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Details on Person Proteomic analysis of ubiquitination substrates reveals a CTLH E3 ligase complex-dependent regulation of glycolysis

Class:IdLiteratureReference:9861717
_displayNameProteomic analysis of ubiquitination substrates reveals a CTLH E3 ligase complex-dependent regulation of glycolysis
_timestamp2024-02-21 15:52:26
author[Person:9861728] Maitland, Matthew E R
[Person:9861630] Kuljanin, Miljan
[Person:5607792] Wang, Xu
[Person:9029662] Lajoie, Gilles A
[Person:9861593] Schild-Poulter, Caroline
created[InstanceEdit:9861650] Stephan, Ralf, 2024-02-21
journalFASEB J
pagese21825
pubMedIdentifier34383978
titleProteomic analysis of ubiquitination substrates reveals a CTLH E3 ligase complex-dependent regulation of glycolysis
volume35
year2021
(literatureReference)[RegulationReference:9861794] Negative regulation by 'PolyUb-LDHA [cytosol]' Proteomic analysis of ubiquitination substrates reveals a CTLH E3 ligase complex-dependent regulation of glycolysis
[RegulationReference:9861891] Negative regulation by 'PolyUb-PKM-1 [cytosol]' Proteomic analysis of ubiquitination substrates reveals a CTLH E3 ligase complex-dependent regulation of glycolysis
[Reaction:70510] LDH tetramer oxidises LACT to PYR [Homo sapiens]
[Reaction:71670] Pyruvate kinase dephosphorylates PEP to PYR [Homo sapiens]
[Reaction:71849] LDH tetramer reduces PYR to LACT [Homo sapiens]
[BlackBoxEvent:9861563] CTLH E3 ligase ubiquitinates LDHA [Homo sapiens]
[BlackBoxEvent:9861640] CTLH E3 ligase ubiquitinates PKM-1 [Homo sapiens]
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