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Identification of Proton-Transfer Pathways in Human Carbonic Anhydrase II
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/(sici)1097-0134(199704)27:4<471::aid-prot1>3.0.co;2-eopenalex-snapshot
Hydration of an α-Helical peptide: comparison of theory and molecular dynamics simulation
inferredcites →https://doi.org/10.1002/(sici)1097-0134(19981001)33:1<119::aid-prot11>3.0.co;2-oopenalex-snapshot
Molecular dynamics simulations of human carbonic anhydrase II: Insight into experimental results and the role of solvation
inferredcites →https://doi.org/10.1002/bip.20516openalex-snapshot
Proton transfer pathways in the mutant His‐64–Ala of human carbonic anhydrase II
inferredcites →https://doi.org/10.1002/cphc.200600128openalex-snapshot
Proton Transfer 200 Years after von Grotthuss: Insights from Ab Initio Simulations
inferredcites →https://doi.org/10.1002/jcc.20289openalex-snapshot
Scalable molecular dynamics with NAMD
inferredcites →https://doi.org/10.1002/jcc.540130812openalex-snapshot
THE weighted histogram analysis method for free‐energy calculations on biomolecules. I. The method
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Protein flexibility predictions using graph theory
inferredcites →https://doi.org/10.1002/prot.20038openalex-snapshot
The mechanism of proton exclusion in aquaporin channels
inferredcites →https://doi.org/10.1002/prot.340040406openalex-snapshot
Refined structure of human carbonic anhydrase II at 2.0 Å resolution
inferredcites →https://doi.org/10.1007/bf01386390openalex-snapshot
A note on two problems in connexion with graphs
inferredcites →https://doi.org/10.1016/0014-5793(88)81156-6openalex-snapshot
Histidine 64 is not required for high CO2 hydration activity of human carbonic anhydrase II
inferredcites →https://doi.org/10.1016/0022-2836(71)90324-xopenalex-snapshot
The interpretation of protein structures: Estimation of static accessibility
inferredcites →https://doi.org/10.1016/0022-2836(92)90531-nopenalex-snapshot
Structure of native and apo carbonic anhydrase II and structure of some of its anion-ligand complexes
inferredcites →https://doi.org/10.1016/0022-2836(92)90572-2openalex-snapshot
Computer simulation of the initial proton transfer step in human carbonic anhydrase I
inferredcites →https://doi.org/10.1016/0263-7855(96)00018-5openalex-snapshot
VMD: Visual molecular dynamics
inferredcites →https://doi.org/10.1016/c2009-0-22837-6openalex-snapshot
Organic Chemistry of Enzyme-Catalyzed Reactions
inferredcites →https://doi.org/10.1016/j.bbabio.2005.09.005openalex-snapshot
Application of classical molecular dynamics for evaluation of proton transfer mechanism on a protein
inferredcites →https://doi.org/10.1016/j.bbabio.2005.12.001openalex-snapshot
Et tu, Grotthuss! and other unfinished stories
inferredcites →https://doi.org/10.1016/j.bbabio.2006.06.017openalex-snapshot
Chance and design—Proton transfer in water, channels and bioenergetic proteins
inferredcites →https://doi.org/10.1016/j.febslet.2004.06.020openalex-snapshot
On the origin of the electrostatic barrier for proton transport in aquaporin
inferredcites →https://doi.org/10.1016/s0005-2728(00)00061-xopenalex-snapshot
Marcus rate theory applied to enzymatic proton transfer
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On the Mechanism of ATP Hydrolysis in F1-ATPase
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Extension to the weighted histogram analysis method: combining umbrella sampling with free energy calculations
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Dynamic proton transfer pathways in proteins: role of sidechain conformational fluctuations
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Proton translocation by bacteriorhodopsin and heme-copper oxidases
inferredcites →https://doi.org/10.1021/ar00145a005openalex-snapshot
