Literature DB >> 1317016

[Ubiquitin-dependent degradation and modification of proteins].

J von Kampen1, M Wettern.   

Abstract

A large part of cellular proteins is in a dynamic state of turnover. Protein breakdown is responsible for essential cellular functions like modulation of key enzyme levels or removal of abnormal proteins. A major pathway for this selective proteolysis is mediated by the ubiquitin system, in which proteins are committed to degradation by their ligation to ubiquitin, a highly conserved 76 amino acid polypeptide. Recent evidence indicates that ubiquitination serves other functions besides marking proteins for destruction. As originally described for histones, the activities of several cellular proteins are reversibly regulated by ubiquitination and a successive de-ubiquitination step mediated by the activity of one or more isopeptidases.

Mesh:

Substances:

Year:  1992        PMID: 1317016     DOI: 10.1007/bf01134433

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


  66 in total

Review 1.  Ubiquitin in health and disease.

Authors:  R J Mayer; J Arnold; L László; M Landon; J Lowe
Journal:  Biochim Biophys Acta       Date:  1991-06-13

Review 2.  The ubiquitin pathway for protein degradation.

Authors:  A Hershko
Journal:  Trends Biochem Sci       Date:  1991-07       Impact factor: 13.807

3.  The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis.

Authors:  D Finley; B Bartel; A Varshavsky
Journal:  Nature       Date:  1989-03-30       Impact factor: 49.962

4.  The eye lens has an active ubiquitin-protein conjugation system.

Authors:  J H Jahngen; A L Haas; A Ciechanover; J Blondin; D Eisenhauer; A Taylor
Journal:  J Biol Chem       Date:  1986-10-15       Impact factor: 5.157

5.  Ubiquitin is a heat shock protein in chicken embryo fibroblasts.

Authors:  U Bond; M J Schlesinger
Journal:  Mol Cell Biol       Date:  1985-05       Impact factor: 4.272

6.  Ubiquitin-lysozyme conjugates. Purification and susceptibility to proteolysis.

Authors:  R Hough; M Rechsteiner
Journal:  J Biol Chem       Date:  1986-02-15       Impact factor: 5.157

7.  Universality and structure of the N-end rule.

Authors:  D K Gonda; A Bachmair; I Wünning; J W Tobias; W S Lane; A Varshavsky
Journal:  J Biol Chem       Date:  1989-10-05       Impact factor: 5.157

8.  Recognition of modified forms of ribonuclease A by the ubiquitin system.

Authors:  R L Dunten; R E Cohen
Journal:  J Biol Chem       Date:  1989-10-05       Impact factor: 5.157

9.  The yeast ubiquitin genes: a family of natural gene fusions.

Authors:  E Ozkaynak; D Finley; M J Solomon; A Varshavsky
Journal:  EMBO J       Date:  1987-05       Impact factor: 11.598

10.  UBA 1: an essential yeast gene encoding ubiquitin-activating enzyme.

Authors:  J P McGrath; S Jentsch; A Varshavsky
Journal:  EMBO J       Date:  1991-01       Impact factor: 11.598

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.