| Year |
Citation |
Score |
| 2024 |
Varshavsky A. N-degron pathways. Proceedings of the National Academy of Sciences of the United States of America. 121: e2408697121. PMID 39264755 DOI: 10.1073/pnas.2408697121 |
0.458 |
|
| 2022 |
Kim BH, Kim MK, Oh SJ, Nguyen KT, Kim JH, Varshavsky A, Hwang CS, Song HK. 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. 119: e2209597119. PMID 35878037 DOI: 10.1073/pnas.2209597119 |
0.608 |
|
| 2021 |
Chen SJ, Kim L, Song HK, Varshavsky A. 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. 118. PMID 34663735 DOI: 10.1073/pnas.2115430118 |
0.644 |
|
| 2020 |
Vu TTM, Mitchell DC, Gygi SP, Varshavsky A. 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. PMID 33229537 DOI: 10.1073/pnas.2020124117 |
0.39 |
|
| 2020 |
Vu TTM, Varshavsky A. The ATF3 Transcription Factor Is a Short-Lived Substrate of the Arg/N-Degron Pathway. Biochemistry. PMID 32692156 DOI: 10.1021/Acs.Biochem.0C00514 |
0.535 |
|
| 2020 |
Dong C, Chen SJ, Melnykov A, Weirich S, Sun K, Jeltsch A, Varshavsky A, Min J. 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. PMID 32513738 DOI: 10.1073/Pnas.2007085117 |
0.546 |
|
| 2020 |
Oh JH, Hyun JY, Chen SJ, Varshavsky A. 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. PMID 32366662 DOI: 10.1073/Pnas.2003043117 |
0.483 |
|
| 2020 |
Chen SJ, Melnykov A, Varshavsky A. Evolution of Substrates and Components of the Pro/N-Degron Pathway. Biochemistry. PMID 31895557 DOI: 10.1021/Acs.Biochem.9B00953 |
0.564 |
|
| 2019 |
Melnykov A, Chen SJ, Varshavsky A. 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. PMID 31337681 DOI: 10.1073/Pnas.1908304116 |
0.585 |
|
| 2019 |
Varshavsky A. 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. PMID 31085645 DOI: 10.1073/Pnas.1904709116 |
0.302 |
|
| 2019 |
Varshavsky A. N-degron and C-degron pathways of protein degradation. Proceedings of the National Academy of Sciences of the United States of America. 116: 358-366. PMID 30622213 DOI: 10.1073/Pnas.1816596116 |
0.514 |
|
| 2018 |
Kim JM, Seok OH, Ju S, Heo JE, Yeom J, Kim DS, Yoo JY, Varshavsky A, Lee C, Hwang CS. Formyl-methionine as an N-degron of a eukaryotic N-end rule pathway. Science (New York, N.Y.). PMID 30409808 DOI: 10.1126/Science.Aat0174 |
0.591 |
|
| 2018 |
Dougan DA, Varshavsky A. Understanding the Pro/N-end rule pathway. Nature Chemical Biology. 14: 415-416. PMID 29662186 DOI: 10.1038/S41589-018-0045-0 |
0.573 |
|
| 2017 |
Oh JH, Chen SJ, Varshavsky A. A reference-based protein degradation assay without global translation inhibitors. The Journal of Biological Chemistry. PMID 29122887 DOI: 10.1074/Jbc.M117.814236 |
0.483 |
|
| 2017 |
Varshavsky A. The Ubiquitin System, Autophagy, and Regulated Protein Degradation. Annual Review of Biochemistry. 86: 123-128. PMID 28654326 DOI: 10.1146/Annurev-Biochem-061516-044859 |
0.426 |
|
| 2017 |
Oh JH, Hyun JY, Varshavsky A. 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. PMID 28515311 DOI: 10.1073/Pnas.1705898114 |
0.542 |
|
| 2017 |
Chen SJ, Wu X, Wadas B, Oh JH, Varshavsky A. An N-end rule pathway that recognizes proline and destroys gluconeogenic enzymes. Science (New York, N.Y.). 355. PMID 28126757 DOI: 10.1126/Science.Aal3655 |
0.812 |
|
| 2016 |
Wadas B, Piatkov K, Brower C, Varshavsky A. Analyzing N-terminal Arginylation Through the Use of Peptide Arrays and Degradation Assays. The Journal of Biological Chemistry. PMID 27510035 DOI: 10.1074/Jbc.M116.747956 |
0.827 |
|
| 2016 |
Wadas B, Borjigin J, Huang Z, Oh JH, Hwang CS, Varshavsky A. Degradation of Serotonin N-Acetyltransferase, a Circadian Regulator, by the N-end Rule Pathway. The Journal of Biological Chemistry. PMID 27339900 DOI: 10.1074/Jbc.M116.734640 |
0.824 |
|
| 2016 |
Liu YJ, Liu C, Chang Z, Wadas B, Brower CS, Song ZH, Xu ZL, Shang YL, Liu WX, Wang LN, Dong W, Varshavsky A, Hu RG, Li W. Degradation of the Separase-cleaved Rec8, a Meiotic Cohesin Subunit, by the N-end Rule Pathway. The Journal of Biological Chemistry. PMID 26858254 DOI: 10.1074/Jbc.M116.714964 |
0.832 |
|
| 2015 |
Piatkov KI, Vu TT, Hwang CS, Varshavsky A. Formyl-methionine as a degradation signal at the N-termini of bacterial proteins. Microbial Cell. 2: 376-393. PMID 26866044 DOI: 10.15698/Mic2015.10.231 |
0.595 |
|
| 2015 |
Park SE, Kim JM, Seok OH, Cho H, Wadas B, Kim SY, Varshavsky A, Hwang CS. Control of mammalian G protein signaling by N-terminal acetylation and the N-end rule pathway. Science (New York, N.Y.). 347: 1249-52. PMID 25766235 DOI: 10.1126/Science.Aaa3844 |
