Results 11 to 20 of about 73,273 (215)
Hsp70 in Redox Homeostasis [PDF]
Cells, 2022 Cellular redox homeostasis is precisely balanced by generation and elimination of reactive oxygen species (ROS). ROS are not only capable of causing oxidation of proteins, lipids and DNA to damage cells but can also act as signaling molecules to modulate transcription factors and epigenetic pathways that determine cell survival and death.
Hong Zhang, Weibin Gong, Si Wu
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Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes [PDF]
Structure, 2016 Protein misfolding and aggregation are pathological events that place a significant amount of stress on the maintenance of protein homeostasis (proteostasis). For prevention and repair of protein misfolding and aggregation, cells are equipped with robust mechanisms that mainly rely on molecular chaperones.
Thomas Reid, Alderson +2 more
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HSP70 and Genomic Stability [PDF]
Cell Cycle, 2004 The 70 kDa heat shock proteins (HSP70s) were initially identified by their elevated expression following hyperthermic cell stress, however, these highly conserved proteins also protect critical cellular functions from a wider range of important environmental and physiological stresses.
Tej K, Pandita +2 more
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The Effect of Canine Ovariohysterectomy on HSP70 and Anti HSP70 Antibodies
Kafkas Universitesi Veteriner Fakultesi Dergisi, 2013 The present study aimed to determine the effects of ovariohysterectomy on blood serum concentrations of Heat Shock Protein (HSP) 70 and anti-HSP70 antibodies in dogs. For this purpose, 87 female stray dogs were used as the materials. Ten milliliters of blood was taken from the animals preoperatively and on the first day postoperatively.
Murat Yüksel +2 more
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Hsp70 gene association with nuclear speckles is Hsp70 promoter specific [PDF]
Journal of Cell Biology, 2010 Many mammalian genes localize near nuclear speckles, nuclear bodies enriched in ribonucleic acid–processing factors. In this paper, we dissect cis-elements required for nuclear speckle association of the heat shock protein 70 (Hsp70) locus. We show that speckle association is a general property of Hsp70 bacterial artificial chromosome transgenes ...
Hu, Yan, Plutz, Matt, Belmont, Andrew S.
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, 2021 Η πρωτεΐνη θερμικού σοκ Hsp70 (HSPA1A: heat shock πρωτεΐνη οικογένειας A (Hsp70) μέλος 1A) είναι η καλύτερα μελετημένη πρωτεΐνη στην οικογένεια A των Hsp70s. Πρόκειται για μια πρωτεΐνη επιβίωσης και πρωτεΐνη αντι-αποπτωτική, που σχετίζεται με πολλές ασθένειες στον άνθρωπο.
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The anti-inflammatory mechanisms of Hsp70 [PDF]
Frontiers in Immunology, 2012 Immune responses to heat shock proteins (Hsp) develop in virtually all inflammatory diseases; however, the significance of such responses is only now becoming clear. In experimental disease models, Hsp administration can prevent or arrest inflammatory damage, and in initial clinical trials in patients with chronic inflammatory diseases, Hsp peptides ...
Borges, T.J. +6 more
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The HSP70 family and cancer [PDF]
Carcinogenesis, 2013 The HSP70 family of heat shock proteins consists of molecular chaperones of approximately 70kDa in size that serve critical roles in protein homeostasis. These adenosine triphosphatases unfold misfolded or denatured proteins and can keep these proteins in an unfolded, folding-competent state.
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The atheroprotective properties of Hsp70: a role for Hsp70-endothelial interactions? [PDF]
Cell Stress and Chaperones, 2009 Although heat shock (stress) proteins are typically regarded as being exclusively intracellular molecules, it is now apparent that they can be released from cells in the absence of cellular necrosis. We and others have reported the presence of Hsp60 (HSPD1) and Hsp70 (HSPA1A) in the circulation of normal individuals and our finding that increases in ...
A Graham, Pockley +2 more
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HSP70 and HSP90 in neurodegenerative diseases [PDF]
Neuroscience Letters, 2020 Molecular chaperones have a role to stabilize proteins or assist them in reaching their native fold. Heat shock proteins (HSPs) are a family of molecular chaperons that protect proteins from cellular stress during the assembly of protein complexes and also prevent the proteins from aggregation and disassembly.
Abha Gupta +2 more
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