Interaction of α-Synuclein with ATP Synthase: Switching Role from Physiological to Pathological | Zendy

Timir Tripathi | Zendy; Krishnananda Chattopadhyay | Zendy

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Interaction of α-Synuclein with ATP Synthase: Switching Role from Physiological to Pathological

Author(s) -

Timir Tripathi,

Krishnananda Chattopadhyay

Publication year - 2018

Publication title -

acs chemical neuroscience

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.158

H-Index - 69

ISSN - 1948-7193

DOI - 10.1021/acschemneuro.8b00407

Subject(s) - atp synthase , protein subunit , mitochondrion , alpha synuclein , microbiology and biotechnology , biology , lewy body , parkinson's disease , chemistry , biochemistry , enzyme , disease , medicine , pathology , gene

The most abundantly present protein found in Lewy bodies, which is the pathological hallmark of Parkinson's disease, is α-synuclein. Native monomeric α-synuclein is localized within mitochondria, interacts with ATP synthase subunit, and enhances ATP synthase efficiency and mitochondrial function. Recently, an advanced study shows that the interaction of α-synuclein oligomer with ATP synthase switches its role from physiological to pathological, which leads to mitochondrial dysfunction.

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