HUGO ID Detailed Result 5232


HUGO ID 5232
Symbol HSPA1A
Name heat shock 70kDa protein 1A
#Occurrence 104
#Paper 6

 


PMID Match String Actual String Score Flanking text Edited by Edit
11679167HSPHSP0.9the Hsf1p increase the expression of heat shock proteins (HSP) HSP and chaperones Yap1p and Skn7p upregulate antioxidant genes 
15896810HSPHSP3.4In the central nervous system heat shock protein (HSP) HSP synthesis is induced not only after hyperthermia but also following 
15896810HSPHSPs3.7Among the various HSPs HSP32 also known as heme oxygenase I (HO-1), HO-1 has 
15896810HSPHSP3.4the central nervous system (CNS), CNS heat shock protein (HSP) HSP synthesis is induced not only after hyperthermia but also following 
15896810HSPHSP3.4is harmful and can lead to cell death induction of HSP synthesis can result in stress tolerance and cytoprotection in a 
15896810HSPHSP3.4In mammalian cells HSP synthesis is induced not only after hyperthermia but also following 
15896810HSPHSP3.4is harmful and can lead to cell death induction of HSP synthesis can result in stress tolerance and cytoprotection against stress-induced 
15896810HSPHSPs3.7Some of the known HSPs include ubiquitin HSP10 HSP27 HSP32 (or or HO-1 HSP47 HSP60 
15896810HSP70HSP705.5ubiquitin HSP10 HSP27 HSP32 (or or HO-1 HSP47 HSP60 HSC70 HSP70 (or or HSP72 HSP90 and HSP100/105 HSP100 105 
15896810HSP72HSP723.4HSP32 (or or HO-1 HSP47 HSP60 HSC70 HSP70 (or or HSP72 HSP90 and HSP100/105 HSP100 105 
15896810HSP70HSP705.5HSP70 
15896810HSP70HSP705.5family are HSC70 (heat heat shock cognate the constitutive form HSP70 (the the inducible form also referred to as HSP72 GRP75 
15896810HSP72HSP723.4form HSP70 (the the inducible form also referred to as HSP72 GRP75 (a a constitutively expressed glucose-regulated protein found in the 
15896810HSP70HSP705.5After a variety of central nervous system (CNS) CNS insults HSP70 is synthesized at high levels and is present in the 
15896810HSPHSPs3.7shock factors (HSFs) HSFs within the cytosol by dissociating other HSPs that are normally bound to HSF 132 
15896810HSPHSPs3.7different heat shock genes leading to transcription and synthesis of HSPs 
15896810HSP70HSP705.5After heat shock for instance the synthesis of HSP70 increases to a point to where it becomes the most 
15896810HSP70HSP705.5Once synthesized HSP70 binds to denaturated proteins in an ATP-dependent manner 
15896810HSPHSPs3.7In the nervous system HSPs are induced in a variety of pathological conditions including cerebral 
15896810HSPHSPs3.7Expression of the gene encoding HSPs has been found in various cell populations within the nervous 
15896810HSPHSPs3.7HSPs consist of both stress-inducible and constitutive family members 
15896810HSP70HSP705.5gene transfer has become possible to overexpress the gene encoding HSP70 to test directly the hypothesis that stress proteins protects cells 
15896810HSP70HSP705.5from injury and it has been demonstrated that overproduction of HSP70 leads to protection in several different models of nervous system 
15896810HSP70HSP705.5Following focal cerebral ischemia mRNA encoding HSP70 is synthesized in most ischemic cells except in areas of 
15896810HSP70HSP705.5HSP70 proteins is produced mainly in endothelial cells in the core 
15896810HSP70HSP705.5It has been suggested that this neuronal expression of HSP70 outside an infarct can be used to define the ischemic 
15896810HSPHSP3.4of in vitro studies show that both heat shock and HSP overproduction protect CNS cells against both necrosis and apoptosis 
15896810HSP70HSP705.5Transfection of cultured astrocytes with HSP70 protects them from ischemia or glucose deprivation 140 
15896810HSP70HSP705.5HSP70 has been demonstrated to inhibit caspase-3 activation caused by ceramide 
15896810HSP70HSP705.5In addition HSP70 binds to and modulates the function of BAG-1 the bcl-2 
15896810HSPHSP3.4between mechanisms of oxidative and/or and or nitrosative stress and HSP induction 143 
