A Short, Strong Hydrogen Bond in the Active Site of Human Carbonic Anhydrase II - Test2 - elhamkhani - TriplyDB

A Short, Strong Hydrogen Bond in the Active Site of Human Carbonic Anhydrase II

A Short, Strong Hydrogen Bond in the Active Site of Human Carbonic Anhydrase II

http://www.wikidata.org/entity/Q27658556

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Protein design: toward functional metalloenzymes Neutron Structure of Human Carbonic Anhydrase II: Implications for Proton Transfer The unique structure of carbonic anhydrase αCA1 from Chlamydomonas reinhardtii Structural Studies of β-Carbonic Anhydrase from the Green Alga Coccomyxa: Inhibitor Complexes with Anions and Acetazolamide Dithiocarbamates Strongly Inhibit Carbonic Anhydrases and Show Antiglaucoma Action in Vivo Nucleophile recognition as an alternative inhibition mode for benzoic acid based carbonic anhydrase inhibitors Structural and catalytic characterization of a thermally stable and acid-stable variant of human carbonic anhydrase II containing an engineered disulfide bond Structural, catalytic and stabilizing consequences of aromatic cluster variants in human carbonic anhydrase II ‘Unconventional’ Coordination Chemistry by Metal Chelating Fragments in a Metalloprotein Active Site Structural elucidation of the hormonal inhibition mechanism of the bile acid cholate on human carbonic anhydrase II Structural insight into activity enhancement and inhibition of H64A carbonic anhydrase II by imidazoles The Structure of Carbonic Anhydrase IX Is Adapted for Low-pH Catalysis Polyamines and α-Carbonic Anhydrases Probing the surface of human carbonic anhydrase for clues towards the design of isoform specific inhibitors Structural and biophysical characterization of the α-carbonic anhydrase from the gammaproteobacterium Thiomicrospira crunogena XCL-2: insights into engineering thermostable enzymes for CO2 sequestration Structural and catalytic effects of proline substitution and surface loop deletion in the extended active site of human carbonic anhydrase II CheckMyMetal: a macromolecular metal-binding validation tool Coupling Protein Dynamics with Proton Transport in Human Carbonic Anhydrase II.NMR studies of active-site properties of human carbonic anhydrase II by using (15) N-labeled 4-methylimidazole as a local probe and histidine hydrogen-bond correlations.Joint neutron crystallographic and NMR solution studies of Tyr residue ionization and hydrogen bonding: Implications for enzyme-mediated proton transfer.Neutron structure of human carbonic anhydrase II in complex with methazolamide: mapping the solvent and hydrogen-bonding patterns of an effective clinical drug.Model-free extraction of spin label position distributions from pseudocontact shift data.Exploring the influence of the protein environment on metal-binding pharmacophores.Structural insights into carbonic anhydrase IX isoform specificity of carbohydrate-based sulfamates.A class of 4-sulfamoylphenyl-ω-aminoalkyl ethers with effective carbonic anhydrase inhibitory action and antiglaucoma effects.Saccharin: a lead compound for structure-based drug design of carbonic anhydrase IX inhibitors.A sucrose-binding site provides a lead towards an isoform-specific inhibitor of the cancer-associated enzyme carbonic anhydrase IX.Insights towards sulfonamide drug specificity in α-carbonic anhydrases Effects of cryoprotectants on the structure and thermostability of the human carbonic anhydrase II-acetazolamide complex Tracking solvent and protein movement during CO2 release in carbonic anhydrase II crystals.Investigating the selectivity of metalloenzyme inhibitors.Update on carbonic anhydrase inhibitors: a patent review (2008 - 2011).Structural annotation of human carbonic anhydrases.Carbonic anhydrases and their biotechnological applications.Targeting carbonic anhydrase IX activity and expression.Carbonic anhydrase inhibitors: a review on the progress of patent literature (2011-2016).Molecular dynamics study of human carbonic anhydrase II in complex with Zn(2+) and acetazolamide on the basis of all-atom force field simulations The pathway for serial proton supply to the active site of nitrogenase: enhanced density functional modeling of the Grotthuss mechanism.Bile Acid Conjugated DNA Chimera that Conditionally Inhibits Carbonic Anhydrase-II in the Presence of MicroRNA-21.Preliminary X-ray crystallographic analysis of α-carbonic anhydrase from Thiomicrospira crunogena XCL-2.

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A Short, Strong Hydrogen Bond in the Active Site of Human Carbonic Anhydrase II

http://www.wikidata.org/entity/Q27658556

description

2010 nî lūn-bûn

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2010 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2010 թվականի հունվարին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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name

A Short, Strong Hydrogen Bond in the Active Site of Human Carbonic Anhydrase II

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A Short, Strong Hydrogen Bond in the Active Site of Human Carbonic Anhydrase II

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A Short, Strong Hydrogen Bond in the Active Site of Human Carbonic Anhydrase II

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A Short, Strong Hydrogen Bond in the Active Site of Human Carbonic Anhydrase II

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A Short, Strong Hydrogen Bond in the Active Site of Human Carbonic Anhydrase II

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A Short, Strong Hydrogen Bond in the Active Site of Human Carbonic Anhydrase II

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A Short, Strong Hydrogen Bond in the Active Site of Human Carbonic Anhydrase II

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A Short, Strong Hydrogen Bond in the Active Site of Human Carbonic Anhydrase II

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A Short, Strong Hydrogen Bond in the Active Site of Human Carbonic Anhydrase II

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A Short, Strong Hydrogen Bond in the Active Site of Human Carbonic Anhydrase II

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Balendu Sankara Avvaru

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Chae Un Kim

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David N Silverman

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Katherine H Sippel

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Sol M Gruner

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P2860

Substitutions in a flexible loop of horse liver alcohol dehydrogenase hinder the conformational change and unmask hydrogen transfer

Structure of cobalt carbonic anhydrase complexed with bicarbonate

Atomic crystal and molecular dynamics simulation structures of human carbonic anhydrase II: insights into the proton transfer mechanism

Speeding up proton transfer in a fast enzyme: kinetic and crystallographic studies on the effect of hydrophobic amino acid substitutions in the active site of human carbonic anhydrase II

Entrapment of Carbon Dioxide in the Active Site of Carbonic Anhydrase II

Structural study of X-ray induced activation of carbonic anhydrase.

Structural analysis of the zinc hydroxide-Thr-199-Glu-106 hydrogen-bond network in human carbonic anhydrase II

Crystallographic analysis of Thr-200-->His human carbonic anhydrase II and its complex with the substrate, HCO3-

Structure and mechanism of carbonic anhydrase

Identification of proton-transfer pathways in human carbonic anhydrase II.

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249-51

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10.1021/BI902007B

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2

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49

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Mavis Agbandje-McKenna

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2010-01-19T00:00:00Z

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40678368

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20000378

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2810610

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