Structural conservation of druggable hot spots in protein-protein interfaces - Wikidata - awgldk - TriplyDB

Structural conservation of druggable hot spots in protein-protein interfaces

Structural conservation of druggable hot spots in protein-protein interfaces

http://www.wikidata.org/entity/Q24614979

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Expanding the number of 'druggable' targets: non-enzymes and protein-protein interactions Structure and dynamics of molecular networks: a novel paradigm of drug discovery: a comprehensive review Molecular Dynamics of "Fuzzy" Transcriptional Activator-Coactivator Interactions Analysis of Binding Site Hot Spots on the Surface of Ras GTPase Small-Molecule Inhibitors of the Interaction between the E3 Ligase VHL and HIF1α Dissecting Fragment-Based Lead Discovery at the von Hippel-Lindau Protein:Hypoxia Inducible Factor 1α Protein-Protein Interface Structure of the trehalose-6-phosphate phosphatase from Brugia malayi reveals key design principles for anthelmintic drugs Predicting where small molecules bind at protein-protein interfaces Interface-resolved network of protein-protein interactions Structure-based druggability assessment of the mammalian structural proteome with inclusion of light protein flexibility Evidence of conformational selection driving the formation of ligand binding sites in protein-protein interfaces Molecular insights into the interaction between Plasmodium falciparum apical membrane antigen 1 and an invasion-inhibitory peptide Emerging Computational Methods for the Rational Discovery of Allosteric Drugs.Structure-based inhibition of protein-protein interactions.Minimal ensembles of side chain conformers for modeling protein-protein interactions Modular organization of α-toxins from scorpion venom mirrors domain structure of their targets, sodium channels.Towards strain-independent anti-influenza peptides: a SAXS- and modeling-based study.Evaluation of a DLA-79 allele associated with multiple immune-mediated diseases in dogs.Robust identification of binding hot spots using continuum electrostatics: application to hen egg-white lysozyme.Protein docking by the interface structure similarity: how much structure is needed?Small-molecule inhibitors of protein-protein interactions: progressing toward the reality.FTMAP: extended protein mapping with user-selected probe molecules.A leap into the chemical space of protein-protein interaction inhibitors Comprehensive peptidomimetic libraries targeting protein-protein interactions.Allosteric inhibition of Epac: computational modeling and experimental validation to identify allosteric sites and inhibitors In silico identification of an aryl hydrocarbon receptor antagonist with biological activity in vitro and in vivo.Ligand binding and activation of PPARγ by Firemaster® 550: effects on adipogenesis and osteogenesis in vitro Improving protocols for protein mapping through proper comparison to crystallography data.FTFlex: accounting for binding site flexibility to improve fragment-based identification of druggable hot spots.Druggable protein interaction sites are more predisposed to surface pocket formation than the rest of the protein surface Hot spots in a network of functional sites.2P2I HUNTER: a tool for filtering orthosteric protein-protein interaction modulators via a dedicated support vector machine.Stimulators of translation identified during a small molecule screening campaign Focused chemical libraries--design and enrichment: an example of protein-protein interaction chemical space.How proteins bind macrocycles.The Fe-S cluster-containing NEET proteins mitoNEET and NAF-1 as chemotherapeutic targets in breast cancer.Environmental contaminants activate human and polar bear (Ursus maritimus) pregnane X receptors (PXR, NR1I2) differently Mitigating risk in academic preclinical drug discovery.Ligand deconstruction: Why some fragment binding positions are conserved and others are not FTSite: high accuracy detection of ligand binding sites on unbound protein structures

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P2860

Structural conservation of druggable hot spots in protein-protein interfaces

http://www.wikidata.org/entity/Q24614979

description

2011 nî lūn-bûn

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2011 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

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2011 թվականի օգոստոսին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Structural conservation of druggable hot spots in protein-protein interfaces

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Structural conservation of druggable hot spots in protein-protein interfaces

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Structural conservation of druggable hot spots in protein-protein interfaces

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Structural conservation of druggable hot spots in protein-protein interfaces

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Structural conservation of druggable hot spots in protein-protein interfaces

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Structural conservation of druggable hot spots in protein-protein interfaces

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Structural conservation of druggable hot spots in protein-protein interfaces

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Structural conservation of druggable hot spots in protein-protein interfaces

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Structural conservation of druggable hot spots in protein-protein interfaces

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PNAS.1101835108

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Proceedings of the National Academy of Sciences of the United States of America

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Structural conservation of druggable hot spots in protein-protein interfaces

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Adrian Whitty

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David R Hall

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Dmitri Beglov

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Gwo-Yu Chuang

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Jerry Pelletier

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Laurie E Grove

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Regina Cencic

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Ryan Brenke

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Sandor Vajda

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P2860

Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain

The Protein Data Bank

The bacterial cell-division protein ZipA and its interaction with an FtsZ fragment revealed by X-ray crystallography

Binding of small molecules to an adaptive protein-protein interface

Crystal structure of the E2 transactivation domain of human papillomavirus type 11 bound to a protein interaction inhibitor

In vivo activation of the p53 pathway by small-molecule antagonists of MDM2

Crystal structure of ABT-737 complexed with Bcl-xL: implications for selectivity of antagonists of the Bcl-2 family

Rational design of small-molecule inhibitors of the LEDGF/p75-integrase interaction and HIV replication

Small Molecule Inhibition of the TNF Family Cytokine CD40 Ligand through a Subunit Fracture Mechanism

Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis

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13528-33

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102846

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10.1073/PNAS.1101835108

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51539247

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21808046

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