15896810HSP70Hsp705.5cytokine-induced nitrosative stress is associated with an increased synthesis of Hsp70 stress proteins 
15896810HSP70Hsp705.5Increase in Hsp70 protein expression was also found after treatment of cells with 
15896810hsp70hsp705.5(SNP), SNP thus suggesting a role for NO in inducing hsp70 proteins 
15896810HSPHSPs3.7Ubiquitin is one of the smallest HSPs and is expressed throughout brain in response to ischemia 
16043017HSPHSPs1.2HSPs are cellular constituents synthesized by living organisms under stress conditions 
16043017HSPHSPs1.2to stabilize other proteins under stress conditions whereas the high-molecular-weight HSPs normally play roles in protein folding during biosynthesis 83 and 
17191135HSPHsp1.9Hsp response is also involved in cellular homeostasis during various physiological 
17191135HSP70Hsp703.5evidence that different NO-releasing agents can markedly increase HO-1 and Hsp70 in a variety of tissues including brain cells 19 20 
17191135HSP70Hsp703.5both iNOS expression and nitrite levels followed by enhancement of Hsp70 3 20 whereas the modulation of HO-1 mRNA expression by 
17191135HSP70Hsp703.5by triggering expression of cytoprotective genes such as HO-1 and Hsp70 may lead to adaptation and resistance of brain cells to 
17191135HSP70Hsp703.5ubiquitin Hsp10 Hsp27 Hsp32 (or or HO-1 Hsp47 Hsp60 Hsc70 Hsp70 (or or Hsp72 Hsp90 and Hsp100/105 Hsp100 105 
17191135HSP72Hsp722.9Hsp32 (or or HO-1 Hsp47 Hsp60 Hsc70 Hsp70 (or or Hsp72 Hsp90 and Hsp100/105 Hsp100 105 
17191135HSP70Hsp703.5family are Hsc70 (heat heat shock cognate the constitutive form Hsp70 (the the inducible form also referred to as Hsp72 GRP75 
17191135HSP72Hsp722.9form Hsp70 (the the inducible form also referred to as Hsp72 GRP75 (a a constitutively expressed glucose-regulated protein found in the 
17191135HSP70Hsp703.5After a variety of central nervous system (CNS) CNS insults Hsp70 is synthesized at high levels and is present in cytosol 
17191135HSP70Hsp703.5After heat shock synthesis of Hsp70 may increase to become the most abundant protein in the 
17191135HSP70Hsp703.5Once synthesized Hsp70 binds to denaturated proteins in an ATP-dependent manner 
17191135HSP70Hsp703.5cytokine-induced nitrosative stress is associated with an increased synthesis of Hsp70 
17191135HSP70Hsp703.5Increase in Hsp70 protein expression was also found after treatment of cells with 
17191135HSP70Hsp703.5(SNP), SNP thus suggesting a role for NO in inducing Hsp70 proteins 
17191135HSP72Hsp722.9Induction of Hsp72 under stress conditions is often accompanied by the induction of 
17191135HSP72Hsp722.9acting at three different levels (i) i inducing HO-1 and Hsp72 proteins (ii) ii decreasing the neuronal 3-nitrotyrosine levels and therefore 
17191135HSP70Hsp703.5During translocation this proteins interact with Hsp70 ATP-dependent binding and the release of Hsp70 provide the major 
17191135HSP70Hsp703.5proteins interact with Hsp70 ATP-dependent binding and the release of Hsp70 provide the major driving force for complete transport of polypeptides 
17191135HSP70Hsp703.5Although most imported polypeptides are released from soluble Hsp70 however a subset of aggregation-sensitive polypeptides must be transferred from 
17191135HSP70Hsp703.5however a subset of aggregation-sensitive polypeptides must be transferred from Hsp70 to Hsp60 for folding 40 
17191135HSP70Hsp703.5the close functional interaction between this chaperonin system and the Hsp70 system it is likely that up-regulation of Hsp60 may be 
17191135HSP70Hsp703.5from the cellular machinery and recruitment of chaperone pairs including Hsp70 and Hsp27 endowed with anti-apoptotic properties 85 
17191135HSP70Hsp703.5Binding of phosphorylated tau to Hsp70 implies that the complex may be a substrate for the 
17191135HSP70Hsp703.5Together with Hsp70 CHIP can regulate tau ubiquitination and degradation in a cell 
