Voorhees, Rebecca

Combined from CaltechAUTHORS

• Watson, Joseph L. and Seinkmane, Estere, et el. (2024) Author Correction: Macromolecular condensation buffers intracellular water potential; Nature; Vol. 628; E4; 10.1038/s41586-024-07346-8
• Muthukumar, Gayathri and Stevens, Taylor A., et el. (2024) Triaging of α-helical proteins to the mitochondrial outer membrane by distinct chaperone machinery based on substrate topology; Molecular Cell; Vol. 84; No. 6; 1101-1119.e9; 10.1016/j.molcel.2024.01.028
• Stevens, Taylor Anthony and Pinton Tomaleri, Giovani, et el. (2023) A nanobody-based strategy for rapid and scalable purification of human protein complexes; Nature Protocols; 10.1038/s41596-023-00904-w
• Guna, Alina and Page, Katharine R., et el. (2023) A dual sgRNA library design to probe genetic modifiers using genome-wide CRISPRi screens; BMC Genomics; Vol. 24; 651; PMCID PMC10614335; 10.1186/s12864-023-09754-y
• Pleiner, Tino and Hazu, Masami, et el. (2023) A selectivity filter in the ER membrane protein complex limits protein misinsertion at the ER; Journal of Cell Biology; Vol. 222; No. 8; Art. No. e202212007; PMCID PMC10200711; 10.1083/jcb.202212007
• Inglis, Alison J. and Guna, Alina, et el. (2023) Coupled protein quality control during nonsense-mediated mRNA decay; Journal of Cell Science; Vol. 136; No. 10; Art. No. jcs261216; PMCID PMC10234110; 10.1242/jcs.261216
• Stevens, Taylor Anthony and Pinton Tomaleri, Giovani, et el. (2023) A nanobody-based strategy for rapid and scalable purification of native human protein complexes; 10.1101/2023.03.09.531980
• Guna, Alina and Page, Katharine R., et el. (2023) A dual sgRNA library design to probe genetic modifiers using genome-wide CRISPRi screens; PMCID PMC9882262; 10.1101/2023.01.22.525086
• Pleiner, Tino and Hazu, Masami, et el. (2023) A selectivity filter in the EMC limits protein mislocalization to the ER; 10.1101/2022.11.29.518402
• Guna, Alina and Hazu, Masami, et el. (2023) A TAle of Two Pathways: Tail-Anchored Protein Insertion at the Endoplasmic Reticulum; Cold Spring Harbor Perspectives in Biology; Vol. 15; No. 3; Art. No. a041252; PMCID PMC9979854; 10.1101/cshperspect.a041252
• Guna, Alina and Stevens, Taylor A., et el. (2023) MTCH2 is a mitochondrial outer membrane protein insertase; 10.1101/2022.09.15.508165
• Guna, Alina and Stevens, Taylor A., et el. (2022) MTCH2 is a mitochondrial outer membrane protein insertase; Science; Vol. 378; No. 6617; 317-322; PMCID PMC9674023; 10.1126/science.add1856
• McCord, Rachel Patton and Taipale, Mikko, et el. (2022) Voices on technology: The molecular biologists' ever-expanding toy box; Molecular Cell; Vol. 82; No. 2; 221-226; 10.1016/j.molcel.2021.12.025
• Inglis, Alison J. and Guna, Alina, et el. (2022) Coupled protein quality control during nonsense mediated mRNA decay; 10.1101/2021.12.22.473893
• Stangherlin, Alessandra and Watson, Joseph L., et el. (2021) Compensatory ion transport buffers daily protein rhythms to regulate osmotic balance and cellular physiology; Nature Communications; Vol. 12; Art. No. 6035; PMCID PMC8520019; 10.1038/s41467-021-25942-4
• Pleiner, Tino and Hazu, Masami, et el. (2021) WNK1 is an assembly factor for the human ER membrane protein complex; Molecular Cell; Vol. 81; No. 13; 2693-2704; PMCID PMC8254792; 10.1016/j.molcel.2021.04.013
