نتایج جستجو برای: small heat shock protein shsps

تعداد نتایج: 2156211  

Background: Salinity is a major environmental limiting factor, which affect agricultural production. The two Manilkara seedlings (M. roxburghiana and M. zapota) with high economic importance, could not adapt well to higher soil salinity and little is known about their proteomic mechanisms. Objectives: The mechanisms responsible ...

Journal: :IUBMB life 2003
John A Carver Agata Rekas David C Thorn Mark R Wilson

Small heat-shock proteins (sHsps) and clusterin are molecular chaperones that share many functional similarities despite their lack of significant sequence similarity. These functional similarities, and some differences, are discussed. sHsps are ubiquitous intracellular proteins whereas clusterin is generally found extracellularly. Both chaperones potently prevent the amorphous aggregation and ...

Journal: :Biochimica et biophysica acta 2014
Dezerae Cox John A Carver Heath Ecroyd

Protein homeostasis, or proteostasis, is the process of maintaining the conformational and functional integrity of the proteome. The failure of proteostasis can result in the accumulation of non-native proteins leading to their aggregation and deposition in cells and in tissues. The amyloid fibrillar aggregation of the protein α-synuclein into Lewy bodies and Lewy neuritis is associated with ne...

Journal: :The EMBO journal 2004
Martin Haslbeck Nathalie Braun Thusnelda Stromer Bettina Richter Natascha Model Sevil Weinkauf Johannes Buchner

Small heat shock proteins (sHsps) are ubiquitous molecular chaperones that prevent the unspecific aggregation of proteins. So far, Hsp26 was the only unambiguously identified member of the sHsp family in Saccharomyces cerevisiae. We show here that the sHsp system in the cytosol of S. cerevisiae consists of two proteins, Hsp26 and Hsp42. Hsp42 forms large dynamic oligomers with a barrel-like str...

2008
Tetsuro FUJISAWA Yoichi ASO Yuichi SHIGEOKA Yoji INOKO

Introduction Abrupt increase in environmental temperature induces the expression of a variety of small heat shock protein (sHSP) genes. sHSP is a family of proteins having an αcrystalline domain and suppressing the thermal aggregation of other proteins. sHSP19.9 and sHSP20.8 are two of six sHSPs from the silkworm, Bombyx mori. Each is composed of identical polypeptides, and each of polypeptides...

2012
Nikos Kourtis Vassiliki Nikoletopoulou Nektarios Tavernarakis

the phenomenon of " hormesis ". Exposure of organisms to mild stress fortifies them against subsequent, more severe insults. Yet, the relevant molecular mechanisms remain poorly understood. Although heat stroke is often fatal and survivors may suffer permanent neurologic damage, the mechanisms underlying heat stroke-induced cell and tissue injury remain elusive. To gain insight, we employed the...

2016
Xiaojing Liu Fengfeng Du Naiwei Li Yajun Chang Dongrui Yao

Lotus (Nelumbo Adans) is an aquatic perennial plant that flourished during the middle Albian stage. In this study, we characterized the digital gene expression signatures for China Antique lotus under conditions of heat shock stress. Using RNA-seq technology, we sequenced four libraries, specifically, two biological replicates for control plant samples and two for heat stress samples. As a resu...

2012
WASEEM SAFDAR HAMID MAJEED BARKAT ALI ISHRAT NAVEED

Small heat shock proteins (sHSPs) are the most abundant proteins and considered as Cinderella of molecular chaperon world. The present study is to understand the evolutionary process that led to the diversification of sHSPs specific to plants because of dramatic daily fluctuation in the temperature and other environmental factors which may prompt more efficient chaperon activity of sHSPs. For t...

2015
Kaiming Zhang Anastasia N. Ezemaduka Zhao Wang Hongli Hu Xiaodong Shi Chuang Liu Xinping Lu Xinmiao Fu Zengyi Chang Chang-Cheng Yin

Small heat shock proteins (sHSPs) are molecular chaperones ubiquitously present in all forms of life, but their function mechanisms remain controversial. Here we show by cryo-electron microscopy and single particle 3D reconstruction that, at the low temperatures (4-25°C), CeHSP17 (a sHSP from Caenorhabditis elegans) exists as a 24-subunit spherical oligomer with tetrahedral symmetry. Our studie...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2014
Georg K A Hochberg Heath Ecroyd Cong Liu Dezerae Cox Duilio Cascio Michael R Sawaya Miranda P Collier James Stroud John A Carver Andrew J Baldwin Carol V Robinson David S Eisenberg Justin L P Benesch Arthur Laganowsky

Mammalian small heat-shock proteins (sHSPs) are molecular chaperones that form polydisperse and dynamic complexes with target proteins, serving as a first line of defense in preventing their aggregation into either amorphous deposits or amyloid fibrils. Their apparently broad target specificity makes sHSPs attractive for investigating ways to tackle disorders of protein aggregation. The two mos...

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