Proteins > Heat shock protein 75 kDa, mitochondrial
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Heat shock protein 75 kDa, mitochondrial
A heat shock protein 75 kDa, mitochondrial that is encoded in the genome of human. [PRO:DAN]
Synonyms
HSP 75;
TNFR-associated protein 1;
Tumor necrosis factor type 1 receptor-associated protein;
TRAP-1
Research
Bioassay Publications (13)
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 7 (53.85) | 24.3611 |
| 2020's | 6 (46.15) | 2.80 |
Compounds (11)
Drugs with Inhibition Measurements
Drugs with Other Measurements
Design and Synthesis of TRAP1 Selective Inhibitors: H-Bonding with Asn171 Residue in TRAP1 Increases Paralog Selectivity.ACS medicinal chemistry letters, , Jul-08, Volume: 12, Issue:7, 2021
Discovery of 2-((4-resorcinolyl)-5-aryl-1,2,3-triazol-1-yl)acetates as potent Hsp90 inhibitors with selectivity over TRAP1.Bioorganic & medicinal chemistry letters, , 01-15, Volume: 30, Issue:2, 2020
Dual Binding to Orthosteric and Allosteric Sites Enhances the Anticancer Activity of a TRAP1-Targeting Drug.Journal of medicinal chemistry, , 03-26, Volume: 63, Issue:6, 2020
Paralog Specificity Determines Subcellular Distribution, Action Mechanism, and Anticancer Activity of TRAP1 Inhibitors.Journal of medicinal chemistry, , 09-14, Volume: 60, Issue:17, 2017
Structure-activity relationship in a purine-scaffold compound series with selectivity for the endoplasmic reticulum Hsp90 paralog Grp94.Journal of medicinal chemistry, , May-14, Volume: 58, Issue:9, 2015
Experimental and structural testing module to analyze paralogue-specificity and affinity in the Hsp90 inhibitors series.Journal of medicinal chemistry, , Sep-12, Volume: 56, Issue:17, 2013
Paralog Specificity Determines Subcellular Distribution, Action Mechanism, and Anticancer Activity of TRAP1 Inhibitors.Journal of medicinal chemistry, , 09-14, Volume: 60, Issue:17, 2017
Correlation between chemotype-dependent binding conformations of HSP90α/β and isoform selectivity-Implications for the structure-based design of HSP90α/β selective inhibitors for treating neurodegenerative diseases.Bioorganic & medicinal chemistry letters, , Jan-01, Volume: 24, Issue:1, 2014
Experimental and structural testing module to analyze paralogue-specificity and affinity in the Hsp90 inhibitors series.Journal of medicinal chemistry, , Sep-12, Volume: 56, Issue:17, 2013
The Development of Hsp90β-Selective Inhibitors to Overcome Detriments Associated with Journal of medicinal chemistry, , 02-11, Volume: 64, Issue:3, 2021
Correlation between chemotype-dependent binding conformations of HSP90α/β and isoform selectivity-Implications for the structure-based design of HSP90α/β selective inhibitors for treating neurodegenerative diseases.Bioorganic & medicinal chemistry letters, , Jan-01, Volume: 24, Issue:1, 2014
Experimental and structural testing module to analyze paralogue-specificity and affinity in the Hsp90 inhibitors series.Journal of medicinal chemistry, , Sep-12, Volume: 56, Issue:17, 2013
Thermodynamic Dissection of Potency and Selectivity of Cytosolic Hsp90 Inhibitors.Journal of medicinal chemistry, , 03-11, Volume: 64, Issue:5, 2021
Heat Shock Protein 90 Inhibitors: An Update on Achievements, Challenges, and Future Directions.Journal of medicinal chemistry, , 03-12, Volume: 63, Issue:5, 2020
New TRAP1 and Hsp90 chaperone inhibitors with cationic components: Preliminary studies on mitochondrial targeting.Bioorganic & medicinal chemistry letters, , 07-15, Volume: 28, Issue:13, 2018
Correlation between chemotype-dependent binding conformations of HSP90α/β and isoform selectivity-Implications for the structure-based design of HSP90α/β selective inhibitors for treating neurodegenerative diseases.Bioorganic & medicinal chemistry letters, , Jan-01, Volume: 24, Issue:1, 2014
Experimental and structural testing module to analyze paralogue-specificity and affinity in the Hsp90 inhibitors series.Journal of medicinal chemistry, , Sep-12, Volume: 56, Issue:17, 2013
Heat shock protein 90: inhibitors in clinical trials.Journal of medicinal chemistry, , Jan-14, Volume: 53, Issue:1, 2010
Discovery of 2-((4-resorcinolyl)-5-aryl-1,2,3-triazol-1-yl)acetates as potent Hsp90 inhibitors with selectivity over TRAP1.Bioorganic & medicinal chemistry letters, , 01-15, Volume: 30, Issue:2, 2020
Experimental and structural testing module to analyze paralogue-specificity and affinity in the Hsp90 inhibitors series.Journal of medicinal chemistry, , Sep-12, Volume: 56, Issue:17, 2013
Enables
This protein enables 8 target(s):
