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AMSH is an endosome-associated ubiquitin isopeptidase
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title
AMSH is an endosome-associated ubiquitin isopeptidase
(English)
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main subject
cell biology
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author
John McCullough
object named as
John McCullough
series ordinal
1
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Sylvie Urbé
object named as
Sylvie Urbé
series ordinal
3
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Michael J. Clague
object named as
Michael J Clague
series ordinal
2
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language of work or name
English
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publication date
16 August 2004
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published in
Journal of Cell Biology
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volume
166
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page(s)
487-92
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issue
4
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cites work
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MPN+, a putative catalytic motif found in a subset of MPN domain proteins from eukaryotes and prokaryotes, is critical for Rpn11 function
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Hrs recruits clathrin to early endosomes
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Possible involvement of a novel STAM-associated molecule "AMSH" in intracellular signal transduction mediated by cytokines
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Hrs is associated with STAM, a signal-transducing adaptor molecule. Its suppressive effect on cytokine-induced cell growth
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The Doa4 deubiquitinating enzyme is functionally linked to the vacuolar protein-sorting and endocytic pathways
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Non-traditional functions of ubiquitin and ubiquitin-binding proteins
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Deubiquitinating enzymes--the importance of driving in reverse along the ubiquitin-proteasome pathway
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7 April 2017
A deubiquitinating enzyme UBPY interacts with the Src homology 3 domain of Hrs-binding protein via a novel binding motif PX(V/I)(D/N)RXXKP
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c-Cbl/Sli-1 regulates endocytic sorting and ubiquitination of the epidermal growth factor receptor
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Multiple monoubiquitination of RTKs is sufficient for their endocytosis and degradation
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7 April 2017
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28 September 2017
COP9 signalosome: a multifunctional regulator of SCF and other cullin-based ubiquitin ligases
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28 September 2017
The UIM domain of Hrs couples receptor sorting to vesicle formation
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28 November 2018
Endocytosis of Receptor Tyrosine Kinases Is Driven by Monoubiquitylation, Not Polyubiquitylation
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28 November 2018
Molecular biology. New proteases in a ubiquitin stew
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28 November 2018
Ubiquitin binding proteins protect ubiquitin conjugates from disassembly
1 reference
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PubMed
reference URL
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retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1083/JCB.200401141
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4502335
OpenCitations bibliographic resource ID
4502335
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4502335
PMCID
2172215
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4502335
PubMed ID
15314065
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4502335
ResearchGate publication ID
8397504
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