The catalytic mechanism of carbonic anhydrase: implications of a rate-limiting protolysis of water
inferredcites →https://doi.org/10.1021/ar0402098openalex-snapshot
Computer Simulation of Proton Solvation and Transport in Aqueous and Biomolecular Systems
inferredcites →https://doi.org/10.1021/ar970218zopenalex-snapshot
Combined Quantum Mechanical/Molecular Mechanical Methodologies Applied to Biomolecular Systems
inferredcites →https://doi.org/10.1021/bi00102a005openalex-snapshot
Conformational mobility of His-64 in the Thr-200 .fwdarw. Ser mutant of human carbonic anhydrase II
inferredcites →https://doi.org/10.1021/bi00110a008openalex-snapshot
Engineering the hydrophobic pocket of carbonic anhydrase II
inferredcites →https://doi.org/10.1021/bi002295zopenalex-snapshot
Structural and Kinetic Analysis of the Chemical Rescue of the Proton Transfer Function of Carbonic Anhydrase II
inferredcites →https://doi.org/10.1021/bi00445a054openalex-snapshot
Role of histidine 64 in the catalytic mechanism of human carbonic anhydrase II studied with a site-specific mutant
inferredcites →https://doi.org/10.1021/bi0480279openalex-snapshot
Structural and Kinetic Characterization of Active-Site Histidine as a Proton Shuttle in Catalysis by Human Carbonic Anhydrase II,
inferredcites →https://doi.org/10.1021/bi062170fopenalex-snapshot
Preferred Orientations of His64 in Human Carbonic Anhydrase II
inferredcites →https://doi.org/10.1021/cr0503052openalex-snapshot
Computational and Theoretical Methods to Explore the Relation between Enzyme Dynamics and Catalysis
inferredcites →https://doi.org/10.1021/ja00025a005openalex-snapshot
Unexpected pH-dependent conformation of His-64, the proton shuttle of carbonic anhydrase II
inferredcites →https://doi.org/10.1021/ja00052a054openalex-snapshot
Mechanism of the human carbonic anhydrase II-catalyzed hydration of carbon dioxide
inferredcites →https://doi.org/10.1021/ja00074a032openalex-snapshot
Theoretical investigation of the CO2 + OH- .fwdarw. HCO3- reaction in the gas and aqueous phases
inferredcites →https://doi.org/10.1021/ja00277a001openalex-snapshot
Theoretical study of the uncatalyzed hydration of carbon dioxide in the gas phase
inferredcites →https://doi.org/10.1021/ja00516a040openalex-snapshot
Rate of exchange of water from the active site of human carbonic anhydrase C
inferredcites →https://doi.org/10.1021/ja016860copenalex-snapshot
Protein Side-Chain Motion and Hydration in Proton-Transfer Pathways. Results for Cytochrome P450cam
inferredcites →https://doi.org/10.1021/ja973397oopenalex-snapshot
Proton Transfer in the Enzyme Carbonic Anhydrase: An ab Initio Study
inferredcites →https://doi.org/10.1021/ja983579yopenalex-snapshot
Solvent Dynamics and Mechanism of Proton Transfer in Human Carbonic Anhydrase II
inferredcites →https://doi.org/10.1021/ja983930fopenalex-snapshot
Dynamics of Functional Water in the Active Site of Native Carbonic Anhydrase from 17O Magnetic Relaxation Dispersion
inferredcites →https://doi.org/10.1021/jp001508ropenalex-snapshot
Proton Transfer in Bacteriorhodopsin: Structure, Excitation, IR Spectra, and Potential Energy Surface Analyses by an ab Initio QM/MM Method
inferredcites →https://doi.org/10.1021/jp0109933openalex-snapshot
Proton Conduction by a Chain of Water Molecules in Carbonic Anhydrase
inferredcites →https://doi.org/10.1021/jp021931vopenalex-snapshot
Is a “Proton Wire” Concerted or Stepwise? A Model Study of Proton Transfer in Carbonic Anhydrase
inferredcites →https://doi.org/10.1021/jp0366015openalex-snapshot
Analyzing Free Energy Relationships for Proton Translocations in Enzymes: Carbonic Anhydrase Revisited
inferredcites →https://doi.org/10.1021/jp052328qopenalex-snapshot
Toward Theoretical Analyis of Long-Range Proton Transfer Kinetics in Biomolecular Pumps
inferredcites →https://doi.org/10.1021/jp973084fopenalex-snapshot
All-Atom Empirical Potential for Molecular Modeling and Dynamics Studies of Proteins
