Full protein flexibility is essential for proper hot-spot mapping. - Wikidata - awgldk - TriplyDB

Full protein flexibility is essential for proper hot-spot mapping.

Full protein flexibility is essential for proper hot-spot mapping.

http://www.wikidata.org/entity/Q30397411

about

Druggability Assessment of Allosteric Proteins by Dynamics Simulations in the Presence of Probe Molecules Fine-tuning multiprotein complexes using small molecules Protein flexibility in docking and surface mapping Expanding the number of 'druggable' targets: non-enzymes and protein-protein interactions Energetics of Ortho-7 (oxime drug) translocation through the active-site gorge of tabun conjugated acetylcholinesterase Expanding the druggable space of the LSD1/CoREST epigenetic target: new potential binding regions for drug-like molecules, peptides, protein partners, and chromatin Structure-based druggability assessment of the mammalian structural proteome with inclusion of light protein flexibility pMD-Membrane: A Method for Ligand Binding Site Identification in Membrane-Bound Proteins Approximating protein flexibility through dynamic pharmacophore models: application to fatty acid amide hydrolase (FAAH)Heterogeneous preferential solvation of water and trifluoroethanol in homologous lysozymes.Parameter choice matters: validating probe parameters for use in mixed-solvent simulations.Targeting YAP/TAZ-TEAD protein-protein interactions using fragment-based and computational modeling approaches.Robust identification of binding hot spots using continuum electrostatics: application to hen egg-white lysozyme.Binding site multiplicity with fatty acid ligands: implications for the regulation of PKR kinase autophosphorylation with palmitate Overcoming Chemical, Biological, and Computational Challenges in the Development of Inhibitors Targeting Protein-Protein Interactions.Improving protocols for protein mapping through proper comparison to crystallography data.Inclusion of multiple fragment types in the site identification by ligand competitive saturation (SILCS) approach Structure-based virtual screening for drug discovery: principles, applications and recent advances.Site Identification by Ligand Competitive Saturation (SILCS) simulations for fragment-based drug design Targeting protein-protein interactions in hematologic malignancies: still a challenge or a great opportunity for future therapies?Identifying binding hot spots on protein surfaces by mixed-solvent molecular dynamics: HIV-1 protease as a test case CryptoSite: Expanding the Druggable Proteome by Characterization and Prediction of Cryptic Binding Sites.Moving Beyond Active-Site Detection: MixMD Applied to Allosteric Systems.Driving Structure-Based Drug Discovery through Cosolvent Molecular Dynamics.The role of long-range intermolecular interactions in discovery of new drugs.Computational solvent mapping in structure-based drug design.Review structure- and dynamics-based computational design of anticancer drugs.Computational allosteric ligand binding site identification on Ras proteins.Computational functional group mapping for drug discovery.Sampling of Organic Solutes in Aqueous and Heterogeneous Environments Using Oscillating Excess Chemical Potentials in Grand Canonical-like Monte Carlo-Molecular Dynamics Simulations.Identification of small-molecule binding pockets in the soluble monomeric form of the Aβ42 peptide.Site-Specific Fragment Identification Guided by Single-Step Free Energy Perturbation Calculations Balancing target flexibility and target denaturation in computational fragment-based inhibitor discovery.Reproducing crystal binding modes of ligand functional groups using Site-Identification by Ligand Competitive Saturation (SILCS) simulations Structured water molecules in the binding site of bromodomains can be displaced by cosolvent.Predicting Displaceable Water Sites Using Mixed-Solvent Molecular Dynamics.Dynamic Docking: A Paradigm Shift in Computational Drug Discovery.A multi-resolution model to capture both global fluctuations of an enzyme and molecular recognition in the ligand-binding site.The importance of hydration thermodynamics in fragment-to-lead optimization.Computational Methods to Support Fragment-based Drug Discovery

P2860

Q24633124-E552C232-31C4-41B1-A741-BF2771C9C8DF Q26822675-C1BC2F40-7D98-4720-AFBA-A3436BC5650D Q26864013-F79F33C7-1327-4623-9E9F-3384F9A8004F Q27003966-6DFC7CF0-0613-48C2-B9D6-CE4B8B65DBBC Q28481270-89EB5187-F523-47FA-8A03-908CE5978440 Q28534702-BAA55C24-A4A7-414A-A373-B0AAA1AF1B21 Q28541379-4090FBD8-8C3C-45A2-9142-CA902531BAF9 Q28550500-19AC2020-783D-4B80-AC7E-70BF638D9681 Q28740837-3A2B6A09-0E24-427B-8084-56644E5725D2 Q30362502-BDDD20E4-2CA3-4627-958B-CF1E3A65D69E Q30365087-C49181D3-38B4-4E9F-AF5F-9380CEB8F706 Q33751702-B488FE31-2F4B-4C16-B73F-ABB68647530D Q34076535-016324BF-4C06-4C78-991E-D3B6B311EE6C Q34254661-A050655F-35CD-4625-8F81-A73655E4364A Q34481459-4E66B18A-49F7-45F2-83F3-DF801495CF64 Q34552566-9FA7361C-61B5-4D5C-85C7-9BEF34728D22 Q35045753-422BC84F-F408-4977-8FDE-98BB70642632 Q35282223-4464FFE8-5A4B-4586-ADB1-AAC91DB26158 Q35566613-1CB38DAC-DED9-4E7F-A11A-22FEB845F39D Q35687836-61F8D6C7-5C20-4439-A7E0-848DB06091C0 Q36218072-4E0D6BCD-4005-4F64-8143-0670DD45A8D9 Q36693185-9EDECE7E-854E-40F6-B63C-7D2506EA2279 Q37558652-21AAAB56-3A65-4973-BE80-96831EC189F8 Q37565935-CC3B1D9E-F270-4381-8489-C20F7E738BB8 Q38014574-50C86303-0F1D-4E0E-9BD2-23E350BDA09F Q38397344-AA1A2CB4-FFFC-4ECB-9F7D-79470CA45C13 Q38589320-5FC5CA43-12D4-4C8C-AC92-6E0034A8BAB8 Q38612789-24F0AADF-B673-4DED-9FB5-AF9D41482641 Q38890648-6D19F851-91C5-4024-A4EA-F4D5FB98AB2B Q40572087-E5EA42A8-5600-43DA-9B2C-B237DECB4FFD Q41015632-E511A1BD-C936-4881-B294-5D427C3BEE77 Q41451646-B78B579D-4C18-4D63-AB60-BF0740A95BAE Q42020428-EFB73E9C-A3EC-4B60-AE11-27DE32A8192E Q42130025-8C925C23-EA1E-48A9-99CC-0ABF6D6A388B Q44579014-56886D43-02DB-4226-B380-32D4580E619C Q47245406-1B22F1BF-78B0-4EF4-942C-D6FF5002B008 Q47374327-B1F6B796-E122-4D78-B589-B1D7E8179ED6 Q51434391-3005F684-B3AE-4C0E-94AF-9AFC2DD36BFB Q54326694-636DF0C4-3619-49D1-A869-EA4BF94D8F5E Q58488998-1B302884-6987-4DFC-A60E-9FA08C397F05

