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	Small heat-shock proteins function in the insoluble protein complex
	Jiao, WW ; Li, PL ; Zhang, JR ; Zhang, H ; Chang, ZY
	2010-05-11 ; 2010-05-11
关键词	small heat-shock protein molecular chaperone chaperone activity protein aggregation insoluble complex ESCHERICHIA-COLI ALPHA-CRYSTALLIN IN-VIVO MOLECULAR CHAPERONES IBPB AGGREGATION FAMILY HSP26 CLPB THERMOTOLERANCE Biochemistry & Molecular Biology Biophysics
中文摘要	Small heat-shock proteins (sHSPs) represent an abundant and ubiquitous family of molecular chaperones. The current model proposes that sHSPs function to prevent irreversible aggregation of non-native proteins by forming soluble complex. The chaperone activity of sHSPs is usually determined by the capacity to suppress thermally or chemically induced protein aggregation. However, sHSPs were frequently found in the insoluble complex particularly in vivo. In this report, it is clearly revealed that the insoluble sHSP/substrate complex is formed when sHSP is overloaded with non-native substrates, which is the very case under in vivo conditions. The proposal that sHSPs function to prevent the protein aggregation seems misleading. sHSPs appear to promote the elimination of protein aggregates by incorporating into the insoluble protein complex. (c) 2005 Elsevier Inc. All rights reserved.
语种	英语 ; 英语
出版者	ACADEMIC PRESS INC ELSEVIER SCIENCE ; SAN DIEGO ; 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA
内容类型	期刊论文
源URL	[http://hdl.handle.net/123456789/27015]
专题	清华大学
推荐引用方式 GB/T 7714	Jiao, WW,Li, PL,Zhang, JR,et al. Small heat-shock proteins function in the insoluble protein complex[J],2010, 2010.
APA	Jiao, WW,Li, PL,Zhang, JR,Zhang, H,&Chang, ZY.(2010).Small heat-shock proteins function in the insoluble protein complex..
MLA	Jiao, WW,et al."Small heat-shock proteins function in the insoluble protein complex".(2010).

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