0.836 |
|
| 2014 |
Brower CS, Rosen CE, Jones RH, Wadas BC, Piatkov KI, Varshavsky A. 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. 111: E4936-45. PMID 25369936 DOI: 10.1073/Pnas.1419587111 |
0.83 |
|
| 2014 |
Piatkov KI, Oh JH, Liu Y, Varshavsky A. 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. 111: E817-26. PMID 24550490 DOI: 10.1073/Pnas.1401639111 |
0.56 |
|
| 2014 |
Kim HK, Kim RR, Oh JH, Cho H, Varshavsky A, Hwang CS. The N-terminal methionine of cellular proteins as a degradation signal. Cell. 156: 158-69. PMID 24361105 DOI: 10.1016/J.Cell.2013.11.031 |
0.595 |
|
| 2013 |
Piatkov K, Graciet E, Varshavsky A. Ubiquitin reference technique and its use in ubiquitin-lacking prokaryotes. Plos One. 8: e67952. PMID 23825692 DOI: 10.1371/Journal.Pone.0067952 |
0.477 |
|
| 2013 |
Shemorry A, Hwang CS, Varshavsky A. Control of protein quality and stoichiometries by N-terminal acetylation and the N-end rule pathway. Molecular Cell. 50: 540-51. PMID 23603116 DOI: 10.1016/J.Molcel.2013.03.018 |
0.831 |
|
| 2013 |
Brower CS, Piatkov KI, Varshavsky A. Neurodegeneration-associated protein fragments as short-lived substrates of the N-end rule pathway. Molecular Cell. 50: 161-71. PMID 23499006 DOI: 10.1016/J.Molcel.2013.02.009 |
0.512 |
|
| 2012 |
Piatkov KI, Colnaghi L, Békés M, Varshavsky A, Huang TT. The auto-generated fragment of the Usp1 deubiquitylase is a physiological substrate of the N-end rule pathway. Molecular Cell. 48: 926-33. PMID 23159736 DOI: 10.1016/J.Molcel.2012.10.012 |
0.503 |
|
| 2012 |
Piatkov KI, Brower CS, Varshavsky A. 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. 109: E1839-47. PMID 22670058 DOI: 10.1073/Pnas.1207786109 |
0.485 |
|
| 2012 |
Varshavsky A. The ubiquitin system, an immense realm. Annual Review of Biochemistry. 81: 167-76. PMID 22663079 DOI: 10.1146/Annurev-Biochem-051910-094049 |
0.486 |
|
| 2012 |
Varshavsky A. Three decades of studies to understand the functions of the ubiquitin family. Methods in Molecular Biology (Clifton, N.J.). 832: 1-11. PMID 22350874 DOI: 10.1007/978-1-61779-474-2_1 |
0.498 |
|
| 2011 |
Hwang CS, Sukalo M, Batygin O, Addor MC, Brunner H, Aytes AP, Mayerle J, Song HK, Varshavsky A, Zenker M. Ubiquitin ligases of the N-end rule pathway: assessment of mutations in UBR1 that cause the Johanson-Blizzard syndrome. Plos One. 6: e24925. PMID 21931868 DOI: 10.1371/Journal.Pone.0024925 |
0.594 |
|
| 2011 |
Varshavsky A. The N-end rule pathway and regulation by proteolysis. Protein Science : a Publication of the Protein Society. 20: 1298-345. PMID 21633985 DOI: 10.1002/Pro.666 |
0.597 |
|
| 2010 |
Hwang CS, Shemorry A, Auerbach D, Varshavsky A. The N-end rule pathway is mediated by a complex of the RING-type Ubr1 and HECT-type Ufd4 ubiquitin ligases. Nature Cell Biology. 12: 1177-85. PMID 21076411 DOI: 10.1038/Ncb2121 |
0.82 |
|
| 2010 |
Brower CS, Veiga L, Jones RH, Varshavsky A. Mouse Dfa is a repressor of TATA-box promoters and interacts with the Abt1 activator of basal transcription. The Journal of Biological Chemistry. 285: 17218-34. PMID 20356838 DOI: 10.1074/Jbc.M110.118638 |
0.42 |
|
| 2010 |
Hwang CS, Shemorry A, Varshavsky A. N-terminal acetylation of cellular proteins creates specific degradation signals. Science (New York, N.Y.). 327: 973-7. PMID 20110468 DOI: 10.1126/Science.1183147 |
0.845 |
|
| 2009 |
Brower CS, Varshavsky A. Ablation of arginylation in the mouse N-end rule pathway: loss of fat, higher metabolic rate, damaged spermatogenesis, and neurological perturbations. Plos One. 4: e7757. PMID 19915679 DOI: 10.1371/Journal.Pone.0007757 |
0.475 |
|
| 2009 |
Graciet E, Walter F, Ó'Maoiléidigh DS, Pollmann S, Meyerowitz EM, Varshavsky A, Wellmer F. 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. 106: 13618-23. PMID 19620738 DOI: 10.1073/Pnas.0906404106 |
0.533 |
|
| 2009 |
Wang H, Piatkov KI, Brower CS, Varshavsky A. Glutamine-specific N-terminal amidase, a component of the N-end rule pathway. Molecular Cell. 34: 686-95. PMID 19560421 DOI: 10.1016/J.Molcel.2009.04.032 |
0.488 |
|
| 2009 |
Hwang CS, Shemorry A, Varshavsky A. 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. 106: 2142-7. PMID 19164530 DOI: 10.1073/Pnas.0812316106 |
0.814 |
|
| 2008 |
Varshavsky A. The N-end rule at atomic resolution. Nature Structural & Molecular Biology. 15: 1238-40. PMID 19050717 DOI: 10.1038/Nsmb1208-1238 |
