Year |
Citation |
Score |
2024 |
Breckel CA, Johnson ZM, Hickey CM, Hochstrasser M. Yeast 26S proteasome nuclear import is coupled to nucleus-specific degradation of the karyopherin adaptor protein Sts1. Scientific Reports. 14: 2048. PMID 38267508 DOI: 10.1038/s41598-024-52352-5 |
0.739 |
|
2023 |
Sultana S, Abdullah M, Li J, Hochstrasser M, Kachroo AH. Species-specific protein-protein interactions govern the humanization of the 20S proteasome in yeast. Genetics. PMID 37364278 DOI: 10.1093/genetics/iyad117 |
0.321 |
|
2023 |
Li Y, Tomko RJ, Hochstrasser M. Proteasomes: Isolation and Activity Assays. Current Protocols. 3: e717. PMID 37026813 DOI: 10.1002/cpz1.717 |
0.307 |
|
2023 |
Mehrtash AB, Hochstrasser M. Ectopic RING activity at the ER membrane differentially impacts ERAD protein quality control pathways. The Journal of Biological Chemistry. 102927. PMID 36682496 DOI: 10.1016/j.jbc.2023.102927 |
0.346 |
|
2022 |
Mehrtash AB, Hochstrasser M. Elements of the ERAD ubiquitin ligase Doa10 regulating sequential poly-ubiquitylation of its targets. Iscience. 25: 105351. PMID 36325070 DOI: 10.1016/j.isci.2022.105351 |
0.33 |
|
2022 |
Zhang M, Berk JM, Mehrtash AB, Kanyo J, Hochstrasser M. A versatile new tool derived from a bacterial deubiquitylase to detect and purify ubiquitylated substrates and their interacting proteins. Plos Biology. 20: e3001501. PMID 35771886 DOI: 10.1371/journal.pbio.3001501 |
0.352 |
|
2022 |
Li J, Hochstrasser M. Selective microautophagy of proteasomes is initiated by ESCRT-0 and is promoted by proteasome ubiquitylation. Journal of Cell Science. 135. PMID 35099016 DOI: 10.1242/jcs.259393 |
0.339 |
|
2021 |
Breckel CA, Hochstrasser M. Ubiquitin Ligase Redundancy and Nuclear-Cytoplasmic Localization in Yeast Protein Quality Control. Biomolecules. 11. PMID 34944465 DOI: 10.3390/biom11121821 |
0.454 |
|
2021 |
Cheng CL, Wong MK, Hochstrasser M. Yeast Nst1 is a Novel Component of P-bodies and is a Specific Suppressor of Proteasome Base Assembly Defects. Molecular Biology of the Cell. mbcE21040178. PMID 34347506 DOI: 10.1091/mbc.E21-04-0178 |
0.314 |
|
2021 |
Cheng CL, Wong MK, Li Y, Hochstrasser M. Conserved Proline Residues in the Coiled Coil-OB Domain Linkers of Rpt Proteins Facilitate Eukaryotic Proteasome Base Assembly. The Journal of Biological Chemistry. 100660. PMID 33862083 DOI: 10.1016/j.jbc.2021.100660 |
0.391 |
|
2021 |
Hickey CM, Breckel C, Zhang M, Theune WC, Hochstrasser M. Protein quality control degron-containing substrates are differentially targeted in the cytoplasm and nucleus by ubiquitin ligases. Genetics. 217: 1-19. PMID 33683364 DOI: 10.1093/genetics/iyaa031 |
0.732 |
|
2021 |
Klionsky DJ, Abdel-Aziz AK, Abdelfatah S, Abdellatif M, Abdoli A, Abel S, Abeliovich H, Abildgaard MH, Abudu YP, Acevedo-Arozena A, Adamopoulos IE, Adeli K, Adolph TE, Adornetto A, Aflaki E, ... ... Hochstrasser M, et al. Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition). Autophagy. 1-382. PMID 33634751 DOI: 10.1080/15548627.2020.1797280 |
0.565 |
|
2020 |
Chen H, Zhang M, Hochstrasser M. The Biochemistry of Cytoplasmic Incompatibility Caused by Endosymbiotic Bacteria Genes. 11: 852. PMID 32722516 DOI: 10.3390/Genes11080852 |
0.326 |
|
2020 |
Ryu HY, Ahn SH, Hochstrasser M. SUMO and cellular adaptive mechanisms. Experimental & Molecular Medicine. PMID 32591648 DOI: 10.1038/S12276-020-0457-2 |
0.398 |
|
2020 |
Berk JM, Lim C, Ronau JA, Chaudhuri A, Chen H, Beckmann JF, Loria JP, Xiong Y, Hochstrasser M. A deubiquitylase with an unusually high-affinity ubiquitin-binding domain from the scrub typhus pathogen Orientia tsutsugamushi. Nature Communications. 11: 2343. PMID 32393759 DOI: 10.1038/S41467-020-15985-4 |
0.794 |
|
2020 |
Li J, Hochstrasser M. Microautophagy regulates proteasome homeostasis. Current Genetics. PMID 32077993 DOI: 10.1007/S00294-020-01059-X |
0.481 |
|
2020 |
Budenholzer L, Breckel C, Hickey CM, Hochstrasser M. The Sts1 nuclear import adaptor uses a noncanonical bipartite NLS and is directly degraded by the proteasome. Journal of Cell Science. PMID 32041904 DOI: 10.1242/Jcs.236158 |
0.759 |
|
2020 |
Broshar CL, Buchanan B, Mehrtash A, Runnebohm A, Snow B, Scanameo L, Hochstrasser M, Rubenstein E. The relationship between ER stress and protein quality contarol at the translocon The Faseb Journal. 34: 1-1. DOI: 10.1096/Fasebj.2020.34.S1.00497 |
0.633 |
|
2019 |
Beckmann JF, Sharma GD, Mendez L, Chen H, Hochstrasser M. The cytoplasmic incompatibility enzyme CidB targets nuclear import and protamine-histone exchange factors. Elife. 8. PMID 31774393 DOI: 10.7554/Elife.50026 |
