Literature DB >> 9789328

Proteasome inhibitors: valuable new tools for cell biologists.

D H Lee1, A L Goldberg.   

Abstract

Proteasomes are major sites for protein degradation in eukaryotic cells. The recent identification of selective proteasome inhibitors has allowed a definition of the roles of the ubiquitin-proteasome pathway in various cellular processes, such as antigen presentation and the degradation of regulatory or membrane proteins. This review describes the actions of these inhibitors, how they can be used to investigate cellular responses, the functions of the proteasome demonstrated by such studies and their potential applications in the future.

Keywords:  Non-programmatic

Mesh:

Substances:

Year:  1998        PMID: 9789328     DOI: 10.1016/s0962-8924(98)01346-4

Source DB:  PubMed          Journal:  Trends Cell Biol        ISSN: 0962-8924            Impact factor:   20.808


  507 in total

Review 1.  The proteasome: a macromolecular assembly designed for controlled proteolysis.

Authors:  P Zwickl; D Voges; W Baumeister
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  1999-09-29       Impact factor: 6.237

2.  Ubiquitin-dependent degradation of multiple F-box proteins by an autocatalytic mechanism.

Authors:  J M Galan; M Peter
Journal:  Proc Natl Acad Sci U S A       Date:  1999-08-03       Impact factor: 11.205

3.  Disruption of heat shock factor 1 reveals an essential role in the ubiquitin proteolytic pathway.

Authors:  L Pirkkala; T P Alastalo; X Zuo; I J Benjamin; L Sistonen
Journal:  Mol Cell Biol       Date:  2000-04       Impact factor: 4.272

4.  Ricin A chain without its partner B chain is degraded after retrotranslocation from the endoplasmic reticulum to the cytosol in plant cells.

Authors:  A Di Cola; L Frigerio; J M Lord; A Ceriotti; L M Roberts
Journal:  Proc Natl Acad Sci U S A       Date:  2001-12-04       Impact factor: 11.205

5.  Proteasome inhibitors block a late step in lysosomal transport of selected membrane but not soluble proteins.

Authors:  P van Kerkhof; C M Alves dos Santos; M Sachse; J Klumperman; G Bu; G J Strous
Journal:  Mol Biol Cell       Date:  2001-08       Impact factor: 4.138

6.  Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein.

Authors:  Y Yedidia; L Horonchik; S Tzaban; A Yanai; A Taraboulos
Journal:  EMBO J       Date:  2001-10-01       Impact factor: 11.598

7.  Transfer of the cholera toxin A1 polypeptide from the endoplasmic reticulum to the cytosol is a rapid process facilitated by the endoplasmic reticulum-associated degradation pathway.

Authors:  Ken Teter; Rebecca L Allyn; Michael G Jobling; Randall K Holmes
Journal:  Infect Immun       Date:  2002-11       Impact factor: 3.441

8.  Inhibition of ubiquitin-proteasome pathway-mediated I kappa B alpha degradation by a naturally occurring antibacterial peptide.

Authors:  Y Gao; S Lecker; M J Post; A J Hietaranta; J Li; R Volk; M Li; K Sato; A K Saluja; M L Steer; A L Goldberg; M Simons
Journal:  J Clin Invest       Date:  2000-08       Impact factor: 14.808

9.  Involvement of the ubiquitin/proteasome system in sorting of the interleukin 2 receptor beta chain to late endocytic compartments.

Authors:  A Rocca; C Lamaze; A Subtil; A Dautry-Varsat
Journal:  Mol Biol Cell       Date:  2001-05       Impact factor: 4.138

10.  Degradation of retinoid X receptor alpha by TPA through proteasome pathway in gastric cancer cells.

Authors:  Xiao-Feng Ye; Su Liu; Qiao Wu; Xiao-Feng Lin; Bing Zhang; Jia-Fa Wu; Ming-Qing Zhang; Wen-Jin Su
Journal:  World J Gastroenterol       Date:  2003-09       Impact factor: 5.742

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