0.349 |
|
| 2008 |
Hwang CS, Varshavsky A. 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. 105: 19188-93. PMID 19033468 DOI: 10.1073/Pnas.0808891105 |
0.422 |
|
| 2008 |
Xia Z, Turner GC, Hwang CS, Byrd C, Varshavsky A. Amino acids induce peptide uptake via accelerated degradation of CUP9, the transcriptional repressor of the PTR2 peptide transporter. The Journal of Biological Chemistry. 283: 28958-68. PMID 18708352 DOI: 10.1074/Jbc.M803980200 |
0.419 |
|
| 2008 |
Xia Z, Webster A, Du F, Piatkov K, Ghislain M, Varshavsky A. Substrate-binding sites of UBR1, the ubiquitin ligase of the N-end rule pathway. The Journal of Biological Chemistry. 283: 24011-28. PMID 18566452 DOI: 10.1074/Jbc.M802583200 |
0.462 |
|
| 2008 |
Connor RE, Piatkov K, Varshavsky A, Tirrell DA. Enzymatic N-terminal addition of noncanonical amino acids to peptides and proteins. Chembiochem : a European Journal of Chemical Biology. 9: 366-9. PMID 18203209 DOI: 10.1002/Cbic.200700605 |
0.458 |
|
| 2008 |
Hu RG, Wang H, Xia Z, Varshavsky A. The N-end rule pathway is a sensor of heme. Proceedings of the National Academy of Sciences of the United States of America. 105: 76-81. PMID 18162538 DOI: 10.1073/Pnas.0710568105 |
0.511 |
|
| 2007 |
Varshavsky A. 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. 104: 14935-40. PMID 17846424 DOI: 10.1073/Pnas.0706546104 |
0.314 |
|
| 2007 |
Schnupf P, Zhou J, Varshavsky A, Portnoy DA. Listeriolysin O secreted by Listeria monocytogenes into the host cell cytosol is degraded by the N-end rule pathway. Infection and Immunity. 75: 5135-47. PMID 17682039 DOI: 10.1128/Iai.00164-07 |
0.458 |
|
| 2007 |
Tasaki T, Sohr R, Xia Z, Hellweg R, Hörtnagl H, Varshavsky A, Kwon YT. Biochemical and genetic studies of UBR3, a ubiquitin ligase with a function in olfactory and other sensory systems. The Journal of Biological Chemistry. 282: 18510-20. PMID 17462990 DOI: 10.1074/Jbc.M701894200 |
0.469 |
|
| 2006 |
Hu RG, Brower CS, Wang H, Davydov IV, Sheng J, Zhou J, Kwon YT, Varshavsky A. Arginyltransferase, its specificity, putative substrates, bidirectional promoter, and splicing-derived isoforms. The Journal of Biological Chemistry. 281: 32559-73. PMID 16943202 DOI: 10.1074/Jbc.M604355200 |
0.592 |
|
| 2006 |
An JY, Seo JW, Tasaki T, Lee MJ, Varshavsky A, Kwon YT. 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. 103: 6212-7. PMID 16606826 DOI: 10.1073/Pnas.0601700103 |
0.526 |
|
| 2006 |
Varshavsky A. The early history of the ubiquitin field. Protein Science : a Publication of the Protein Society. 15: 647-54. PMID 16501229 DOI: 10.1110/Ps.052012306 |
0.464 |
|
| 2006 |
Graciet E, Hu RG, Piatkov K, Rhee JH, Schwarz EM, Varshavsky A. 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. 103: 3078-83. PMID 16492767 DOI: 10.1073/Pnas.0511224103 |
0.422 |
|
| 2006 |
Varshavsky A. The origins of the ubiquitin field Israel Journal of Chemistry. 46: 137-144. DOI: 10.1560/5E71-3Uu5-1Nh2-6Uyj |
0.465 |
|
| 2006 |
Zenker M, Mayerle J, Lerch MM, Tagariello A, Zerres K, Durie PR, Beier M, Hülskamp G, Guzman C, Rehder H, Beemer FA, Hamel B, Vanlieferinghen P, Gershoni-Baruch R, Vieira MW, ... ... Varshavsky A, et al. Erratum: Deficiency of UBR1, a ubiquitin ligase of the N-end rule pathway, causes pancreatic dysfunction, malformations and mental retardation (Johanson-Blizzard syndrome) (Nature Genetics (2005) 37 (1345-1350)) Nature Genetics. 38. DOI: 10.1038/Ng0206-265 |
0.356 |
|
| 2005 |
Dohmen RJ, Varshavsky A. Heat-inducible degron and the making of conditional mutants. Methods in Enzymology. 399: 799-822. PMID 16338396 DOI: 10.1016/S0076-6879(05)99052-6 |
0.387 |
|
| 2005 |
Varshavsky A. Ubiquitin fusion technique and related methods. Methods in Enzymology. 399: 777-99. PMID 16338395 DOI: 10.1016/S0076-6879(05)99051-4 |
0.379 |
|
| 2005 |
Zenker M, Mayerle J, Lerch MM, Tagariello A, Zerres K, Durie PR, Beier M, Hülskamp G, Guzman C, Rehder H, Beemer FA, Hamel B, Vanlieferinghen P, Gershoni-Baruch R, Vieira MW, ... ... Varshavsky A, et al. Deficiency of UBR1, a ubiquitin ligase of the N-end rule pathway, causes pancreatic dysfunction, malformations and mental retardation (Johanson-Blizzard syndrome). Nature Genetics. 37: 1345-50. PMID 16311597 DOI: 10.1038/Ng1681 |
0.415 |
|
| 2005 |