| Target | Category | Definition |
|---|
| RNA binding | molecular function | Binding to an RNA molecule or a portion thereof. [GOC:jl, GOC:mah] |
| tumor necrosis factor receptor binding | molecular function | Binding to a tumor necrosis factor receptor. [GOC:ai] |
| protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
| ATP binding | molecular function | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. [ISBN:0198506732] |
| ATP hydrolysis activity | molecular function | Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient. [RHEA:13065] |
| protein kinase binding | molecular function | Binding to a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate. [GOC:jl] |
| ATP-dependent protein folding chaperone | molecular function | Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis. [PMID:27365453] |
| unfolded protein binding | molecular function | Binding to an unfolded protein. [GOC:ai] |
Located In
This protein is located in 7 target(s):
| Target | Category | Definition |
|---|
| nucleoplasm | cellular component | That part of the nuclear content other than the chromosomes or the nucleolus. [GOC:ma, ISBN:0124325653] |
| mitochondrion | cellular component | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. [GOC:giardia, ISBN:0198506732] |
| mitochondrial inner membrane | cellular component | The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae. [GOC:ai] |
| mitochondrial intermembrane space | cellular component | The region between the inner and outer lipid bilayers of the mitochondrial envelope. [GOC:mah] |
| mitochondrial matrix | cellular component | The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation. [GOC:as, ISBN:0198506732] |
| membrane | cellular component | A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. [GOC:dos, GOC:mah, ISBN:0815316194] |
| cell periphery | cellular component | The broad region around and including the plasma membrane of a cell, encompassing the cell cortex (inside the cell), the plasma membrane, and any external encapsulating structures. [GOC:pdt] |
Active In
This protein is active in 1 target(s):
| Target | Category | Definition |
|---|
| mitochondrial inner membrane | cellular component | The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae. [GOC:ai] |
Involved In
This protein is involved in 6 target(s):
| Target | Category | Definition |
|---|
| translational attenuation | biological process | Translational attenuation is a regulatory mechanism analogous to ribosome-mediated transcriptional attenuation. The system requires the presence of a short ORF, called a leader peptide, encoded in the mRNA upstream of the ribosome-binding site and start codon of the gene whose translation is to be regulated. Certain conditions, such as presence of the antibiotic tetracycline in bacteria or amino acid starvation, may cause slowing or stalling of the ribosome translating the leader peptide. The stalled ribosome masks a region of the mRNA and affects which of two alternative mRNA folded structures will form, therefore controlling whether or not a ribosome will bind and initiate translation of the downstream gene. Translational attenuation is analogous to ribosome-mediated transcriptional attenuation, in which mRNA remodeling caused by ribosome stalling regulates transcriptional termination rather than translational initiation. [PMID:15694341, PMID:15805513] |
| chaperone-mediated protein folding | biological process | The process of inhibiting aggregation and assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that is dependent on interaction with a chaperone. [GOC:dph, GOC:vw] |
| negative regulation of cellular respiration | biological process | Any process that stops, prevents or reduces the frequency, rate or extent of cellular respiration. [GOC:TermGenie, GOC:yaf, PMID:23150719] |
| negative regulation of reactive oxygen species biosynthetic process | biological process | Any process that stops, prevents or reduces the frequency, rate or extent of reactive oxygen species biosynthetic process. [GO_REF:0000058, GOC:bf, GOC:PARL, GOC:TermGenie, PMID:24252804] |
| negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide | biological process | Any process that stops, prevents or reduces the frequency, rate or extent of intrinsic apoptotic signaling pathway in response to hydrogen peroxide. [GO_REF:0000058, GOC:TermGenie, PMID:18681888] |
| protein folding | biological process | The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure. [GOC:go_curators, GOC:rb] |