hsp70.com
HSP70 Scientific Resource GuideHeat Shock Protein 70 (HSP70) information database. A resource for all HSP70 structure, isoform, function, disease relevance, and inhibitor information.
http://www.hsp70.com/
Heat Shock Protein 70 (HSP70) information database. A resource for all HSP70 structure, isoform, function, disease relevance, and inhibitor information.
http://www.hsp70.com/
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HSP70 Scientific Resource Guide | hsp70.com Reviews
https://hsp70.com
Heat Shock Protein 70 (HSP70) information database. A resource for all HSP70 structure, isoform, function, disease relevance, and inhibitor information.
hsp70.com
HSP70 Localization
http://hsp70.com/localization
Mechanisms & Interactions. Immunofluorescent detection of cell membrane embedded Hsp70 using Mouse anti-HSP70 Antibody. Clone 1H11 (green) in non-permeabilized HCT116 cells. Members of the HSP70 family of chaperones represent one of the most ubiquitous classes of chaperones and can be found not only in eukaryotic cytosol, chloroplasts, ER and mitochondria but also in the extracellular milieu as well as in bacteria and certain archaea. An interaction of Hsp70-1 with the sphingolipid globoyltriaosylceramid...
HSP70 Apoptosis, Mechanisms & Interactions
http://hsp70.com/mechanisms-interactions
Mechanisms & Interactions. HSP70: Mechanisms & Interactions. Immunofluorescent detection of Hsp70 using rabbit anti-Hsp70 polyclonal antibody. In heat shocked HeLa cells. The most studied member of the HSP70 family is the major stress-inducible Hsp70, also known as HSPA1A, Hsp70-1, Hsp72 or HspA1. CHIP contains three TPR domains interacting with both, HSP70s and HSP90s. Hop is a co-chaperone that binds to both HSP70s and HSP90s thereby stabilizing client proteins and their transfer to Hsp90. Are far from...
HSP70 Disease Relevance
http://hsp70.com/disease-relevance
Mechanisms & Interactions. Immunohistochemical detection of Hsp70 in mouse inflamed colon tissue using Mouse Anti-Hsp70 Monoclonal Antibody, clone BB70. A growing wealth of evidence indicates the pivotal role of Hsp70-1 in tumorigenesis. Constitutively elevated levels of Hsp70-1 can be found in a wide spectrum of cancer cells where Hsp70-1 enhances cell growth. Suppresses senescence, and confers resistance to stress-induced apoptosis including protection against cytostatic drugs and radiation therapy.
HSP70 Structure
http://hsp70.com/structure
Mechanisms & Interactions. Click image for larger version). HSP70s are highly conserved and consist of two functional domains ( Figure 1. A 44 kDa N-terminal nucleotide binding domain (NBD; also termed ATP-binding domain, ABD) which binds and hydrolizes ATP and a 28 kDa C-terminal substrate binding domain (SBD) which binds extended polypeptides. The ABD is conserved in all of its members with the exception of the two HSPA12. Click image for larger version). Click image for larger version). In the ATP-bou...
Database IDs - HSP70
http://hsp70.com/database-ids
Mechanisms & Interactions. Table 1 summarizes the most relevant database IDs of the major stress inducible member of the HSP70 family, Hsp70-1 (HspA1A). Provides an overview of UniProt and Gene IDs of various pro- and eukaryotic HSP70s. Table 1: Human and mouse orthologs of Hsp70-1 (HspA1A). Chr 6:31,789,963-31,798,031. Chr 17: 35.11 35.11 Mb. Table 2: HSP70s of various pro- and eukaryotic organisms. Hsp70-1, Hsp72, HspA1, Hsp70-1a, Hsp70i. Hsp70-1L, Hsp70-hom, Hsp70-1t, Hum70t. Hsp70-5, BiP, Grp78, Mif-2.
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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.
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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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