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HSP60 Introduction | HSP60Heat shock protein 60 (Hsp60) is one of the most conserved proteins and is present in all three
http://www.hsp60.com/
Heat shock protein 60 (Hsp60) is one of the most conserved proteins and is present in all three
http://www.hsp60.com/
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HSP60 Introduction | HSP60 | hsp60.com Reviews
https://hsp60.com
Heat shock protein 60 (Hsp60) is one of the most conserved proteins and is present in all three
hsp60.com
Tables - HSP60 | HSP60
http://hsp60.com/tables
Table 1: Human and mouse orthologs of Hsp60 (HspD1). Chr 2: 197,486,581-197,516,737. Chr 1: 55,077,835-55,088,243. Table 2: HSP60s of various pro- and eukaryotic organisms. Hsp60, mitochondrial Hsp60 (mtHsp60), 60 kDa chaperonin (Cpn60), mitochondrial matrix protein P1, P60 lymphocyte protein. CCT-1, TCP-1, CCTA, CCT-alpha, T-complex protein 1 subunit alpha (TCP-1-alpha). CCT-2, CCTB, CCT-beta, T-complex protein 1 subunit beta (TCP-1-beta). CCT-6A, CCTZ, CCT-zeta, CCT-zeta-1, HTR3,. CCT-2, CCTB, CCT-beta...
HSP60 Mechanisms and Interactions | HSP60
http://hsp60.com/mechanisms-interactions
HSP60: Mechanisms and Interactions. IHC staining of human colon cancer, 1:100,000, using Anti-Hsp60 (clone: LK1). Hsp60 is a molecular chaperone which assists protein folding in prokaryotes and in eukaryotic cell organelles. In mitochondria, Hsp60 is considered an essential chaperone for the protein import into the mitochondrial matrix. Hsp60 functions together with its co-chaperone Hsp10 also residing in mitochondria. Adenine nucleotides and GroES. For GroES oligomeriztaion, no specific factor is ne...
HSP60 Species Variation | HSP60
http://hsp60.com/species-variation
IHC staining of Listeria infected mice spleens 6 days after infection with L-monocytogenes, using Anti-Hsp60 (clone: LK2). The 60 kDa chaperonin family has homologs in many eukaryotes like Danio rerio. An examination of the Arabidopsis thaliana. Genome sequence led to the identification of 29 predicted genes with the potential to encode members of the chaperonin family of chaperones (Hsp60, Cpn60). Amongst them, eleven Arabidopsis. And an apparent mitochondrial protein pseudogene. Hsp60-2 is the longest ...
HSP60 Function | HSP60
http://hsp60.com/function
IHC staining of human colon cancer, using Anti-Hsp60 (clone: LK2). The 60 kDa heat-shock proteins are abundant in prokaryotes and eukaryotes and are required in the folding, translocation, and assembly of native proteins. Eukaryotic species are nuclear encoded but exhibit their function in certain organelles and the cytosol as well as on the cell surface and in the extracellular space. In addition to its classical chaperone function, mitochondrial Hsp60 is critically involved in the replication. Crosslin...
HSP60 Structure | HSP60
http://hsp60.com/structure
IHC staining of human colon cancer, 1:100,000, using Anti-Hsp60 (clone: LK1). Most information on structure and function of Hsp60 is available from the prokaryotic homolog, GroEL. GroEL consists of 14 identical subunits of 57 kDa each forming two heptameric rings arranged back-to-back. The conformation of GroEL could be characterized as a barrel-like structure (145 Å in height and 135 Å in diameter) with an inner cavity of about 45 Å in diameter. It has been shown previously that the mobility of the inte...
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Figures - HSP90 | HSP90
http://hsp90.ca/figures
Mechanisms & Interactions. Structure of the tetragonal form of the N-terminal domain of Hsp90 from yeast ( PDB ID: 1ah6. Figure 1. Structure of the tetragonal form of the N-terminal domain of Hsp90 from yeast ( PDB ID: 1ah6. Structure of full-length yeast Hsp90. Figure 2. Structure of full-length yeast Hsp90. Crystal structure of dimeric full-length yeast Hsp90 in complex with an ATP analogue and the co-chaperone p23/Sba-1 ( PDB ID: 2CG9. Structures of the full-length Hsp90 dimer. The N-terminal nucleoti...
