates specific genes; Proceedings of the National Academy of Sciences of the United States of America; Vol. 117; No. 49; 31094-31104; PMCID PMC7733807; 10.1073/pnas.2020124117
• Vu, Tri T. M. and Varshavsky, Alexander (2020) The ATF3 Transcription Factor Is a Short-Lived Substrate of the Arg/N-Degron Pathway; Biochemistry; Vol. 59; No. 30; 2796-2812; PMCID PMC7669821; 10.1021/acs.biochem.0c00514
• Dong, Cheng and Chen, Shun-Jia, et el. (2020) Recognition of nonproline N-terminal residues by the Pro/N-degron pathway; Proceedings of the National Academy of Sciences of the United States of America; Vol. 117; No. 25; 14158-14167; PMCID PMC7322002; 10.1073/pnas.2007085117
• Oh, Jang-Hyun and Hyun, Ju-Yeon, et el. (2020) Five enzymes of the Arg/N-degron pathway form a targeting complex: The concept of superchanneling; Proceedings of the National Academy of Sciences of the United States of America; Vol. 117; No. 20; 10778-10788; PMCID PMC7245096; 10.1073/pnas.2003043117
• Chen, Shun-Jia and Melnykov, Artem, et el. (2020) Evolution of Substrates and Components of the Pro/N-Degron Pathway; Biochemistry; Vol. 59; No. 4; 582-593; PMCID PMC7286083; 10.1021/acs.biochem.9b00953
• Melnykov, Artem and Chen, Shun-Jia, et el. (2019) Gid10 as an alternative N-recognin of the Pro/N-degron pathway; Proceedings of the National Academy of Sciences of the United States of America; Vol. 116; No. 32; 15914-15923; PMCID PMC6689949; 10.1073/pnas.1908304116
• Varshavsky, Alexander (2019) On the cause of sleep: Protein fragments, the concept of sentinels, and links to epilepsy; Proceedings of the National Academy of Sciences of the United States of America; Vol. 116; No. 22; 10773-10782; PMCID PMC6561186; 10.1073/pnas.1904709116
• Varshavsky, Alexander (2019) N-degron and C-degron pathways of protein degradation; Proceedings of the National Academy of Sciences of the United States of America; Vol. 116; No. 2; 358-366; PMCID PMC6329975; 10.1073/pnas.1816596116
• Kim, Jeong-Mok and Seok, Ok-Hee, et el. (2018) Formyl-methionine as an N-degron of a eukaryotic N-end rule pathway; Science; Vol. 362; No. 6418; Art. No. eaat0174; PMCID PMC6551516; 10.1126/science.aat0174
• Dougan, David A. and Varshavsky, Alexander (2018) Understanding the Pro/N-end rule pathway; Nature Chemical Biology; Vol. 14; No. 5; 415-416; 10.1038/s41589-018-0045-0
• Oh, Jang-Hyun and Chen, Shun-Jia, et el. (2017) A reference-based protein degradation assay without global translation inhibitors; Journal of Biological Chemistry; Vol. 292; No. 52; 21457-21465; PMCID PMC5766948; 10.1074/jbc.M117.814236
• Varshavsky, Alexander (2017) The Ubiquitin System, Autophagy, and Regulated Protein Degradation; Annual Review of Biochemistry; Vol. 86; 123-128; 10.1146/annurev-biochem-061516-044859
• Oh, Jang-Hyun and Hyun, Ju-Yeon, et el. (2017) Control of Hsp90 chaperone and its clients by N-terminal acetylation and the N-end rule pathway; Proceedings of the National Academy of Sciences of the United States of America; Vol. 114; No. 22; E4370-E4379; PMCID PMC5465900; 10.1073/pnas.1705898114
• Chen, Shun-Jia and Wu, Xia, et el. (2017) An N-end rule pathway that recognizes proline and destroys gluconeogenic enzymes; Science; Vol. 355; No. 6323; Art. No. eaal3655; PMCID PMC5457285; 10.1126/science.aal3655
• Wadas, Brandon and Piatkov, Konstantin, et el. (2016) Analyzing N-terminal Arginylation Through the Use of Peptide Arrays and Degradation Assays; Journal of Biological Chemistry; Vol. 291; No. 40; Art. No. 20976; PMCID PMC5076509; 10.1074/jbc.M116.747956
• Wadas, Brandon and Borjigin, Jimo, et el. (2016) Degradation of Serotonin N-Acetyltransferase, a Circadian Regulator, by the N-end Rule Pathway; Journal of Biological Chemistry; Vol. 291; No. 33; 17178-17196; PMCID PMC5016120; 10.1074/jbc.M116.734640
• Liu, Yu-Jiao and Liu, Chao, et el. (2016) Degradation of the Separase-cleaved Rec8, a Meiotic Cohesin Subunit, by the N-end Rule Pathway; Journal of Biological Chemistry; Vol. 291; No. 14; 7426-7438; PMCID PMC4817174; 10.1074/jbc.M116.714964
• Piatkov, Konstantin and Vu, Tri, et el. (2015) Formyl-methionine as a degradation signal at the N-termini of bacterial proteins; Microbial Cell; Vol. 2; No. 10; 376-393; PMCID PMC4745127; 10.15698/mic2015.10.231
• Park, Sang-Eun and Kim, Jeong-Mok, et el. (2015) Control of mammalian G protein signaling by N-terminal acetylation and the N-end rule pathway; Science; Vol. 347; No. 6227; 1249-1252; PMCID PMC4748709; 10.1126/science.aaa3844
• Brower, Christopher S. and Rosen, Connor E., et el. (2014) Liat1, an arginyltransferase-binding protein whose evolution among primates involved changes in the numbers of its 10-residue repeats; Proceedings of the National Academy of Sciences of the United States of America; Vol. 111; No. 46; E4936-E4945; PMCID PMC4246273; 10.1073/pnas.1419587111
• Varshavsky, Alexander (2014) Discovery of the Biology of the Ubiquitin System; JAMA : the journal of the American Medical Association; Vol. 311; No. 19; 1969-1970; 10.1001/jama.2014.5549
• Piatkov, Konstantin I. and Oh, Jang-Hyun, et el. (2014) Calpain-generated natural protein fragments as short-lived substrates of the N-end rule pathway; Proceedings of the National Academy of Sciences of the United States of America; Vol. 111; No. 9; E817-E826; PMCID PMC3948289; 10.1073/pnas.1401639111
