‘Unconventional’ Coordination Chemistry by Metal Chelating Fragments in a Metalloprotein Active Site - Test2 - elhamkhani - TriplyDB

‘Unconventional’ Coordination Chemistry by Metal Chelating Fragments in a Metalloprotein Active Site

‘Unconventional’ Coordination Chemistry by Metal Chelating Fragments in a Metalloprotein Active Site

http://www.wikidata.org/entity/Q27682257

about

Exploring the influence of the protein environment on metal-binding pharmacophores.Fragment-Based Approaches to the Development of Mycobacterium tuberculosis CYP121 Inhibitors.Histone demethylases in physiology and cancer: a tale of two enzymes, JMJD3 and UTX.Methanethiol Binding Strengths and Deprotonation Energies in Zn(II)-Imidazole Complexes from M05-2X and MP2 Theories: Coordination Number and Geometry Influences Relevant to Zinc Enzymes.A Bioinorganic Approach to Fragment-Based Drug Discovery Targeting Metalloenzymes.Effect of donor atom identity on metal-binding pharmacophore coordination.HTS by NMR for the Identification of Potent and Selective Inhibitors of Metalloenzymes.

P2860

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P2860

‘Unconventional’ Coordination Chemistry by Metal Chelating Fragments in a Metalloprotein Active Site

http://www.wikidata.org/entity/Q27682257

description

2014 nî lūn-bûn

@nan

2014 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2014 թվականի ապրիլին հրատարակված գիտական հոդված

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2014年の論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年论文

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‘Unconventional’ Coordination ...... n a Metalloprotein Active Site

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Journal of the American Chemical Society

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‘Unconventional’ Coordination ...... n a Metalloprotein Active Site

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Amy R Marts

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César A F de Oliveira

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David L Tierney

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David P Martin

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Patrick G Blachly

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P2860

Development of the Colle-Salvetti correlation-energy formula into a functional of the electron density

Crystal structures of alpha-mercaptoacyldipeptides in the thermolysin active site: structural parameters for a Zn monodentation or bidentation in metalloendopeptidases

Insight into the stereochemistry in the inhibition of carboxypeptidase A with N-(hydroxyaminocarbonyl)phenylalanine: binding modes of an enantiomeric pair of the inhibitor to carboxypeptidase A

Inhibition of carbonic anhydrase II by thioxolone: a mechanistic and structural study

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

Bidentate Zinc Chelators for α-Carbonic Anhydrases that Produce a Trigonal Bipyramidal Coordination Geometry

Metalloprotein–Inhibitor Binding: Human Carbonic Anhydrase II as a Model for Probing Metal–Ligand Interactions in a Metalloprotein Active Site

Nucleophile recognition as an alternative inhibition mode for benzoic acid based carbonic anhydrase inhibitors

Coot: model-building tools for molecular graphics

PRODRG: a tool for high-throughput crystallography of protein-ligand complexes

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5400-6

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scholarly article

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5106245

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10.1021/JA500616M

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14

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136

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J. Andrew McCammon

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2014-04-09T00:00:00Z

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260873464

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24635441

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