Literature DB >> 7643904

[Proteasomes. Complex proteases lead to a new understanding of cellular regulation through proteolysis].

W Hilt1, D H Wolf.   

Abstract

Proteasomes are large multicatalytic protease complexes which fulfill central functions in major proteolytic pathways of the eukaryotic cell. Two types of proteasomes are known: the cylindrically shaped 20S proteasome (700 kDa) and the 26S proteasome (1700 kDa) which contains the 20S proteasome as a functional core. Proteasomes are needed for stress-dependent and ubiquitin-mediated proteolysis. They are involved in degradation of abnormal, short-lived, and regulatory proteins. Proteasomes are important for cell differentiation and adaptation to environmental changes. Proteasomes have been shown to function in the control of the cell cycle and are suggested to be involved in antigen presentation by processing of intracellular proteins to antigenic peptides.

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Year:  1995        PMID: 7643904     DOI: 10.1007/bf01134523

Source DB:  PubMed          Journal:  Naturwissenschaften        ISSN: 0028-1042


  112 in total

1.  Isolation and characterization of a novel endogenous inhibitor of the proteasome.

Authors:  X C Li; M Z Gu; J D Etlinger
Journal:  Biochemistry       Date:  1991-10-08       Impact factor: 3.162

2.  Proteasome subunits encoded by the major histocompatibility complex are not essential for antigen presentation.

Authors:  F Momburg; V Ortiz-Navarrete; J Neefjes; E Goulmy; Y van de Wal; H Spits; S J Powis; G W Butcher; J C Howard; P Walden
Journal:  Nature       Date:  1992-11-12       Impact factor: 49.962

Review 3.  Proteasomes: multicatalytic proteinase complexes.

Authors:  A J Rivett
Journal:  Biochem J       Date:  1993-04-01       Impact factor: 3.857

4.  In vivo degradation of a transcriptional regulator: the yeast alpha 2 repressor.

Authors:  M Hochstrasser; A Varshavsky
Journal:  Cell       Date:  1990-05-18       Impact factor: 41.582

5.  The type 1 human immunodeficiency virus Tat binding protein is a transcriptional activator belonging to an additional family of evolutionarily conserved genes.

Authors:  B Ohana; P A Moore; S M Ruben; C D Southgate; M R Green; C A Rosen
Journal:  Proc Natl Acad Sci U S A       Date:  1993-01-01       Impact factor: 11.205

6.  Activation of the multicatalytic proteinase from rat skeletal muscle by fatty acids or sodium dodecyl sulphate.

Authors:  B Dahlmann; M Rutschmann; L Kuehn; H Reinauer
Journal:  Biochem J       Date:  1985-05-15       Impact factor: 3.857

7.  Interferon-gamma induces different subunit organizations and functional diversity of proteasomes.

Authors:  M Aki; N Shimbara; M Takashina; K Akiyama; S Kagawa; T Tamura; N Tanahashi; T Yoshimura; K Tanaka; A Ichihara
Journal:  J Biochem       Date:  1994-02       Impact factor: 3.387

8.  Purification and characterization of a protein inhibitor of the 20S proteasome (macropain).

Authors:  M Chu-Ping; C A Slaughter; G N DeMartino
Journal:  Biochim Biophys Acta       Date:  1992-03-12

9.  Tat-binding protein 7 is a subunit of the 26S protease.

Authors:  W Dubiel; K Ferrell; M Rechsteiner
Journal:  Biol Chem Hoppe Seyler       Date:  1994-04

10.  Proteinase yscE, the yeast proteasome/multicatalytic-multifunctional proteinase: mutants unravel its function in stress induced proteolysis and uncover its necessity for cell survival.

Authors:  W Heinemeyer; J A Kleinschmidt; J Saidowsky; C Escher; D H Wolf
Journal:  EMBO J       Date:  1991-03       Impact factor: 11.598

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  2 in total

1.  DeepCleave: a deep learning predictor for caspase and matrix metalloprotease substrates and cleavage sites.

Authors:  Fuyi Li; Jinxiang Chen; André Leier; Tatiana Marquez-Lago; Quanzhong Liu; Yanze Wang; Jerico Revote; A Ian Smith; Tatsuya Akutsu; Geoffrey I Webb; Lukasz Kurgan; Jiangning Song
Journal:  Bioinformatics       Date:  2020-02-15       Impact factor: 6.937

Review 2.  The fates of proteins in cells.

Authors:  P Bohley
Journal:  Naturwissenschaften       Date:  1995-12
  2 in total

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