HSP90 Isoforms | HSP90
http://hsp90.ca/isoforms
Mechanisms & Interactions. IHC staining of inflammatory cells in mouse colon tissue, using Anti-Hsp90 (clone: D7A). The HSP90 proteins are ubiquitous and highly conserved molecular chaperones present from bacteria to mammals. HSP90 proteins can be found in the cytosol, ER, chloroplasts, mitochondria, and the nucleus. Eubacteria express a single Hsp90 homolog, referred to as. High-temperature protein G) which is absent in Archaebacteria with the exception of. 1 (Hsp90AA1, HspC1) and the constitutive Hsp90.
HSP90 Mechanisms & Interactions | HSP90
http://hsp90.ca/mechanisms-interactions
Mechanisms & Interactions. HSP90: Mechanisms and Interactions. IF detection of Hsp90 in cancerous human colon tissue, using Anti-Hsp90 (clone: H9010). A comprehensive list of Hsp90-interacting proteins can be found at the website of Didier Picard. According to their biological function, Hsp90 client proteins can be classified in several groups such as transcription factors, TPR-domain proteins, protein kinases, structural proteins, and others. The Cdc-37/Hsp90 complex can be formed in an open or closed c...
Tables - HSP90 | HSP90
http://hsp90.ca/tables
Mechanisms & Interactions. Table 1: Human and mouse orthologs of Hsp90α1 (HspC1). Chr 14:102,547,075-102,606,086. Chr 12: 110,691,036-110,696,395. Table 2: HSP90s of various pro- and eukaryotic organisms. Hsp90α1, Hsp90AA1, Hsp86, HspCA, Hsp89, Hsp90A, renal carcinoma antigen NY-REN-38. Hsp90α2, Hsp90AA2, Hsp90α-like 3, HspCA. Hsp90β, Hsp90AB1, Hsp84, HSP90B, HspCB. Endoplasmin, Grp94, Gp96, Tra-1, Hsp90B1. Trap-1, Hsp75, Hsp90L. Slo, sloth, akineto, heat shock protein 90-alpha 1. AtHsp90.2, Hsp81-2.
HSP90 Structure | HSP90
http://hsp90.ca/structure
Mechanisms & Interactions. HSP90s are abundant and highly specialized molecular chaperones crucially involved in several signalling pathways. They primarily exist as homodimers whose activity is regulated by ATP. Dimerization is essential for the vital functions of HSP90s. Nevertheless, higher oligomeric states including hexamers have been reported. It has been shown previously that oligomerization is induced after heat shock and in the presence of non-ionic detergents. Click image for larger version).
HSP90 Protein Type | HSP90
http://hsp90.ca/protein-type
Mechanisms & Interactions. Hsp90 (total) visualized on a human keratinocyte line HaCat, using Anti-Hsp90 (total) (clone: 4F3.E8). The HSP90 family represents a group of well-conserved proteins with an average molecular mass of 90 kDa. There are two major cytosolic Hsp90 isoforms, the inducible Hsp90. 1 (HspC1) and the constitutive Hsp90. HspC3), commonly termed Hsp90. The HSP90 family members are encoded by a multigene family encompassing six genes and 11 pseudogenes in humans. The most studied genes are.
Discovery of HSP90 | HSP90
http://hsp90.ca/history
Mechanisms & Interactions. IHC staining of inflammatory cells in mouse colon tissue, using Anti-Hsp90 alpha (clone: Hyb-K41009). Heat shock protein 90 (Hsp90) was originally described amongst a defined set of heat shock proteins (HSPs) that are rapidly induced in fungal, plant and animal cells in response to acute thermal up-regulation. This HSP induction is referred to as the heat shock response (HSR) that is ubiquitous across the bacterial, archaeal and eukaryotic kingdoms. 83 kDa heat shock protein 2.