• Kim, Heon-Ki and Kim, Ryu-Ryun, et el. (2014) The N-Terminal Methionine of Cellular Proteins as a Degradation Signal; Cell; Vol. 156; No. 1; 158-169; PMCID PMC3988316; 10.1016/j.cell.2013.11.031
• Piatkov, Konstantin and Graciet, Emmanuelle, et el. (2013) Ubiquitin Reference Technique and Its Use in Ubiquitin-Lacking Prokaryotes; PLoS ONE; Vol. 8; No. 6; Art. No. e67952; PMCID PMC3692480; 10.1371/journal.pone.0067952
• Shemorry, Anna and Hwang, Cheol-Sang, et el. (2013) Control of Protein Quality and Stoichiometries by N-Terminal Acetylation and the N-End Rule Pathway; Molecular Cell; Vol. 50; No. 4; 540-551; PMCID PMC3665649; 10.1016/j.molcel.2013.03.018
• Brower, Christopher S. and Piatkov, Konstantin I., et el. (2013) Neurodegeneration-Associated Protein Fragments as Short-Lived Substrates of the N-End Rule Pathway; Molecular Cell; Vol. 50; No. 2; 161-171; PMCID PMC3640747; 10.1016/j.molcel.2013.02.009
• Piatkov, Konstantin I. and Colnaghi, Luca, et el. (2012) The Auto-Generated Fragment of the Usp1 Deubiquitylase Is a Physiological Substrate of the N-End Rule Pathway; Molecular Cell; Vol. 48; No. 6; 926-933; PMCID PMC3889152; 10.1016/j.molcel.2012.10.012
• Varshavsky, Alexander (2012) Augmented generation of protein fragments during wakefulness as the molecular cause of sleep: A hypothesis; Protein Science; Vol. 21; No. 11; PMCID PMC3527701; 10.1002/pro.2148
• Piatkov, Konstantin I. and Brower, Christopher S., et el. (2012) The N-end rule pathway counteracts cell death by destroying proapoptotic protein fragments; Proceedings of the National Academy of Sciences of the United States of America; Vol. 109; No. 27; E1839-E1847; PMCID PMC3390858; 10.1073/pnas.1207786109
• Varshavsky, Alexander (2012) The Ubiquitin System, an Immense Realm; Annual Review of Biochemistry; Vol. 81; 167-176; 10.1146/annurev-biochem-051910-094049
• Varshavsky, Alexander (2012) Three decades of studies to understand the functions of the ubiquitin family; ISBN 9781617794742; Ubiquitin family modifiers and the proteasome: reviews and protocols; 1-11; 10.1007/978-1-61779-474-2_1
• Hwang, Cheol-Sang and Sukalo, Maja, et el. (2011) Ubiquitin Ligases of the N-End Rule Pathway: Assessment of Mutations in UBR1 That Cause the Johanson-Blizzard Syndrome; PLoS ONE; Vol. 6; No. 9; Art.No. e24925; PMCID PMC3172311; 10.1371/journal.pone.0024925
• Varshavsky, Alexander (2011) The N-end rule pathway and regulation by proteolysis; Protein Science; Vol. 20; No. 8; 1298-1345; PMCID PMC3189519; 10.1002/pro.666
• Hwang, Cheol-Sang and Shemorry, Anna, et el. (2010) The N-end rule pathway is mediated by a complex of the RING-type Ubr1 and HECT-type Ufd4 ubiquitin ligases; Nature Cell Biology; Vol. 12; No. 12; 1177-1185; PMCID PMC3003441; 10.1038/ncb2121
• Brower, Christopher S. and Veiga, Lucia, et el. (2010) Mouse Dfa Is a Repressor of TATA-box Promoters and Interacts with the Abt1 Activator of Basal Transcription; Journal of Biological Chemistry; Vol. 285; No. 22; 17218-17234; PMCID PMC2878062; 10.1074/jbc.M110.118638
• Hwang, Cheol-Sang and Shemorry, Anna, et el. (2010) N-Terminal Acetylation of Cellular Proteins Creates Specific Degradation Signals; Science; Vol. 327; No. 5968; 973-977; PMCID PMC4259118; 10.1126/science.1183147
• Brower, Christopher S. and Varshavsky, Alexander (2009) Ablation of Arginylation in the Mouse N-End Rule Pathway: Loss of Fat, Higher Metabolic Rate, Damaged Spermatogenesis, and Neurological Perturbations; PLoS ONE; Vol. 4; No. 11; Art. No. e7757; PMCID PMC2773024; 10.1371/journal.pone.0007757
• Graciet, Emmanuelle and Walter, Franziska, et el. (2009) The N-end rule pathway controls multiple functions during Arabidopsis shoot and leaf development; Proceedings of the National Academy of Sciences of the United States of America; Vol. 106; No. 32; 13618-13623; PMCID PMC2726413; 10.1073/pnas.0906404106
• Wang, Haiqing and Piatkov, Konstantin I., et el. (2009) Glutamine-Specific N-Terminal Amidase, a Component of the N-End Rule Pathway; Molecular Cell; Vol. 34; No. 6; 686-695; PMCID PMC2749074; 10.1016/j.molcel.2009.04.032
• Hwang, Cheol-Sang and Shemorry, Anna, et el. (2009) Two proteolytic pathways regulate DNA repair by cotargeting the Mgt1 alkylguanine transferase; Proceedings of the National Academy of Sciences of the United States of America; Vol. 106; No. 7; 2142-2147; PMCID PMC2650122; 10.1073/pnas.0812316106
• Varshavsky, Alexander (2008) Discovery of cellular regulation by protein degradation; Journal of Biological Chemistry; Vol. 283; No. 50; 34469-34489; PMCID PMC3259866; 10.1074/jbc.X800009200
• Hwang, Cheol-Sang and Varshavsky, Alexander (2008) Regulation of peptide import through phosphorylation of Ubr1, the ubiquitin ligase of the N-end rule pathway; Proceedings of the National Academy of Sciences of the United States of America; Vol. 105; No. 49; 19188-19193; PMCID PMC2614737; 10.1073/pnas.0808891105
• Varshavsky, Alexander (2008) The N-end rule at atomic resolution; Nature Structural & Molecular Biology; Vol. 15; No. 12; 1238-1240; 10.1038/nsmb1208-1238
• Xia, Zanxian and Turner, Glenn C., et el. (2008) Amino acids induce peptide uptake via accelerated degradation of CUP9, the transcriptional repressor of the PTR2 peptide transporter; Journal of Biological Chemistry; Vol. 283; No. 43; 28958-28968; PMCID PMC2570885; 10.1074/jbc.M803980200
• Xia, Zanxian and Webster, Ailsa, et el. (2008) Substrate-binding sites of UBR1, the ubiquitin ligase of the N-end rule pathway; Journal of Biological Chemistry; Vol. 283; No. 35; 24011-24028; PMCID PMC2527112; 10.1074/jbc.M802583200