Hu RG, Sheng J, Qi X, Xu Z, Takahashi TT, Varshavsky A. The N-end rule pathway as a nitric oxide sensor controlling the levels of multiple regulators. Nature. 437: 981-6. PMID 16222293 DOI: 10.1038/Nature04027 |
0.513 |
|
| 2005 |
Tasaki T, Mulder LC, Iwamatsu A, Lee MJ, Davydov IV, Varshavsky A, Muesing M, Kwon YT. A family of mammalian E3 ubiquitin ligases that contain the UBR box motif and recognize N-degrons. Molecular and Cellular Biology. 25: 7120-36. PMID 16055722 DOI: 10.1128/Mcb.25.16.7120-7136.2005 |
0.572 |
|
| 2004 |
Yin J, Kwon YT, Varshavsky A, Wang W. 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. 13: 2421-30. PMID 15317757 DOI: 10.1093/Hmg/Ddh269 |
0.491 |
|
| 2004 |
Finley D, Ciechanover A, Varshavsky A. Ubiquitin as a central cellular regulator. Cell. 116: S29-32, 2 p followin. PMID 15055578 DOI: 10.1016/S0092-8674(03)00971-1 |
0.548 |
|
| 2003 |
Kwon YT, Xia Z, An JY, Tasaki T, Davydov IV, Seo JW, Sheng J, Xie Y, Varshavsky A. Female lethality and apoptosis of spermatocytes in mice lacking the UBR2 ubiquitin ligase of the N-end rule pathway. Molecular and Cellular Biology. 23: 8255-71. PMID 14585983 DOI: 10.1128/Mcb.23.22.8255-8271.2003 |
0.473 |
|
| 2003 |
Varshavsky A. The N-end rule and regulation of apoptosis. Nature Cell Biology. 5: 373-6. PMID 12724766 DOI: 10.1038/Ncb0503-373 |
0.534 |
|
| 2002 |
Xie Y, Varshavsky A. UFD4 lacking the proteasome-binding region catalyses ubiquitination but is impaired in proteolysis. Nature Cell Biology. 4: 1003-7. PMID 12447385 DOI: 10.1038/Ncb889 |
0.425 |
|
| 2002 |
Sheng J, Kumagai A, Dunphy WG, Varshavsky A. Dissection of c-MOS degron. The Embo Journal. 21: 6061-71. PMID 12426378 DOI: 10.1093/Emboj/Cdf626 |
0.398 |
|
| 2002 |
Du F, Navarro-Garcia F, Xia Z, Tasaki T, Varshavsky A. 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. 99: 14110-5. PMID 12391316 DOI: 10.1073/Pnas.172527399 |
0.532 |
|
| 2002 |
Kwon YT, Kashina AS, Davydov IV, Hu RG, An JY, Seo JW, Du F, Varshavsky A. An essential role of N-terminal arginylation in cardiovascular development. Science (New York, N.Y.). 297: 96-9. PMID 12098698 DOI: 10.1126/Science.1069531 |
0.55 |
|
| 2001 |
Kwon YT, Xia Z, Davydov IV, Lecker SH, Varshavsky A. Construction and analysis of mouse strains lacking the ubiquitin ligase UBR1 (E3alpha) of the N-end rule pathway. Molecular and Cellular Biology. 21: 8007-21. PMID 11689692 DOI: 10.1128/Mcb.21.23.8007-8021.2001 |
0.559 |
|
| 2001 |
Rao H, Uhlmann F, Nasmyth K, Varshavsky A. Degradation of a cohesin subunit by the N-end rule pathway is essential for chromosome stability. Nature. 410: 955-9. PMID 11309624 DOI: 10.1038/35073627 |
0.557 |
|
| 2001 |
Xie Y, Varshavsky A. 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. 98: 3056-61. PMID 11248031 DOI: 10.1073/Pnas.071022298 |
0.452 |
|
| 2000 |
Varshavsky A. Recent studies of the ubiquitin system and the N-end rule pathway. Harvey Lectures. 96: 93-116. PMID 12200873 |
0.401 |
|
| 2000 |
Varshavsky A, Turner G, Du F, Xie Y. Felix Hoppe-Seyler Lecture 2000. The ubiquitin system and the N-end rule pathway. Biological Chemistry. 381: 779-89. PMID 11076011 DOI: 10.1515/Bc.2000.101 |
0.535 |
|
| 2000 |
Varshavsky A. Ubiquitin fusion technique and its descendants. Methods in Enzymology. 327: 578-93. PMID 11045010 DOI: 10.1016/S0076-6879(00)27303-5 |
0.397 |
|
| 2000 |
Turner GC, Varshavsky A. Detecting and measuring cotranslational protein degradation in vivo. Science (New York, N.Y.). 289: 2117-20. PMID 11000112 DOI: 10.1126/Science.289.5487.2117 |
0.473 |
|
| 2000 |
Turner GC, Du F, Varshavsky A. Peptides accelerate their uptake by activating a ubiquitin-dependent proteolytic pathway. Nature. 405: 579-83. PMID 10850718 DOI: 10.1038/35014629 |
0.496 |
|
| 2000 |
Kwon YT, Balogh SA, Davydov IV, Kashina AS, Yoon JK, Xie Y, Gaur A, Hyde L, Denenberg VH, Varshavsky A. 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. 20: 4135-48. PMID 10805755 DOI: 10.1128/Mcb.20.11.4135-4148.2000 |
0.528 |
|
| 2000 |
Davydov IV, Varshavsky A. RGS4 is arginylated and degraded by the N-end rule pathway in vitro. The Journal of Biological Chemistry. 275: 22931-41. PMID 10783390 DOI: 10.1074/Jbc.M001605200 |
0.583 |
|
| 2000 |
Xie Y, Varshavsky A. Physical association of ubiquitin ligases and the 26S proteasome. Proceedings of the National Academy of Sciences of the United States of America. 97: 2497-502. PMID 10688918 DOI: 10.1073/Pnas.060025497 |
0.425 |
|
| 1999 |