HSP90 Disease Relevance | HSP90
http://hsp90.ca/disease-relevance
Mechanisms & Interactions. IHC detection of Hsp90 in cancerous human colon tissue, using Anti-Hsp90 (clone: H9010). A growing wealth of evidence indicates the pivotal role of Hsp90 in tumourigenesis. Constitutively elevated levels of Hsp90 can be found in a broad spectrum of cancers suggesting a central role in survival and growth of malignant cells. 1 to the heterodimeric cell surface receptor Her-2/Her-3 thereby inducing HSF-1 stabilization which consequently enhanced cell survival and transformation.
HSP90 Molecular Weight | HSP90
http://hsp90.ca/molecular-weight
Mechanisms & Interactions. IHC staining of inflammatory cells and epithelia mucosa in mouse colon tissues, using Anti-Hsp90 (clone: AC-16). The HSP90 family represents a group of well-conserved proteins with an average molecular mass of 90 kDa. There are two major cytosolic Hsp90 isoforms, the inducible Hsp90. 1 (HspC1) and the constitutive Hsp90. HspC3), commonly termed Hsp90. The HSP90 family members are encoded by a multigene family encompassing six genes and 11 pseudogenes in humans.
References - HSP90 | HSP90
http://hsp90.ca/references
Mechanisms & Interactions. 1 Csermely,P., Schnaider,T., Soti,C., Prohaszka,Z., and Nardai,G. The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review. Pharmacol. Ther. 79, 129-168 (1998). [PubMed]. 2 Felts,S.J. et al. The hsp90-related protein TRAP1 is a mitochondrial protein with distinct functional properties. J. Biol. Chem. 275, 3305-3312 (2000). [PubMed]. Novartis. Found. Symp. 291, 86-95 (2008). [PubMed]. 10 Lindquist,S. Regulation of protein ...
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HSP60 Introduction | HSP60
The 60 kDa heat shock protein 60 (Hsp60), also known as 60 kDa chaperonin (Cpn60). Represents one of the most conserved proteins in living organisms and is present in all three “primary kingdoms” of life: eukaryotes, eubacteria, and Archaea. HSP60 chaperones can be found not only in the cytosol, chloroplasts, hydrogenosomes and mitochondria. But also on the cell surface and in the extracellular milieu. Relevant database IDs for Human Hsp60 (HspD1).
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British Columbia Centre for Disease Controls (BCCDC) Mycobacterium hsp65 BLAST Database
Welcome to the British Columbia Centre for Disease Control s ( BCCDC. 65 Kilodalton Heat Shock Protein Gene (. BLAST database. This web site provides a high quality set of sequences for BLAST searches. We acknowledge and thank the National Center for Biotechnology Information ( NCBI. For the use of their, web based, Basic Local Alignment Search Tool ( BLAST. 65 Kilodalton Heat Shock Protein Gene. This web site is provided as a free service to advance the identification of. J Clin. Microbiol. Based identi...
HSP70 Scientific Resource Guide
Mechanisms & Interactions. In many cases HSP70s can function redundantly. All of the cellular activities of HSP70s depend on their ATP-regulated ability to interact with exposed hydrophobic surfaces of proteins. Herein, focus is given on the regulation, function and disease relevance of the molecular HSP70 chaperones as well as their impact as therapeutic drug targets. Ribbon and tube representation of the tertiary Hsp70-1 structure in the presence of ADP. Relevant database IDs for Human Hsp70-1 (HspA1A).
hsp70 inhibitor | Potent HSP90 Inhibitors Widely Used in NCBI's Publications
Potent HSP90 Inhibitors Widely Used in NCBI's Publications. Skip to primary content. Skip to secondary content. Bifidobacteria were enumerated on modified. March 29, 2018. Bifidobacteria were enumerated on modified Z-VAD-FMK molecular weight. Of uniform diameter were then bored into the medium and 50 μL of the fermented kefir milk was then added to each well. Plates were incubated overnight aerobically at 30 C and examined for zones of clearing. For 16S compositional. March 29, 2018. March 27, 2018.
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