• Connor, Rebecca E. and Piatkov, Konstantin, et el. (2008) Enzymatic N-terminal Addition of Noncanonical Amino Acids to Peptides and Proteins; ChemBioChem; Vol. 9; No. 3; 366-369; 10.1002/cbic.200700605
• Hu, Rong-Gui and Wang, Haiqing, et el. (2008) The N-end rule pathway is a sensor of heme; Proceedings of the National Academy of Sciences of the United States of America; Vol. 105; No. 1; 76-81; PMCID PMC2224235; 10.1073/pnas.0710568105
• Schnupf, Pamela and Zhou, Jianmin, et el. (2007) Listeriolysin O Secreted by Listeria monocytogenes into the Host Cell Cytosol Is Degraded by the N-End Rule Pathway; Infection and Immunity; Vol. 75; No. 11; 5135-5147; PMCID PMC2168281; 10.1128/IAI.00164-07
• Varshavsky, Alexander (2007) Targeting the absence: Homozygous DNA deletions as immutable signposts for cancer therapy; Proceedings of the National Academy of Sciences of the United States of America; Vol. 104; No. 38; 14935-14940; PMCID PMC1986591; 10.1073/pnas.0706546104
• Tasaki, Takafumi and Sohr, Reinhard, et el. (2007) Biochemical and Genetic Studies of UBR3, a Ubiquitin Ligase with a Function in Olfactory and Other Sensory Systems; Journal of Biological Chemistry; Vol. 282; No. 25; 18510-18520; 10.1074/jbc.M701894200
• Hu, Rong-Gui and Brower, Christopher S., et el. (2006) Arginyltransferase, Its Specificity, Putative Substrates, Bidirectional Promoter, and Splicing-derived Isoforms; Journal of Biological Chemistry; Vol. 281; No. 43; 32559-32573; 10.1074/jbc.M604355200
• An, Jee Young and Seo, Jai Wha, et el. (2006) Impaired neurogenesis and cardiovascular development in mice lacking the E3 ubiquitin ligases UBR1 and UBR2 of the N-end rule pathway; Proceedings of the National Academy of Sciences of the United States of America; Vol. 103; No. 16; 6212-6217; PMCID PMC1458857; 10.1073/pnas.0601700103
• Graciet, Emmanuelle and Hu, Rong-Gui, et el. (2006) Aminoacyl-transferases and the N-end rule pathway of prokaryotic/eukaryotic specificity in a human pathogen; Proceedings of the National Academy of Sciences of the United States of America; Vol. 103; No. 9; 3078-3083; PMCID PMC1413915; 10.1073/pnas.0511224103
• Zenker, Martin and Varshavsky, Alexander (2005) Deficiency of UBR1, a ubiquitin ligase of the N-end rule pathway, causes pancreatic dysfunction, malformations and mental retardation (Johanson-Blizzard syndrome); Nature Genetics; Vol. 37; No. 12; 1345-1350; 10.1038/ng1681
• Hu, Rong-Gui and Sheng, Jun, et el. (2005) The N-end rule pathway as a nitric oxide sensor controlling the levels of multiple regulators; Nature; Vol. 437; No. 7061; 981-989; 10.1038/nature04027
• Tasaki, Takafumi and Mulder, Lubbertus C. F., et el. (2005) A Family of Mammalian E3 Ubiquitin Ligases That Contain the UBR Box Motif and Recognize N-Degrons; Molecular and Cellular Biology; Vol. 25; No. 16; 7120-7136; PMCID PMC1190250; 10.1128/MCB.25.16.7120-7136.2005
• Yin, Jinhu and Kwon, Yong Tae, et el. (2004) RECQL4, mutated in the Rothmund–Thomson and RAPADILINO syndromes, interacts with ubiquitin ligases UBR1 and UBR2 of the N-end rule pathway; Human Molecular Genetics; Vol. 13; No. 20; 2421-2430; 10.1093/hmg/ddh269
• Kwon, Yong Tae and Xia, Zanxian, et el. (2003) Female Lethality and Apoptosis of Spermatocytes in Mice Lacking the UBR2 Ubiquitin Ligase of the N-End Rule Pathway; Molecular and Cellular Biology; Vol. 23; No. 22; 8255-8271; PMCID PMC262401; 10.1128/MCB.23.22.8255-8271.2003
• Varshavsky, Alexander (2003) The N-end rule and regulation of apoptosis; Nature Cell Biology; Vol. 5; No. 5; 373-376; 10.1038/ncb0503-373
• Xie, Youming and Varshavsky, Alexander (2002) UFD4 lacking the proteasome-binding region catalyses ubiquitination but is impaired in proteolysis; Nature Cell Biology; Vol. 4; No. 12; 1003-1007; 10.1038/ncb889
• Du, Fangyong and Navarro-Garcia, Federico, et el. (2002) Pairs of dipeptides synergistically activate the binding of substrate by ubiquitin ligase through dissociation of its autoinhibitory domain; Proceedings of the National Academy of Sciences of the United States of America; Vol. 99; No. 22; 14110-14115; PMCID PMC137845; 10.1073/pnas.172527399
• Kwon, Yong Tae and Kashina, Anna S., et el. (2002) An Essential Role of N-Terminal Arginylation in Cardiovascular Development; Science; Vol. 297; No. 5578; 96-99; 10.1126/science.1069531
• Kwon, Yong Tae and Xia, Zanxian, et el. (2001) Construction and Analysis of Mouse Strains Lacking the Ubiquitin Ligase UBR1 (E3α) of the N-End Rule Pathway; Molecular and Cellular Biology; Vol. 21; No. 23; 8007-8021; PMCID PMC99968; 10.1128/MCB.21.23.8007-8021.2001
• Rao, Hai and Uhlmann, Frank, et el. (2001) Degradation of a cohesin subunit by the N-end rule pathway is essential for chromosome stability; Nature; Vol. 410; No. 6831; 955; 10.1038/35073627
• Xie, Youming and Varshavsky, Alexander (2001) RPN4 is a ligand, substrate, and transcriptional regulator of the 26S proteasome: A negative feedback circuit; Proceedings of the National Academy of Sciences of the United States of America; Vol. 98; No. 6; 3056-3061; PMCID PMC30606; 10.1073/pnas.071022298
• Hershko, Avram and Ciechanover, Aaron, et el. (2000) The ubiquitin system; Nature Medicine; Vol. 6; No. 10; 1073-1081; 10.1038/80384
