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Search results 101 to 123 out of 123 for Hspa4

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0.018s
Type Details Score
Publication      
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
Publication      
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
Publication      
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
Publication
First Author: Yang Y
Year: 2022
Journal: Biochim Biophys Acta Mol Basis Dis
Title: SIRT1 attenuates neuroinflammation by deacetylating HSPA4 in a mouse model of Parkinson's disease.
Volume: 1868
Issue: 5
Pages: 166365
HT Experiment
Series Id: GSE32885
Experiment Type: transcription profiling by array
Study Type: WT vs. Mutant
Source: ArrayExpress
Publication
First Author: Kang CM
Year: 2002
Journal: Radiat Res
Title: Hspa4 (HSP70) is involved in the radioadaptive response: results from mouse splenocytes.
Volume: 157
Issue: 6
Pages: 650-5
Publication  
First Author: Wu CY
Year: 2011
Journal: J Biomed Sci
Title: Induction of HSPA4 and HSPA14 by NBS1 overexpression contributes to NBS1-induced in vitro metastatic and transformation activity.
Volume: 18
Pages: 1
Publication
First Author: Ferlin A
Year: 2010
Journal: J Urol
Title: Heat shock protein and heat shock factor expression in sperm: relation to oligozoospermia and varicocele.
Volume: 183
Issue: 3
Pages: 1248-52
Protein Domain
Type: Domain
Description: Human HSPA4 (also known as 70kDa heat shock protein 4, APG-2, HS24/P52, hsp70 RY, and HSPH2) responds to acidic pH stress, is involved in the radioadaptive response, is required for normal spermatogenesis and is overexpressed in hepatocellular carcinoma [, , ]. It participates in a pathway along with NBS1 (Nijmegen breakage syndrome 1, also known as p85 or nibrin), heat shock transcription factor 4b (HDF4b), and HSPA14 (belonging to a different HSP70 subfamily) that induces tumor migration, invasion, and transformation []. HSPA4 expression in sperm was increased in men with oligozoospermia, especially in those with varicocele []. HSPA4 belongs to the 105/110kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family []. HSP105/110s are believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent 'client' proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD) [].This entry represents the N-terminal nucleotide-binding domain of HSPA4.
Publication
First Author: Gu Y
Year: 2019
Journal: Nat Med
Title: Tumor-educated B cells selectively promote breast cancer lymph node metastasis by HSPA4-targeting IgG.
Volume: 25
Issue: 2
Pages: 312-322
Publication
First Author: Otto H
Year: 2005
Journal: Proc Natl Acad Sci U S A
Title: The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex.
Volume: 102
Issue: 29
Pages: 10064-9
Publication
First Author: Wan T
Year: 2004
Journal: Blood
Title: Novel heat shock protein Hsp70L1 activates dendritic cells and acts as a Th1 polarizing adjuvant.
Volume: 103
Issue: 5
Pages: 1747-54
Publication
First Author: Fang H
Year: 2011
Journal: J Biol Chem
Title: Toll-like receptor 4 (TLR4) is essential for Hsp70-like protein 1 (HSP70L1) to activate dendritic cells and induce Th1 response.
Volume: 286
Issue: 35
Pages: 30393-400
Protein Domain
Type: Domain
Description: Human HSPA14 (also known as 70kDa heat shock protein 14 or HSP70L1), is ribosome-associated and belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent 'client' proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). HSPA14 interacts with the J-protein MPP11 to form the mammalian ribosome-associated complex (mRAC) []. HSPA14 participates in a pathway along with Nijmegen breakage syndrome 1 (NBS1, also known as p85 or nibrin), heat shock transcription factor 4b (HSF4b), and HSPA4 (belonging to a different subfamily), that induces tumor migration, invasion, and transformation []. HSPA14 is a potent T helper cell (Th1) polarizing adjuvant that contributes to antitumor immune responses [, ].
Protein
Organism: Mus musculus/domesticus
Length: 841  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 841  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 930  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 842  
Fragment?: false
Publication
First Author: Mayer MP
Year: 2005
Journal: Cell Mol Life Sci
Title: Hsp70 chaperones: cellular functions and molecular mechanism.
Volume: 62
Issue: 6
Pages: 670-84
Protein
Organism: Mus musculus/domesticus
Length: 509  
Fragment?: false