Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Wangwang, Jiao"'
Publikováno v:
Biochemistry (00062979). May2004, Vol. 69 Issue 5, p552-557. 6p.
Publikováno v:
Journal of Molecular Evolution. Mar2006, Vol. 62 Issue 3, p257-266. 10p. 3 Diagrams, 1 Chart, 2 Graphs.
Autor:
Dorota B Pawlak, Wangwang Jiao, Karen A. Weikel, James T. Handa, Michael Brownlee, Fu Shang, Tomoaki Uchiki, Andrea Caceres, Allen Taylor, Ram H. Nagaraj
Publikováno v:
Aging Cell. 11:1-13
Epidemiologic studies indicate that the risks for major age-related debilities including CHD, diabetes, and age-related macular degeneration (AMD) are diminished in people who consume lower glycemic index (GI) diets but lack of a unifying physiobioch
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::856ed6d14807f59ee579aad355dd0975
https://doi.org/10.1111/j.1474-9726.2011.00752.x
https://doi.org/10.1111/j.1474-9726.2011.00752.x
Publikováno v:
Science in China Series C: Life Sciences. 52:997-1002
Many proteins exist as homo-oligomers in living organisms wherein the change of oligomeric status apparently serves as an effective means for modulating their biological activities. We have previously reported that the homo-decameric RbsD from Escher
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0e9156e9f4ab46af6f264d45411df884
https://doi.org/10.1007/s11427-009-0141-1
https://doi.org/10.1007/s11427-009-0141-1
Autor:
Jing Ma, Mengdie Hu, Pulin Li, Wangwang Jiao, Weizhe Hong, Zengyi Chang, Mengding Qian, Shihu Sun
Publikováno v:
Biochemical Journal. 410:63-70
sHSP (small heat-shock protein) IbpB (inclusion-body-binding protein B) from Escherichia coli is known as an ATP-independent holding chaperone which prevents the insolubilization of aggregation-prone proteins by forming stable complexes with them. It
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::456f481a0f33979d5a3ffe1177fdf1cc
https://doi.org/10.1042/bj20071120
https://doi.org/10.1042/bj20071120
Publikováno v:
Protein Science. 15:1441-1448
Many cellular proteins exist as homo-oligomers. The mechanism of the assembly process of such proteins is still poorly understood. We have previously observed that Hsp16.3, a protein exhibiting chaperone-like activity, undergoes stepwise disassembly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f0613b8a9a5b5cc3295bd818b42ee9a
https://doi.org/10.1110/ps.062175806
https://doi.org/10.1110/ps.062175806
Autor:
Wangwang Jiao, Dan Shen, Bin Xia, Xinmiao Fu, Chong Liu, Weizhe Hong, Zengyi Chang, Jicheng Hu, Junrui Zhang
Publikováno v:
Journal of Biological Chemistry. 280:27029-27034
The extremely acidic environment of the mammalian stomach, with a pH range usually between 1 and 3, represents a stressful challenge for enteric pathogenic bacteria such as Escherichia coli before they enter into the intestine. The hdeA gene of E. co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b6202c18980dcb7a51b466eee227653a
https://doi.org/10.1074/jbc.m503934200
https://doi.org/10.1074/jbc.m503934200
Publikováno v:
Biochemical and Biophysical Research Communications. 330:1055-1061
Hsp16.3, a small heat shock protein from Mycobacterium tuberculosis (MTB), was originally identified as an immuno-dominant antigen and later found to be a major membrane protein. In vitro studies show that Hsp16.3 exists as nonamers and undergoes dyn
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e83b6a844b56958547503322d9e0c1e6
https://doi.org/10.1016/j.bbrc.2005.03.092
https://doi.org/10.1016/j.bbrc.2005.03.092
Publikováno v:
Journal of Molecular Biology. 347:871-884
Small heat shock proteins (sHSPs) represent an abundant and ubiquitous family of molecular chaperones that are believed to prevent irreversible aggregation of other cellular proteins under stress conditions. One of the most prominent features of sHSP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::66a4da1f9322e28f9e033b3aef6f9d0f
https://doi.org/10.1016/j.jmb.2005.01.029
https://doi.org/10.1016/j.jmb.2005.01.029
Autor:
Abuduaini Abulimiti, Yang Song, Chong Liu, Yang Cao, Wangwang Jiao, Xuefeng Zhang, Xinmiao Fu, Hui Zhang, Zengyi Chang
Publikováno v:
Journal of Biological Chemistry. 280:6337-6348
The N-terminal regions, which are highly variable in small heat-shock proteins, were found to be structurally disordered in all the 24 subunits of Methanococcus jannaschii Hsp16.5 oligomer and half of the 12 subunits of wheat Hsp16.9 oligomer. The st
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62012970feb1b3e477b04f9fad2fa4ac
https://doi.org/10.1074/jbc.m406319200
https://doi.org/10.1074/jbc.m406319200