About: Ubiquitin-dependent proteolysis of the microtubule end-binding protein 1, EB1, is controlled by the COP9 signalosome: possible consequences for microtubule filament stability.

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About: Ubiquitin-dependent proteolysis of the microtubule end-binding protein 1, EB1, is controlled by the COP9 signalosome: possible consequences for microtubule filament stability. Goto Sponge NotDistinct Permalink

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scientific article published on 22 February 2007

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rdf:type	Item
description	videnskabelig artikel (da) article científic (ca) articol științific (ro) articolo scientifico (it) artigo científico (gl) artigo científico (pt) artigo científico (pt-br) artikull shkencor (sq) artículo científico (es) bilimsel makale (tr) scienca artikolo (eo) vedecký článok (sk) vetenskaplig artikel (sv) vitenskapelig artikkel (nb) vitskapeleg artikkel (nn) vědecký článek (cs) wetenschappelijk artikel (nl) wissenschaftlicher Artikel (de) научная статья (ru) научни чланак (sr) מאמר מדעי (he) artikel ilmiah (id) article scientifique (fr) বৈজ্ঞানিক নিবন্ধ (bn) artículu científicu espublizáu en 2007 (ast) 2007 nî lūn-bûn (nan) 2007年の論文 (ja) 2007年論文 (zh-hk) 2007年論文 (zh-tw) 2007年論文 (zh-hant) 2007年論文 (yue) 2007年論文 (zh-mo) 2007年论文 (zh) 2007年论文 (zh-cn) 2007年论文 (zh-sg) 2007年论文 (zh-hans) 2007年论文 (wuu) 2007年论文 (zh-my) 2007년 논문 (ko) наукова стаття, опублікована в лютому 2007 (uk) scientific article published on 22 February 2007 (en-ca) scientific article published on 22 February 2007 (en-gb) مقالة علمية نشرت في 22 فبراير 2007 (ar) scientific article published on 22 February 2007 (en)
publication date	wds:Q38303871-89EF885C-EA3D-4551-B456-611F014D84A5
publication date	2007-02-22 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q38303871-D765A55B-0C8B-48BD-ACE7-6255811D106A
language of work or name	English
author name string	wds:Q38303871-B635D1AF-3937-4C86-9292-A860ACF2253C wds:Q38303871-D328C232-F44D-40E9-B1F1-C095064DC369
author name string	Andreas Peth Jan Peter Boettcher
rdfs:label	Ubiquitin-dependent proteolysis of the microtubule end-binding protein 1, EB1, is controlled by the COP9 signalosome: possible consequences for microtubule filament stability. (en) Ubiquitin-dependent proteolysis of the microtubule end-binding protein 1, EB1, is controlled by the COP9 signalosome: possible consequences for microtubule filament stability. (nl) Ubiquitin-dependent proteolysis of the microtubule end-binding protein 1, EB1, is controlled by the COP9 signalosome: possible consequences for microtubule filament stability. (ast)
skos:prefLabel	Ubiquitin-dependent proteolysis of the microtubule end-binding protein 1, EB1, is controlled by the COP9 signalosome: possible consequences for microtubule filament stability. (en) Ubiquitin-dependent proteolysis of the microtubule end-binding protein 1, EB1, is controlled by the COP9 signalosome: possible consequences for microtubule filament stability. (nl) Ubiquitin-dependent proteolysis of the microtubule end-binding protein 1, EB1, is controlled by the COP9 signalosome: possible consequences for microtubule filament stability. (ast)
name	Ubiquitin-dependent proteolysis of the microtubule end-binding protein 1, EB1, is controlled by the COP9 signalosome: possible consequences for microtubule filament stability. (en) Ubiquitin-dependent proteolysis of the microtubule end-binding protein 1, EB1, is controlled by the COP9 signalosome: possible consequences for microtubule filament stability. (nl) Ubiquitin-dependent proteolysis of the microtubule end-binding protein 1, EB1, is controlled by the COP9 signalosome: possible consequences for microtubule filament stability. (ast)
author	wds:Q38303871-CED21193-69FD-4189-82C6-959FDAAF082B
author	Wolfgang Dubiel
title	wds:Q38303871-6C0A386B-36C3-454E-A80D-15B70EEE6D1F
title	Ubiquitin-dependent proteolysis of the microtubule end-binding protein 1, EB1, is controlled by the COP9 signalosome: possible consequences for microtubule filament stability (en)
page(s)	wds:Q38303871-4EE72F82-FC77-4767-B583-E9B8D56DDEB0
page(s)	550-563
instance of	wds:Q38303871-FEBF90CA-E080-4C19-9451-11C79D18185F
instance of	scholarly article
main subject	wds:Q38303871-AE93BE5B-47CF-47C4-ADB5-1FAC0D5CC019
main subject	proteolysis
PubMed ID	wds:Q38303871-F94ADA1D-B9E4-47DB-B101-4BF2FA45138A
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/17350042
PubMed ID	17350042
published in	wds:Q38303871-A3DA1C3F-2564-4601-AC33-50E3E74C9B14
published in	Journal of Molecular Biology
issue	wds:Q38303871-1CDD7C2C-0010-4A87-9E0E-E42C99CD2F31
volume	wds:Q38303871-C975E3DF-55C6-4179-980E-F5C0536C1542
issue	2
volume	368
DOI	wds:Q38303871-FECE11DE-EB3A-42C7-87F7-814C57C9D159
DOI	http://dx.doi.org/10.1016/J.JMB.2007.02.052
DOI	10.1016/J.JMB.2007.02.052
Fatcat ID	wds:Q38303871-348C04B8-C4E9-47D6-AA1B-E322D930916A
Fatcat ID	release_yapjjl7tsvcuhntbqnlthbe3zq
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q38303871
is cites work of	Downregulation of COP9 signalosome subunits differentially affects the CSN complex and target protein stability CYLD coordinates with EB1 to regulate microtubule dynamics and cell migration COP9 signalosome function in the DDR. Control of microtubule organization and dynamics: two ends in the limelight Mitotic regulation of the stability of microtubule plus-end tracking protein EB3 by ubiquitin ligase SIAH-1 and Aurora mitotic kinases. Salt stress-induced disassembly of Arabidopsis cortical microtubule arrays involves 26S proteasome-dependent degradation of SPIRAL1 USP15 negatively regulates Nrf2 through deubiquitination of Keap1. Analysis of the role of COP9 Signalosome (CSN) subunits in K562; the first link between CSN and autophagy The COP9 signalosome negatively regulates proteasome proteolytic function and is essential to transcription. Enhanced protein expression in the baculovirus/insect cell system using engineered SUMO fusions. The COP9 signalosome, cullin 3 and Keap1 supercomplex regulates CHOP stability and adipogenesis Roles of Multifunctional COP9 Signalosome Complex in Cell Fate and Implications for Drug Discovery USP15 regulates dynamic protein-protein interactions of the spliceosome through deubiquitination of PRP31.

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