نتایج جستجو برای: heat shock protein 27

تعداد نتایج: 1616333  

2015
Ponni Rajagopal Eric Tse Andrew J Borst Scott P Delbecq Lei Shi Daniel R Southworth Rachel E Klevit Volker Dötsch

Small heat shock proteins (sHSPs) are essential 'holdase' chaperones that form large assemblies and respond dynamically to pH and temperature stresses to protect client proteins from aggregation. While the alpha-crystallin domain (ACD) dimer of sHSPs is the universal building block, how the ACD transmits structural changes in response to stress to promote holdase activity is unknown. We found t...

Journal: :Journal of cell science 1989
J F Beaulieu A P Arrigo R M Tanguay

The intracellular localization and expression of hsp27 (heat-shock protein 27) were investigated by cellular fractionation and immunofluorescence microscopy in Drosophila S3 cells. In unstressed cells, hsp27 is expressed in only 2% of the cells, whereas following heat shock, during recovery or after induction by ecdysone, the protein is detected in all cells. Under all these conditions, hsp27 a...

Journal: :FEMS microbiology letters 2000
U Meyer C Monnerjahn D Techel L Rensing

The interaction of the heat shock factor (HSF) with the heat shock element (HSE) was determined by a non-radioactive electrophoretic mobility shift assay, in order to analyze HSF regulation in Neurospora crassa. HSF binds to HSE under normal, non-stress conditions and is thus constitutively trimerized. Upon heat shock, the HSF-HSE complex shows a retarded mobility. This was also observed in Sac...

Journal: :Annual review of physiology 1999
M E Feder G E Hofmann

Molecular chaperones, including the heat-shock proteins (Hsps), are a ubiquitous feature of cells in which these proteins cope with stress-induced denaturation of other proteins. Hsps have received the most attention in model organisms undergoing experimental stress in the laboratory, and the function of Hsps at the molecular and cellular level is becoming well understood in this context. A com...

2017
Zhi-Wei Kang Fang-Hua Liu Xiang Liu Wen-Bo Yu Xiao-Ling Tan Shi-Ze Zhang Hong-Gang Tian Tong-Xian Liu

Aphidius gifuensis is one of the most important aphid natural enemies and has been successfully used to control Myzys persicae and other aphid species. High temperature in summer is one of the key barriers for the application of A. gifuensis in the field and greenhouse. In this work, we investigated the biological performance of A. gifuensis and the response of heat-shock proteins and antioxida...

2015
Bhavna Daswani Manoj Kumar Gupta Shubhangi Gavali Meena Desai Gajanan J. Sathe Anushree Patil Priyanka Parte Ravi Sirdeshmukh M. Ikram Khatkhatay

Peripheral monocytes, precursors of osteoclasts, have emerged as important candidates for identifying proteins relevant to osteoporosis, a condition characterized by low Bone Mineral Density (BMD) and increased susceptibility for fractures. We employed 4-plex iTRAQ (isobaric tags for relative and absolute quantification) coupled with LC-MS/MS (liquid chromatography coupled with tandem mass spec...

2009
Fukumi Hiragami Hirotoshi Motoda Toshiaki Takezawa Chiyuki Takabayashi Shigeki Inoue Yuji Wakatake Yoshio Kano

The aim of this study was to determine the optimal heat treatment conditions for enhancement of pressed silk-mediated 3D-like proliferation of normal human dermal fibroblasts, as well as to determine the responses to heat shock of cells and intracellular signaling pathways. The beginning of 3D-like pattern formation of cells was observed in the second week after the start of the experiment. The...

2015
Fumitaka Kawakami Takafumi Ichikawa

There is now a considerable body of experimental evidence that Parkinson's disease arises through physiological interaction of causative molecules, leading to tau pathology. In this review, we discuss the physiological role of α-synuclein and LRRK2 in the abnormal phosphorylation of tau. In addition, as recent reports have indicated that heat shock proteins- (HSPs-) inducing drugs can help to a...

Journal: :Journal of molecular biology 2004
Martin Haslbeck Athanasios Ignatiou Helen Saibil Sonja Helmich Elke Frenzl Thusnelda Stromer Johannes Buchner

Small heat-shock proteins (Hsps) are ubiquitous molecular chaperones which prevent the unspecific aggregation of non-native proteins. For Hsp26, a cytosolic sHsp from of Saccharomyces cerevisiae, it has been shown that, at elevated temperatures, the 24 subunit complex dissociates into dimers. This dissociation is required for the efficient interaction with non-native proteins. Deletion analysis...

Journal: :Acta biochimica et biophysica Sinica 2014
Xinmiao Fu

Small heat-shock proteins (sHSPs) are ubiquitous ATP-independent molecular chaperones that play crucial roles in protein quality control in cells. They are able to prevent the aggregation and/or inactivation of various non-native substrate proteins and assist the refolding of these substrates independently or under the help of other ATP-dependent chaperones. Substrate recognition and binding by...

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