17191135HSP70Hsp703.5Increased levels of CHIP and Hsp70 has ben detected in AD compared with normal controls 86 
17191135HSP70Hsp703.5specifically coimmunoprecipitate with AB has identified chaperone proteins such as Hsp70 and alpha B-crystallin-related small Hsp (Hsp16) Hsp16 
17191135HSPHsp1.9identified chaperone proteins such as Hsp70 and alpha B-crystallin-related small Hsp (Hsp16) Hsp16 
17191135HSP72Hsp722.9showed an increased expression of inducible nitric oxide synthase HO-1 Hsp72 Hsp60 and TrxR 96 
17191135HSP72hsp722.9modulates specific genes in the rat CNS such as the hsp72 gene the gene for the isoform of 14-3-3 protein and 
17496232HSPHSP0.9cardiac muscles (dystrophin) dystrophin and to heat shock protein (HSP) HSP 90 or 70 chaperones ( 79 
17496232HSPHSPs0.9effects include S -nitrosylation and inhibition of caspases increase of HSPs and Bcl-2 and activation of Akt/PKB, Akt PKB which induces 
17496232HSP70Hsp700.9antiapoptotic genes like that of heme oxygenase ( 127 and Hsp70 which protects hepatocytes from apoptosis induced by oxidative and nitrative 
12125078heat shock protein 70heat shock protein 701.0gga was found to induce the expression of heat shock protein 70 as well as thioredoxin which may partly contribute to the protective effect of gga.  
15896810hsp 70hsp701.0some of the known hsps include ubiquitin hsp10 hsp27 hsp32 or ho 1 hsp47 hsp60 hsc70 hsp70 or hsp72 hsp90 and hsp100/105.  
15896810hsp 70hsp701.0hsp70 .  
15896810hsp 70hsp701.0included in this family are hsc70 heat shock cognate the constitutive form hsp70 the inducible form also referred to as hsp72 grp75 a constitutively expressed glucose regulated protein found in the endoplasmic reticulum .  
15896810hsp 70hsp701.0after a variety of central nervous system cns insults hsp70 is synthesized at high levels and is present in the cytosol nucleus and endoplasmic reticulum .  
15896810hsp 70hsp701.0after heat shock for instance the synthesis of hsp70 increases to a point to where it becomes the most abundant single protein in a cell.  
15896810hsp 70hsp701.0once synthesized hsp70 binds to denaturated proteins in an atp dependent manner.  
15896810hsp 70hsp701.0only recently however with the availability of transgenic animals and gene transfer has become possible to overexpress the gene encoding hsp70 to test directly the hypothesis that stress proteins protects cells from injury and it has been demonstrated that overproduction of hsp70 leads to protection in several different models of nervous sy 
15896810hsp 70hsp701.0 to test directly the hypothesis that stress proteins protects cells from injury and it has been demonstrated that overproduction of hsp70 leads to protection in several different models of nervous system injury [136] and [137] .  
15896810hsp 70hsp701.0following focal cerebral ischemia mrna encoding hsp70 is synthesized in most ischemic cells except in areas of very low blood flow because of limited atp levels.  
15896810hsp 70hsp701.0hsp70 proteins is produced mainly in endothelial cells in the core of infarcts in the cells that are most resistant to ischemia in glial cells at the edges of infarcts and in neurons outside the areas of i 
15896810hsp 70hsp701.0it has been suggested that this neuronal expression of hsp70 outside an infarct can be used to define the ischemic penumbras which means the zone of protein denaturation in the ischemic areas [138] .  
15896810hsp 70hsp701.0transfection of cultured astrocytes with hsp70 protects them from ischemia or glucose deprivation [140] .  
15896810hsp 70hsp701.0hsp70 has been demonstrated to inhibit caspase 3 activation caused by ceramide and also affect jun kinase and p38 kinase activation [141] .  
15896810hsp 70hsp701.0in addition hsp70 binds to and modulates the function of bag 1 the bcl 2 binding protein [142] thus modulating some type of apoptosis related cell death.  
