| Ubiquitin-dependent proteolysis and cell cycle control in yeast. | |
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MedLine Citation:
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PMID: 9552389 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Genetic and biochemical data indicate that ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression. In general, mutations in some genes that encode proteins involved in the ubiquitin pathway cause cell cycle defects and affect the turnover of cell cycle regulatory proteins. Furthermore, some cell cycle regulatory proteins are short-lived, ubiquitinated, and degraded by the ubiquitin pathway. This review will examine how the ubiquitin pathway plays a role in regulating progression from the G1 to the S phase of the cell cycle, as well as the G2 to M phase transition. |
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Authors:
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K T Chun; N Mathias; M G Goebl |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.; Review |
Journal Detail:
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Title: Progress in cell cycle research Volume: 2 ISSN: 1087-2957 ISO Abbreviation: Prog Cell Cycle Res Publication Date: 1996 |
Date Detail:
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Created Date: 1998-05-13 Completed Date: 1998-05-13 Revised Date: 2009-11-19 |
Medline Journal Info:
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Nlm Unique ID: 9609058 Medline TA: Prog Cell Cycle Res Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 115-27 Citation Subset: IM |
Affiliation:
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Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis 46202-5122, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Cell Cycle
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genetics,
physiology* Cyclin-Dependent Kinase Inhibitor Proteins Cyclins / metabolism Cysteine Endopeptidases / genetics, metabolism Fungal Proteins / metabolism Genes, Fungal Ligases / metabolism Multienzyme Complexes / genetics, metabolism Peptide Hydrolases / metabolism Proteasome Endopeptidase Complex Saccharomyces cerevisiae / cytology*, genetics, metabolism* Saccharomyces cerevisiae Proteins* Ubiquitin-Protein Ligase Complexes* Ubiquitin-Protein Ligases Ubiquitins / metabolism* |
| Grant Support | |
ID/Acronym/Agency:
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GM-45460/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/CLN1 protein, S cerevisiae; 0/CLN2 protein, S cerevisiae; 0/CLN3 protein, S cerevisiae; 0/Cyclin-Dependent Kinase Inhibitor Proteins; 0/Cyclins; 0/Fungal Proteins; 0/Multienzyme Complexes; 0/SIC1 protein, S cerevisiae; 0/Saccharomyces cerevisiae Proteins; 0/Ubiquitins; EC 3.4.-/Peptide Hydrolases; EC 3.4.22.-/Cysteine Endopeptidases; EC 3.4.25.1/Proteasome Endopeptidase Complex; EC 6.-/Ligases; EC 6.3.2.19/Ubiquitin-Protein Ligase Complexes; EC 6.3.2.19/Ubiquitin-Protein Ligases; EC 6.3.2.19/anaphase-promoting complex |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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