Chemical rescue of enzymes: proton transfer in mutants of human carbonic anhydrase II. - Wikidata - wikimedia - TriplyDB

Chemical rescue of enzymes: proton transfer in mutants of human carbonic anhydrase II.

Chemical rescue of enzymes: proton transfer in mutants of human carbonic anhydrase II.

http://www.wikidata.org/entity/Q33998251

about

Structural insight into activity enhancement and inhibition of H64A carbonic anhydrase II by imidazoles Out of the active site binding pocket for carbonic anhydrase inhibitors Metal Ion Modeling Using Classical Mechanics Coupling Protein Dynamics with Proton Transport in Human Carbonic Anhydrase II.Transitioning pharmacoperones to therapeutic use: in vivo proof-of-principle and design of high throughput screens.Multiscale simulation reveals a multifaceted mechanism of proton permeation through the influenza A M2 proton channel.Water in the active site of ketosteroid isomerase.Modification of residue 42 of the active site loop with a lysine-mimetic side chain rescues isochorismate-pyruvate lyase activity in Pseudomonas aeruginosa PchB.3-{[(4Z)-1,2-Dimethyl-5-oxoimidazol-4-yl-idene]meth-yl}-4-hy-droxy-benzonitrile.(Z)-4-(2-Hy-droxy-benzyl-idene)-1-methyl-2-phenyl-1H-imidazol-5(4H)-one.(E)-4-[(4-Diethyl-amino-2-hy-droxy-benzyl-idene)amino]-benzonitrile.Structure-based drug discovery of carbonic anhydrase inhibitors.Update on carbonic anhydrase inhibitors: a patent review (2008 - 2011).Structural annotation of human carbonic anhydrases.Exploiting the hydrophobic and hydrophilic binding sites for designing carbonic anhydrase inhibitors.Synthesis, X-ray Structure, Optical, and Electrochemical Properties of a White-Light-Emitting Molecule.Classical Molecular Dynamics with Mobile Protons.Kinetics of CO2 diffusion in human carbonic anhydrase: a study using molecular dynamics simulations and the Markov-state model.In what time scale proton transfer takes place in a live CHO cell?Multiscale modelization in a small virus: Mechanism of proton channeling and its role in triggering capsid disassembly.Crystallography and Its Impact on Carbonic Anhydrase Research A White-Light-Emitting Small Molecule: Synthesis, Crystal Structure, and Optical Properties

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P2860

Chemical rescue of enzymes: proton transfer in mutants of human carbonic anhydrase II.

http://www.wikidata.org/entity/Q33998251

description

2011 nî lūn-bûn

@nan

2011 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի մարտին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

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2011年論文

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2011年论文

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name

Chemical rescue of enzymes: proton transfer in mutants of human carbonic anhydrase II.

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Chemical rescue of enzymes: proton transfer in mutants of human carbonic anhydrase II.

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type

label

Chemical rescue of enzymes: proton transfer in mutants of human carbonic anhydrase II.

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Chemical rescue of enzymes: proton transfer in mutants of human carbonic anhydrase II.

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prefLabel

Chemical rescue of enzymes: proton transfer in mutants of human carbonic anhydrase II.

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Chemical rescue of enzymes: proton transfer in mutants of human carbonic anhydrase II.

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Journal of the American Chemical Society

P1476

Chemical rescue of enzymes: proton transfer in mutants of human carbonic anhydrase II.

@en

P2093

C Mark Maupin

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Chingkuang Tu

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David N Silverman

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Norberto Castillo

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Robert McKenna

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Srabani Taraphder

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P2860

Crystallographic studies of inhibitor binding sites in human carbonic anhydrase II: a pentacoordinated binding of the SCN- ion to the zinc at high pH

Structural and kinetic analysis of the chemical rescue of the proton transfer function of carbonic anhydrase II

The refined atomic structure of carbonic anhydrase II at 1.05 A resolution: implications of chemical rescue of proton transfer

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

Neutron Structure of Human Carbonic Anhydrase II: Implications for Proton Transfer

Refined structure of human carbonic anhydrase II at 2.0 A resolution

The structure and function of the aspartic proteinases

Structural and kinetic characterization of active-site histidine as a proton shuttle in catalysis by human carbonic anhydrase II

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

A theoretical study on the detection of proton transfer pathways in some mutants of human carbonic anhydrase II.

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6223-6234

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scholarly article

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10.1021/JA1097594

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16

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Gregory A. Voth

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2011-03-31T00:00:00Z

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21452838

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4120857

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