P2860

Full protein flexibility is essential for proper hot-spot mapping.

http://www.wikidata.org/entity/Q30397411

description

2010 nî lūn-bûn

@nan

2010 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի դեկտեմբերին 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

Full protein flexibility is essential for proper hot-spot mapping.

@ast

Full protein flexibility is essential for proper hot-spot mapping.

@en

type

label

Full protein flexibility is essential for proper hot-spot mapping.

@ast

Full protein flexibility is essential for proper hot-spot mapping.

@en

prefLabel

Full protein flexibility is essential for proper hot-spot mapping.

@ast

Full protein flexibility is essential for proper hot-spot mapping.

@en

P1433

Q30397411-619E363F-47D3-4F0C-9D95-96323A9D8B3D

P1476

Q30397411-44BAA5AE-9CC9-4697-9B0F-1811D00E40E2

P2093

Q30397411-7A5D4F86-02FF-4EE6-8B91-D5BD1172AA68

P2860

Q30397411-19614E77-4091-46B0-911A-374D37CD49EA

Q30397411-32398055-FD80-4E51-B13C-9581215D3AC2

Q30397411-3895E06A-A5B1-4605-8403-F9C8C52CDFDF

Q30397411-5922AF08-60D3-46C2-8E6A-40A931BEB08E

Q30397411-6245774C-BEA1-467C-BF47-DE59A234C749

Q30397411-75D032DF-CDEF-4115-8539-4BCEEEF37FF8

Q30397411-8020E701-8B5A-46FF-8652-D7DA619FC199

Q30397411-8E8FFCC1-9630-4C69-B106-D9ADB87DE7F0

Q30397411-9A7D33E5-A3D0-4716-83A8-352F72802711

Q30397411-A06DCF3D-99D1-4EBF-AE4B-47C68A5DE96C

P304

Q30397411-F4F4CBEF-89C5-4804-8E17-9B992DE9183D

P31

Q30397411-0D5710AC-2C21-45C2-A20C-91B22EAA6A05

P356

Q30397411-ED79B0D3-B70D-4265-9359-0F21B2EF2E05

P407

Q30397411-1F93C59D-639E-4807-82D3-D7355B6BF06F

P433

Q30397411-F8D2D606-68F2-4846-9D34-B19A76270FF9

P478

Q30397411-237871CC-5CEC-42D9-AA11-29CE379FB74E

P50

Q30397411-C313577D-926A-47C4-8F25-D313EE906EE2

P577

Q30397411-D81FC305-B7D9-4981-8C23-394C54ABE261

P5875

Q30397411-E5DB23D7-81CD-42C7-9A48-13FE3D39D09D

P698

Q30397411-018EF04E-31ED-48D0-A156-ECB393D38D16

P932

Q30397411-24EF51E8-8F11-4A7E-8E0A-D5D9AAB2E1D4

P356

P1433

Journal of the American Chemical Society

P1476

Full protein flexibility is essential for proper hot-spot mapping

@en

P2093

Katrina W Lexa

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

P2860

The Protein Data Bank

X-ray studies on cross-linked lysozyme crystals in acetonitrile-water mixture

Comparison of multiple Amber force fields and development of improved protein backbone parameters

Computational fragment-based binding site identification by ligand competitive saturation

Refining the multiple protein structure pharmacophore method: consistency across three independent HIV-1 protease models.

Protein flexibility and species specificity in structure-based drug discovery: dihydrofolate reductase as a test system.

Small molecule inhibitors of the MDM2-p53 interaction discovered by ensemble-based receptor models.

Novel druggable hot spots in avian influenza neuraminidase H5N1 revealed by computational solvent mapping of a reduced and representative receptor ensemble.

A poke in the eye: inhibiting HIV-1 protease through its flap-recognition pocket

A computational procedure for determining energetically favorable binding sites on biologically important macromolecules.

P304

200-202

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

P31

scholarly article

P356

10.1021/JA1079332

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

P407

P433

2

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

P478

133

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

P50

Heather A Carlson

P577

2010-12-15T00:00:00Z

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

P5875

49683709

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

P698

21158470

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

P932

3081398

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