Xie Y, Varshavsky A. The E2-E3 interaction in the N-end rule pathway: the RING-H2 finger of E3 is required for the synthesis of multiubiquitin chain. The Embo Journal. 18: 6832-44. PMID 10581257 DOI: 10.1093/Emboj/18.23.6832 |
0.447 |
|
| 1999 |
Suzuki T, Varshavsky A. Degradation signals in the lysine-asparagine sequence space. The Embo Journal. 18: 6017-26. PMID 10545113 DOI: 10.1093/Emboj/18.21.6017 |
0.524 |
|
| 1999 |
Xie Y, Varshavsky A. The N-end rule pathway is required for import of histidine in yeast lacking the kinesin-like protein Cin8p. Current Genetics. 36: 113-23. PMID 10501933 DOI: 10.1007/S002940050480 |
0.529 |
|
| 1999 |
Kwon YT, Lévy F, Varshavsky A. Bivalent inhibitor of the N-end rule pathway. The Journal of Biological Chemistry. 274: 18135-9. PMID 10364269 DOI: 10.1074/Jbc.274.25.18135 |
0.511 |
|
| 1999 |
Dünnwald M, Varshavsky A, Johnsson N. Detection of transient in vivo interactions between substrate and transporter during protein translocation into the endoplasmic reticulum. Molecular Biology of the Cell. 10: 329-44. PMID 9950680 DOI: 10.1091/Mbc.10.2.329 |
0.426 |
|
| 1999 |
Lévy F, Johnston JA, Varshavsky A. Analysis of a conditional degradation signal in yeast and mammalian cells. European Journal of Biochemistry / Febs. 259: 244-52. PMID 9914499 DOI: 10.1046/J.1432-1327.1999.00024.X |
0.565 |
|
| 1999 |
Kwon YT, Kashina AS, Varshavsky A. 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. 19: 182-93. PMID 9858543 DOI: 10.1128/Mcb.19.1.182 |
0.507 |
|
| 1998 |
Davydov IV, Patra D, Varshavsky A. The N-end rule pathway in Xenopus egg extracts. Archives of Biochemistry and Biophysics. 357: 317-25. PMID 9735173 DOI: 10.1006/Abbi.1998.0829 |
0.508 |
|
| 1998 |
Finley D, Tanaka K, Mann C, Feldmann H, Hochstrasser M, Vierstra R, Johnston S, Hampton R, Haber J, Mccusker J, Silver P, Frontali L, Thorsness P, Varshavsky A, Byers B, et al. Unified nomenclature for subunits of the Saccharomyces cerevisiae proteasome regulatory particle. Trends in Biochemical Sciences. 23: 244-5. PMID 9697412 DOI: 10.1016/S0968-0004(98)01222-5 |
0.712 |
|
| 1998 |
Kwon YT, Reiss Y, Fried VA, Hershko A, Yoon JK, Gonda DK, Sangan P, Copeland NG, Jenkins NA, Varshavsky A. 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. 95: 7898-903. PMID 9653112 DOI: 10.1073/Pnas.95.14.7898 |
0.541 |
|
| 1998 |
Ramos PC, Höckendorff J, Johnson ES, Varshavsky A, Dohmen RJ. Ump1p is required for proper maturation of the 20S proteasome and becomes its substrate upon completion of the assembly. Cell. 92: 489-99. PMID 9491890 DOI: 10.1016/S0092-8674(00)80942-3 |
0.344 |
|
| 1998 |
Byrd C, Turner GC, Varshavsky A. The N-end rule pathway controls the import of peptides through degradation of a transcriptional repressor. The Embo Journal. 17: 269-77. PMID 9427760 DOI: 10.1093/Emboj/17.1.269 |
0.546 |
|
| 1997 |
Varshavsky A. The ubiquitin system. Trends in Biochemical Sciences. 22: 383-7. PMID 9357313 DOI: 10.1016/S0968-0004(97)01122-5 |
0.465 |
|
| 1997 |
Varshavsky A. The N-end rule pathway of protein degradation. Genes to Cells : Devoted to Molecular & Cellular Mechanisms. 2: 13-28. PMID 9112437 DOI: 10.1046/J.1365-2443.1997.1020301.X |
0.577 |
|
| 1997 |
Varshavsky A, Byrd C, Kwon YT. Recent studies of the n-end rule pathway Faseb Journal. 11: A995. |
0.363 |
|
| 1996 |
Grigoryev S, Stewart AE, Kwon YT, Arfin SM, Bradshaw RA, Jenkins NA, Copeland NG, Varshavsky A. A mouse amidase specific for N-terminal asparagine. The gene, the enzyme, and their function in the N-end rule pathway. The Journal of Biological Chemistry. 271: 28521-32. PMID 8910481 DOI: 10.1074/Jbc.271.45.28521 |
0.539 |
|
| 1996 |
Varshavsky A. The N-end rule: functions, mysteries, uses. Proceedings of the National Academy of Sciences of the United States of America. 93: 12142-9. PMID 8901547 DOI: 10.1073/Pnas.93.22.12142 |
0.524 |
|
| 1996 |
Ghislain M, Dohmen RJ, Levy F, Varshavsky A. Cdc48p interacts with Ufd3p, a WD repeat protein required for ubiquitin-mediated proteolysis in Saccharomyces cerevisiae. The Embo Journal. 15: 4884-99. PMID 8890162 DOI: 10.1002/J.1460-2075.1996.Tb00869.X |
0.553 |
|
| 1996 |
Lévy F, Johnsson N, Rümenapf T, Varshavsky A. Using ubiquitin to follow the metabolic fate of a protein. Proceedings of the National Academy of Sciences of the United States of America. 93: 4907-12. PMID 8643502 DOI: 10.1073/Pnas.93.10.4907 |
0.488 |
|
| 1995 |
