Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding. - Test2 - elhamkhani - TriplyDB

Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding.

Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding.

http://www.wikidata.org/entity/Q37108161

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XModeScore: a novel method for accurate protonation/tautomer-state determination using quantum-mechanically driven macromolecular X-ray crystallographic refinement.Apo-Human Carbonic Anhydrase II Revisited: Implications of the Loss of a Metal in Protein Structure, Stability, and Solvent Network ,Structure of a 129 Xe-Cryptophane Biosensor Complexed with Human Carbonic Anhydrase II Design of a Carbonic Anhydrase IX Active-Site Mimic To Screen Inhibitors for Possible Anticancer Properties † ‡Amidation of Bioactive Peptides: The Structure of the Lyase Domain of the Amidating Enzyme High-resolution structure of human carbonic anhydrase II complexed with acetazolamide reveals insights into inhibitor drug design Thermodynamic optimisation in drug discovery: a case study using carbonic anhydrase inhibitors Inhibition and binding studies of carbonic anhydrase isozymes I, II and IX with benzimidazo[1,2-c][1,2,3]thiadiazole-7-sulphonamides Synchrotron Radiation Provides a Plausible Explanation for the Generation of a Free Radical Adduct of Thioxolone in Mutant Carbonic Anhydrase II Molecular Recognition of Insulin by a Synthetic Receptor Human carbonic anhydrase II as a host for piano-stool complexes bearing a sulfonamide anchor Fluoroalkyl and Alkyl Chains Have Similar Hydrophobicities in Binding to the “Hydrophobic Wall” of Carbonic Anhydrase Carbonic anhydrase inhibitors: X-ray crystallographic studies for the binding of N-substituted benzenesulfonamides to human isoform II Mechanism of the hydrophobic effect in the biomolecular recognition of arylsulfonamides by carbonic anhydrase Protein crystal structures with ferrocene and ruthenocene-based enzyme inhibitors Dithiocarbamates Strongly Inhibit Carbonic Anhydrases and Show Antiglaucoma Action in Vivo 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 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 The binding of benzoarylsulfonamide ligands to human carbonic anhydrase is insensitive to formal fluorination of the ligand Structure of a complex formed by a protein and a helical aromatic oligoamide foldamer at 2.1 Å resolution Carborane-based carbonic anhydrase inhibitors 4-amino-substituted benzenesulfonamides as inhibitors of human carbonic anhydrases Functionalization of fluorinated benzenesulfonamides and their inhibitory properties toward carbonic anhydrases Phenols and Polyphenols as Carbonic Anhydrase Inhibitors Cadmium-containing carbonic anhydrase CDCA1 in marine diatom Thalassiosira weissflogii Probing the surface of human carbonic anhydrase for clues towards the design of isoform specific inhibitors Intrinsic Thermodynamics and Structure Correlation of Benzenesulfonamides with a Pyrimidine Moiety Binding to Carbonic Anhydrases I, II, VII, XII, and XIII Titration calorimetry standards and the precision of isothermal titration calorimetry data Differences in the pathways of proteins unfolding induced by urea and guanidine hydrochloride: molten globule state and aggregates.Revisiting zinc coordination in human carbonic anhydrase II.Stabilization of anionic and neutral forms of a fluorophoric ligand at the active site of human carbonic anhydrase I Exploring the influence of the protein environment on metal-binding pharmacophores.Saccharin sulfonamides as inhibitors of carbonic anhydrases I, II, VII, XII, and XIII.Active/inactive dual-probe system for selective photoaffinity labeling of small molecule-binding proteins.Selective fluorescence detection of small-molecule-binding proteins by using a dual photoaffinity labeling system.Ligand-induced protein mobility in complexes of carbonic anhydrase II and benzenesulfonamides with oligoglycine chains A class of 4-sulfamoylphenyl-ω-aminoalkyl ethers with effective carbonic anhydrase inhibitory action and antiglaucoma effects.Enantiopure Cryptophane-(129)Xe Nuclear Magnetic Resonance Biosensors Targeting Carbonic Anhydrase

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Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding.

http://www.wikidata.org/entity/Q37108161

description

article científic

@ca

article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on March 2008

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Carbonic anhydrase as a model ...... ns and protein-ligand binding.

@en

Carbonic anhydrase as a model ...... ns and protein-ligand binding.

@nl

type

label

Carbonic anhydrase as a model ...... ns and protein-ligand binding.

@en

Carbonic anhydrase as a model ...... ns and protein-ligand binding.

@nl

prefLabel

Carbonic anhydrase as a model ...... ns and protein-ligand binding.

@en

Carbonic anhydrase as a model ...... ns and protein-ligand binding.

@nl

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Chemical Reviews

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Carbonic anhydrase as a model ...... ns and protein-ligand binding.

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Adam R Urbach

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Douglas B Weibel

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George K Kaufman

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George M Whitesides

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Irina Gitlin

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Katherine L Gudiksen

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Vijay M Krishnamurthy

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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

Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin

Characterization of CA XV, a new GPI-anchored form of carbonic anhydrase

Crystal structure of the dimeric extracellular domain of human carbonic anhydrase XII, a bitopic membrane protein overexpressed in certain cancer tumor cells

A left-hand beta-helix revealed by the crystal structure of a carbonic anhydrase from the archaeon Methanosarcina thermophila

Entropic contributions to rate accelerations in enzymic and intramolecular reactions and the chelate effect

A novel evolutionary lineage of carbonic anhydrase (epsilon class) is a component of the carboxysome shell

On the attribution and additivity of binding energies

Mitochondrial carbonic anhydrase CA VB: differences in tissue distribution and pattern of evolution from those of CA VA suggest distinct physiological roles

Crystal structure of the secretory form of membrane-associated human carbonic anhydrase IV at 2.8-A resolution

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946-1051

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scholarly article

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10.1021/CR050262P

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3

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108

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2008-03-01T00:00:00Z

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5516329

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18335973

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2740730

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