DOI: 10.1074/mcp.r110.003871. Trimming of Ubiquitin Chains by Proteasome-associated Deubiquitinating Enzymes

Trimming of Ubiquitin Chains by Proteasome-associated Deubiquitinating Enzymes

10.1074/mcp.r110.003871

Crossref journal-article

Elsevier BV

Molecular & Cellular Proteomics (78)

Bibliography

Lee, M. J., Lee, B.-H., Hanna, J., King, R. W., & Finley, D. (2011). Trimming of Ubiquitin Chains by Proteasome-associated Deubiquitinating Enzymes. Molecular & Cellular Proteomics, 10(5), R110.003871.

Authors 5

Min Jae Lee (first)
Byung-Hoon Lee (additional)
John Hanna (additional)
Randall W. King (additional)
Daniel Finley (additional)

References 30 Referenced 189

10.1146/annurev.biochem.78.081507.101607 / Annu. Rev. Biochem / Recognition and processing of ubiquitin-protein conjugates by the proteasome by Finley (2009)
10.1038/nchembio.250 / Nat. Chem. Biol / Targeting proteins for degradation by Schrader (2009)
10.1016/j.tibs.2006.10.006 / Trends Biochem. Sci / ATP-dependent proteases of bacteria: recognition logic and operating principles by Baker (2006)
10.1038/nature06926 / Nature / Proteasome subunit Rpn13 is a novel ubiquitin receptor by Husnjak (2008)
10.1016/0005-2795(77)90140-4 / Biochim. Biophys. Acta / Nuclear magnetic resonance studies of the denaturation of ubiquitin by Lenkinski (1977)
10.1128/MCB.23.24.9251-9261.2003 / Mol. Cell. Biol / Ubiquitin depletion as a key mediator of toxicity by translational inhibitors by Hanna (2003)
10.1073/pnas.0905746106 / Proc. Natl. Acad. Sci. U.S.A / Ubiquitin degradation with its substrate, or as a monomer in a ubiquitination-independent mode, provides clues to proteasome regulation by Shabek (2009)
10.1146/annurev.biochem.78.082307.091526 / Annu. Rev. Biochem / Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes by Reyes-Turcu (2009)
10.1038/nature01071 / Nature / A cryptic protease couples deubiquitination and degradation by the proteasome by Yao (2002)
10.1126/science.1075898 / Science / Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome by Verma (2002)
10.1038/nature09299 / Nature / Enhancement of proteasome activity by a small-molecule inhibitor of USP14 by Lee (2010)
10.1038/385737a0 / Nature / Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome by Lam (1997)
10.1091/mbc.e07-10-1040 / Mol. Biol. Cell / Relative structural and functional roles of multiple deubiquitylating proteins associated with mammalian 26S proteasome by Koulich (2008)
10.1074/jbc.M109.052928 / J. Biol. Chem / The lysine 48 and lysine 63 ubiquitin conjugates are processed differently by the 26 S proteasome by Jacobson (2009)
10.1016/j.cell.2006.07.038 / Cell / Deubiquitinating enzyme Ubp6 functions noncatalytically to delay proteasomal degradation by Hanna (2006)
10.1093/emboj/19.1.94 / EMBO J / Recognition of the polyubiquitin proteolytic signal by Thrower (2000)
10.1038/ncb1436 / Nat. Cell Biol / Quantitative analysis of in vitro ubiquitinated cyclin B1 reveals complex chain topology by Kirkpatrick (2006)
10.1016/S0076-6879(05)99014-9 / Methods Enzymol / Preparation of ubiquitinated substrates by the PY motif-insertion method for monitoring 26S proteasome activity by Saeki (2005)
10.1080/10715760600918142 / Free Radic. Res / Protein oxidation and aging by Stadtman (2006)
10.1038/emboj.2009.27 / EMBO J / K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-associated Brcc36 and proteasomal Poh1 by Cooper (2009)
10.1016/j.molcel.2009.11.015 / Mol. Cell / Ubiquitinated proteins activate the proteasome by binding to Usp14/Ubp6, which causes 20S gate opening by Peth (2009)
10.1038/ncb1460 / Nat. Cell Biol / Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1 by Yao (2006)
10.1021/bi972274d / Biochemistry / Substrate specificity of deubiquitinating enzymes: ubiquitin C-terminal hydrolases by Larsen (1998)
10.1111/j.1749-6632.1998.tb10501.x / Ann. N.Y. Acad. Sci / Enhancement by ubiquitin aldehyde of proteolysis of hemoglobin α-subunits in β-thalassemic hemolysates by Shaeffer (1998)
10.1038/nature06924 / Nature / Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction by Schreiner (2008)
10.1073/pnas.0913495107 / Proc. Natl. Acad. Sci. U.S.A / Regulation of NF-κB activity and inducible nitric oxide synthase by regulatory particle non-ATPase subunit 13 (Rpn13) by Mazumdar (2010)
10.1016/j.cell.2007.03.042 / Cell / A ubiquitin stress response induces altered proteasome composition by Hanna (2007)
10.1016/j.ydbio.2008.09.021 / Dev. Biol / Transgenic rescue of ataxia mice reveals a male-specific sterility defect by Crimmins (2009)
10.1007/978-3-642-01222-8_12 / Recent Results Cancer Res / Bortezomib by Einsele (2010)
10.1073/pnas.0905081106 / Proc. Natl. Acad. Sci. U.S.A / Insights into the molecular architecture of the 26S proteasome by Nickell (2009)

Dates

Type	When
Created	14 years, 11 months ago (Sept. 7, 2010, 9:34 p.m.)
Deposited	4 years, 1 month ago (July 29, 2021, 5:44 p.m.)
Indexed	1 month ago (July 25, 2025, 6:51 a.m.)
Issued	14 years, 3 months ago (May 1, 2011)
Published	14 years, 3 months ago (May 1, 2011)
Published Print	14 years, 3 months ago (May 1, 2011)

Funders 0

None

BibTeX

@article{Lee_2011, title={Trimming of Ubiquitin Chains by Proteasome-associated Deubiquitinating Enzymes}, volume={10}, ISSN={1535-9476}, url={http://dx.doi.org/10.1074/mcp.r110.003871}, DOI={10.1074/mcp.r110.003871}, number={5}, journal={Molecular & Cellular Proteomics}, publisher={Elsevier BV}, author={Lee, Min Jae and Lee, Byung-Hoon and Hanna, John and King, Randall W. and Finley, Daniel}, year={2011}, month=may, pages={R110.003871} }

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