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Select item 43581131.

Solution Structure of Yeast Rpn9: INSIGHTS INTO PROTEASOME LID ASSEMBLY

Yunfei Hu, Yujie Wu, Qianwen Li, Wenbo Zhang, Changwen Jin

J Biol Chem. 2015 Mar 13; 290(11): 6878–6889. Published online 2015 Jan 28. doi: 10.1074/jbc.M114.626762

PMCID:: PMC4358113

Abstract Article PDF–5.2M

Select item 50594532.

Structure of ubiquitylated-Rpn10 provides insight into its autoregulation mechanism

Tal Keren-Kaplan, Lee Zeev Peters, Olga Levin-Kravets, Ilan Attali, Oded Kleifeld, Noa Shohat, Shay Artzi, Ori Zucker, Inbar Pilzer, Noa Reis, Michael H. Glickman, Shay Ben-Aroya, Gali Prag

Nat Commun. 2016; 7: 12960. Published online 2016 Oct 4. doi: 10.1038/ncomms12960

PMCID:: PMC5059453

Abstract Article PDF–3.1M

Select item 846273.

Rpn9 Is Required for Efficient Assembly of the Yeast 26S Proteasome

Junko Takeuchi, Masahiro Fujimuro, Hideyosi Yokosawa, Keiji Tanaka, Akio Toh-e

Mol Cell Biol. 1999 Oct; 19(10): 6575–6584. doi: 10.1128/mcb.19.10.6575

PMCID:: PMC84627

Abstract Article PDF–6.0M

Select item 33400504.

Dual functions of the Hsm3 protein in chaperoning and scaffolding regulatory particle subunits during the proteasome assembly

Marie-Bénédicte Barrault, Nicolas Richet, Chloe Godard, Brice Murciano, Benoît Le Tallec, Erwann Rousseau, Pierre Legrand, Jean-Baptiste Charbonnier, Marie-Hélène Le Du, Raphaël Guérois, Françoise Ochsenbein, Anne Peyroche

Proc Natl Acad Sci U S A. 2012 Apr 24; 109(17): E1001–E1010. Published online 2012 Mar 29. doi: 10.1073/pnas.1116538109

PMCID:: PMC3340050

Abstract Article PDF–2.0M

Select item 47495695.

Atomic structure of the 26S proteasome lid reveals the mechanism of deubiquitinase inhibition

Corey M Dambacher, Evan J Worden, Mark A Herzik, Jr., Andreas Martin, Gabriel C Lander

eLife. 2016; 5: e13027. Published online 2016 Jan 8. doi: 10.7554/eLife.13027

PMCID:: PMC4749569

Abstract Article PDF–2.8M

Select item 46010816.

A Single α Helix Drives Extensive Remodeling of the Proteasome Lid and Completion of Regulatory Particle Assembly

Robert J. Tomko, Jr., David W. Taylor, Zhuo A. Chen, Hong-Wei Wang, Juri Rappsilber, Mark Hochstrasser

Cell. 2015 Oct 8; 163(2): 432–444. doi: 10.1016/j.cell.2015.09.022

PMCID:: PMC4601081

Abstract Article PDF–4.0M

Select item 39475547.

The Intrinsically Disordered Sem1 Protein Functions as a Molecular Tether During Proteasome Lid Biogenesis

Robert J. Tomko, Jr., Mark Hochstrasser

Mol Cell. Author manuscript; available in PMC 2015 Feb 6.

Published in final edited form as: Mol Cell. 2014 Feb 6; 53(3): 433–443. Published online 2014 Jan 9. doi: 10.1016/j.molcel.2013.12.009

PMCID:: PMC3947554

Abstract Article PDF–5.8M

Select item 15232308.

Structural Organization of the 19S Proteasome Lid: Insights from MS of Intact Complexes

Michal Sharon, Thomas Taverner, Xavier I Ambroggio, Raymond J Deshaies, Carol V Robinson

PLoS Biol. 2006 Aug; 4(8): e267. Published online 2006 Aug 1. doi: 10.1371/journal.pbio.0040267

PMCID:: PMC1523230

Abstract Article PDF–1.1M

Select item 32515159.

Incorporation of the Rpn12 Subunit Couples Completion of Proteasome Regulatory Particle Lid Assembly to Lid-Base Joining

Robert J. Tomko, Jr., Mark Hochstrasser

Mol Cell. Author manuscript; available in PMC 2012 Dec 23.

Published in final edited form as: Mol Cell. 2011 Dec 23; 44(6): 907–917. doi: 10.1016/j.molcel.2011.11.020

PMCID:: PMC3251515

Abstract Article PDF–4.9M

Select item 156973110.

Cumulative Mutations Affecting Sterol Biosynthesis in the Yeast Saccharomyces cerevisiae Result in Synthetic Lethality That Is Suppressed by Alterations in Sphingolipid Profiles

Martin Valachovic, Bart M. Bareither, M. Shah Alam Bhuiyan, James Eckstein, Robert Barbuch, Dina Balderes, Lisa Wilcox, Stephen L. Sturley, Robert C. Dickson, Martin Bard

Genetics. 2006 Aug; 173(4): 1893–1908. doi: 10.1534/genetics.105.053025

PMCID:: PMC1569731

Abstract Article PDF–454K

Select item 691082911.