• Turner, Glenn C. and Varshavsky, Alexander (2000) Detecting and Measuring Cotranslational Protein Degradation in Vivo; Science; Vol. 289; No. 5487; 2117-2120; 10.1126/science.289.5487.2117
• Varshavsky, Alexander and Turner, Glenn, et el. (2000) The Ubiquitin System and the N-End Rule Pathway; Biological Chemistry; Vol. 381; No. 9-10; 779-789; 10.1515/BC.2000.101
• Kwon, Yong Tae and Balogh, Seth A., et el. (2000) Altered Activity, Social Behavior, and Spatial Memory in Mice Lacking the NTAN1p Amidase and the Asparagine Branch of the N-End Rule Pathway; Molecular and Cellular Biology; Vol. 20; No. 11; 4135-4148; PMCID PMC85783
• Turner, Glenn C. and Du, Fangyong, et el. (2000) Peptides accelerate their uptake by activating a ubiquitin-dependent proteolytic pathway; Nature; Vol. 405; No. 6786; 579; 10.1038/35014629
• Davydov, Ilia V. and Varshavsky, Alexander (2000) RGS4 is arginylated and degraded by the N-end rule pathway in vitro; Journal of Biological Chemistry; Vol. 275; No. 30; 22931-22941; 10.1074/jbc.M001605200
• Xie, Youming and Varshavsky, Alexander (2000) Physical association of ubiquitin ligases and the 26S proteasome; Proceedings of the National Academy of Sciences of the United States of America; Vol. 97; No. 6; 2497-2502; PMCID PMC15957; 10.1073/pnas.060025497
• Kwon, Yong Tae and Lévy, Frédéric, et el. (1999) Bivalent Inhibitor of the N-end Rule Pathway; Journal of Biological Chemistry; Vol. 274; No. 25; 18135-18139; 10.1074/jbc.274.25.18135
• Dünnwald, Martin and Varshavsky, Alexander, et el. (1999) Detection of Transient In Vivo Interactions between Substrate and Transporter during Protein Translocation into the Endoplasmic Reticulum; Molecular Biology of the Cell; Vol. 10; No. 2; 329-344; PMCID PMC25172; 10.1091/mbc.10.2.329
• Kwon, Yong Tae and Kashina, Anna S., et el. (1999) Alternative Splicing Results in Differential Expression, Activity, and Localization of the Two Forms of Arginyl-tRNA-Protein Transferase, a Component of the N-End Rule Pathway; Molecular and Cellular Biology; Vol. 19; No. 1; 182-193; PMCID PMC83877; 10.1128/mcb.19.1.182
• Varshavsky, Alexander (1999) Recent studies of the ubiquitin system and the N-end rule pathway; Harvey lectures; Vol. 96; 93-116
• Kwon, Yong Tae and Reiss, Yuval, et el. (1998) The mouse and human genes encoding the recognition component of the N-end rule pathway; Proceedings of the National Academy of Sciences of the United States of America; Vol. 95; No. 14; 7898-7903; PMCID PMC20901; 10.1073/pnas.95.14.7898
• Varshavsky, Alexander (1998) Codominant interference, antieffectors, and multitarget drugs; Proceedings of the National Academy of Sciences of the United States of America; Vol. 95; No. 5; 2094-2099; PMCID PMC19261
• Ramos, Paula C. and Höckendorff, Jörg, et el. (1998) Ump1p Is Required for Proper Maturation of the 20S Proteasome and Becomes Its Substrate upon Completion of the Assembly; Cell; Vol. 92; No. 4; 489-499; 10.1016/s0092-8674(00)80942-3
• Byrd, Christopher and Turner, Glenn C., et el. (1998) The N-end rule pathway controls the import of peptides through degradation of a transcriptional repressor; EMBO Journal; Vol. 17; No. 1; 269-277; PMCID PMC1170377; 10.1093/emboj/17.1.269
• Varshavsky, Alexander (1997) The ubiquitin system; Trends in Biochemical Sciences; Vol. 22; No. 10; 383-387; 10.1016/s0968-0004(97)01122-5
• Varshavsky, Alexander (1997) The N-end rule pathway of protein degradation; Genes to Cells; Vol. 2; No. 1; 13-28; 10.1046/j.1365-2443.1997.1020301.x
• Grigoryev, Sergei and Stewart, Albert E., et el. (1996) A Mouse Amidase Specific for N-terminal Asparagine: the gene, the enzyme, and their function in the N-end rule pathway; Journal of Biological Chemistry; Vol. 271; No. 45; 28521-28532; 10.1074/jbc.271.45.28521
• Varshavsky, Alexander (1996) The N-end rule: Functions, mysteries, uses; Proceedings of the National Academy of Sciences of the United States of America; Vol. 93; No. 22; 12142-12149; PMCID PMC37957; 10.1073/pnas.93.22.12142
• Ghislain, Michel and Dohmen, R. Jürgen, et el. (1996) Cdc48p interacts with Ufd3p, a WD repeat protein required for ubiquitin-mediated proteolysis in Saccharomyces cerevisiae; EMBO Journal; Vol. 15; No. 18; 4884-4899; PMCID PMC452226; 10.1002/j.1460-2075.1996.tb00869.x
• Lévy, Frédéric and Johnsson, Nils, et el. (1996) Using ubiquitin to follow the metabolic fate of a protein; Proceedings of the National Academy of Sciences of the United States of America; Vol. 93; No. 10; 4907-4912; PMCID PMC39378; 10.1073/pnas.93.10.4907
• Dohmen, R. Jürgen and Stappen, Reiner, et el. (1995) An Essential Yeast Gene Encoding a Homolog of Ubiquitin-activating Enzyme; Journal of Biological Chemistry; Vol. 270; No. 30; 18099-18109; 10.1074/jbc.270.30.18099
• Baker, Rohan T. and Varshavsky, Alexander (1995) Yeast N-terminal Amidase: a new enzyme and component of the N-end rule pathway; Journal of Biological Chemistry; Vol. 270; No. 20; 12065-12074; 10.1074/jbc.270.20.12065
• Varshavsky, Alexander (1995) Codominance and toxins: A path to drugs of nearly unlimited selectivity; Proceedings of the National Academy of Sciences of the United States of America; Vol. 92; No. 9; 3663-3667; PMCID PMC42021; 10.1073/pnas.92.9.3663
• Johnston, Jennifer A. and Johnson, Erica S., et el. (1995) Methotrexate Inhibits Proteolysis of Dihydrofolate Reductase by the N-end Rule Pathway; Journal of Biological Chemistry; Vol. 270; No. 14; 8172-8178; 10.1074/jbc.270.14.8172