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Reliable treatment of electrostatics in combined QM/MM simulation of macromolecules
inferredcites →https://doi.org/10.1063/1.470648openalex-snapshot
Constant pressure molecular dynamics simulation: The Langevin piston method
inferredcites →https://doi.org/10.1073/pnas.0408117102openalex-snapshot
Computer simulation of explicit proton translocation in cytochrome c oxidase: The D-pathway
inferredcites →https://doi.org/10.1093/nar/gkh381openalex-snapshot
PDB2PQR: an automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations
inferredcites →https://doi.org/10.1111/j.1432-1033.1975.tb02449.xopenalex-snapshot
The Catalytic Mechanism of Carbonic Anhydrase. Hydrogen-Isotope Effects on the Kinetic Parameters of the Human C Isoenzyme
inferredcites →https://doi.org/10.1146/annurev.biophys.32.110601.142445openalex-snapshot
The Role of Dynamics in Enzyme Activity
inferredcites →https://doi.org/10.1529/biophysj.104.043257openalex-snapshot
Studies of Proton Translocations in Biological Systems: Simulating Proton Transport in Carbonic Anhydrase by EVB-Based Models
inferredcites →https://doi.org/10.5860/choice.27-0304openalex-snapshot
Biomembranes: molecular structure and function
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.1002/cbic.70519openalex-snapshot
Proton Transport as a Missing Design Variable in Immobilized Enzyme Catalysis
inferred← citeshttps://doi.org/10.1002/cphc.202500573openalex-snapshot
Effect of Glycosylation on the Reorganization at the Active Site of Human Carbonic Anhydrase IX
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inferred← citeshttps://doi.org/10.1002/med.21497openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/poc.3570openalex-snapshot
Solution properties of phenothiazine drug promazine hydrochloride with cationic hydrotropes in aqueous/electrolyte solution at different temperature
inferred← citeshttps://doi.org/10.1002/prot.24980openalex-snapshot
Identification of putative unfolding intermediates of the mutant His‐107‐tyr of human carbonic anhydrase II in a multidimensional property space
inferred← citeshttps://doi.org/10.1007/978-94-007-7359-2_3openalex-snapshot
Catalytic Mechanism of α-Class Carbonic Anhydrases: CO2 Hydration and Proton Transfer
inferred← citeshttps://doi.org/10.1007/s00726-021-03063-yopenalex-snapshot
Post-translational modifications in tumor-associated carbonic anhydrases
inferred← citeshttps://doi.org/10.1007/s00894-012-1549-2openalex-snapshot
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inferred← citeshttps://doi.org/10.1007/s12039-007-0068-7openalex-snapshot
Effect of electrostatic interactions on the formation of proton transfer pathways in human carbonic anhydrase II
inferred← citeshttps://doi.org/10.1007/s12104-024-10166-6openalex-snapshot
1H, 15N and13C resonance assignments of S2A mutant of human carbonic anhydrase II
inferred← citeshttps://doi.org/10.1007/s12104-024-10203-4openalex-snapshot
1H, 15N and 13C resonance assignments of the S2A and H64A double mutant of human carbonic anhydrase II
inferred← citeshttps://doi.org/10.1016/b978-0-444-63258-6.00009-3openalex-snapshot
Carbonic Anhydrase VII
inferred← citeshttps://doi.org/10.1016/j.apcatb.2014.06.055openalex-snapshot
Selective photocatalytic decomposition of formic acid over AuPd nanoparticle-decorated TiO2 nanofibers toward high-yield hydrogen production
inferred← citeshttps://doi.org/10.1016/j.bbagen.2019.129480openalex-snapshot
Oxygen-oxygen distances in protein-bound crystallographic water suggest the presence of protonated clusters
inferred← citeshttps://doi.org/10.1016/j.bbapap.2009.09.004openalex-snapshot
Role of protein motions on proton transfer pathways in human carbonic anhydrase II
inferred← citeshttps://doi.org/10.1016/j.bbapap.2009.09.006openalex-snapshot
Proton transport in carbonic anhydrase: Insights from molecular simulation