0.436 |
|
2019 |
Li J, Breker M, Graham M, Schuldiner M, Hochstrasser M. AMPK regulates ESCRT-dependent microautophagy of proteasomes concomitant with proteasome storage granule assembly during glucose starvation. Plos Genetics. 15: e1008387. PMID 31738769 DOI: 10.1371/Journal.Pgen.1008387 |
0.477 |
|
2019 |
Buchanan BW, Mehrtash AB, Broshar CL, Runnebohm AM, Snow BJ, Scanameo LN, Hochstrasser M, Rubenstein EM. Endoplasmic reticulum stress differentially inhibits endoplasmic reticulum and inner nuclear membrane protein quality control degradation pathways. The Journal of Biological Chemistry. PMID 31723032 DOI: 10.1074/Jbc.Ra119.010295 |
0.651 |
|
2019 |
Chen H, Ronau JA, Beckmann JF, Hochstrasser M. A nuclease and its binding partner provide a distinct mechanism for cytoplasmic incompatibility. Proceedings of the National Academy of Sciences of the United States of America. PMID 31615889 DOI: 10.1073/Pnas.1914571116 |
0.783 |
|
2019 |
Ryu HY, Su D, Wilson-Eisele NR, Zhao D, López-Giráldez F, Hochstrasser M. The Ulp2 SUMO protease promotes transcription elongation through regulation of histone sumoylation. The Embo Journal. e102003. PMID 31313851 DOI: 10.15252/Embj.2019102003 |
0.405 |
|
2019 |
Beckmann JF, Sharma GD, Mendez L, Chen H, Hochstrasser M. Author response: The Wolbachia cytoplasmic incompatibility enzyme CidB targets nuclear import and protamine-histone exchange factors Elife. DOI: 10.7554/Elife.50026.Sa2 |
0.314 |
|
2018 |
Ryu HY, López-Giráldez F, Knight J, Hwang SS, Renner C, Kreft SG, Hochstrasser M. Distinct adaptive mechanisms drive recovery from aneuploidy caused by loss of the Ulp2 SUMO protease. Nature Communications. 9: 5417. PMID 30575729 DOI: 10.1038/S41467-018-07836-0 |
0.37 |
|
2018 |
Sharpe LJ, Howe V, Scott NA, Luu W, Phan L, Berk JM, Hochstrasser M, Brown AJ. Cholesterol increases protein levels of the E3 ligase MARCH6, and thereby stimulates protein degradation. The Journal of Biological Chemistry. PMID 30545937 DOI: 10.1074/Jbc.Ra118.005069 |
0.397 |
|
2018 |
Kanaujiya J, Bastow E, Luxmi R, Hao Z, Zattas D, Hochstrasser M, Reichenberger EJ, Chen IP. Rapid degradation of progressive ankylosis protein (ANKH) in craniometaphyseal dysplasia. Scientific Reports. 8: 15710. PMID 30356088 DOI: 10.1038/S41598-018-34157-5 |
0.387 |
|
2018 |
Mehrtash AB, Hochstrasser M. Ubiquitin-dependent Protein Degradation at the Endoplasmic Reticulum and Nuclear Envelope. Seminars in Cell & Developmental Biology. PMID 30278225 DOI: 10.1016/J.Semcdb.2018.09.013 |
0.477 |
|
2018 |
Hickey CM, Xie Y, Hochstrasser M. DNA Binding by the MATα2 Transcription Factor Controls its Access to Alternative Ubiquitin-modification Pathways. Molecular Biology of the Cell. PMID 29298839 DOI: 10.1091/Mbc.E17-10-0589 |
0.765 |
|
2017 |
Budenholzer L, Cheng CL, Li Y, Hochstrasser M. Proteasome Structure and Assembly. Journal of Molecular Biology. PMID 28583440 DOI: 10.1016/J.Jmb.2017.05.027 |
0.441 |
|
2017 |
Ronau JA, Hochstrasser M. Novel ubiquitin cleavage: The DUB blade goes snicker-snack. Cell Research. PMID 28574056 DOI: 10.1038/Cr.2017.80 |
0.811 |
|
2017 |
Beckmann JF, Ronau JA, Hochstrasser M. A Wolbachia deubiquitylating enzyme induces cytoplasmic incompatibility. Nature Microbiology. 2: 17007. PMID 28248294 DOI: 10.1038/Nmicrobiol.2017.7 |
0.778 |
|
2016 |
Hochstrasser M. Gyre and gimble in the proteasome. Proceedings of the National Academy of Sciences of the United States of America. 113: 12896-12898. PMID 27810957 DOI: 10.1073/Pnas.1616055113 |
0.468 |
|
2016 |
Wilson NR, Hochstrasser M. The Regulation of Chromatin by Dynamic SUMO Modifications. Methods in Molecular Biology (Clifton, N.J.). 1475: 23-38. PMID 27631795 DOI: 10.1007/978-1-4939-6358-4_2 |
0.408 |
|
2016 |
Ryu HY, Wilson NR, Mehta S, Hwang SS, Hochstrasser M. Loss of the SUMO protease Ulp2 triggers a specific multichromosome aneuploidy. Genes & Development. PMID 27585592 DOI: 10.1101/Gad.282194.116 |
0.38 |
|
2016 |
Berk JM, Hochstrasser M. Protein Modification: Bacterial Effectors Rewrite the Rules of Ubiquitylation. Current Biology : Cb. 26: R539-R542. PMID 27404243 DOI: 10.1016/J.Cub.2016.05.032 |
0.379 |
|
2016 |
Zattas D, Berk JM, Kreft SG, Hochstrasser M. A Conserved C-terminal Element in the Yeast Doa10 and Human MARCH6 Ubiquitin Ligases Required for Selective Substrate Degradation. The Journal of Biological Chemistry. 291: 12105-18. PMID 27068744 DOI: 10.1074/Jbc.M116.726877 |
0.5 |
|
2016 |