• Varshavsky, A. J. (1995) The N-end Rule; Cold Spring Harbor Symposia on Quantitative Biology; Vol. 60; 461-478; 10.1101/sqb.1995.060.01.051
• Johnsson, Nils and Varshavsky, Alexander (1994) Split ubiquitin as a sensor of protein interactions in vivo; Proceedings of the National Academy of Sciences of the United States of America; Vol. 91; No. 22; 10340-10344; PMCID PMC45015; 10.1073/pnas.91.22.10340
• Madura, Kiran and Varshavsky, Alexander (1994) Degradation of Gα by the N-End Rule Pathway; Science; Vol. 265; No. 5177; 1454-1458; 10.1126/science.8073290
• Johnsson, Nils and Varshavsky, Alexander (1994) Ubiquitin-assisted dissection of protein transport across membranes; EMBO Journal; Vol. 13; No. 11; 2686-2698; PMCID PMC395143; 10.1002/j.1460-2075.1994.tb06559.x
• Dohmen, R. Jürgen and Wu, Peipei, et el. (1994) Heat-Inducible Degron: A Method for Constructing Temperature-Sensitive Mutants; Science; Vol. 263; No. 5151; 1273-1276; 10.1126/science.8122109
• Ota, Irene M. and Varshavsky, Alexander (1993) A yeast protein similar to bacterial two-component regulators; Science; Vol. 262; No. 5133; 566-569; 10.1126/science.8211183
• Shrader, Thomas E. and Tobias, John W., et el. (1993) The N-End Rule in Escherichia coli: Cloning and Analysis of the Leucyl, Phenylalanyl-tRNA-Protein Transferase Gene aat; Journal of Bacteriology; Vol. 175; No. 14; 4364-4374; PMCID PMC204876; 10.1128/jb.175.14.4364-4374.1993
• Madura, Kiran and Dohmen, R. Jürgen, et el. (1993) N-recognin/Ubc2 interactions in the N-end rule pathway; Journal of Biological Chemistry; Vol. 268; No. 16; 12046-12054; 10.1016/s0021-9258(19)50306-4
• Baker, Rohan T. and Tobias, John W., et el. (1992) Ubiquitin-specific proteases of Saccharomyces cerevisiae. Cloning of UBP2 and UBP3, and functional analysis of the UBP gene family; Journal of Biological Chemistry; Vol. 267; No. 32; 23364-23375; 10.1016/s0021-9258(18)50100-9
• Varshavsky, Alexander (1992) The N-end rule; Cell; Vol. 69; No. 5; 725-735; 10.1016/0092-8674(92)90285-k
• Ota, Irene M. and Varshavsky, Alexander (1992) A gene encoding a putative tyrosine phosphatase suppresses lethality of an N-end rule-dependent mutant; Proceedings of the National Academy of Sciences of the United States of America; Vol. 89; No. 6; 2355-2359; PMCID PMC48656; 10.1073/pnas.89.6.2355
• Johnson, Erica S. and Bartel, Bonnie, et el. (1992) Ubiquitin as a degradation signal; EMBO Journal; Vol. 11; No. 2; 497-505; PMCID PMC556480; 10.1002/j.1460-2075.1992.tb05080.x
• Tobias, John W. and Shrader, Thomas E., et el. (1991) The N-end rule in bacteria; Science; Vol. 254; No. 5036; 1374-1377; 10.1126/science.1962196
• Dohmen, R. Jürgen and Madura, Kiran, et el. (1991) The N-End Rule is Mediated by the UBC2(RAD6) Ubiquitin-Conjugating Enzyme; Proceedings of the National Academy of Sciences of the United States of America; Vol. 88; No. 16; 7351-7355; PMCID PMC52293; 10.1073/pnas.88.16.7351
• Tobias, John W. and Varshavsky, Alexander (1991) Cloning and functional analysis of the ubiquitin-specific protease gene UBP1 of Saccharomyces cerevisiae; Journal of Biological Chemistry; Vol. 266; No. 18; 12021-12028; 10.1016/s0021-9258(18)99059-9
• Hochstrasser, Mark and Ellison, Michael J., et el. (1991) The short-lived MATα2 transcriptional regulator is ubiquitinated in vivo; Proceedings of the National Academy of Sciences of the United States of America; Vol. 88; No. 11; 4606-4610; PMCID PMC51714; 10.1073/pnas.88.11.4606
• Baker, Rohan T. and Varshavsky, Alexander (1991) Inhibition of the N-end rule pathway in living cells; Proceedings of the National Academy of Sciences of the United States of America; Vol. 88; No. 4; 1090-1094; PMCID PMC50962; 10.1073/pnas.88.4.1090
• Varshavsky, Alexander (1991) Naming a targeting signal; Cell; Vol. 64; No. 1; 13-15; 10.1016/0092-8674(91)90202-a
• McGrath, John P. and Jentsch, Stefan, et el. (1991) UBA 1: an essential yeast gene encoding ubiquitin-activating enzyme; EMBO Journal; Vol. 10; No. 1; 227-236; PMCID PMC452634; 10.1002/j.1460-2075.1991.tb07940.x
• Johnson, Erica S. and Gonda, David K., et el. (1990) Cis-trans recognition and subunit-specific degradation of short-lived proteins; Nature; Vol. 346; No. 6281; 287-291; 10.1038/346287a0
• Hochstrasser, Mark and Varshavsky, Alexander (1990) In vivo degradation of a transcriptional regulator: The yeast α2 repressor; Cell; Vol. 61; No. 4; 697-708; 10.1016/0092-8674(90)90481-s
• Balzi, Elisabetta and Choder, Mordechai, et el. (1990) Cloning and functional analysis of the arginyl-tRNA-protein transferase gene ATE1 of Saccharomyces cerevisiae; Journal of Biological Chemistry; Vol. 265; No. 13; 7464-7471; 10.1016/s0021-9258(19)39136-7
• Gonda, David K. and Bachmair, Andreas, et el. (1989) Universality and Structure of the N-end Rule; Journal of Biological Chemistry; Vol. 264; No. 28; 16700-16712; 10.1016/s0021-9258(19)84762-2
• McGrath, John P. and Varshavsky, Alexander (1989) The yeast STE6 gene encodes a homologue of the mammalian multidrug resistance P-glycoprotein; Nature; Vol. 340; No. 6232; 400-404; 10.1038/340400a0
• Winter, Edward and Varshavsky, Alexander (1989) A DNA binding protein that recognizes oligo(dA)•oligo(dT) tracts; EMBO Journal; Vol. 8; No. 6; 1867-1877; PMCID PMC401036; 10.1002/j.1460-2075.1989.tb03583.x
• Finley, Daniel and Bartel, Bonnie, et el. (1989) The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis; Nature; Vol. 338; No. 6214; 394-401; 10.1038/338394a0
