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Cbl-ArgBP2 complex mediates ubiquitination and degradation of c-Abl
scientific article
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instance of
scholarly article
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title
Cbl-ArgBP2 complex mediates ubiquitination and degradation of c-Abl
(English)
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main subject
cell biology
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protein ubiquitination
1 reference
based on heuristic
inferred from title
author
Philippe Soubeyran
object named as
Philippe Soubeyran
series ordinal
1
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Ana Barac
object named as
Ana Barac
series ordinal
2
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Ivan Đikić
object named as
Ivan Dikic
series ordinal
4
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author name string
Iwona Szymkiewicz
series ordinal
3
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language of work or name
English
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publication date
15 February 2003
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number of pages
6
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based on heuristic
inferred from page(s)
published in
Biochemical Journal
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volume
370
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issue
Pt 1
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page(s)
29-34
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cites work
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ArgBP2, a multiple Src homology 3 domain-containing, Arg/Abl-interacting protein, is phosphorylated in v-Abl-transformed cells and localized in stress fibers and cardiocyte Z-disks
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The complete coding sequence of arg defines the Abelson subfamily of cytoplasmic tyrosine kinases
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Negative regulation of Lck by Cbl ubiquitin ligase
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The endophilin-CIN85-Cbl complex mediates ligand-dependent downregulation of c-Met
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Cbl-CIN85-endophilin complex mediates ligand-induced downregulation of EGF receptors
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The non-receptor tyrosine kinase Syk is a target of Cbl-mediated ubiquitylation upon B-cell receptor stimulation.
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Regulation of Cbl phosphorylation by the Abl tyrosine kinase and the Nck SH2/SH3 adaptor
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CIN85/CMS family of adaptor molecules
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Autoinhibition of c-Abl
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Activated c-Abl is degraded by the ubiquitin-dependent proteasome pathway
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Ubiquitin and the control of protein fate in the secretory and endocytic pathways
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12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1042/BJ20021539
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PMC publication ID
1223168
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PubMed publication ID
12475393
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ResearchGate publication ID
10997492
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