Hu R, Hochstrasser M. Recent progress in ubiquitin and ubiquitin-like protein (Ubl) signaling. Cell Research. 26: 389-90. PMID 27033807 DOI: 10.1038/Cr.2016.43 |
0.444 |
|
2016 |
Ronau JA, Beckmann JF, Hochstrasser M. Substrate specificity of the ubiquitin and Ubl proteases. Cell Research. PMID 27012468 DOI: 10.1038/Cr.2016.38 |
0.82 |
|
2016 |
Padmanabhan A, Vuong SA, Hochstrasser M. Assembly of an Evolutionarily Conserved Alternative Proteasome Isoform in Human Cells. Cell Reports. 14: 2962-74. PMID 26997268 DOI: 10.1016/J.Celrep.2016.02.068 |
0.777 |
|
2016 |
Huber EM, Heinemeyer W, Li X, Arendt CS, Hochstrasser M, Groll M. A unified mechanism for proteolysis and autocatalytic activation in the 20S proteasome. Nature Communications. 7: 10900. PMID 26964885 DOI: 10.1038/Ncomms10900 |
0.787 |
|
2016 |
Gillies J, Hickey CM, Su D, Wu Z, Peng J, Hochstrasser M. SUMO Pathway Modulation of Regulatory Protein Binding at the Ribosomal DNA Locus in Saccharomyces cerevisiae. Genetics. PMID 26837752 DOI: 10.1534/Genetics.116.187252 |
0.756 |
|
2015 |
Li X, Li Y, Arendt CS, Hochstrasser M. Distinct Elements in the Proteasomal β5 Subunit Propeptide Required for Autocatalytic Processing and Proteasome Assembly. The Journal of Biological Chemistry. PMID 26627836 DOI: 10.1074/Jbc.M115.677047 |
0.771 |
|
2015 |
Tomko RJ, Taylor DW, Chen ZA, Wang HW, Rappsilber J, Hochstrasser M. A Single α Helix Drives Extensive Remodeling of the Proteasome Lid and Completion of Regulatory Particle Assembly. Cell. 163: 432-44. PMID 26451487 DOI: 10.1016/J.Cell.2015.09.022 |
0.385 |
|
2015 |
Hickey CM, Hochstrasser M. STUbL-mediated degradation of the transcription factor MATα2 requires degradation elements that coincide with corepressor binding sites. Molecular Biology of the Cell. 26: 3401-12. PMID 26246605 DOI: 10.1091/Mbc.E15-06-0436 |
0.661 |
|
2015 |
Li Y, Tomko RJ, Hochstrasser M. Proteasomes: Isolation and Activity Assays. Current Protocols in Cell Biology. 67: 3.43.1-20. PMID 26061243 DOI: 10.1002/0471143030.Cb0343S67 |
0.483 |
|
2015 |
Zattas D, Hochstrasser M. Ubiquitin-dependent protein degradation at the yeast endoplasmic reticulum and nuclear envelope. Critical Reviews in Biochemistry and Molecular Biology. 50: 1-17. PMID 25231236 DOI: 10.3109/10409238.2014.959889 |
0.474 |
|
2014 |
Kang H, Bradley MJ, Cao W, Zhou K, Grintsevich EE, Michelot A, Sindelar CV, Hochstrasser M, De La Cruz EM. Site-specific cation release drives actin filament severing by vertebrate cofilin. Proceedings of the National Academy of Sciences of the United States of America. 111: 17821-6. PMID 25468977 DOI: 10.1073/Pnas.1413397111 |
0.323 |
|
2014 |
Tomko RJ, Hochstrasser M. The intrinsically disordered Sem1 protein functions as a molecular tether during proteasome lid biogenesis. Molecular Cell. 53: 433-43. PMID 24412063 DOI: 10.1016/J.Molcel.2013.12.009 |
0.453 |
|
2014 |
Kunjappu MJ, Hochstrasser M. Assembly of the 20S proteasome. Biochimica Et Biophysica Acta. 1843: 2-12. PMID 23507199 DOI: 10.1016/J.Bbamcr.2013.03.008 |
0.806 |
|
2013 |
Sá-Moura B, Funakoshi M, Tomko RJ, Dohmen RJ, Wu Z, Peng J, Hochstrasser M. A conserved protein with AN1 zinc finger and ubiquitin-like domains modulates Cdc48 (p97) function in the ubiquitin-proteasome pathway. The Journal of Biological Chemistry. 288: 33682-96. PMID 24121501 DOI: 10.1074/Jbc.M113.521088 |
0.546 |
|
2013 |
Tomko RJ, Hochstrasser M. Molecular architecture and assembly of the eukaryotic proteasome. Annual Review of Biochemistry. 82: 415-45. PMID 23495936 DOI: 10.1146/Annurev-Biochem-060410-150257 |
0.459 |
|
2013 |
Zattas D, Adle DJ, Rubenstein EM, Hochstrasser M. N-terminal acetylation of the yeast Derlin Der1 is essential for Hrd1 ubiquitin-ligase activity toward luminal ER substrates. Molecular Biology of the Cell. 24: 890-900. PMID 23363603 DOI: 10.1091/Mbc.E12-11-0838 |
0.724 |
|
2012 |
Hickey CM, Wilson NR, Hochstrasser M. Function and regulation of SUMO proteases. Nature Reviews. Molecular Cell Biology. 13: 755-66. PMID 23175280 DOI: 10.1038/Nrm3478 |
0.762 |
|
2012 |
Stuerner E, Kuraku S, Hochstrasser M, Kreft SG. Split-Doa10: a naturally split polytopic eukaryotic membrane protein generated by fission of a nuclear gene. Plos One. 7: e45194. PMID 23071509 DOI: 10.1371/Journal.Pone.0045194 |
0.421 |
|
2012 |
Rubenstein EM, Kreft SG, Greenblatt W, Swanson R, Hochstrasser M. Aberrant substrate engagement of the ER translocon triggers degradation by the Hrd1 ubiquitin ligase. The Journal of Cell Biology. 197: 761-73. PMID 22689655 DOI: 10.1083/Jcb.201203061 |
0.802 |
|
2012 |