Specific lid-base contacts in the 26s proteasome control the conformational switching required for substrate degradation

Eric R Greene, Ellen A Goodall, Andres H de la Peña, Mary E Matyskiela, Gabriel C Lander, Andreas Martin

eLife. 2019; 8: e49806. Published online 2019 Nov 28. doi: 10.7554/eLife.49806

PMCID:: PMC6910829

Abstract Article PDF–1.6M

Select item 533983312.

High-resolution cryo-EM structure of the proteasome in complex with ADP-AlFx

Zhanyu Ding, Zhenglin Fu, Cong Xu, Yifan Wang, Yanxing Wang, Junrui Li, Liangliang Kong, Jinhuan Chen, Na Li, Rongguang Zhang, Yao Cong

Cell Res. 2017 Mar; 27(3): 373–385. Published online 2017 Jan 20. doi: 10.1038/cr.2017.12

PMCID:: PMC5339833

Abstract Article PDF–2.7M

Select item 450720613.

Structural characterization of the interaction of Ubp6 with the 26S proteasome

Antje Aufderheide, Florian Beck, Florian Stengel, Michaela Hartwig, Andreas Schweitzer, Günter Pfeifer, Alfred L. Goldberg, Eri Sakata, Wolfgang Baumeister, Friedrich Förster

Proc Natl Acad Sci U S A. 2015 Jul 14; 112(28): 8626–8631. Published online 2015 Jun 30. doi: 10.1073/pnas.1510449112

PMCID:: PMC4507206

Abstract Article PDF–1.8M

Select item 10889714.

The Regulatory Particle of the Saccharomyces cerevisiae Proteasome

Michael H. Glickman, David M. Rubin, Victor A. Fried, Daniel Finley

Mol Cell Biol. 1998 Jun; 18(6): 3149–3162. doi: 10.1128/mcb.18.6.3149

PMCID:: PMC108897

Abstract Article PDF–3.8M

Select item 443830415.

Base-CP proteasome can serve as a platform for stepwise lid formation

Zanlin Yu, Nurit Livnat-Levanon, Oded Kleifeld, Wissam Mansour, Mark A. Nakasone, Carlos A. Castaneda, Emma K. Dixon, David Fushman, Noa Reis, Elah Pick, Michael H. Glickman

Biosci Rep. 2015 Jun; 35(3): e00194. Prepublished online 2015 Jan 27. Published online 2015 May 19. doi: 10.1042/BSR20140173

PMCID:: PMC4438304

Abstract Article PDF–1.8M

Select item 479099816.

Structure of an endogenous yeast 26S proteasome reveals two major conformational states

Bai Luan, Xiuliang Huang, Jianping Wu, Ziqing Mei, Yiwei Wang, Xiaobin Xue, Chuangye Yan, Jiawei Wang, Daniel J. Finley, Yigong Shi, Feng Wang

Proc Natl Acad Sci U S A. 2016 Mar 8; 113(10): 2642–2647. Published online 2016 Feb 29. doi: 10.1073/pnas.1601561113

PMCID:: PMC4790998

Abstract Article PDF–2.7M

Select item 470598617.

Proteomic Analysis Identifies Ribosome Reduction as an Effective Proteotoxic Stress Response

Angel Guerra-Moreno, Marta Isasa, Meera K. Bhanu, David P. Waterman, Vinay V. Eapen, Steven P. Gygi, John Hanna

J Biol Chem. 2015 Dec 11; 290(50): 29695–29706. Published online 2015 Oct 21. doi: 10.1074/jbc.M115.684969

PMCID:: PMC4705986

Abstract Article PDF–2.4M

Select item 371228918.

Conformational switching of the 26S proteasome enables substrate degradation

Mary E. Matyskiela, Gabriel C. Lander, Andreas Martin

Nat Struct Mol Biol. Author manuscript; available in PMC 2014 Jan 1.

Published in final edited form as: Nat Struct Mol Biol. 2013 Jul; 20(7): 781–788. Published online 2013 Jun 16. doi: 10.1038/nsmb.2616

PMCID:: PMC3712289

Abstract Article PDF–3.9M

Select item 992282319.

The penultimate step of proteasomal ATPase assembly is mediated by a switch dependent on the chaperone Nas2

Suganya Sekaran, Soyeon Park

J Biol Chem. 2023 Feb; 299(2): 102870. Published online 2023 Jan 5. doi: 10.1016/j.jbc.2023.102870

PMCID:: PMC9922823

Abstract Article PDF–2.0M

Select item 678705820.

Ubiquitin receptors are required for substrate-mediated activation of the proteasome’s unfolding ability

Mary D. Cundiff, Christina M. Hurley, Jeremy D. Wong, Joseph A. Boscia, IV, Aarti Bashyal, Jake Rosenberg, Eden L. Reichard, Nicholas D. Nassif, Jennifer S. Brodbelt, Daniel A. Kraut

Sci Rep. 2019; 9: 14506. Published online 2019 Oct 10. doi: 10.1038/s41598-019-50857-y