Varshavsky A. The N-end rule. Cold Spring Harbor Symposia On Quantitative Biology. 60: 461-78. PMID 8824420 DOI: 10.1101/Sqb.1995.060.01.051 |
0.444 |
|
| 1995 |
Baker RT, Varshavsky A. Yeast N-terminal amidase. A new enzyme and component of the N-end rule pathway. The Journal of Biological Chemistry. 270: 12065-74. PMID 7744855 DOI: 10.1074/Jbc.270.20.12065 |
0.561 |
|
| 1995 |
Varshavsky A. Codominance and toxins: a path to drugs of nearly unlimited selectivity. Proceedings of the National Academy of Sciences of the United States of America. 92: 3663-7. PMID 7731961 DOI: 10.1073/Pnas.92.9.3663 |
0.327 |
|
| 1995 |
Johnston JA, Johnson ES, Waller PR, Varshavsky A. Methotrexate inhibits proteolysis of dihydrofolate reductase by the N-end rule pathway. The Journal of Biological Chemistry. 270: 8172-8. PMID 7713922 DOI: 10.1074/Jbc.270.14.8172 |
0.58 |
|
| 1995 |
Dohmen RJ, Stappen R, McGrath JP, Forrová H, Kolarov J, Goffeau A, Varshavsky A. An essential yeast gene encoding a homolog of ubiquitin-activating enzyme. The Journal of Biological Chemistry. 270: 18099-109. PMID 7629121 DOI: 10.1074/Jbc.270.30.18099 |
0.426 |
|
| 1995 |
Johnson ES, Ma PC, Ota IM, Varshavsky A. A proteolytic pathway that recognizes ubiquitin as a degradation signal. The Journal of Biological Chemistry. 270: 17442-56. PMID 7615550 DOI: 10.1074/Jbc.270.29.17442 |
0.562 |
|
| 1994 |
Dohmen RJ, Wu P, Varshavsky A. Heat-inducible degron: a method for constructing temperature-sensitive mutants. Science (New York, N.Y.). 263: 1273-6. PMID 8122109 DOI: 10.1126/Science.8122109 |
0.452 |
|
| 1994 |
Madura K, Varshavsky A. Degradation of G alpha by the N-end rule pathway. Science (New York, N.Y.). 265: 1454-8. PMID 8073290 DOI: 10.1126/Science.8073290 |
0.487 |
|
| 1994 |
Johnsson N, Varshavsky A. Ubiquitin-assisted dissection of protein transport across membranes. The Embo Journal. 13: 2686-98. PMID 8013467 DOI: 10.1002/J.1460-2075.1994.Tb06559.X |
0.42 |
|
| 1994 |
Johnsson N, Varshavsky A. Split ubiquitin as a sensor of protein interactions in vivo. Proceedings of the National Academy of Sciences of the United States of America. 91: 10340-4. PMID 7937952 DOI: 10.1073/Pnas.91.22.10340 |
0.469 |
|
| 1993 |
Madura K, Dohmen RJ, Varshavsky A. N-recognin/Ubc2 interactions in the N-end rule pathway. The Journal of Biological Chemistry. 268: 12046-54. PMID 8505328 |
0.455 |
|
| 1993 |
Shrader TE, Tobias JW, Varshavsky A. The N-end rule in Escherichia coli: cloning and analysis of the leucyl, phenylalanyl-tRNA-protein transferase gene aat. Journal of Bacteriology. 175: 4364-74. PMID 8331068 DOI: 10.1128/Jb.175.14.4364-4374.1993 |
0.535 |
|
| 1993 |
Ota IM, Varshavsky A. A yeast protein similar to bacterial two-component regulators. Science (New York, N.Y.). 262: 566-9. PMID 8211183 DOI: 10.1126/Science.8211183 |
0.431 |
|
| 1992 |
Ota IM, Varshavsky A. 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. 89: 2355-9. PMID 1549598 DOI: 10.1073/Pnas.89.6.2355 |
0.564 |
|
| 1992 |
Baker RT, Tobias JW, Varshavsky A. Ubiquitin-specific proteases of Saccharomyces cerevisiae. Cloning of UBP2 and UBP3, and functional analysis of the UBP gene family. The Journal of Biological Chemistry. 267: 23364-75. PMID 1429680 |
0.34 |
|
| 1992 |
Varshavsky A. The N-end rule. Cell. 69: 725-35. PMID 1317266 DOI: 10.1016/0092-8674(92)90285-K |
0.444 |
|
| 1992 |
Johnson ES, Bartel B, Seufert W, Varshavsky A. Ubiquitin as a degradation signal. The Embo Journal. 11: 497-505. PMID 1311250 DOI: 10.1002/J.1460-2075.1992.Tb05080.X |
0.692 |
|
| 1991 |
Tobias JW, Varshavsky A. Cloning and functional analysis of the ubiquitin-specific protease gene UBP1 of Saccharomyces cerevisiae. The Journal of Biological Chemistry. 266: 12021-8. PMID 2050695 |
0.365 |
|
| 1991 |
McGrath JP, Jentsch S, Varshavsky A. UBA 1: an essential yeast gene encoding ubiquitin-activating enzyme. The Embo Journal. 10: 227-36. PMID 1989885 DOI: 10.1002/J.1460-2075.1991.Tb07940.X |
0.673 |
|
| 1991 |
Varshavsky A. Naming a targeting signal. Cell. 64: 13-5. PMID 1986863 DOI: 10.1016/0092-8674(91)90202-A |
0.368 |
|
| 1991 |
Tobias JW, Shrader TE, Rocap G, Varshavsky A. The N-end rule in bacteria. Science (New York, N.Y.). 254: 1374-7. PMID 1962196 DOI: 10.1126/Science.1962196 |
0.559 |
|
| 1991 |
Baker RT, Varshavsky A. Inhibition of the N-end rule pathway in living cells. Proceedings of the National Academy of Sciences of the United States of America. 88: 1090-4. PMID 1899923 |
