Discovering high-affinity ligands for proteins: SAR by NMR
about
Identification of direct protein targets of small moleculesAllosteric regulation of E2:E3 interactions promote a processive ubiquitination machineRole of purine nucleoside phosphorylase in interactions between 2',3'-dideoxyinosine and allopurinol, ganciclovir, or tenofovirThe extracellular human melanoma inhibitory activity (MIA) protein adopts an SH3 domain-like fold.Structural model of ligand-G protein-coupled receptor (GPCR) complex based on experimental double mutant cycle data: MT7 snake toxin bound to dimeric hM1 muscarinic receptorStructural basis of ligand interactions of the large extracellular domain of tetraspanin CD81CHARMM: the biomolecular simulation programThe maximal affinity of ligandsProcess of Fragment-Based Lead Discovery-A Perspective from NMRNative Mass Spectrometry in Fragment-Based Drug DiscoveryGenetics and biology of pancreatic ductal adenocarcinomaSurfing the Protein-Protein Interaction Surface Using Docking Methods: Application to the Design of PPI InhibitorsFragment screening and HIV therapeuticsTargeting BCL2-Proteins for the Treatment of Solid TumoursProtein flexibility in docking and surface mappingComputational methods in drug discoveryBinding Isotherms and Time Courses Readily from Magnetic ResonanceA virtual screen discovers novel, fragment-sized inhibitors of Mycobacterium tuberculosis InhASolution structure and peptide binding studies of the C-terminal src homology 3-like domain of the diphtheria toxin repressor proteinInteractions of human nucleotide excision repair protein XPA with DNA and RPA70 Delta C327: chemical shift mapping and 15N NMR relaxation studiesSite-directed ligand discoverySolution structure of a neurotrophic ligand bound to FKBP12 and its effects on protein dynamicsTransverse relaxation-optimized NMR spectroscopy with the outer membrane protein OmpX in dihexanoyl phosphatidylcholine micellesExperimental and computational mapping of the binding surface of a crystalline proteinIn situ assembly of enzyme inhibitors using extended tetheringThe solution structure of the N-terminal domain of E3L shows a tyrosine conformation that may explain its reduced affinity to Z-DNA in vitroDiscovery of Leukotriene A4 Hydrolase Inhibitors Using Metabolomics Biased Fragment Crystallography †Structural genomics of protein phosphatasesMinimal Pharmacophoric Elements and Fragment Hopping, an Approach Directed at Molecular Diversity and Isozyme Selectivity. Design of Selective Neuronal Nitric Oxide Synthase InhibitorsFunctional and Structural Characterization of DR_0079 from Deinococcus radiodurans , a Novel Nudix Hydrolase with a Preference for Cytosine (Deoxy)ribonucleoside 5′-Di- and Triphosphates †The SOCS Box Domain of SOCS3: Structure and Interaction with the ElonginBC-Cullin5 Ubiquitin LigaseThe RRM domain in GW182 proteins contributes to miRNA-mediated gene silencingMolecular docking and ligand specificity in fragment-based inhibitor discoveryImpact of linker strain and flexibility in the design of a fragment-based inhibitorFragment-based design of ligands targeting a novel site on the integrase enzyme of