Ubiquitin S65 phosphorylation engenders a pH-sensitive conformational switch

Proceedings of the National Academy of Sciences of the United States of America

Volumn 114, Issue 26, 2017, Pages 6770-6775

  Dong, Xu ^a,b   Gong, Zhou ^a,b   Lu, Yun Bi ^c   Liu, Kan ^a,b   Qin, Ling Yun ^a,b   Ran, Meng Lin ^a,b   Zhang, Chang Li ^d   Liu, Zhu ^c   Zhang, Wei Ping ^c   Tang, Chun ^a,b,e  

^a INSTITUTE OF GEOLOGY AND GEOPHYSICS   (China)

^b Chinese Academy of Sciences   (China)

^c ZHEJIANG UNIVERSITY SCHOOL OF MEDICINE   (China)

^d GUILIN MEDICAL UNIVERSITY   (China)

^e HUAZHONG UNIVERSITY OF SCIENCE AND TECHNOLOGY   (China)

Author keywords

Conformational switch; pH sensitivity; Phosphorylation; Protein dynamics; Ubiquitin

Indexed keywords

POLYUBIQUITIN; UBIQUITIN; UBIQUITIN S65; UNCLASSIFIED DRUG;

ALPHA HELIX; ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; FLUORESCENCE RESONANCE ENERGY TRANSFER; MUTANT; NUCLEAR MAGNETIC RESONANCE; PH; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; PROTON TRANSPORT; CHEMISTRY; GENETICS; HUMAN; METABOLISM; PHOSPHORYLATION; PROTEIN DOMAIN;

HUMANS; HYDROGEN-ION CONCENTRATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PHOSPHORYLATION; PROTEIN DOMAINS; UBIQUITIN;

EID: 85021395072     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1705718114     Document Type: Article

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