Atomic analysis of protein-protein interfaces with known inhibitors: the 2P2I database
about
Systematic analysis of helical protein interfaces reveals targets for synthetic inhibitorsFine-tuning multiprotein complexes using small moleculesFeatures of protein-protein interactions that translate into potent inhibitors: topology, surface area and affinityChemical libraries dedicated to protein-protein interactionsTargeting protein-protein interactions for parasite controlUsing a Fragment-Based Approach To Target Protein-Protein InteractionsStructure-Based Design, Synthesis, and Characterization of Dual Hotspot Small-Molecule HIV-1 Entry InhibitorsStructural Basis for LMO2-Driven Recruitment of the SCL:E47bHLH Heterodimer to Hematopoietic-Specific Transcriptional TargetsCrystal structure of the human fatty acid synthase enoyl-acyl carrier protein-reductase domain complexed with triclosan reveals allosteric protein-protein interface inhibitionEnhancements to the Rosetta Energy Function Enable Improved Identification of Small Molecules that Inhibit Protein-Protein InteractionsFractal Dimensions of Macromolecular Structures."Solvent hydrogen-bond occlusion": A new model of polar desolvation for biomolecular energetics.Modulating protein-protein interactions with small molecules: the importance of binding hotspots.Dr. PIAS: an integrative system for assessing the druggability of protein-protein interactions.Essential multimeric enzymes in kinetoplastid parasites: A host of potentially druggable protein-protein interactions.Small-molecule inhibitor starting points learned from protein-protein interaction inhibitor structure.Visualisation of variable binding pockets on protein surfaces by probabilistic analysis of related structure sets.A leap into the chemical space of protein-protein interaction inhibitorsBreak CDK2/Cyclin E1 interface allosterically with small peptides.2P2Idb: a structural database dedicated to orthosteric modulation of protein-protein interactions.Plucking the high hanging fruit: a systematic approach for targeting protein-protein interactionsTIMBAL v2: update of a database holding small molecules modulating protein-protein interactionsComputational analysis of protein-protein interfaces involving an alpha helix: insights for terphenyl-like molecules binding.2P2I HUNTER: a tool for filtering orthosteric protein-protein interaction modulators via a dedicated support vector machine.HADDOCK(2P2I): a biophysical model for predicting the binding affinity of protein-protein interaction inhibitors.Focused chemical libraries--design and enrichment: an example of protein-protein interaction chemical space.Computational and biophysical approaches to protein-protein interaction inhibition of Plasmodium falciparum AMA1/RON2 complex.DARC 2.0: Improved Docking and Virtual Screening at Protein Interaction SitesStructural Disorder within Paramyxoviral Nucleoproteins and Phosphoproteins in Their Free and Bound Forms: From Predictions to Experimental Assessment.Imbalance in chemical space: How to facilitate the identification of protein-protein interaction inhibitors.AlphaSpace: Fragment-Centric Topographical Mapping To Target Protein-Protein Interaction Interfaces.Flexibility and small pockets at protein-protein interfaces: New insights into druggability.Structural properties of non-traditional drug targets present new challenges for virtual screening.The FAK scaffold inhibitor C4 disrupts FAK-VEGFR-3 signaling and inhibits pancreatic cancer growth.Computational analysis of C-reactive protein for assessment of molecular dynamics and interaction properties.Druggability assessment of protein-protein interfaces.On the binding affinity of macromolecular interactions: daring to ask why proteins interact.Understanding the molecular dynamics of type-2 diabetes drug target DPP-4 and its interaction with Sitagliptin and inhibitor Diprotin-A.From workstations to workbenches: Towards predicting physicochemically viable protein-protein interactions across a host and a pathogen.How order and disorder within paramyxoviral nucleoproteins and phosphoproteins orchestrate the molecular interplay of transcription and replication.
P2860
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P2860
Atomic analysis of protein-protein interfaces with known inhibitors: the 2P2I database
description
2010 nî lūn-bûn
@nan
2010 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի մարտին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Atomic analysis of protein-protein interfaces with known inhibitors: the 2P2I database
@ast
Atomic analysis of protein-protein interfaces with known inhibitors: the 2P2I database
@en
Atomic analysis of protein-protein interfaces with known inhibitors: the 2P2I database
@nl
type
label
Atomic analysis of protein-protein interfaces with known inhibitors: the 2P2I database
@ast
Atomic analysis of protein-protein interfaces with known inhibitors: the 2P2I database
@en
Atomic analysis of protein-protein interfaces with known inhibitors: the 2P2I database
@nl
prefLabel
Atomic analysis of protein-protein interfaces with known inhibitors: the 2P2I database
@ast
Atomic analysis of protein-protein interfaces with known inhibitors: the 2P2I database
@en
Atomic analysis of protein-protein interfaces with known inhibitors: the 2P2I database
@nl
P2860
P3181
P1433
P1476
Atomic analysis of protein-protein interfaces with known inhibitors: the 2P2I database
@en
P2093
Marie-Jeanne Basse
Philippe Roche
P2860
P3181
P356
10.1371/JOURNAL.PONE.0009598
P407
P577
2010-03-09T00:00:00Z