Hochstrasser M, Funakoshi M. Disulfide Engineering to Map Subunit Interactions in the Proteasome and Other Macromolecular Complexes Methods of Molecular Biology. 832: 349-362. PMID 22350897 DOI: 10.1007/978-1-61779-474-2_24 |
0.426 |
|
2012 |
Felberbaum R, Wilson NR, Cheng D, Peng J, Hochstrasser M. Desumoylation of the endoplasmic reticulum membrane VAP family protein Scs2 by Ulp1 and SUMO regulation of the inositol synthesis pathway. Molecular and Cellular Biology. 32: 64-75. PMID 22025676 DOI: 10.1128/Mcb.05878-11 |
0.831 |
|
2011 |
Tomko RJ, Hochstrasser M. Incorporation of the Rpn12 subunit couples completion of proteasome regulatory particle lid assembly to lid-base joining. Molecular Cell. 44: 907-17. PMID 22195964 DOI: 10.1016/J.Molcel.2011.11.020 |
0.344 |
|
2011 |
Laney JD, Hochstrasser M. Analysis of protein ubiquitination. Current Protocols in Protein Science / Editorial Board, John E. Coligan ... [Et Al.]. Unit14.5. PMID 22045559 DOI: 10.1002/0471140864.Ps1405S66 |
0.485 |
|
2011 |
Kusmierczyk AR, Kunjappu MJ, Kim RY, Hochstrasser M. A conserved 20S proteasome assembly factor requires a C-terminal HbYX motif for proteasomal precursor binding. Nature Structural & Molecular Biology. 18: 622-9. PMID 21499243 DOI: 10.1038/Nsmb.2027 |
0.808 |
|
2011 |
Kreft SG, Hochstrasser M. An unusual transmembrane helix in the endoplasmic reticulum ubiquitin ligase Doa10 modulates degradation of its cognate E2 enzyme Journal of Biological Chemistry. 286: 20163-20174. PMID 21467040 DOI: 10.1074/Jbc.M110.196360 |
0.482 |
|
2011 |
Tomko RJ, Hochstrasser M. Order of the proteasomal ATPases and eukaryotic proteasome assembly. Cell Biochemistry and Biophysics. 60: 13-20. PMID 21461838 DOI: 10.1007/S12013-011-9178-4 |
0.446 |
|
2010 |
Rubenstein EM, Hochstrasser M. Redundancy and variation in the ubiquitin-mediated proteolytic targeting of a transcription factor. Cell Cycle (Georgetown, Tex.). 9: 4282-5. PMID 20980825 DOI: 10.4161/Cc.9.21.13741 |
0.725 |
|
2010 |
Su D, Hochstrasser M. A WLM protein with SUMO-directed protease activity Molecular and Cellular Biology. 30: 3734-3736. PMID 20566698 DOI: 10.1128/Mcb.00673-10 |
0.524 |
|
2010 |
Tomko RJ, Funakoshi M, Schneider K, Wang J, Hochstrasser M. Heterohexameric ring arrangement of the eukaryotic proteasomal ATPases: implications for proteasome structure and assembly. Molecular Cell. 38: 393-403. PMID 20471945 DOI: 10.1016/J.Molcel.2010.02.035 |
0.39 |
|
2010 |
Xie Y, Rubenstein EM, Matt T, Hochstrasser M. SUMO-independent in vivo activity of a SUMO-targeted ubiquitin ligase toward a short-lived transcription factor. Genes & Development. 24: 893-903. PMID 20388728 DOI: 10.1101/Gad.1906510 |
0.741 |
|
2010 |
Cortajarena AL, Liu TY, Hochstrasser M, Regan L. Designed proteins to modulate cellular networks. Acs Chemical Biology. 5: 545-52. PMID 20020775 DOI: 10.1021/Cb9002464 |
0.402 |
|
2009 |
Osmulski PA, Hochstrasser M, Gaczynska M. A Tetrahedral Transition State at the Active Sites of the 20S Proteasome Is Coupled to Opening of the α-Ring Channel Structure. 17: 1137-1147. PMID 19679091 DOI: 10.1016/J.Str.2009.06.011 |
0.343 |
|
2009 |
Funakoshi M, Tomko RJ, Kobayashi H, Hochstrasser M. Multiple assembly chaperones govern biogenesis of the proteasome regulatory particle base. Cell. 137: 887-99. PMID 19446322 DOI: 10.1016/J.Cell.2009.04.061 |
0.427 |
|
2009 |
Xu P, Duong DM, Seyfried NT, Cheng D, Xie Y, Robert J, Rush J, Hochstrasser M, Finley D, Peng J. Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation. Cell. 137: 133-45. PMID 19345192 DOI: 10.1016/J.Cell.2009.01.041 |
0.614 |
|
2009 |
Hochstrasser M. Origin and function of ubiquitin-like proteins Nature. 458: 422-429. PMID 19325621 DOI: 10.1038/Nature07958 |
0.502 |
|
2009 |
Cook CE, Hochstrasser M, Kerscher O. The SUMO-targeted ubiquitin ligase subunit Slx5 resides in nuclear foci and at sites of DNA breaks. Cell Cycle (Georgetown, Tex.). 8: 1080-9. PMID 19270524 DOI: 10.4161/Cc.8.7.8123 |
0.432 |
|
2009 |
Hochstrasser M. Introduction to Intracellular Protein Degradation Chemical Reviews. 109: 1479-1480. PMID 19253968 DOI: 10.1021/Cr900054T |
0.456 |
|
2009 |
Funakoshi M, Hochstrasser M. Small epitope‐linker modules for PCR‐based C‐terminal tagging in Saccharomyces cerevisiae Yeast. 26: 185-192. PMID 19243080 DOI: 10.1002/Yea.1658 |
0.357 |
|
2009 |
Kroetz MB, Su D, Hochstrasser M. Essential role of nuclear localization for yeast Ulp2 SUMO protease function. Molecular Biology of the Cell. 20: 2196-206. PMID 19225149 DOI: 10.1091/Mbc.E08-10-1090 |
0.825 |
|
2009 |
