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Functions of the 19S complex in proteasomal degradation
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title
Functions of the 19S complex in proteasomal degradation
(English)
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author name string
Chang-Wei Liu
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1
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Andrew D. Jacobson
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2
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language of work or name
English
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publication date
February 2013
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published in
Trends in Biochemical Sciences
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PubMed
volume
38
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PubMed
issue
2
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PubMed
page(s)
103-10
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PubMed
cites work
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Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation
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Distinct modes of regulation of the Uch37 deubiquitinating enzyme in the proteasome and in the Ino80 chromatin-remodeling complex
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Regulation of Pax3 by proteasomal degradation of monoubiquitinated protein in skeletal muscle progenitors
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hRpn13/ADRM1/GP110 is a novel proteasome subunit that binds the deubiquitinating enzyme, UCH37
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Structure of the S5a:K48-Linked Diubiquitin Complex and Its Interactions with Rpn13
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RING domain E3 ubiquitin ligases
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Lysine 63-linked polyubiquitin chain may serve as a targeting signal for the 26S proteasome
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Deubiquitinating enzyme Ubp6 functions noncatalytically to delay proteasomal degradation.
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Multiple associated proteins regulate proteasome structure and function
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A cryptic protease couples deubiquitination and degradation by the proteasome
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Localization of the proteasomal ubiquitin receptors Rpn10 and Rpn13 by electron cryomicroscopy
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Characterization of Two Polyubiquitin Binding Sites in the 26 S Protease Subunit 5a
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Regulators of the proteasome pathway, Uch37 and Rpn13, play distinct roles in mouse development
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28 September 2017
Dependence of phospholipase D1 multi-monoubiquitination on its enzymatic activity and palmitoylation
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28 September 2017
Degradation of some polyubiquitinated proteins requires an intrinsic proteasomal binding element in the substrates
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The lysine 48 and lysine 63 ubiquitin conjugates are processed differently by the 26 s proteasome
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Rpn10-mediated degradation of ubiquitinated proteins is essential for mouse development
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28 September 2017
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Molecular model of the human 26S proteasome
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Ubiquitin Chain Trimming Recycles the Substrate Binding Sites of the 26 S Proteasome and Promotes Degradation of Lysine 48-linked Polyubiquitin Conjugates
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Mechanism of substrate unfolding and translocation by the regulatory particle of the proteasome from Methanocaldococcus jannaschii
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28 November 2018
Quantitative analysis of in vitro ubiquitinated cyclin B1 reveals complex chain topology
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28 November 2018
Uch2/Uch37 is the major deubiquitinating enzyme associated with the 26S proteasome in fission yeast.
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28 November 2018
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inferred from PubMed ID database lookup
Structure of S5a bound to monoubiquitin provides a model for polyubiquitin recognition
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/23290100
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Functional differences between two major ubiquitin receptors in the proteasome; S5a and hRpn13
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/23290100
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Modification by single ubiquitin moieties rather than polyubiquitination is sufficient for proteasomal processing of the p105 NF-κB precursor
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/23290100
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1016/J.TIBS.2012.11.009
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3560967
OpenCitations bibliographic resource ID
3560967
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3560967
PMC publication ID
3557657
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3560967
PubMed publication ID
23290100
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3560967
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