Proteomics

Dataset Information

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Mapping of a N-terminal alpha-helix domain required for human PINK1 stabilisation, Serine228 autophosphorylation and activation in cells


ABSTRACT: Comparative hydrogen deuterium exchange mass spectrometry of WT and I507A mutant for above titled manuscript.

INSTRUMENT(S): Synapt MS

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: James Ault  

LAB HEAD: Miratul Muqit

PROVIDER: PXD030382 | Pride | 2022-02-17

REPOSITORIES: Pride

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Publications


Autosomal recessive mutations in the <i>PINK1</i> gene are causal for Parkinson's disease (PD). PINK1 encodes a mitochondrial localized protein kinase that is a master-regulator of mitochondrial quality control pathways. Structural studies to date have elaborated the mechanism of how mutations located within the kinase domain disrupt PINK1 function; however, the molecular mechanism of PINK1 mutations located upstream and downstream of the kinase domain is unknown. We have employed mutagenesis st  ...[more]

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