Thermodynamics of aryl-dihydroxyphenyl-thiadiazole binding to human Hsp90 - Wikidata - awgldk - TriplyDB

Thermodynamics of aryl-dihydroxyphenyl-thiadiazole binding to human Hsp90

Thermodynamics of aryl-dihydroxyphenyl-thiadiazole binding to human Hsp90

http://www.wikidata.org/entity/Q34288879

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CSAR data set release 2012: ligands, affinities, complexes, and docking decoys Protein polymer nanoparticles engineered as chaperones protect against apoptosis in human retinal pigment epithelial cells SEDPHAT--a platform for global ITC analysis and global multi-method analysis of molecular interactions.Intrinsic thermodynamics of trifluoromethanesulfonamide and ethoxzolamide binding to human carbonic anhydrase VII.

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Thermodynamics of aryl-dihydroxyphenyl-thiadiazole binding to human Hsp90

http://www.wikidata.org/entity/Q34288879

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2012 nî lūn-bûn

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2012 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2012 թվականի մայիսին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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name

Thermodynamics of aryl-dihydroxyphenyl-thiadiazole binding to human Hsp90

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Thermodynamics of aryl-dihydroxyphenyl-thiadiazole binding to human Hsp90

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Thermodynamics of aryl-dihydroxyphenyl-thiadiazole binding to human Hsp90

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type

label

Thermodynamics of aryl-dihydroxyphenyl-thiadiazole binding to human Hsp90

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Thermodynamics of aryl-dihydroxyphenyl-thiadiazole binding to human Hsp90

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Thermodynamics of aryl-dihydroxyphenyl-thiadiazole binding to human Hsp90

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prefLabel

Thermodynamics of aryl-dihydroxyphenyl-thiadiazole binding to human Hsp90

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Thermodynamics of aryl-dihydroxyphenyl-thiadiazole binding to human Hsp90

@en

Thermodynamics of aryl-dihydroxyphenyl-thiadiazole binding to human Hsp90

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JOURNAL.PONE.0036899

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Thermodynamics of aryl-dihydroxyphenyl-thiadiazole binding to human Hsp90

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Jurgita Matulienė

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Jurgita Revuckienė

http://www.w3.org/2001/XMLSchema#string

Leonas Grinius

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Vilma Michailovienė

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Vilma Petrikaitė

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P2860

Combining hit identification strategies: fragment-based and in silico approaches to orally active 2-aminothieno[2,3-d]pyrimidine inhibitors of the Hsp90 molecular chaperone

Dihydroxyphenylisoindoline amides as orally bioavailable inhibitors of the heat shock protein 90 (hsp90) molecular chaperone

The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability

Rapid measurement of binding constants and heats of binding using a new titration calorimeter

HSP90 at the hub of protein homeostasis: emerging mechanistic insights

High-density miniaturized thermal shift assays as a general strategy for drug discovery

Development of a purine-scaffold novel class of Hsp90 binders that inhibit the proliferation of cancer cells and induce the degradation of Her2 tyrosine kinase.

Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery.

Discovery of novel 2-aminobenzamide inhibitors of heat shock protein 90 as potent, selective and orally active antitumor agents.

Hsp90 and co-chaperones twist the functions of diverse client proteins.

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scholarly article

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10.1371/JOURNAL.PONE.0036899

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Daumantas Matulis

Egidijus Kazlauskas

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2012-05-24T00:00:00Z

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