• Chau, Vincent and Tobias, John W., et el. (1989) A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein; Science; Vol. 243; No. 4898; 1576-1583; 10.1126/science.2538923
• Bachmair, Andreas and Varshavsky, Alexander (1989) The degradation signal in a short-lived protein; Cell; Vol. 56; No. 6; 1019-1032; 10.1016/0092-8674(89)90635-1
• Varshavsky, A. and Bachmair, A., et el. (1989) Targeting of proteins for degradation; Biotechnology (Reading, Mass.); Vol. 13; 109-43
• Goebl, Mark G. and Yochem, John, et el. (1988) The yeast cell cycle gene CDC34 encodes a ubiquitin-conjugating enzyme; Science; Vol. 241; No. 4871; 1331-1335; 10.1126/science.2842867
• Solomon, Mark J. and Larsen, Pamela L., et el. (1988) Mapping protein-DNA interactions in vivo with formaldehyde: Evidence that histone H4 is retained on a highly transcribed gene; Cell; Vol. 53; No. 6; 937-947; 10.1016/s0092-8674(88)90469-2
• Bartel, Bonnie and Varshavsky, Alexander (1988) Hypersensitivity to heavy water: A new conditional phenotype; Cell; Vol. 52; No. 6; 935-941; 10.1016/0092-8674(88)90435-7
• Varshavsky, Alexander and Bachmair, Andreas, et el. (1987) N-end rule of selective protein turnover: mechanistic aspects and functional implications; Biochemical Society Transactions; Vol. 15; No. 5; 815-816; 10.1042/bst0150815
• Peck, Lawrence J. and Millstein, Larry, et el. (1987) Transcriptionally inactive oocyte-type 5S RNA genes of Xenopus laevis are complexed with TFIIIA in vitro; Molecular and Cellular Biology; Vol. 7; No. 10; 3503-3510; PMCID PMC368002; 10.1128/mcb.7.10.3503
• Solomon, Mark J. and Varshavsky, Alexander (1987) A nuclease-hypersensitive region forms de novo after chromosome replication; Molecular and Cellular Biology; Vol. 7; No. 10; 3822-3825; PMCID PMC368040; 10.1128/mcb.7.10.3822
• Jentsch, Stefan and McGrath, John P., et el. (1987) The yeast DNA repair gene RAD6 encodes a ubiquitin-conjugating enzyme; Nature; Vol. 329; No. 6135; 131-134; 10.1038/329131a0
• Özkaynak, Engin and Finley, Daniel, et el. (1987) The yeast ubiquitin genes: a family of natural gene fusions; EMBO Journal; Vol. 6; No. 5; 1429-1439; PMCID PMC553949; 10.1002/j.1460-2075.1987.tb02384.x
• Finley, Daniel and Özkaynak, Engin, et el. (1987) The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation, and other stresses; Cell; Vol. 48; No. 6; 1035-1046; 10.1016/0092-8674(87)90711-2
• Varshavsky, Alexander (1987) Electrophoretic assay for DNA-binding proteins; ISBN 9780121820527; Methods in Enzymology; 551-565; 10.1016/s0076-6879(87)51044-8
• Snapka, Robert M. and Kwok, Kwan, et el. (1986) Post-separation detection of nucleic acids and proteins by neutron activation; Proceedings of the National Academy of Sciences of the United States of America; Vol. 83; No. 23; 8939-8942; PMCID PMC387049; 10.1073/pnas.83.23.8939
• Bachmair, Andreas and Finley, Daniel, et el. (1986) In vivo half-life of a protein is a function of its amino-terminal residue; Science; Vol. 234; No. 4773; 179-186; 10.1126/science.3018930
• Swerdlow, Paul S. and Finley, Daniel, et el. (1986) Enhancement of immunoblot sensitivity by heating of hydrated filters; Analytical Biochemistry; Vol. 156; No. 1; 147-153; 10.1016/0003-2697(86)90166-1
• Solomon, Mark J. and Strauss, Francois, et el. (1986) A mammalian high mobility group protein recognizes any stretch of six A·T base pairs in duplex DNA; Proceedings of the National Academy of Sciences of the United States of America; Vol. 83; No. 5; 1276-1280; PMCID PMC323058; 10.1073/pnas.83.5.1276
• Gros, Philippe and Croop, James, et el. (1986) Isolation and characterization of DNA sequences amplified in multidrug-resistant hamster cells; Proceedings of the National Academy of Sciences of the United States of America; Vol. 83; No. 2; 337-341; PMCID PMC322853; 10.1073/pnas.83.2.337
• Ciccarelli, Richard B. and Solomon, Mark J., et el. (1985) In vivo effects of cis- and trans-diamminedichloroplatinum(II) on SV40 chromosomes: differential repair, DNA-protein crosslinking, and inhibition of replication; Biochemistry; Vol. 24; No. 26; 7533-7540; 10.1021/bi00347a005
• Solomon, Mark J. and Varshavsky, Alexander (1985) Formaldehyde-mediated DNA-protein crosslinking: A probe for in vivo chromatin structures; Proceedings of the National Academy of Sciences of the United States of America; Vol. 82; No. 19; 6470-6474; PMCID PMC390738; 10.1073/pnas.82.19.6470
• Barsoum, James and Varshavsky, Alexander (1985) Preferential localization of variant nucleosomes near the 5'-end of the mouse dihydrofolate reductase gene; Journal of Biological Chemistry; Vol. 260; No. 12; 7688-7697; 10.1016/s0021-9258(17)39663-1
• Ciechanover, A. and Finley, D., et el. (1985) Mammalian cell cycle mutant defective in intracellular protein degradation and ubiquitin-protein conjugation; Progress in clinical and biological research; Vol. 180; 17-31
• Özkaynak, Engin and Finley, Daniel, et el. (1984) The yeast ubiquitin gene: head-to-tail repeats encoding a polyubiquitin precursor protein; Nature; Vol. 312; No. 5995; 663-666; 10.1038/312663a0
• Strauss, François and Varshavsky, Alexander (1984) A protein binds to a satellite DNA repeat at three specific sites that would be brought into mutual proximity by DNA folding in the nucleosome; Cell; Vol. 37; No. 3; 889-901; 10.1016/0092-8674(84)90424-0