Kroetz MB, Hochstrasser M. Identification of SUMO-interacting proteins by yeast two-hybrid analysis. Methods in Molecular Biology (Clifton, N.J.). 497: 107-20. PMID 19107413 DOI: 10.1007/978-1-59745-566-4_7 |
0.807 |
|
2008 |
Wang L, Dong H, Soroka CJ, Wei N, Boyer JL, Hochstrasser M. Degradation of the bile salt export pump at endoplasmic reticulum in progressive familial intrahepatic cholestasis type II. Hepatology (Baltimore, Md.). 48: 1558-69. PMID 18798335 DOI: 10.1002/Hep.22499 |
0.353 |
|
2008 |
Kusmierczyk AR, Hochstrasser M. Some assembly required: dedicated chaperones in eukaryotic proteasome biogenesis. Biological Chemistry. 389: 1143-1151. PMID 18713001 DOI: 10.1515/Bc.2008.130 |
0.477 |
|
2008 |
Ravid T, Hochstrasser M. Diversity of degradation signals in the ubiquitin–proteasome system Nature Reviews Molecular Cell Biology. 9: 679-689. PMID 18698327 DOI: 10.1038/Nrm2468 |
0.488 |
|
2008 |
Kusmierczyk AR, Kunjappu MJ, Funakoshi M, Hochstrasser M. A multimeric assembly factor controls the formation of alternative 20S proteasomes. Nature Structural & Molecular Biology. 15: 237-44. PMID 18278055 DOI: 10.1038/Nsmb.1389 |
0.813 |
|
2008 |
Felberbaum R, Hochstrasser M. Ulp2 and the DNA damage response: Desumoylation enables safe passage through mitosis Cell Cycle. 7: 52-56. PMID 18196960 DOI: 10.4161/Cc.7.1.5218 |
0.774 |
|
2007 |
Xie Y, Kerscher O, Kroetz MB, McConchie HF, Sung P, Hochstrasser M. The yeast Hex3.Slx8 heterodimer is a ubiquitin ligase stimulated by substrate sumoylation. The Journal of Biological Chemistry. 282: 34176-84. PMID 17848550 DOI: 10.1074/Jbc.M706025200 |
0.839 |
|
2007 |
Lewis A, Felberbaum R, Hochstrasser M. A nuclear envelope protein linking nuclear pore basket assembly, SUMO protease regulation, and mRNA surveillance. Journal of Cell Biology. 178: 813-827. PMID 17724121 DOI: 10.1083/Jcb.200702154 |
0.808 |
|
2007 |
Schwartz DC, Felberbaum R, Hochstrasser M. The Ulp2 SUMO protease is required for cell division following termination of the DNA damage checkpoint. Molecular and Cellular Biology. 27: 6948-61. PMID 17664284 DOI: 10.1128/Mcb.00774-07 |
0.776 |
|
2007 |
Hochstrasser M. Ubiquitin ligation without a ligase. Developmental Cell. 13: 4-6. PMID 17609103 DOI: 10.1016/J.Devcel.2007.06.003 |
0.349 |
|
2007 |
Li X, Kusmierczyk AR, Wong P, Emili A, Hochstrasser M. β‐Subunit appendages promote 20S proteasome assembly by overcoming an Ump1‐dependent checkpoint The Embo Journal. 26: 2339-2349. PMID 17431397 DOI: 10.1038/Sj.Emboj.7601681 |
0.372 |
|
2007 |
Ravid T, Hochstrasser M. Autoregulation of an E2 enzyme by ubiquitin-chain assembly on its catalytic residue Nature Cell Biology. 9: 422-427. PMID 17310239 DOI: 10.1038/Ncb1558 |
0.45 |
|
2006 |
Amerik A, Sindhi N, Hochstrasser M. A conserved late endosome-targeting signal required for Doa4 deubiquitylating enzyme function. Journal of Cell Biology. 175: 825-835. PMID 17145966 DOI: 10.1083/Jcb.200605134 |
0.45 |
|
2006 |
Deng M, Hochstrasser M. Spatially regulated ubiquitin ligation by an ER/nuclear membrane ligase Nature. 443: 827-831. PMID 17051211 DOI: 10.1038/Nature05170 |
0.414 |
|
2006 |
Arteaga MF, Wang L, Ravid T, Hochstrasser M, Canessa CM. An amphipathic helix targets serum and glucocorticoid-induced kinase 1 to the endoplasmic reticulum-associated ubiquitin-conjugation machinery. Proceedings of the National Academy of Sciences of the United States of America. 103: 11178-83. PMID 16847254 DOI: 10.1073/Pnas.0604816103 |
0.477 |
|
2006 |
Kerscher O, Felberbaum R, Hochstrasser M. Modification of proteins by ubiquitin and ubiquitin-like proteins. Annual Review of Cell and Developmental Biology. 22: 159-80. PMID 16753028 DOI: 10.1146/Annurev.Cellbio.22.010605.093503 |
0.834 |
|
2006 |
Ravid T, Kreft SG, Hochstrasser M. Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathways. The Embo Journal. 25: 533-543. PMID 16437165 DOI: 10.1038/Sj.Emboj.7600946 |
0.505 |
|
2006 |
Hochstrasser M. Lingering mysteries of ubiquitin-chain assembly. Cell. 124: 27-34. PMID 16413479 DOI: 10.1016/J.Cell.2005.12.025 |
0.395 |
|
2006 |
Kreft SG, Wang L, Hochstrasser M. Membrane topology of the yeast endoplasmic reticulum-localized ubiquitin ligase Doa10 and comparison with its human ortholog TEB4 (MARCH-VI) Journal of Biological Chemistry. 281: 4646-4653. PMID 16373356 DOI: 10.1074/Jbc.M512215200 |
0.46 |
|
2006 |
Laney JD, Mobley EF, Hochstrasser M. The short-lived Matalpha2 transcriptional repressor is protected from degradation in vivo by interactions with its corepressors Tup1 and Ssn6. Molecular and Cellular Biology. 26: 371-80. PMID 16354707 DOI: 10.1128/Mcb.26.1.371-380.2006 |
