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Scientific Reports|October 6, 2015
Hypoionic shock treatment enables aminoglycosides antibiotics to eradicate bacterial persistersLiu Jiafeng, Xinmiao Fu, Zengyi ChangScience China. Life Sciences|January 1, 2016
A reciprocating motion-driven rotation mechanism for the ATP synthaseJiafeng Liu, Xinmiao Fu, Zengyi ChangBiochemical and Biophysical Research Communications|March 27, 2004
Truncated hemoglobin o of Mycobacterium tuberculosis: the oligomeric state change and the interaction with membrane componentsChong Liu, Yuan He, Zengyi ChangBiochemical and Biophysical Research Communications|March 9, 2005
4,4'-Dianilino-1,1'-binaphthyl-5,5'-sulfonate, a novel molecule having chaperone-like activityXinmiao Fu, Xuefeng Zhang, Zengyi ChangProtein Science : a Publication of the Protein Society|May 30, 2006
Stepwise disassembly and apparent nonstepwise reassembly for the oligomeric RbsD proteinYongjun Feng, Wangwang Jiao, Xinmiao Fu, et al.Biochemistry. Biokhimiia|June 15, 2004
Inter-subunit cross-linking suppressed the dynamic oligomeric dissociation of Mycobacterium tuberculosis Hsp16.3 and reduced its chaperone activityXinmiao Fu, Wangwang Jiao, Abuduaini Abulimiti, et al.Journal of Molecular Biology|June 8, 2002
Monodisperse Hsp16.3 nonamer exhibits dynamic dissociation and reassociation, with the nonamer dissociation prerequisite for chaperone-like activityLiangcai Gu, Abuduaini Abulimiti, Wen Li, et al.Biochemical and Biophysical Research Communications|August 14, 2003
Disulfide bonds convert small heat shock protein Hsp16.3 from a chaperone to a non-chaperone: implications for the evolution of cysteine in molecular chaperonesXinmiao Fu, Wen Li, Qilong Mao, et al.Biochemistry. Biokhimiia|October 11, 2005
Chaperone-like activity of Mycobacterium tuberculosis Hsp16.3 does not require its intact (native) structuresXiaoyou Chen, Xinmiao Fu, Yu Ma, et al.Cell Discovery|January 25, 2019
Regrowth-delay body as a bacterial subcellular structure marking multidrug-tolerant persistersJiayu Yu, Yang Liu, Huijia Yin, et al.Pageof 7