Secondary interactions significantly removed from the sulfonamide binding pocket of carbonic anhydrase II influence inhibitor binding constants
about
Structural Analysis of Charge Discrimination in the Binding of Inhibitors to Human Carbonic Anhydrases I and IIHigh-Resolution Crystal Structure of the Subclass B3 Metallo- -Lactamase BJP-1: Rational Basis for Substrate Specificity and Interaction with SulfonamidesThe lab oddity prevails: discovery of pan-CDK inhibitor (R)-S-cyclopropyl-S-(4-{[4-{[(1R,2R)-2-hydroxy-1-methylpropyl]oxy}-5-(trifluoromethyl)pyrimidin-2-yl]amino}phenyl)sulfoximide (BAY 1000394) for the treatment of cancerDependence of Effective Molarity on Linker Length for an Intramolecular Protein−Ligand SystemProbing the energetics of dissociation of carbonic anhydrase-ligand complexes in the gas phase.Designing ligands to bind proteinsThe paradoxical thermodynamic basis for the interaction of ethylene glycol, glycine, and sarcosine chains with bovine carbonic anhydrase II: an unexpected manifestation of enthalpy/entropy compensation.Ultrahigh resolution crystal structures of human carbonic anhydrases I and II complexed with "two-prong" inhibitors reveal the molecular basis of high affinity.Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding.Synthesis, characterization, and anti-amoebic activity of N-(pyrimidin-2-yl)benzenesulfonamide derivatives.Structural analysis of inhibitor binding to human carbonic anhydrase IINovel aromatic/heterocyclic sulfonamides and their metal complexes as inhibitors of carbonic anhydrase isozymes I, II and IV.
P2860
Q27644345-04AC14C6-AE75-4978-8B71-C279AB1ACCA9Q27664009-9E048E62-C093-4DD3-9DA1-982661F81077Q27684613-CE7532D4-D54A-4C04-BE54-2B4ABE8CA936Q29038357-5980A05E-B908-4BE5-8C8F-87B25881205AQ34170705-0CCB3C05-7BFB-47E2-BC0A-FD3C6F942D7DQ36526030-B893399E-287D-47FB-9363-BC2233DDC590Q36842985-76CE091F-E7EF-4AA7-961E-82167FE10A87Q36857153-0E87B7B6-4A14-4C0A-90B2-5DA9BC2DF604Q37108161-6762E3EA-78B5-41BD-A788-6F92492A07C2Q39044582-85D669D9-280F-406E-A9E5-B74DF0004CD8Q42008430-3385991A-1B65-44F7-B0B1-F7DB831AAF8DQ54567997-805F0A1A-3723-43D2-B07A-92139401F8E4
P2860
Secondary interactions significantly removed from the sulfonamide binding pocket of carbonic anhydrase II influence inhibitor binding constants
description
1995 nî lūn-bûn
@nan
1995 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Secondary interactions signifi ...... ce inhibitor binding constants
@ast
Secondary interactions signifi ...... ce inhibitor binding constants
@en
Secondary interactions signifi ...... ce inhibitor binding constants
@nl
type
label
Secondary interactions signifi ...... ce inhibitor binding constants
@ast
Secondary interactions signifi ...... ce inhibitor binding constants
@en
Secondary interactions signifi ...... ce inhibitor binding constants
@nl
prefLabel
Secondary interactions signifi ...... ce inhibitor binding constants
@ast
Secondary interactions signifi ...... ce inhibitor binding constants
@en
Secondary interactions signifi ...... ce inhibitor binding constants
@nl
P2093
P356
P1476
Secondary interactions signifi ...... ce inhibitor binding constants
@en
P2093
D W Christianson
G M Whitesides
J Kingery-Wood
P A Boriack
P304
P356
10.1021/JM00013A004
P407
P577
1995-06-23T00:00:00Z