HUGO ID Detailed Result 5232


HUGO ID 5232
Symbol HSPA1A
Name heat shock 70kDa protein 1A
#Occurrence 69
#Paper 5

 


PMID Match String Actual String Score Flanking text Edited by Edit
15341181HSPHSP1.4genes termed vitagenes and including among others members of the HSP system such as HSP70 and HSP32 to detect and control 
15341181HSP70HSP701.4including among others members of the HSP system such as HSP70 and HSP32 to detect and control diverse forms of stress 
16909005HSP70HSP701.2acts potently to increase expression of heat shock proteins including HSP70 
16909005HSP70HSP701.2HSP70 immunoreactivity was increased in lumbar spinal cord neurons of celastrol-treated 
17015226HSPHSPs0.6examined the protein folding chaperone machinery the heat-shock proteins (HSPs), HSPs in the context of disease 
17015226HSPHSPs0.6Paradoxically some HSPs such as _amp_#x3b1 B-crystallin and Hsp27 are elevated in the 
17015226HSP70Hsp700.6Hsp70 Hsp40 and Hsp90 are also elevated but only in the 
17015226HSPHSPs0.6Mutant SOD1-mediated depletion of HSPs is a plausible possibility given that Hsp70 and Hsp25 preferentially 
17015226HSP70Hsp700.6SOD1-mediated depletion of HSPs is a plausible possibility given that Hsp70 and Hsp25 preferentially bind mutant SOD1 ( Okado-Matsumoto and Fridovich 
17015226HSPHSPs0.6Expression of several different HSPs (Hsp70, Hsp70 Hsp40 Hsp27 in cultured cells and primary motor 
17015226HSP70Hsp700.6Expression of several different HSPs (Hsp70, Hsp70 Hsp40 Hsp27 in cultured cells and primary motor neurons decreases 
17015226HSP70Hsp700.6Unfortunately applying this strategy in vivo by increased expression of Hsp70 in four different mutant SOD1 mouse lines did not ameliorate 
17015226HSPHSP0.6arimoclomol a drug which induces the phosphorylation-mediated activation of the HSP inducing factor HSF-1 thereby leading to increased levels of Hsp70 
17015226HSP70Hsp700.6HSP inducing factor HSF-1 thereby leading to increased levels of Hsp70 and Hsp90 in spinal cords ( Kieran et_amp_#xa0 al. 2004 
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 
17582695HSPHSPs0.9their association with variable levels of heat shock proteins (HSPs) HSPs 50 
17582695HSPHSPs0.9HSPs may have a role in postulated VN autoimmune disorders 51 
15341181hsp 70hsp701.0uries brain cells have evolved integrated responses the so called longevity assurance processes composed of several genes termed vitagenes and including among others members of the hsp system such as hsp70 and hsp32 to detect and control diverse forms of stress.  
16909005hsp 70hsp701.0hsp70 immunoreactivity was increased in lumbar spinal cord neurons of celastrol treated g93a mice.  
17015226hsp 70hsp701.0hsp70 hsp40 and hsp90 are also elevated but only in the spinal cords of hsod1 g85r mice liu et_amp_#xa0;al. 2005 vleminckx et_amp_#xa0;al. 2002 and wang et_amp_#xa0;al. 2003 .  
17015226hsp 70hsp701.0mutant sod1 mediated depletion of hsps is a plausible possibility given that hsp70 and hsp25 preferentially bind mutant sod1 okado matsumoto and fridovich 2002 .  
17015226hsp 70hsp701.0expression of several different hsps hsp70 hsp40 hsp27 in cultured cells and primary motor neurons decreases aggregate content and apoptosis and improves axonal outgrowth bruening et_amp_#xa0;al. 1999 patel et_amp_#xa0;al. 2005 and takeuchi e 
17015226hsp 70hsp701.0unfortunately applying this strategy in vivo by increased expression of hsp70 in four different mutant sod1 mouse lines did not ameliorate disease or pathology liu et_amp_#xa0;al. 2005 .  
17015226hsp 70hsp701.0a small cohort of hsod1 g93a mice after treatment with arimoclomol a drug which induces the phosphorylation mediated activation of the hsp inducing factor hsf 1 thereby leading to increased levels of hsp70 and hsp90 in spinal cords kieran et_amp_#xa0;al. 2004 .  
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 .