• Banerjee, Abhik K. and Blanco, Mario R., et el. (2020) SARS-CoV-2 disrupts splicing, translation, and protein trafficking to suppress host defenses; Cell; Vol. 183; No. 5; 1325-1339; PMCID PMC7543886; 10.1016/j.cell.2020.10.004
• Pleiner, Tino and Pinton Tomaleri, Giovani, et el. (2020) Structural basis for membrane insertion by the human ER membrane protein complex; Science; Vol. 369; No. 6502; 433-436; PMCID PMC7547852; 10.1126/science.abb5008
• Inglis, Alison J. and Page, Katharine R., et el. (2020) Differential modes of orphan subunit recognition for the WRB/CAML complex; Cell Reports; Vol. 30; No. 11; 3691-3698; PMCID PMC7147533; 10.1016/j.celrep.2020.02.084
• Voorhees, Rebecca M. and Hegde, Ramanujan S. (2016) Toward a structural understanding of co-translational protein translocation; Current Opinion in Cell Biology; Vol. 41; 91-99; 10.1016/j.ceb.2016.04.009
• Voorhees, Rebecca M. and Hegde, Ramanujan S. (2016) Structure of the Sec61 channel opened by a signal sequence; Science; Vol. 351; No. 6268; 88-91; PMCID PMC4700591; 10.1126/science.aad4992
• Voorhees, Rebecca M. and Hegde, Ramanujan S. (2015) Structures of the scanning and engaged states of the mammalian SRP-ribosome complex; eLife; Vol. 4; Art. No. e07975; PMCID PMC4497383; 10.7554/eLife.07975
• Voorhees, Rebecca M. and Fernández, Israel S., et el. (2014) Structure of the Mammalian Ribosome-Sec61 Complex to 3.4 Å Resolution; Cell; Vol. 157; No. 7; 1632-1643; PMCID PMC4081569; 10.1016/j.cell.2014.05.024
• Voorhees, Rebecca M. and Ramakrishnan, V. (2013) Structural Basis of the Translational Elongation Cycle; Annual Review of Biochemistry; Vol. 82; 203-236; 10.1146/annurev-biochem-113009-092313
• Voorhees, Rebecca M. and Mandal, Debabrata, et el. (2013) The structural basis for specific decoding of AUA by isoleucine tRNA on the ribosome; Nature Structural and Molecular Biology; Vol. 20; No. 5; 641-643; PMCID PMC3672977; 10.1038/nsmb.2545
• Voorhees, Rebecca M. and Schmeing, T. Martin, et el. (2011) Response to Comment on "The Mechanism for Activation of GTP Hydrolysis on the Ribosome"; Science; Vol. 333; No. 6038; 37-37; 10.1126/science.1202532
• Schmeing, T. Martin and Voorhees, Rebecca M., et el. (2011) How mutations in tRNA distant from the anticodon affect the fidelity of decoding; Nature Structural and Molecular Biology; Vol. 18; No. 4; 432-436; PMCID PMC3072312; 10.1038/nsmb.2003
• Voorhees, Rebecca M. and Schmeing, T. Martin, et el. (2010) The Mechanism for Activation of GTP Hydrolysis on the Ribosome; Science; Vol. 330; No. 6005; 835-838; PMCID PMC3763471; 10.1126/science.1194460
• Schmeing, T. Martin and Voorhees, Rebecca M., et el. (2009) The Crystal Structure of the Ribosome Bound to EF-Tu and Aminoacyl-tRNA; Science; Vol. 326; No. 5953; 688-694; PMCID PMC3763470; 10.1126/science.1179700
• Voorhees, Rebecca M. and Weixlbaumer, Albert, et el. (2009) Insights into substrate stabilization from snapshots of the peptidyl transferase center of the intact 70S ribosome; Nature Structural and Molecular Biology; Vol. 16; No. 5; 528-533; PMCID PMC2679717; 10.1038/nsmb.1577
• Weixlbaumer, Albert and Jin, Hong, et el. (2008) Insights into Translational Termination from the Structure of RF2 Bound to the Ribosome; Science; Vol. 322; No. 5903; 953-956; PMCID PMC2642913; 10.1126/science.1164840
• Kingery, David A. and Pfund, Emmanuel, et el. (2008) An Uncharged Amine in the Transition State of the Ribosomal Peptidyl Transfer Reaction; Chemistry and Biology; Vol. 15; No. 5; 493-500; PMCID PMC2851197; 10.1016/j.chembiol.2008.04.005