human immunodeficiency virus 1Leveraging structure determination with fragment screening for infectious disease drug targets: MECP synthase from Burkholderia pseudomalleiStructure of micelle-bound adrenomedullin: a first step toward the analysis of its interactions with receptors and small moleculesStructure of a Monomeric Mutant of the HIV-1 Capsid ProteinDiscovery of Potent Myeloid Cell Leukemia 1 (Mcl-1) Inhibitors Using Fragment-Based Methods and Structure-Based DesignPyrrolamide DNA Gyrase Inhibitors: Fragment-Based Nuclear Magnetic Resonance Screening To Identify Antibacterial Agents
P2860
Q21558640-2EC78DFD-E436-4B43-99BB-937843611B2CQ24317405-8474372E-B266-4C93-B695-04E5D6034381Q24321512-AF6EC45B-E7C3-4564-BC5E-C96A26CC839CQ24536791-76B57AF2-1684-42A4-A98E-ED95FD141EB8Q24595276-8D2B537D-71AE-44B2-9A4F-FC371AE15D6EQ24598370-5B611296-0054-4CB1-8607-723BA4533754Q24658108-F66DADE8-E49A-4555-A141-E14EE0D3D195Q24682680-9DFC2113-3DA1-4208-8A43-C8D624DDE804Q26738768-16D45014-3D30-4A80-AE76-EB3618DED6DFQ26740022-D8333230-969C-4DD9-ABA7-7FDF3E294252Q26765438-5897D69C-6A66-4CD4-9313-BD1C5F08958DQ26823990-A7C30A2C-E06D-4EA8-9D23-36A4DFA23068Q26826945-8F016300-256A-48F9-808A-B07FF9737E16Q26853686-CFA8DDBE-C1F8-486B-8D47-5DE66B5F0682Q26864013-7D22F2CD-8B80-4ACD-BCF4-93669DAFBB38Q26997089-00EB5507-82D1-476E-81F4-3A35AFB80528Q27301803-C2E04580-C107-4A46-B174-C2A50475CB5CQ27339306-E4E32B48-72F2-4598-82DD-964BB8B11A71Q27618358-6EBC7311-A2BE-47D3-A110-264E1E42528BQ27620414-485575F3-5795-4FDD-9A09-830CAA7235ACQ27626501-92AAE046-CD06-45C5-81F9-9E25729CB644Q27626637-E3DC3A43-32AE-44D0-9747-B69A043DB3E8Q27630191-724B121B-3FF6-493B-893F-914F4FA6E4AFQ27631035-418DF9C9-E407-4D2E-AD4B-872A5529DC5DQ27640418-EFBB7B68-5C04-48D5-B49F-12983C05E810Q27643187-D3DF4459-EE5D-4159-8414-3C39BFB117C8Q27646546-F7756F19-DB1B-4D1D-9FB6-3AB1E10A1F7EQ27649211-EDACAABC-64A3-4CBE-844B-3AB638B97806Q27649995-225288C9-C698-4480-A84F-0E96EBF2A25AQ27650724-7CAE105B-478B-455A-83F5-1194613FEAB5Q27651007-5755F6EF-084C-4348-86FD-2DCB0C367EADQ27654194-F3934E9B-E8DF-481B-B958-82AA4E0D1950Q27654237-54215B66-ACB5-4325-85D6-B06FCE23AE97Q27655287-2F2BE6C8-1440-438F-9BB0-B5A8BC5181DAQ27666603-8900B557-7965-41E5-9A80-FBED1A2FAA34Q27667103-35CC2C6A-C1BB-4CF5-BCED-D9AFF74B877CQ27671655-56584302-5AED-4525-9912-208F8DA09ADFQ27675009-FD404089-8882-4DDA-8723-06E38E55C114Q27675512-DB80E326-B2B7-4A89-AB7B-9E4F87981D09Q27676314-F6919056-4BC1-4E18-8E88-5EC9A73FBBBA
P2860
Discovering high-affinity ligands for proteins: SAR by NMR
description
1996 nî lūn-bûn
@nan
1996 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
Discovering high-affinity ligands for proteins: SAR by NMR
@ast
Discovering high-affinity ligands for proteins: SAR by NMR
@en
type
label
Discovering high-affinity ligands for proteins: SAR by NMR
@ast
Discovering high-affinity ligands for proteins: SAR by NMR
@en
prefLabel
Discovering high-affinity ligands for proteins: SAR by NMR
@ast
Discovering high-affinity ligands for proteins: SAR by NMR
@en
P2093
P3181
P1433
P1476
Discovering high-affinity ligands for proteins: SAR by NMR
@en
P2093
P304
P3181
P356
10.1126/SCIENCE.274.5292.1531
P407
P577
1996-11-29T00:00:00Z