15896810hsp 70hsp701.0we have demonstrated in astroglial cell cultures that cytokine induced nitrosative stress is associated with an increased synthesis of hsp70 stress proteins.  
15896810hsp 70hsp701.0increase in hsp70 protein expression was also found after treatment of cells with the no generating compound sodium nitroprusside snp thus suggesting a role for no in inducing hsp70 proteins.  
17191135hsp 70hsp701.0the conception that no and rns can be directly involved in the modulation of ho 1 expression in eukaryotes is based on the evidence that different no releasing agents can markedly increase ho 1 and hsp70 in a variety of tissues including brain cells [ 19 20 ].  
17191135hsp 70hsp701.0in rat glial cells treatment with lipopolysaccaride lps and interferon g ifn g promotes a rapid increase in both inos expression and nitrite levels followed by enhancement of hsp70 [ 3 20 ] whereas the modulation of ho 1 mrna expression by inos derived no following stimulation with lps has also been reported in different brain regions particularly in the hippocampus and substan 
17191135hsp 70hsp701.0taken together these findings point to a possible role of the no as a signaling molecule which by triggering expression of cytoprotective genes such as ho 1 and hsp70 may lead to adaptation and resistance of brain cells to subsequent more severe nitrosative and oxidative stress [ 21 23 ].  
17191135hsp 70hsp701.0some of the known hsps include ubiquitin hsp10 hsp27 hsp32 or ho 1 hsp47 hsp60 hsc70 hsp70 or hsp72 hsp90 and hsp100/105.  
17191135hsp 70hsp701.0included in this family are hsc70 heat shock cognate the constitutive form hsp70 the inducible form also referred to as hsp72 grp75 a constitutively expressed glucose regulated protein found in the endoplasmic reticulum .  
17191135hsp 70hsp701.0after a variety of central nervous system cns insults hsp70 is synthesized at high levels and is present in cytosol nucleus and endoplasmic reticulum [ 24 32 ].  
17191135hsp 70hsp701.0after heat shock synthesis of hsp70 may increase to become the most abundant protein in the cell.  
17191135hsp 70hsp701.0once synthesized hsp70 binds to denaturated proteins in an atp dependent manner.  
17191135hsp 70hsp701.0increase in hsp70 protein expression was also found after treatment of cells with the no generating compound sodium nitroprusside snp thus suggesting a role for no in inducing hsp70 proteins.  
17191135hsp 70hsp701.0during translocation this proteins interact with hsp70 atp dependent binding and the release of hsp70 provide the major driving force for complete transport of polypeptides into the matrix.  
17191135hsp 70hsp701.0although most imported polypeptides are released from soluble hsp70 however a subset of aggregation sensitive polypeptides must be transferred from hsp70 to hsp60 for folding [ 40 ].  
17191135hsp 70hsp701.0owing to the close functional interaction between this chaperonin system and the hsp70 system it is likely that up regulation of hsp60 may be a fundamental site targeted by lac action with consequent restoration of complex iv function under conditions of nitrosative stress dependent pe 
17191135hsp 70hsp701.0onal changes of the protein and ubiquitination clearing misfolded proteins to the proteasome and segregation of tau aggregates from the cellular machinery and recruitment of chaperone pairs including hsp70 and hsp27 endowed with anti apoptotic properties [ 85 ].  
17191135hsp 70hsp701.0binding of phosphorylated tau to hsp70 implies that the complex may be a substrate for the e3 ligase carboxyl terminus of heat shock cognate hsc 70 interacting protein chip [ 86 88 ].  
17191135hsp 70hsp701.0together with hsp70 chip can regulate tau ubiquitination and degradation in a cell culture system [ 87 ].  
17191135hsp 70hsp701.0increased levels of chip and hsp70 has ben detected in ad compared with normal controls [ 86 ].  
17191135hsp 70hsp701.0mass spectrometry analysis of proteins that specifically coimmunoprecipitate with ab has identified chaperone proteins such as hsp70 and alpha b crystallin related small hsp hsp16 .  
17496232hsp 70hsp701.0other antiapoptotic no pathways include s nitrosylation and inactivation of caspases thiols and upregulation of antiapoptotic genes like that of heme oxygenase 127 and hsp70 which protects hepatocytes from apoptosis induced by oxidative and nitrative stress 46 .