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

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

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

http://www.wikidata.org/entity/Q28303903

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Non-Classical Inhibition of Carbonic Anhydrase Golgi -mannosidase II cleaves two sugars sequentially in the same catalytic site Role of Hydrophilic Residues in Proton Transfer during Catalysis by Human Carbonic Anhydrase II † ‡Design of a Carbonic Anhydrase IX Active-Site Mimic To Screen Inhibitors for Possible Anticancer Properties † ‡Neutron Structure of Human Carbonic Anhydrase II: Implications for Proton Transfer Structural and Kinetic Study of the Extended Active Site for Proton Transfer in Human Carbonic Anhydrase II Comparison of solution and crystal properties of Co(II)–substituted human carbonic anhydrase II Neutron Structure of Human Carbonic Anhydrase II: A Hydrogen-Bonded Water Network “Switch” Is Observed between pH 7.8 and 10.0 Water Networks in Fast Proton Transfer during Catalysis by Human Carbonic Anhydrase II Kinetic and structural characterization of thermostabilized mutants of human carbonic anhydrase II Voltage-gated proton channels: molecular biology, physiology, and pathophysiology of the H(V) family Interactions of oligomers of organic polyethers with histidine amino acid.Joint neutron crystallographic and NMR solution studies of Tyr residue ionization and hydrogen bonding: Implications for enzyme-mediated proton transfer.Tautomerism of histidine 64 associated with proton transfer in catalysis of carbonic anhydrase.Proton transport in carbonic anhydrase: Insights from molecular simulation.Characterization of CamH from Methanosarcina thermophila, founding member of a subclass of the {gamma} class of carbonic anhydrases.Chemical rescue of enzymes: proton transfer in mutants of human carbonic anhydrase II.Transport activity of the sodium bicarbonate cotransporter NBCe1 is enhanced by different isoforms of carbonic anhydrase Enzymes for carbon sequestration: neutron crystallographic studies of carbonic anhydrase.Malaria parasite carbonic anhydrase: inhibition of aromatic/heterocyclic sulfonamides and its therapeutic potential.Location of binding sites in small molecule rescue of human carbonic anhydrase II.A High-Resolution Crystal Structure of a Psychrohalophilic α-Carbonic Anhydrase from Photobacterium profundum Reveals a Unique Dimer Interface.Production and X-ray crystallographic analysis of fully deuterated human carbonic anhydrase II.Decarboxylation of Lactones over Zn/ZSM-5: Elucidation of the Structure of the Active Site and Molecular Interactions.X-ray crystallographic studies reveal that the incorporation of spacer groups in carbonic anhydrase inhibitors causes alternate binding modes.Insights towards sulfonamide drug specificity in α-carbonic anhydrases Tracking solvent and protein movement during CO2 release in carbonic anhydrase II crystals."Proton holes" in long-range proton transfer reactions in solution and enzymes: A theoretical analysis.Origins of enhanced proton transport in the Y7F mutant of human carbonic anhydrase II.Preferred orientations of His64 in human carbonic anhydrase II Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding.Preliminary joint neutron and X-ray crystallographic study of human carbonic anhydrase II.Functional role of Asp160 and the deprotonation mechanism of ammonium in the Escherichia coli ammonia channel protein AmtB.Toward theoretical analysis of long-range proton transfer kinetics in biomolecular pumps.Effect of active-site mutation at Asn67 on the proton transfer mechanism of human carbonic anhydrase II.Peregrination of the selectivity filter delineates the pore of the human voltage-gated proton channel hHV1.Elucidation of the proton transport mechanism in human carbonic anhydrase II.Identifying Zn-bound histidine residues in metalloproteins using hydrogen-deuterium exchange mass spectrometry.Structural annotation of human carbonic anhydrases.Responsive materials for self-regulated insulin delivery.

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P2860

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

http://www.wikidata.org/entity/Q28303903

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2005 թուականի Փետրուարին հրատարակուած գիտական յօդուած

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