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Heat shock protein

About: Heat shock protein is a research topic. Over the lifetime, 20701 publications have been published within this topic receiving 1040593 citations. The topic is also known as: Heat-Shock Proteins & heat shock protein.


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Journal ArticleDOI
TL;DR: A comparison of different Organisms and Stages of Development and Heat-Induced Lethality and Thermotolerance and the role of RNA Processing are presented.
Abstract: PERSPECTIVES AND SUMMARY . . . . . 1151 CHARACTERIZATION OF THE RESPONSE 1153 Comparison: Different Organisms and Stages of Development. ll53 The Proteins Induced by Heat ... . 1155 RNAs Induced by Heat 1167 OTHER INDUCTIONS OF HSPs 1168 Developmental Inductions .. . ... . . . . . . .. .. .. . ... ...... . .... . .. . . . 1168 Other Inducers 1 1 69 Is There a Common Mechanism? ........ ... 1170 GENOME ORGANIZATION 1172 REGULATION OF THE RESPONSE 1173 Transcription 1173 Translation . . . . .. ..... ......... .. . . .. .. .. .... . .. ...... . . . .. . . . . .. .. .. . .. .. .. . . . . . . . . . 1177 RNA Processing 1178 TOLERANCE TO HEAT AND OTHER FORMS OF STRESS . . . 1179 Heat-Induced Lethality and Thermotolerance . . . . . . . . . . . . . 1179 Phenocopies 1182 CONCLUDING REMARKS 1184

4,655 citations

Journal ArticleDOI
24 May 1991-Science
TL;DR: This method was used to delineate coiled-coil domains in otherwise globular proteins, such as the leucine zipper domains in transcriptional regulators, and to predict regions of discontinuity within coiled -coil structures,such as the hinge region in myosin.
Abstract: The probability that a residue in a protein is part of a coiled-coil structure was assessed by comparison of its flanking sequences with sequences of known coiled-coil proteins. This method was used to delineate coiled-coil domains in otherwise globular proteins, such as the leucine zipper domains in transcriptional regulators, and to predict regions of discontinuity within coiled-coil structures, such as the hinge region in myosin. More than 200 proteins that probably have coiled-coil domains were identified in GenBank, including alpha- and beta-tubulins, flagellins, G protein beta subunits, some bacterial transfer RNA synthetases, and members of the heat shock protein (Hsp70) family.

4,040 citations

Journal ArticleDOI
TL;DR: This work discloses that expression of Hsps can occur in nature, all species have hsp genes but they vary in the patterns of their expression, and Hsp expression can be correlated with resistance to stress, and species' thresholds for HSP expression are correlated with levels of stress that they naturally undergo.
Abstract: 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 complementary focus is now emerging on the Hsps of both model and nonmodel organisms undergoing stress in nature, on the roles of Hsps in the stress physiology of whole multicellular eukaryotes and the tissues and organs they comprise, and on the ecological and evolutionary correlates of variation in Hsps and the genes that encode them. This focus discloses that (a) expression of Hsps can occur in nature, (b) all species have hsp genes but they vary in the patterns of their expression, (c) Hsp expression can be correlated with resistance to stress, and (d) species' thresholds for Hsp expression are correlated with levels of stress that they naturally undergo. These conclusions are now well established and may require little additional confirmation; many significant questions remain unanswered concerning both the mechanisms of Hsp-mediated stress tolerance at the organismal level and the evolutionary mechanisms that have diversified the hsp genes.

3,841 citations

Journal ArticleDOI
TL;DR: C crop heat tolerance can be enhanced by preconditioning of plants under different environmental stresses or exogenous application of osmoprotectants such as glycinebetaine and proline, and by traditional and contemporary molecular breeding protocols and transgenic approaches.

3,037 citations

Journal ArticleDOI
TL;DR: This work has shown that for specific tasks the Hsp70 cycle is coupled to the action of other chaperones, such as Hsp90 and Hsp100, and this ATPase cycle is controlled by co-chaperones of the family of J-domain proteins, which target H Sp70s to their substrates, and by nucleotide exchange factors, which determine the lifetime of the HSp70-substrate complex.
Abstract: Hsp70 proteins are central components of the cellular network of molecular chaperones and folding catalysts. They assist a large variety of protein folding processes in the cell by transient association of their substrate binding domain with short hydrophobic peptide segments within their substrate proteins. The substrate binding and release cycle is driven by the switching of Hsp70 between the low-affinity ATP bound state and the high-affinity ADP bound state. Thus, ATP binding and hydrolysis are essential in vitro and in vivo for the chaperone activity of Hsp70 proteins. This ATPase cycle is controlled by co-chaperones of the family of J-domain proteins, which target Hsp70s to their substrates, and by nucleotide exchange factors, which determine the lifetime of the Hsp70-substrate complex. Additional co-chaperones fine-tune this chaperone cycle. For specific tasks the Hsp70 cycle is coupled to the action of other chaperones, such as Hsp90 and Hsp100.

2,564 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023671
2022856
2021568
2020597
2019631
2018587