About: Degradation of proteins with acetylated amino termini by the ubiquitin system

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scientific article published on 01 June 1989

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rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в червні 1989 (uk) article scientifique publié en 1989 (fr) im Juni 1989 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu en xunu de 1989 (ast) scientific article published on 01 June 1989 (en)
publication date	wds:Q69350820-D3828322-5B08-46F0-A67E-A7288A8A6422
publication date	1989-06-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q69350820-5E14FB8F-0BC5-41F4-8A4E-70C30B4C5EDB
language of work or name	English
cites work	wds:Q69350820-0BA0DA94-68FC-4EC1-9838-222C89DFEECF wds:Q69350820-1B8F6CAD-68FA-4182-9296-6A8144A8CF3A wds:Q69350820-24B5742A-D160-41B9-944F-B20572B0BAEC wds:Q69350820-45F18FF7-ABC6-4E3E-A462-9B1DE18D2F53 wds:Q69350820-50E4BDA3-1356-41E2-B7B9-505E277C83FC wds:Q69350820-545B3F58-8592-4451-B952-29B6CD5C30AF wds:Q69350820-5D4CFC45-077D-423F-BF64-9CA8D6FEB900 wds:Q69350820-5D5E9E40-73A7-4B46-B286-9611A3513DF7 wds:Q69350820-6819397D-D84C-4212-95E0-20413C172642 wds:Q69350820-994EF4F4-5B6C-4DC2-B218-14FEAA6D1332 wds:Q69350820-A0283E4C-D2B9-42E8-9B4A-0873723BAE95 wds:Q69350820-B086162A-40C7-47CB-BAF8-AB4E31A433B4 wds:Q69350820-CB69F258-65BA-484B-B6BE-D989943E500E wds:Q69350820-D028F268-4C62-4B4D-94E6-ED9F432C27FC wds:Q69350820-DE549B9F-133C-478F-9763-9770CCC45691 wds:Q69350820-EA0DC8D7-E12D-447D-9482-5FE7A5BDA519 wds:Q69350820-F1EBFDC3-0627-4486-B819-BACB79C4B8D0
cites work	In vivo chemical modification of proteins (post-translational modification). In vivo half-life of a protein is a function of its amino-terminal residue A heat-stable polypeptide component of an ATP-dependent proteolytic system from reticulocytes Arthrin, a myofibrillar protein of insect flight muscle, is an actin-ubiquitin conjugate. Intracellular protein degradation in mammalian and bacterial cells: Part 2 High-sensitivity sequencing with a gas-phase sequenator Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 Structure of polyubiquitinated histone H2A Role of the alpha-amino group of protein in ubiquitin-mediated protein breakdown Thermolability of ubiquitin-activating enzyme from the mammalian cell cycle mutant ts85 Mechanisms of Intracellular Protein Breakdown Amino-terminal sequence identity of ubiquitin and the nonhistone component of nuclear protein A24 Role of arginine-tRNA in protein degradation by the ubiquitin pathway Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85 ATP serves two distinct roles in protein degradation in reticulocytes, one requiring and one independent of ubiquitin Red light-induced formation of ubiquitin-phytochrome conjugates: Identification of possible intermediates of phytochrome degradation. In vivo deacetylation of N-acetyl amino acids by kidney acylases in mice and rats. A possible role of acylase system in mammalian kidneys
author name string	wds:Q69350820-19456B15-87F3-449D-B863-7F33328F6AC3 wds:Q69350820-DF152C90-DA11-4931-9586-35EB27197A2A wds:Q69350820-FC711CF5-1560-4D46-BAC4-F838F786A087
author name string	A L Schwartz A Mayer N R Siegel
rdfs:label	Degradation of proteins with acetylated amino termini by the ubiquitin system (en) Degradation of proteins with acetylated amino termini by the ubiquitin system (nl)
skos:prefLabel	Degradation of proteins with acetylated amino termini by the ubiquitin system (en) Degradation of proteins with acetylated amino termini by the ubiquitin system (nl)
name	Degradation of proteins with acetylated amino termini by the ubiquitin system (en) Degradation of proteins with acetylated amino termini by the ubiquitin system (nl)
author	wds:Q69350820-5E4C3FD7-1C11-4741-87C2-4DB0480E79A9
author	Aaron Ciechanover
title	wds:Q69350820-9A119785-34F4-4088-BEB1-67580EA7355A
title	Degradation of proteins with acetylated amino termini by the ubiquitin system (en)
page(s)	wds:Q69350820-2AE0364D-A419-4548-8DFF-BBE69938E358
page(s)	1480-1483
instance of	wds:Q69350820-B6D64566-5D30-49B1-91DE-353D1593B0CC
instance of	scholarly article
PubMed ID	wds:Q69350820-60E9BEFD-45F4-4910-B331-15792EBD1191
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/2544030
PubMed ID	2544030
published in	wds:Q69350820-600EEE79-4AA6-4C0C-AE3D-2F8BA81FE75B
published in	Science
issue	wds:Q69350820-6212C7A4-DE2F-41DA-A6E7-8A5FFCAC7A3A
volume	wds:Q69350820-A2FFF9F3-AAA8-4D99-B2DA-D93D0F833767
issue	4911
volume	244
DOI	wds:Q69350820-A75548F0-2F14-4ED9-9144-47A7C223A113
DOI	http://dx.doi.org/10.1126/SCIENCE.2544030
DOI	10.1126/SCIENCE.2544030
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q69350820
is cites work of	Degradation of nuclear oncoproteins by the ubiquitin system in vitro Rosenthal fibers contain ubiquitinated alpha B-crystallin Ubiquitin-dependent degradation of certain protein substrates in vitro requires the molecular chaperone Hsc70 Amino acid residue penultimate to the amino-terminal gly residue strongly affects two cotranslational protein modifications, N-myristoylation and N-acetylation Oxidative stress and recovery from oxidative stress are associated with altered ubiquitin conjugating and proteolytic activities in bovine lens epithelial cells The intrinsically disordered N-terminal domain of thymidylate synthase targets the enzyme to the ubiquitin-independent proteasomal degradation pathway Protein synthesis elongation factor EF-1 alpha is essential for ubiquitin-dependent degradation of certain N alpha-acetylated proteins and may be substituted for by the bacterial elongation factor EF-Tu A function for lipoxygenase in programmed organelle degradation The ubiquitin pathway for protein degradation Human catecholamine sulfotransferase (SULT1A3) pharmacogenetics: functional genetic polymorphism The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides Histone ubiquitination: a tagging tail unfolds? The recognition component of the N-end rule pathway N-terminal acetylation of cellular proteins creates specific degradation signals Effect of ubiquitin on platelet functions: possible identity with platelet activity suppressive lymphokine (PASL) Basic Medical Research Award. The ubiquitin system. Rosenthal fibers share epitopes with alpha B-crystallin, glial fibrillary acidic protein, and ubiquitin, but not with vimentin. Immunoelectron microscopy with colloidal gold ClpS is an essential component of the N-end rule pathway in Escherichia coli. Phosphorylation and N-terminal region of yeast ribosomal protein P1 mediate its degradation, which is prevented by protein P2. How are substrates recognized by the ubiquitin-mediated proteolytic system? The N-end rule pathway: emerging functions and molecular principles of substrate recognition Structural characterization of Saccharomyces cerevisiae prion-like protein Ure2

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