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Insights into the structure of the CCR4-NOT complex by electron microscopy
scientific article
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instance of
scholarly article
1 reference
stated in
PubMed
PubMed ID
21669201
retrieved
1 December 2016
title
Insights into the structure of the CCR4-NOT complex by electron microscopy
(English)
1 reference
stated in
PubMed
PubMed ID
21669201
retrieved
1 December 2016
main subject
biophysics
0 references
cell biology
0 references
structural biology
0 references
CCR4-NOT core DEDD family RNase subunit POP2 YNR052C
1 reference
stated in
GOA release 2020-03-11
CCR4-NOT core exoribonuclease subunit CCR4 YAL021C
1 reference
stated in
GOA release 2020-03-11
CCR4-NOT core subunit CDC39 YCR093W
1 reference
stated in
GOA release 2020-03-11
author
Dietrich Suck
series ordinal
4
0 references
Bettina Böttcher
series ordinal
5
0 references
Meikel Diepholz
series ordinal
3
0 references
Fariborz Nasertorabi
series ordinal
1
0 references
Claire Batisse
object named as
Claire Batisse
series ordinal
2
0 references
language of work or name
English
0 references
publication date
21 July 2011
0 references
published in
FEBS Letters
1 reference
stated in
PubMed
PubMed ID
21669201
retrieved
1 December 2016
volume
585
0 references
issue
14
0 references
page(s)
2182-6
0 references
copyright license
Creative Commons Attribution 3.0 Unported
1 reference
reference URL
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3171648
copyright status
copyrighted
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on focus list of Wikimedia project
ScienceSource
0 references
cites work
Crystal structure of the human CNOT6L nuclease domain reveals strict poly(A) substrate specificity
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Structural basis for the antiproliferative activity of the Tob-hCaf1 complex
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The 1.4-A crystal structure of the S. pombe Pop2p deadenylase subunit unveils the configuration of an active enzyme
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20 March 2017
X-ray structure and activity of the yeast Pop2 protein: a nuclease subunit of the mRNA deadenylase complex
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reference URL
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20 March 2017
CCR4, a 3'-5' poly(A) RNA and ssDNA exonuclease, is the catalytic component of the cytoplasmic deadenylase
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reference URL
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Functional organization of the yeast proteome by systematic analysis of protein complexes
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20 March 2017
Purification and characterization of the 1.0 MDa CCR4-NOT complex identifies two novel components of the complex
1 reference
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PubMed Central
reference URL
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The yeast POP2 gene encodes a nuclease involved in mRNA deadenylation
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PubMed Central
reference URL
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20 March 2017
The transcription factor associated Ccr4 and Caf1 proteins are components of the major cytoplasmic mRNA deadenylase in Saccharomyces cerevisiae
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PubMed Central
reference URL
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20 March 2017
Characterization of CAF4 and CAF16 reveals a functional connection between the CCR4-NOT complex and a subset of SRB proteins of the RNA polymerase II holoenzyme
1 reference
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PubMed Central
reference URL
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Isolation and characterization of human orthologs of yeast CCR4-NOT complex subunits
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20 March 2017
The CCR4 and CAF1 proteins of the CCR4-NOT complex are physically and functionally separated from NOT2, NOT4, and NOT5.
1 reference
stated in
PubMed Central
reference URL
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Identification of a mouse protein whose homolog in Saccharomyces cerevisiae is a component of the CCR4 transcriptional regulatory complex
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Global control of gene expression in yeast by the Ccr4-Not complex
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A different conformation for EGC stator subcomplex in solution and in the assembled yeast V-ATPase: possible implications for regulatory disassembly
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The NOT proteins are part of the CCR4 transcriptional complex and affect gene expression both positively and negatively
1 reference
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PubMed Central
reference URL
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CCR4 is a glucose-regulated transcription factor whose leucine-rich repeat binds several proteins important for placing CCR4 in its proper promoter context
1 reference
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PubMed Central
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27 November 2018
The essential function of Not1 lies within the Ccr4-Not complex
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/21669201
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1016/J.FEBSLET.2011.05.071
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3963755
OpenCitations bibliographic resource ID
3963755
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3963755
PMCID
3171648
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3963755
PubMed ID
21669201
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3963755
ResearchGate publication ID
51215389
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