Výsledky vyhledávání - "Abuduaini Abulimiti"

Akademický článek

MAPK target sites of eyes absent are not required for eye development or survival in Drosophila.

Autor: Barbara Jusiak, Abuduaini Abulimiti, Nele Haelterman, Rui Chen, Graeme Mardon

Publikováno v: PLoS ONE, Vol 7, Iss 12, p e50776 (2012)

Eyes absent (Eya) is a highly conserved transcription cofactor and protein phosphatase that plays an essential role in eye development and survival in Drosophila. Ectopic eye induction assays using cDNA transgenes have suggested that mitogen activate

Externí odkaz: https://doaj.org/article/80dba8d86508409f9db50db75e3b4b0a

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A Dual Role for the N-terminal Region of Mycobacterium tuberculosis Hsp16.3 in Self-oligomerization and Binding Denaturing Substrate Proteins

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

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Mycobacterium tuberculosis Hsp16.3 Nonamers are Assembled and Re-assembled via Trimer and Hexamer Intermediates

Autor: Xinmiao Fu, Liangcai Gu, Zengyi Chang, Abuduaini Abulimiti, Xiuguang Feng

Publikováno v: Journal of Molecular Biology. 326:1013-1023

Hsp16.3, a small heat shock protein from Mycobacterium tuberculosis proposed to form specific trimer-of-trimers structures, acts as a molecular chaperone in vitro. The assembly and re-assembly mechanisms of this oligomeric protein were studied and co

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f1843aa2dfa7b797f3c5d1dbe458267e
https://doi.org/10.1016/s0022-2836(03)00018-4

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[Untitled]

Autor: Z. Chang, Abuduaini Abulimiti

Publikováno v: Biochemistry (Moscow). 68:269-274

Hsp16.3, a small heat shock protein from Mycobacterium tuberculosis proposed to form specific trimer-of-trimers structures, acts as a molecular chaperone in vitro. The assembly mechanisms of this oligomeric protein were studied using in vitro transcr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::174bd5e75278f39bdaa01e19f730c558
https://doi.org/10.1023/a:1023098015504

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MAPK Target Sites of Eyes Absent Are Not Required for Eye Development or Survival in Drosophila

Autor: Rui Chen, Graeme Mardon, Nele A Haelterman, Abuduaini Abulimiti, Barbara Jusiak

Publikováno v: PLoS ONE
PLoS ONE, Vol 7, Iss 12, p e50776 (2012)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::58c2a35b15ded0cb569c61e28cbaddbe
http://europepmc.org/articles/PMC3520925

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Inter-subunit cross-linking suppressed the dynamic oligomeric dissociation of Mycobacterium tuberculosis Hsp16.3 and reduced its chaperone activity

Autor: Abuduaini Abulimiti, Zengyi Chang, Xinmiao Fu, Wangwang Jiao

Publikováno v: Biochemistry. Biokhimiia. 69(5)

Small heat shock proteins (sHsps) usually exist as dynamic oligomers and oligomeric dissociation was believed to be a prerequisite for their chaperone activities. The truth of this hypothesis was verified in our present study on Hsp16.3, one member o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3306b8df51f66992395c5fb85b080392
https://pubmed.ncbi.nlm.nih.gov/15193130

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Reversible methionine sulfoxidation of Mycobacterium tuberculosis small heat shock protein Hsp16.3 and its possible role in scavenging oxidants

Autor: Xiaolei Qiu, Abuduaini Abulimiti, Zengyi Chang, Yang Liu, Jing Chen

Publikováno v: Biochemical and biophysical research communications. 305(1)

Mycobacterium tuberculosis (TB) small heat shock protein Hsp16.3 was found to be a major membrane protein that is most predominantly expressed under oxidative stress and is localized to the thickened cell envelope. Gene knock-out studies indicate tha

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::38d5e89a97891dfa66d68aeb60290517
https://pubmed.ncbi.nlm.nih.gov/12732200

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Monodisperse Hsp16.3 nonamer exhibits dynamic dissociation and reassociation, with the nonamer dissociation prerequisite for chaperone-like activity

Autor: Wen Li, Liangcai Gu, Abuduaini Abulimiti, Zengyi Chang

Publikováno v: Journal of molecular biology. 319(2)

Small heat-shock proteins (sHsps) of various origins exist commonly as oligomers and exhibit chaperone-like activities in vitro. Hsp16.3, the sHsp from Mycobacterium tuberculosis, was previously shown to exist as a monodisperse nonamer in solution wh

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c359bb80175e39f0ef0c419ab459b299
https://pubmed.ncbi.nlm.nih.gov/12051925

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The reassembling process of the nonameric Mycobacterium tuberculosis small heat-shock protein Hsp16.3 occurs via a stepwise mechanism

Autor: Xiuguang FENG, Sufang HUANG, Xinmiao FU, Abuduaini ABULIMITI, Zengyi CHANG

Conditions are reported under which the reassembled intermediates of the heat-shock protein Hsp16.3 after being denatured in 8M urea were detected by mainly using urea-gradient PAGE (with modifications) and urea-denaturing pore-gradient PAGE. Hsp16.3

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::95188453d95dc90317ed40147fa0e9fa
https://europepmc.org/articles/PMC1222482/

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