0.405 |
|
2005 |
Huang S, Zhou H, Katzmann D, Hochstrasser M, Atanasova E, Zhang Z. Rtt106p is a histone chaperone involved in heterochromatin-mediated silencing. Proceedings of the National Academy of Sciences of the United States of America. 102: 13410-5. PMID 16157874 DOI: 10.1073/Pnas.0506176102 |
0.336 |
|
2005 |
Hannich JT, Lewis A, Kroetz MB, Li SJ, Heide H, Emili A, Hochstrasser M. Defining the SUMO-modified proteome by multiple approaches in Saccharomyces cerevisiae. The Journal of Biological Chemistry. 280: 4102-10. PMID 15590687 DOI: 10.1074/Jbc.M413209200 |
0.827 |
|
2004 |
Funakoshi M, Li X, Velichutina I, Hochstrasser M, Kobayashi H. Sem1, the yeast ortholog of a human BRCA2-binding protein, is a component of the proteasome regulatory particle that enhances proteasome stability. Journal of Cell Science. 117: 6447-54. PMID 15572408 DOI: 10.1242/Jcs.01575 |
0.486 |
|
2004 |
Amerik AY, Hochstrasser M. Mechanism and function of deubiquitinating enzymes. Biochimica Et Biophysica Acta. 1695: 189-207. PMID 15571815 DOI: 10.1016/J.Bbamcr.2004.10.003 |
0.51 |
|
2004 |
Laney JD, Hochstrasser M. Ubiquitin-dependent control of development in Saccharomyces cerevisiae. Current Opinion in Microbiology. 7: 647-54. PMID 15556038 DOI: 10.1016/J.Mib.2004.10.016 |
0.348 |
|
2004 |
Baumeister W, Bachmair A, Chau V, Cohen R, Coffino P, Demartino G, Deshaies R, Dohmen J, Emr S, Finley D, Hampton R, Hill C, Hochstrasser M, Huber R, Jackson P, et al. Varshavsky's contributions. Science (New York, N.Y.). 306: 1290-2. PMID 15550643 DOI: 10.1126/Science.306.5700.1290 |
0.705 |
|
2004 |
Ravid T, Hochstrasser M. NF-κB signaling: Flipping the Switch with Polyubiquitin Chains Current Biology. 14. PMID 15498483 DOI: 10.1016/J.Cub.2004.09.074 |
0.358 |
|
2004 |
Huyer G, Piluek WF, Fansler Z, Kreft SG, Hochstrasser M, Brodsky JL, Michaelis S. Distinct machinery is required in Saccharomyces cerevisiae for the endoplasmic reticulum-associated degradation of a multispanning membrane protein and a soluble luminal protein. The Journal of Biological Chemistry. 279: 38369-78. PMID 15252059 DOI: 10.1074/Jbc.M402468200 |
0.496 |
|
2004 |
Hochstrasser M. Ubiquitin signalling: what's in a chain? Nature Cell Biology. 6: 571-572. PMID 15232583 DOI: 10.1038/Ncb0704-571 |
0.437 |
|
2004 |
Velichutina I, Connerly PL, Arendt CS, Li X, Hochstrasser M. Plasticity in eucaryotic 20S proteasome ring assembly revealed by a subunit deletion in yeast. The Embo Journal. 23: 500-10. PMID 14739934 DOI: 10.1038/Sj.Emboj.7600059 |
0.79 |
|
2003 |
Laney JD, Hochstrasser M. Ubiquitin-dependent degradation of the yeast Mat(alpha)2 repressor enables a switch in developmental state. Genes & Development. 17: 2259-70. PMID 12952895 DOI: 10.1101/Gad.1115703 |
0.398 |
|
2003 |
Schwartz DC, Hochstrasser M. A superfamily of protein tags: ubiquitin, SUMO and related modifiers. Trends in Biochemical Sciences. 28: 321-8. PMID 12826404 DOI: 10.1016/S0968-0004(03)00113-0 |
0.504 |
|
2003 |
Li S, Hochstrasser M. The Ulp1 SUMO isopeptidase distinct domains required for viability, nuclear envelope localization, and substrate specificity Journal of Cell Biology. 160: 1069-1082. PMID 12654900 DOI: 10.1083/Jcb.200212052 |
0.479 |
|
2002 |
Laney JD, Hochstrasser M. Analysis of protein ubiquitination. Current Protocols in Protein Science / Editorial Board, John E. Coligan ... [Et Al.]. Unit 14.5. PMID 18429222 DOI: 10.1002/0471140864.Ps1405S29 |
0.513 |
|
2002 |
Hochstrasser M. New Proteases in a Ubiquitin Stew Science. 298: 549-552. PMID 12386321 DOI: 10.1126/Science.1078097 |
0.486 |
|
2002 |
Laney JD, Hochstrasser M. Assaying protein ubiquitination in Saccharomyces cerevisiae. Methods in Enzymology. 351: 248-57. PMID 12073348 DOI: 10.1016/S0076-6879(02)51851-6 |
0.519 |
|
2002 |
Hochstrasser M. New structural clues to substrate specificity in the "ubiquitin system". Molecular Cell. 9: 453-454. PMID 11931752 DOI: 10.1016/S1097-2765(02)00486-0 |
0.468 |
|
2001 |
Swanson R, Locher M, Hochstrasser M. A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation. Genes & Development. 15: 2660-74. PMID 11641273 DOI: 10.1101/Gad.933301 |
0.714 |
|
2001 |
Hochstrasser M. SP-RING for SUMO: New Functions Bloom for a Ubiquitin-like Protein Cell. 107: 5-8. PMID 11595179 DOI: 10.1016/S0092-8674(01)00519-0 |
0.444 |
|
2001 |
Hochstrasser M, Wang J. Unraveling the means to the end in ATP-dependent proteases. Nature Structural & Molecular Biology. 8: 294-296. PMID 11276243 DOI: 10.1038/86153 |