• Roninson, Igor B. and Abelson, Herbert T., et el. (1984) Amplification of specific DNA sequences correlates with multi-drug resistance in Chinese hamster cells; Nature; Vol. 309; No. 5969; 626-628; 10.1038/309626a0
• Ciechanover, Aaron and Finley, Daniel, et el. (1984) Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85; Cell; Vol. 37; No. 1; 57-66; 10.1016/0092-8674(84)90300-3
• Finley, Daniel and Ciechanover, Aaron, et el. (1984) Thermolability of ubiquitin-activating enzyme from the mammalian cell cycle mutant ts85; Cell; Vol. 37; No. 1; 43-55; 10.1016/0092-8674(84)90299-x
• Ciechanover, Aaron and Finley, Daniel, et el. (1984) The ubiquitin-mediated proteolytic pathway and mechanisms of energy‐dependent intracellular protein degradation; Journal of Cellular Biochemistry; Vol. 24; No. 1; 27-53; 10.1002/jcb.240240104
• Varshavsky, Alexander (1983) Do stalled replication forks synthesize a specific alarmone?; Journal of Theoretical Biology; Vol. 105; No. 4; 707-714; 10.1016/0022-5193(83)90228-x
• Snapka, Robert M. and Varshavsky, Alexander (1983) Loss of unstably amplified dihydrofolate reductase genes from mouse cells is greatly accelerated by hydroxyurea; Proceedings of the National Academy of Sciences of the United States of America; Vol. 80; No. 24; 7533-7537; PMCID PMC389986; 10.1073/pnas.80.24.7533
• Wu, Kun Chi and Strauss, François, et el. (1983) Nucleosome arrangement in green monkey α-satellite chromatin: Superimposition of non-random and apparently random patterns; Journal of Molecular Biology; Vol. 170; No. 1; 93-117; 10.1016/s0022-2836(83)80228-9
• Varshavsky, Alexander (1983) Diadenosine 5′, 5′′′-P¹, P⁴-tetraphosphate: a pleiotropically acting alarmone?; Cell; Vol. 34; No. 3; 711-712; 10.1016/0092-8674(83)90526-3
• Barsoum, James and Varshavsky, Alexander (1983) Mitogenic hormones and tumor promoters greatly increase the incidence of colony-forming cells bearing amplified dihydrofolate reductase genes; Proceedings of the National Academy of Sciences of the United States of America; Vol. 80; No. 17; 5330-5334; PMCID PMC384249; 10.1073/pnas.80.17.5330
• Swerdlow, Paul S. and Varshavsky, Alexander (1983) Affinity of HMG17 for a mononucleosome is not influenced by the presence of ubiquitin-H2A semihistone but strongly depends on DNA fragment size; Nucleic Acids Research; Vol. 11; No. 2; 387-401; PMCID PMC325721; 10.1093/nar/11.2.387
• Varshavsky, A. and Levinger, L., et el. (1983) Cellular and SV40 Chromatin: Replication, Segregation, Ubiqiritination, Nuclease-hypersensitive Sites, HMG-containing Nueleosomes, and Heterochromatin-specific Protein; Cold Spring Harbor Symposia on Quantitative Biology; Vol. 47; 511-528; 10.1101/sqb.1983.047.01.061
• Varshavsky, A. and Barsoum, J., et el. (1983) Acquisition and loss of amplified genes: dramatic effects of hormones, tumor promoters and cytotoxic drugs; Princess Takamatsu symposia; Vol. 14; 235-254
• Levinger, Louis and Varshavsky, Alexander (1982) Protein D1 preferentially binds A+T-rich DNA in vitro and is a component of Drosophila melanogaster nucleosomes containing A+T-rich satellite DNA; Proceedings of the National Academy of Sciences of the United States of America; Vol. 79; No. 23; 7152-7156; PMCID PMC347296; 10.1073/pnas.79.23.7152
• Barsoum, James and Levinger, Louis, et el. (1982) On the chromatin structure of the amplified, transcriptionally active gene for dihydrofolate reductase in mouse cells; Journal of Biological Chemistry; Vol. 257; No. 9; 5274-5282; 10.1016/s0021-9258(18)34667-2
• Boyce, Frederick M. and Sundin, Olof, et el. (1982) New way to isolate simian virus 40 nucleoprotein complexes from infected cells: use of a thiol-specific reagent; Journal of Virology; Vol. 42; No. 1; 292-296; PMCID PMC256070; 10.1128/jvi.42.1.292-296.1982
• Levinger, Louis and Varshavsky, Alexander (1982) Selective arrangement of ubiquitinated and D1 protein-containing nucleosomes within the drosophila genome; Cell; Vol. 28; No. 2; 375-385; 10.1016/0092-8674(82)90355-5
• Levinger, Louis and Varshavsky, Alexander (1981) Heat-shock proteins of Drosophila are associated with nuclease-resistant, high-salt-resistant nuclear structures; Journal of Cell Biology; Vol. 90; No. 3; 793-796; PMCID PMC2111893; 10.1083/jcb.90.3.793
• Sundin, Olof and Varshavsky, Alexander (1981) Arrest of segregation leads to accumulation of highly intertwined catenated dimers: Dissection of the final stages of SV40 DNA replication; Cell; Vol. 25; No. 3; 659-669; 10.1016/0092-8674(81)90173-2
• Varshavsky, Alexander (1981) On the possibility of metabolic control of replicon "misfiring": Relationship to emergence of malignant phenotypes in mammalian cell lineages; Proceedings of the National Academy of Sciences of the United States of America; Vol. 78; No. 6; 3673-3677; PMCID PMC319633; 10.1073/pnas.78.6.3673
• Levinger, Louis and Barsoum, James, et el. (1981) Two-dimensional hybridization mapping of nucleosomes: Comparison of DNA and protein patterns; Journal of Molecular Biology; Vol. 146; No. 3; 287-304; 10.1016/0022-2836(81)90389-2
• Sundin, Olof and Varshavsky, Alexander (1980) Terminal stages of SV40 DNA replication proceed via multiply intertwined catenated dimers; Cell; Vol. 21; No. 1; 103-114; 10.1016/0092-8674(80)90118-x
