SCOPUS 정보 검색 플랫폼

Volumn 118, Issue , 2013, Pages 68-73

Conversion of natively unstructured α-synuclein to its α-helical conformation significantly attenuates production of reactive oxygen species

(6) Zhou, Binbin a Hao, Yuanqiang a Wang, Chengshan b Li, Ding a Liu, You Nian a Zhou, Feimeng b

a CENTRAL SOUTH UNIVERSITY (China)

b CALIFORNIA STATE UNIVERSITY (United States)

Author keywords

Helix; Synuclein; Binding affinity; Copper; Parkinson's disease; Reactive oxygen species

Indexed keywords

ALPHA SYNUCLEIN; COPPER; HYDROGEN PEROXIDE; HYDROXYL RADICAL; REACTIVE OXYGEN METABOLITE; TRIFLUOROETHANOL;

ALPHA HELIX; AQUEOUS SOLUTION; ARTICLE; BINDING AFFINITY; CIRCULAR DICHROISM; ELECTROCHEMISTRY; NERVE CELL LESION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE; ULTRAVIOLET SPECTROSCOPY;

ALPHA-SYNUCLEIN; AMINO ACID SEQUENCE; COPPER; HUMANS; HYDROGEN PEROXIDE; HYDROXIDES; KINETICS; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY; REACTIVE OXYGEN SPECIES; SOLVENTS; TRIFLUOROETHANOL; WATER;

EID: 84868228227 PISSN: 01620134 EISSN: 18733344 Source Type: Journal
DOI: 10.1016/j.jinorgbio.2012.09.001 Document Type: Article

Times cited : (13)

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