0.403 |
|
2000 |
Amerik AY, Li S, Hochstrasser M. Analysis of the deubiquitinating enzymes of the yeast Saccharomyces cerevisiae. Biological Chemistry. 381: 981-992. PMID 11076031 DOI: 10.1515/Bc.2000.121 |
0.459 |
|
2000 |
Amerik AY, Nowak J, Swaminathan S, Hochstrasser M. The Doa4 Deubiquitinating Enzyme Is Functionally Linked to the Vacuolar Protein-sorting and Endocytic Pathways Molecular Biology of the Cell. 11: 3365-3380. PMID 11029042 DOI: 10.1091/Mbc.11.10.3365 |
0.694 |
|
2000 |
Hochstrasser M. Biochemistry. All in the ubiquitin family. Science. 289: 563-564. PMID 10939967 DOI: 10.1126/Science.289.5479.563 |
0.438 |
|
2000 |
Hochstrasser M. Evolution and function of ubiquitin-like protein-conjugation systems Nature Cell Biology. 2. PMID 10934491 DOI: 10.1038/35019643 |
0.507 |
|
2000 |
Swanson R, Hochstrasser M. A viable ubiquitin-activating enzyme mutant for evaluating ubiquitin system function in Saccharomyces cerevisiae. Febs Letters. 477: 193-198. PMID 10908719 DOI: 10.1016/S0014-5793(00)01802-0 |
0.715 |
|
2000 |
Li S, Hochstrasser M. The Yeast ULP2 (SMT4) Gene Encodes a Novel Protease Specific for the Ubiquitin-Like Smt3 Protein Molecular and Cellular Biology. 20: 2367-2377. PMID 10713161 DOI: 10.1128/Mcb.20.7.2367-2377.2000 |
0.578 |
|
1999 |
Hochstrasser M, Johnson PR, Arendt CS, Amerik AYu, Swaminathan S, Swanson R, Li SJ, Laney J, Pals-Rylaarsdam R, Nowak J, Connerly PL. The Saccharomyces cerevisiae ubiquitin-proteasome system. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 354: 1513-22. PMID 10582237 DOI: 10.1098/Rstb.1999.0495 |
0.808 |
|
1999 |
Swaminathan S, Amerik AY, Hochstrasser M. The Doa4 Deubiquitinating Enzyme Is Required for Ubiquitin Homeostasis in Yeast Molecular Biology of the Cell. 10: 2583-2594. PMID 10436014 DOI: 10.1091/Mbc.10.8.2583 |
0.698 |
|
1999 |
Arendt CS, Hochstrasser M. Eukaryotic 20S proteasome catalytic subunit propeptides prevent active site inactivation by N-terminal acetylation and promote particle assembly. The Embo Journal. 18: 3575-85. PMID 10393174 DOI: 10.1093/Emboj/18.13.3575 |
0.811 |
|
1999 |
Fu H, Girod PA, Doelling JH, Van Nocker S, Hochstrasser M, Finley D, Vierstra RD. Structure and functional analyses of the 26S proteasome subunits from plants Plant 26S proteasome Molecular Biology Reports. 26: 137-146. PMID 10363660 DOI: 10.1023/A:1006926322501 |
0.615 |
|
1999 |
Laney JD, Hochstrasser M. Substrate targeting in the ubiquitin system Cell. 97: 427-430. PMID 10338206 DOI: 10.1016/S0092-8674(00)80752-7 |
0.5 |
|
1999 |
Li S, Hochstrasser M. A new protease required for cell-cycle progression in yeast Nature. 398: 246-251. PMID 10094048 DOI: 10.1038/18457 |
0.521 |
|
1999 |
Papa FR, Amerik AY, Hochstrasser M. Interaction of the Doa4 deubiquitinating enzyme with the yeast 26S proteasome Molecular Biology of the Cell. 10: 741-756. PMID 10069815 DOI: 10.1091/Mbc.10.3.741 |
0.659 |
|
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 |
0.731 |
|
1998 |
Johnson PR, Swanson R, Rakhilina L, Hochstrasser M. Degradation signal masking by heterodimerization of MATα2 and MATa1 blocks their mutual destruction by the ubiquitin-proteasome pathway Cell. 94: 217-227. PMID 9695950 DOI: 10.1016/S0092-8674(00)81421-X |
0.662 |
|
1998 |
Hansen-Hagge TE, Janssen JWG, Hameister H, Papa FR, Zechner U, Seriu T, Jauch A, Becke D, Hochstrasser M, Bartram CR. An evolutionarily conserved gene on human chromosome 5q33-q34, UBH1, encodes a novel deubiquitinating enzyme Genomics. 49: 411-418. PMID 9615226 DOI: 10.1006/Geno.1998.5275 |
0.578 |
|
1998 |
Hochstrasser M. There's the rub : a novel ubiquitin-like modification linked to cell cycle regulation Genes & Development. 12: 901-907. PMID 9531529 DOI: 10.1101/Gad.12.7.901 |
0.534 |
|
1997 |
Johnson PR, Hochstrasser M. SUMO-1: Ubiquitin gains weight. Trends in Cell Biology. 7: 408-13. PMID 17708991 DOI: 10.1016/S0962-8924(97)01132-X |
0.528 |
|
1997 |
Amerik AY, Swaminathan S, Krantz BA, Wilkinson KD, Hochstrasser M. In vivo disassembly of free polyubiquitin chains by yeast Ubp14 modulates rates of protein degradation by the proteasome Embo Journal. 16: 4826-4838. PMID 9305625 DOI: 10.1093/Emboj/16.16.4826 |
0.671 |
|
1997 |
Arendt CS, Hochstrasser M. Identification of the yeast 20S proteasome catalytic centers and subunit interactions required for active-site formation. Proceedings of the National Academy of Sciences of the United States of America. 94: 7156-61. PMID 9207060 DOI: 10.1073/Pnas.94.14.7156 |
0.795 |
|
1996 |
