Topic
HSPA1B
About: HSPA1B is a research topic. Over the lifetime, 379 publications have been published within this topic receiving 24039 citations. The topic is also known as: Heat shock 70 kDa protein 1 & heat shock 70kDa protein 1B.
Papers published on a yearly basis
Papers
TL;DR: Analysis of HSF cDNA clones from many species has defined structural and regulatory regions responsible for the inducible activities of the conserved heat shock transcription factor.
Abstract: Organisms respond to elevated temperatures and to chemical and physiological stresses by an increase in the synthesis of heat shock proteins. The regulation of heat shock gene expression in eukaryotes is mediated by the conserved heat shock transcription factor (HSF). HSF is present in a latent state under normal conditions; it is activated upon heat stress by induction of trimerization and high-affinity binding to DNA and by exposure of domains for transcriptional activity. Analysis of HSF cDNA clones from many species has defined structural and regulatory regions responsible for the inducible activities. The heat stress signal is thought to be transduced to HSF by changes in the physical environment, in the activity of HSF-modifying enzymes, or by changes in the intracellular level of heat shock proteins.
1,275 citations
Book•
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24 Jun 1991
TL;DR: The heat shock-Induced changes of Cell Ultrastructure, Chromatin Structure, Transcription and Pre-mRNP Processing, and Cell Cycle and DNA Synthesis led to the development of HSP-Coding Genes.
Abstract: INTRODUCTION: HISTORICAL ROOTS. STRESS PROTEINS and GENES. Inducers: Heat Shock and Chemical Stressors. Heat Shock Proteins. HSP-Coding Genes. The Glucose-Regulated Proteins (GRP). RNAs as Heat Shock Products. Gene Technology and Functional Analyses of hs Genes. The Heat Shock Transcription Factor. Control of HSP Synthesis. PROGRAMMING of CELLULAR ACTIVITIES. Chromatin Structure, Transcription and Pre-mRNP Processing. Synthesis and Degradation of Ribosomes. Translational Control. Modification and Degradation of Proteins. Recovery of Gene Expression. Heat Shock-Induced Changes of Cell Ultrastructure. Cell Cycle and DNA Synthesis. Intracellular Localization of Heat Shock Proteins. Induced Thermotolerance. Heat Shock Induced Developmental Effects. Hyperthermia and Virus Multiplication. Hyperthermic Treatment of Cancer.
639 citations
TL;DR: There is increasing evidence that the sequestration of the DnaK chaperone system through binding to misfolded proteins is a direct determinant of the modulation of the heat shock genes expression.
528 citations
TL;DR: Human HSF1 expressed in Xenopus oocytes does not bind DNA, but derepression of DNA-binding activity, as well as oligomerization of HSF 1 occurs during heat treatment at the same temperature at which hsp gene expression is induced in this organism, suggesting that a conserved Xenopus protein(s) plays a role in this regulation.
Abstract: Transcriptional activity of heat shock (hsp) genes is controlled by a heat-activated, group-specific transcription factor(s) recognizing arrays of inverted repeats of the element NGAAN. To date genes for two human factors, HSF1 and HSF2, have been isolated. To define their properties as well as the changes they undergo during heat stress activation, we prepared polyclonal antibodies to these factors. Using these tools, we have shown that human HeLa cells constitutively synthesize HSF1, but we were unable to detect HSF2. In unstressed cells HSF1 is present mainly in complexes with an apparent molecular mass of about 200 kDa, unable to bind to DNA. Heat treatment induces a shift in the apparent molecular mass of HSF1 to about 700 kDa, concomitant with the acquisition of DNA-binding ability. Cross-linking experiments suggest that this change in complex size may reflect the trimerization of monomeric HSF1. Human HSF1 expressed in Xenopus oocytes does not bind DNA, but derepression of DNA-binding activity, as well as oligomerization of HSF1, occurs during heat treatment at the same temperature at which hsp gene expression is induced in this organism, suggesting that a conserved Xenopus protein(s) plays a role in this regulation. Inactive HSF1 resides in the cytoplasm of human cells; on activation it rapidly translocates to a soluble nuclear fraction, and shortly thereafter it becomes associated with the nuclear pellet. On heat shock, activatable HSF1, which might already have been posttranslationally modified in the unstressed cell, undergoes further modification. These different process provide multiple points of regulation of hsp gene expression.
491 citations
Book•
6 Dec 2011
TL;DR: Heat Shock Proteins as Virulence Factors of Pathogens as Antigens of Bacterial and Parasitic Pathogens and stress-Induced Protein in Immune Response to Cancer are described.
Abstract: List of Contents.- Basic Features of Heat Shock Proteins.- Heat Shock Proteins hsp60 and hsp70: Their Roles in Folding, Assembly, and Membrane Translocation of Proteins.- Response of Mammalian Cells to Metabolic Stress Changes in Cell Physiology and Structure/Function of Stress Proteins.- Heat Shock Protein Genes and the Major Histocompatibility Complex.- Heat Shock Protein Functions Related to Immunity.- BiP-A Heat Shock Protein Involved in. Immunoglobulin Chain Assembly.- A Role for Heat Shock Proteins in Antigen Processing and Presentation.- Heat Shock Proteins and Inflammation.- Heat Shock Proteins as Antigens.- Stress-Induced Proteins in Immune Response to Cancer.- Heat Shock Proteins as Virulence Factors of Pathogens.- Heat Shock Proteins as Antigens of Bacterial and Parasitic Pathogens.- Stress Proteins, Autoimmunity, and Autoimmune Disease.- Gamma/Delta T Lymphocytes and Heat Shock Proteins.
473 citations
Related Topics (5)
Performance Metrics
| Year | Papers |
|---|---|
| 2021 | 6 |
| 2020 | 1 |
| 2019 | 3 |
| 2018 | 2 |
| 2017 | 4 |
| 2016 | 4 |