• Levinger, Louis and Varshavsky, Alexander (1980) High-resolution fractionation of nucleosomes: minor particles, "whiskers," and separation of mononucleosomes containing and lacking A24 semihistone; Proceedings of the National Academy of Sciences of the United States of America; Vol. 77; No. 6; 3244-3248; PMCID PMC349591; 10.1073/pnas.77.6.3244
• Sundin, Olof and Varshavsky, Alexander (1979) Staphylococcal nuclease makes a single non-random cut in the simian virus 40 viral minichromosome; Journal of Molecular Biology; Vol. 132; No. 3; 535-546; 10.1016/0022-2836(79)90274-2
• Varshavsky, Alexander J. and Sundin, Olof, et el. (1979) A stretch of "late" SV40 viral DNA about 400 bp long which includes the origin of replication is specifically exposed in SV40 minichromosomes; Cell; Vol. 16; No. 2; 453-466; 10.1016/0092-8674(79)90021-7
• Varshavsky, A. J. and Sundin, O. H., et el. (1978) SV40 viral minichromosome: preferential exposure of the origin of replication as probed by restriction endonucleases; Nucleic Acids Research; Vol. 5; No. 10; 3469-3478; PMCID PMC342688; 10.1093/nar/5.10.3469
• Varshavsky, A. J. and Bakayev, V. V., et el. (1978) On the structure of cellular and viral chromatin; Philosophical Transactions of the Royal Society of London. B, Biological Sciences; Vol. 283; No. 997; 275-285; 10.1098/rstb.1978.0024
• Shmatchenko, V. V. and Varshavsky, A. J. (1978) A technique of low-pH gel electrophoresis of chromosomal proteins which does not require preliminary removal of DNA; Analytical Biochemistry; Vol. 85; No. 1; 42-46; 10.1016/0003-2697(78)90271-3
• Varshavsky, A. J. and Bakayev, V. V., et el. (1978) On the Structure of Eukaryotic, Prokaryotic, and Viral Chromatin; Cold Spring Harbor Symposia on Quantitative Biology; Vol. 42; No. 1; 457-473; 10.1101/sqb.1978.042.01.049
• Varshavsky, A. J. and Nedospasov, S. A., et el. (1977) Compact form of SV40 viral minichromosome is resistant to nuclease: possible implications for chromatin structure; Nucleic Acids Research; Vol. 4; No. 10; 3303-3325; PMCID PMC342655; 10.1093/nar/4.10.3303
• Varshavsky, A. J. and Nedospasov, S. A., et el. (1977) Histone-like proteins in the purified Escherichia coli deoxyribonucleoprotein; Nucleic Acids Research; Vol. 4; No. 8; 2725-2746; PMCID PMC342604; 10.1093/nar/4.8.2725
• Bakayev, V. V. and Bakayeva, T. G., et el. (1977) Nucleosomes and subnucleosomes: heterogeneity and composition; Cell; Vol. 11; No. 3; 619-629; 10.1016/0092-8674(77)90079-4
• Varshavsky, A. J. and Georgiev, G. P. (1976) Free DNA stretches in histone H1-depleted chromatin and their possible relation to chromomere structure; Molecular Biology Reports; Vol. 3; No. 1; 27-38; 10.1007/bf00357206
• Varshavsky, A. J. and Bakayev, V. V., et el. (1976) Minichromosome of simian virus 40: presence of histone HI; Nucleic Acids Research; Vol. 3; No. 8; 2101-2114; PMCID PMC343065; 10.1093/nar/3.8.2101
• Varshavsky, Alexander J. and Bakayev, Valery V., et el. (1976) Studies on Chromatin. Free DNA in Sheared Chromatin; European Journal of Biochemistry; Vol. 66; No. 2; 211-223; 10.1111/j.1432-1033.1976.tb10510.x
• Varshavsky, A. J. and Bakayev, V. V., et el. (1976) Heterogeneity of chromatin subunits in vitro and location of histone H1; Nucleic Acids Research; Vol. 3; No. 2; 477-492; PMCID PMC342917; 10.1093/nar/3.2.477
• Varshavsky, A. J. and Georgiev, G. P. (1975) Studies on chromatin. V. A model for the structure of chromatin subunit; Molecular Biology Reports; Vol. 2; No. 3; 255-262; 10.1007/bf00356996
• Varshavsky, A. J. and Bakayev, V. V. (1975) Studies on chromatin. III. v-Bodies and Free DNA in Chromatin Lacking Histone H1; Molecular Biology Reports; Vol. 2; No. 3; 209-217; 10.1007/bf00356990
• Varshavsky, A. J. and Bakayev, V. V. (1975) Studies on chromatin. IV. Evidence for a toroidal shape of chromatin subunits; Molecular Biology Reports; Vol. 2; No. 3; 247-254; 10.1007/bf00356995
• Varshavsky, A. J. and Ilyin, Yu. V., et el. (1974) Very long stretches of free DNA in chromatin; Nature; Vol. 250; No. 5467; 602-606; 10.1038/250602a0
• Ilyin, Yu. V. and Bayev, A. A., Jr., et el. (1974) Histone-histone proximity in chromatin as seen by imidoester cross-linking; Molecular Biology Reports; Vol. 1; No. 6; 343-348; 10.1007/bf00309568
• Georgiev, Georgiy P. and Varshavsky, Alexandr Ja., et el. (1974) On the Structural Organization of the Transcriptional Unit in Animal Chromosomes; Cold Spring Harbor Symposia on Quantitative Biology; Vol. 38; 869-884; 10.1101/sqb.1974.038.01.089
• Varshavsky, A. J. and Ilyin, Yu. V., et el. (1973) Long molecules of free DNA in the sheared chromatin preparation; Molecular Biology Reports; Vol. 1; No. 4; 201-207; 10.1007/bf00357642
• Varshavsky, Alexander J. and Georgiev, Georgii P. (1973) Redistribution of histones during unfolding of chromosomal DNA; Molecular Biology Reports; Vol. 1; No. 3; 143-148; 10.1007/bf00357154
• Varshavsky, A. J. and Georgiev, G. P. (1973) Arrangement of histones along DNA in chromosomal deoxyribonucleoprotein lacking histone F1; Molecular Biology Reports; Vol. 1; No. 2; 87-92; 10.1007/bf00357586
• Varshavsky, A. J. and Georgiev, G. P. (1972) Clustered arrangement of histones F2a1 and F3 along DNA in chromosomal deoxyribonucleoproteins; Biochimica et Biophysica Acta; Vol. 281; No. 4; 669-674; 10.1016/0005-2787(72)90166-9
• Varshavsky, A. Ya. and Ilyin, Yu. V., et el. (1971) Collapse of extended deoxyribonucleoprotein molecules upon increase of the ionic strength of solution; Biochimica et Biophysica Acta; Vol. 246; No. 3; 583-588; 10.1016/0005-2787(71)90797-0