0.477 |
|
| 1991 |
Dohmen RJ, Madura K, Bartel B, Varshavsky A. 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. 88: 7351-5. PMID 1651502 DOI: 10.1073/Pnas.88.16.7351 |
0.753 |
|
| 1991 |
Hochstrasser M, Ellison MJ, Chau V, Varshavsky A. The short-lived MAT alpha 2 transcriptional regulator is ubiquitinated in vivo. Proceedings of the National Academy of Sciences of the United States of America. 88: 4606-10. PMID 1647011 DOI: 10.1073/Pnas.88.11.4606 |
0.709 |
|
| 1990 |
Bartel B, Wünning I, Varshavsky A. The recognition component of the N-end rule pathway. The Embo Journal. 9: 3179-89. PMID 2209542 DOI: 10.1002/J.1460-2075.1990.Tb07516.X |
0.768 |
|
| 1990 |
Balzi E, Choder M, Chen WN, Varshavsky A, Goffeau A. Cloning and functional analysis of the arginyl-tRNA-protein transferase gene ATE1 of Saccharomyces cerevisiae. The Journal of Biological Chemistry. 265: 7464-71. PMID 2185248 |
0.438 |
|
| 1990 |
Johnson ES, Gonda DK, Varshavsky A. cis-trans recognition and subunit-specific degradation of short-lived proteins. Nature. 346: 287-91. PMID 2165217 DOI: 10.1038/346287A0 |
0.57 |
|
| 1990 |
Hochstrasser M, Varshavsky A. In vivo degradation of a transcriptional regulator: the yeast alpha 2 repressor. Cell. 61: 697-708. PMID 2111732 DOI: 10.1016/0092-8674(90)90481-S |
0.428 |
|
| 1989 |
Winter E, Varshavsky A. A DNA binding protein that recognizes oligo(dA).oligo(dT) tracts. The Embo Journal. 8: 1867-77. PMID 2670564 DOI: 10.1002/J.1460-2075.1989.Tb03583.X |
0.425 |
|
| 1989 |
McGrath JP, Varshavsky A. The yeast STE6 gene encodes a homologue of the mammalian multidrug resistance P-glycoprotein. Nature. 340: 400-4. PMID 2569166 DOI: 10.1038/340400A0 |
0.352 |
|
| 1989 |
Varshavsky A, Bachmair A, Finley D, Gonda DK, Wünning I. Targeting of proteins for degradation. Biotechnology (Reading, Mass.). 13: 109-43. PMID 2553172 |
0.539 |
|
| 1989 |
Chau V, Tobias JW, Bachmair A, Marriott D, Ecker DJ, Gonda DK, Varshavsky A. A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein. Science (New York, N.Y.). 243: 1576-83. PMID 2538923 DOI: 10.1126/Science.2538923 |
0.372 |
|
| 1989 |
Finley D, Bartel B, Varshavsky A. The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis. Nature. 338: 394-401. PMID 2538753 DOI: 10.1038/338394A0 |
0.745 |
|
| 1989 |
Bachmair A, Varshavsky A. The degradation signal in a short-lived protein. Cell. 56: 1019-32. PMID 2538246 DOI: 10.1016/0092-8674(89)90635-1 |
0.475 |
|
| 1989 |
Gonda DK, Bachmair A, Wünning I, Tobias JW, Lane WS, Varshavsky A. Universality and structure of the N-end rule. The Journal of Biological Chemistry. 264: 16700-12. PMID 2506181 |
0.397 |
|
| 1988 |
Goebl MG, Yochem J, Jentsch S, McGrath JP, Varshavsky A, Byers B. The yeast cell cycle gene CDC34 encodes a ubiquitin-conjugating enzyme. Science (New York, N.Y.). 241: 1331-5. PMID 2842867 DOI: 10.1126/Science.2842867 |
0.64 |
|
| 1988 |
Bartel B, Varshavsky A. Hypersensitivity to heavy water: a new conditional phenotype. Cell. 52: 935-41. PMID 2832067 DOI: 10.1016/0092-8674(88)90435-7 |
0.586 |
|
| 1988 |
Solomon MJ, Larsen PL, Varshavsky A. Mapping protein-DNA interactions in vivo with formaldehyde: evidence that histone H4 is retained on a highly transcribed gene. Cell. 53: 937-47. PMID 2454748 DOI: 10.1016/S0092-8674(88)90469-2 |
0.578 |
|
| 1987 |
Varshavsky A, Bachmair A, Finley D. The N-end rule of selective protein turnover: mechanistic aspects and functional implications. Biochemical Society Transactions. 15: 815-6. PMID 3691950 DOI: 10.1042/Bst0150815 |
0.652 |
|
| 1987 |
Varshavsky A. Electrophoretic assay for DNA-binding proteins. Methods in Enzymology. 151: 551-65. PMID 3431454 DOI: 10.1016/S0076-6879(87)51044-8 |
0.337 |
|
| 1987 |
Jentsch S, McGrath JP, Varshavsky A. The yeast DNA repair gene RAD6 encodes a ubiquitin-conjugating enzyme. Nature. 329: 131-4. PMID 3306404 DOI: 10.1038/329131A0 |
0.641 |
|
| 1987 |
Ozkaynak E, Finley D, Solomon MJ, Varshavsky A. The yeast ubiquitin genes: a family of natural gene fusions. The Embo Journal. 6: 1429-39. PMID 3038523 DOI: 10.1002/J.1460-2075.1987.Tb02384.X |
0.711 |
|
| 1987 |
Finley D, Ozkaynak E, Varshavsky A. The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation, and other stresses. Cell. 48: 1035-46. PMID 3030556 DOI: 10.1016/0092-8674(87)90711-2 |
0.597 |
|
| 1987 |