Hochstrasser M. Ubiquitin-Dependent Protein Degradation Annual Review of Genetics. 30: 405-439. PMID 8982460 DOI: 10.1146/Annurev.Genet.30.1.405 |
0.529 |
|
1996 |
Chen P, Hochstrasser M. Autocatalytic subunit processing couples active site formation in the 20S proteasome to completion of assembly. Cell. 86: 961-72. PMID 8808631 DOI: 10.1016/S0092-8674(00)80171-3 |
0.534 |
|
1996 |
Zhu Y, Carroll M, Papa FR, Hochstrasser M, D'Andrea AD. DUB-1, a deubiquitinating enzyme with growth-suppressing activity Proceedings of the National Academy of Sciences of the United States of America. 93: 3275-3279. PMID 8622927 DOI: 10.1073/Pnas.93.8.3275 |
0.625 |
|
1996 |
Hochstrasser M. Protein Degradation or Regulation: Ub the Judge Cell. 84: 813-815. PMID 8601303 DOI: 10.1016/S0092-8674(00)81058-2 |
0.506 |
|
1995 |
Hochstrasser M, Papa FR, Chen P, Swaminathan S, Johnson P, Stillman L, Amerik AY, Li SJ. The DOA pathway: Studies on the functions and mechanisms of ubiquitin- dependent protein degradation in the yeast Saccharomyces cerevisiae Cold Spring Harbor Symposia On Quantitative Biology. 60: 503-513. PMID 8824423 DOI: 10.1101/Sqb.1995.060.01.054 |
0.769 |
|
1995 |
Hochstrasser M. Ubiquitin, proteasomes, and the regulation of intracellular protein degradation. Current Opinion in Cell Biology. 7: 215-223. PMID 7612274 DOI: 10.1016/0955-0674(95)80031-X |
0.523 |
|
1995 |
DeMarini DJ, Papa FR, Swaminathan S, Ursic D, Rasmussen TP, Culbertson MR, Hochstrasser M. The yeast SEN3 gene encodes a regulatory subunit of the 26S proteasome complex required for ubiquitin-dependent protein degradation in vivo. Molecular and Cellular Biology. 15: 6311-21. PMID 7565784 DOI: 10.1128/Mcb.15.11.6311 |
0.779 |
|
1995 |
Richter-Ruoff B, Wolf DH, Hochstrasser M. Degradation of the MATα2 transcriptional regulator is mediated by the proteasome Febs Letters. 354: 50-52. DOI: 10.1016/0014-5793(95)90822-F |
0.526 |
|
1995 |
Chen P, Hochstrasser M. Biogenesis, structure and function of the yeast 20S proteasome. The Embo Journal. 14: 2620-2630. DOI: 10.1002/J.1460-2075.1995.Tb07260.X |
0.548 |
|
1993 |
Chen P, Johnson P, Sommer T, Jentsch S, Hochstrasser M. Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MAT alpha 2 repressor. Cell. 74: 357-69. PMID 8393731 DOI: 10.1016/0092-8674(93)90426-Q |
0.7 |
|
1993 |
Papa FR, Hochstrasser M. The yeast DOA4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene Nature. 366: 313-319. PMID 8247125 DOI: 10.1038/366313A0 |
0.658 |
|
1992 |
Hochstrasser M. Ubiquitin and intracellular protein degradation. Current Opinion in Cell Biology. 4: 1024-1031. PMID 1336669 DOI: 10.1016/0955-0674(92)90135-Y |
0.534 |
|
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 |
0.721 |
|
1991 |
Hochstrasser M. Functions of intracellular protein degradation in yeast. Genetic Engineering. 13: 307-329. PMID 1369338 DOI: 10.1007/978-1-4615-3760-1_14 |
0.415 |
|
1987 |
Hochstrasser M, Sedat JW. Three-dimensional organization of Drosophila melanogaster interphase nuclei. II. Chromosome spatial organization and gene regulation. The Journal of Cell Biology. 104: 1471-83. PMID 3108265 DOI: 10.1083/Jcb.104.6.1471 |
0.572 |
|
1987 |
Hochstrasser M, Sedat JW. Three-dimensional organization of Drosophila melanogaster interphase nuclei. I. Tissue-specific aspects of polytene nuclear architecture. The Journal of Cell Biology. 104: 1455-70. PMID 3108264 DOI: 10.1083/Jcb.104.6.1455 |
0.551 |
|
1986 |
Hochstrasser M, Mathog D, Gruenbaum Y, Saumweber H, Sedat JW. Spatial organization of chromosomes in the salivary gland nuclei of Drosophila melanogaster. The Journal of Cell Biology. 102: 112-23. PMID 3079766 DOI: 10.1083/Jcb.102.1.112 |
0.552 |
|
1985 |
Mathog D, Hochstrasser M, Sedat JW. Light microscope based analysis of three-dimensional structure: applications to the study of Drosophila salivary gland nuclei. I. Data collection and analysis. Journal of Microscopy. 137: 241-52. PMID 3999131 DOI: 10.1111/J.1365-2818.1985.Tb02582.X |
0.524 |
|
1984 |
Gruenbaum Y, Hochstrasser M, Mathog D, Saumweber H, Agard DA, Sedat JW. Spatial organization of the Drosophila nucleus: a three-dimensional cytogenetic study. Journal of Cell Science. Supplement. 1: 223-34. PMID 6442295 DOI: 10.1242/Jcs.1984.Supplement_1.14 |
0.637 |
|
1984 |
Mathog D, Hochstrasser M, Gruenbaum Y, Saumweber H, Sedat J. Characteristic folding pattern of polytene chromosomes in Drosophila salivary gland nuclei. Nature. 308: 414-21. PMID 6424026 DOI: 10.1038/308414A0 |
0.549 |
|
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