Solomon MJ, Varshavsky A. A nuclease-hypersensitive region forms de novo after chromosome replication. Molecular and Cellular Biology. 7: 3822-5. PMID 2824998 DOI: 10.1128/Mcb.7.10.3822 |
0.494 |
|
| 1987 |
Varshavsky A, Bachmair A, Finley D. The N-End Rule of Selective Protein Turnover and Its Implications [Abstract Only] Philosophical Transactions of the Royal Society B. 317: 471-471. DOI: 10.1098/Rstb.1987.0073 |
0.707 |
|
| 1986 |
Solomon MJ, Strauss F, Varshavsky A. 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. 83: 1276-80. PMID 3456586 DOI: 10.1073/Pnas.83.5.1276 |
0.568 |
|
| 1986 |
Bachmair A, Finley D, Varshavsky A. In vivo half-life of a protein is a function of its amino-terminal residue. Science (New York, N.Y.). 234: 179-86. PMID 3018930 DOI: 10.1126/Science.3018930 |
0.609 |
|
| 1986 |
Swerdlow PS, Finley D, Varshavsky A. Enhancement of immunoblot sensitivity by heating of hydrated filters. Analytical Biochemistry. 156: 147-53. PMID 3017146 DOI: 10.1016/0003-2697(86)90166-1 |
0.48 |
|
| 1985 |
Ciccarelli RB, Solomon MJ, Varshavsky A, Lippard SJ. In vivo effects of cis- and trans-diamminedichloroplatinum(II) on SV40 chromosomes: differential repair, DNA-protein cross-linking, and inhibition of replication. Biochemistry. 24: 7533-40. PMID 3004558 DOI: 10.1021/Bi00347A005 |
0.529 |
|
| 1985 |
Solomon MJ, Varshavsky A. 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. 82: 6470-4. PMID 2995966 DOI: 10.1073/Pnas.82.19.6470 |
0.565 |
|
| 1985 |
Ciechanover A, Finley D, Varshavsky A. Mammalian cell cycle mutant defective in intracellular protein degradation and ubiquitin-protein conjugation. Progress in Clinical and Biological Research. 180: 17-31. PMID 2994083 |
0.605 |
|
| 1985 |
Finley D, Varshavsky A. The ubiquitin system: functions and mechanisms Trends in Biochemical Sciences. 10: 343-347. DOI: 10.1016/0968-0004(85)90108-2 |
0.623 |
|
| 1984 |
Strauss F, Varshavsky A. 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. 37: 889-901. PMID 6540146 DOI: 10.1016/0092-8674(84)90424-0 |
0.356 |
|
| 1984 |
Ciechanover A, Finley D, Varshavsky A. The ubiquitin-mediated proteolytic pathway and mechanisms of energy-dependent intracellular protein degradation. Journal of Cellular Biochemistry. 24: 27-53. PMID 6327743 DOI: 10.1002/Jcb.240240104 |
0.593 |
|
| 1984 |
Ciechanover A, Finley D, Varshavsky A. Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85. Cell. 37: 57-66. PMID 6327060 DOI: 10.1016/0092-8674(84)90300-3 |
0.611 |
|
| 1984 |
Finley D, Ciechanover A, Varshavsky A. Thermolability of ubiquitin-activating enzyme from the mammalian cell cycle mutant ts85. Cell. 37: 43-55. PMID 6327059 DOI: 10.1016/0092-8674(84)90299-X |
0.626 |
|
| 1984 |
Ozkaynak E, Finley D, Varshavsky A. The yeast ubiquitin gene: head-to-tail repeats encoding a polyubiquitin precursor protein. Nature. 312: 663-6. PMID 6095120 DOI: 10.1038/312663A0 |
0.648 |
|
| 1983 |
Varshavsky A. Do stalled replication forks synthesize a specific alarmone? Journal of Theoretical Biology. 105: 707-14. PMID 6672476 DOI: 10.1016/0022-5193(83)90228-X |
0.323 |
|
| 1983 |
Varshavsky A, Levinger L, Sundin O, Barsoum J, Ozkaynak E, Swerdlow P, Finley D. Cellular and SV40 chromatin: replication, segregation, ubiquitination, nuclease-hypersensitive sites, HMG-containing nucleosomes, and heterochromatin-specific protein. Cold Spring Harbor Symposia On Quantitative Biology. 47: 511-28. PMID 6305564 DOI: 10.1101/Sqb.1983.047.01.061 |
0.592 |
|
| 1983 |
Swerdlow PS, Varshavsky A. 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. 11: 387-401. PMID 6298725 DOI: 10.1093/Nar/11.2.387 |
0.34 |
|
| 1982 |
Levinger L, Varshavsky A. 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. 79: 7152-6. PMID 6818540 DOI: 10.1073/Pnas.79.23.7152 |
0.314 |
|
| 1982 |
Levinger L, Varshavsky A. Selective arrangement of ubiquitinated and D1 protein-containing nucleosomes within the Drosophila genome. Cell. 28: 375-85. PMID 6277512 DOI: 10.1016/0092-8674(82)90355-5 |
0.355 |
|
| 1981 |
Levinger L, Barsoum J, Varshavsky A. Two-dimensional hybridization mapping of nucleosomes. comparison of DNA and protein patterns. Journal of Molecular Biology. 146: 287-304. PMID 7265232 DOI: 10.1016/0022-2836(81)90389-2 |
0.325 |
|
| 1980 |
Levinger L, Varshavsky A. 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. 77: 3244-8. PMID 6932019 DOI: 10.1073/Pnas.77.6.3244 |
0.314 |
|
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