inferred← citeshttps://doi.org/10.1016/j.bmc.2012.08.019openalex-snapshot
Insights towards sulfonamide drug specificity in α-carbonic anhydrases
inferred← citeshttps://doi.org/10.1016/j.bmcl.2010.07.051openalex-snapshot
Crystal structure of the C183S/C217S mutant of human CA VII in complex with acetazolamide
inferred← citeshttps://doi.org/10.1016/j.chemphys.2021.111281openalex-snapshot
Molecular modelling of two coordination states of Zn(II) ion at the active site of human carbonic anhydrase II
inferred← citeshttps://doi.org/10.1016/j.chphi.2024.100625openalex-snapshot
Structure and non-reactive dynamics of the dimeric catalytic domain of human carbonic anhydrase IX
inferred← citeshttps://doi.org/10.1016/j.comptc.2013.02.001openalex-snapshot
Proton affinity of polar amino acid sidechain analogues anchored to the outer wall of single walled carbon nanotubes
inferred← citeshttps://doi.org/10.1016/j.comptc.2013.10.022openalex-snapshot
Free energies of proton transfer by polar amino acid sidechain analogues anchored to the outer wall of single walled carbon nanotubes
inferred← citeshttps://doi.org/10.1016/j.jcat.2024.115384openalex-snapshot
Bifunctional Metal-Acid Sites on Nickel Boride Catalysts:Phenol Hydrodeoxygenation and Water-Promoted C=C Hydrogenation
inferred← citeshttps://doi.org/10.1016/j.jmgm.2019.03.023openalex-snapshot
Orthogonal order parameters to model the reaction coordinate of an enzyme catalyzed reaction
inferred← citeshttps://doi.org/10.1016/j.molcata.2008.07.005openalex-snapshot
Synthesis and photoactivity of Pd substituted nano-TiO2
inferred← citeshttps://doi.org/10.1021/acs.jpcb.3c04721openalex-snapshot
pH-Dependent Structure and Dynamics of the Catalytic Domains of Human Carbonic Anhydrase II and IX
inferred← citeshttps://doi.org/10.1021/acs.jpcb.5b03655openalex-snapshot
Determination of the Reaction Coordinate for a Key Conformational Fluctuation in Human Carbonic Anhydrase II
inferred← citeshttps://doi.org/10.1021/acs.jpcb.6b02166openalex-snapshot
Coupling Protein Dynamics with Proton Transport in Human Carbonic Anhydrase II
inferred← citeshttps://doi.org/10.1021/acs.jpcb.7b10713openalex-snapshot
Reaction Coordinate, Free Energy, and Rate of Intramolecular Proton Transfer in Human Carbonic Anhydrase II
inferred← citeshttps://doi.org/10.1021/acscatal.9b04637openalex-snapshot
Water-Mediated Heterogeneously Catalyzed Reactions
inferred← citeshttps://doi.org/10.1021/acsomega.2c03356openalex-snapshot
Structure and Dynamics of the Isozymes II and IX of Human Carbonic Anhydrase
inferred← citeshttps://doi.org/10.1021/bi801473wopenalex-snapshot
Role of Hydrophilic Residues in Proton Transfer during Catalysis by Human Carbonic Anhydrase II
inferred← citeshttps://doi.org/10.1021/bi802035fopenalex-snapshot
Design of a Carbonic Anhydrase IX Active-Site Mimic To Screen Inhibitors for Possible Anticancer Properties
inferred← citeshttps://doi.org/10.1021/bi901995nopenalex-snapshot
Neutron Structure of Human Carbonic Anhydrase II: Implications for Proton Transfer
inferred← citeshttps://doi.org/10.1021/bi902007bopenalex-snapshot
A Short, Strong Hydrogen Bond in the Active Site of Human Carbonic Anhydrase II
inferred← citeshttps://doi.org/10.1021/cr050262popenalex-snapshot
Carbonic Anhydrase as a Model for Biophysical and Physical-Organic Studies of Proteins and Protein−Ligand Binding
inferred← citeshttps://doi.org/10.1021/cr200176ropenalex-snapshot
Multiple Binding Modes of Inhibitors to Carbonic Anhydrases: How to Design Specific Drugs Targeting 15 Different Isoforms?
inferred← citeshttps://doi.org/10.1021/ic8002004openalex-snapshot
Photochemical Reactions of fac-[Mn(CO)3(phen)imidazole]+: Evidence for Long-Lived Radical Species Intermediates
inferred← citeshttps://doi.org/10.1021/ja1097594openalex-snapshot
Chemical Rescue of Enzymes: Proton Transfer in Mutants of Human Carbonic Anhydrase II
inferred← citeshttps://doi.org/10.1021/ja802264jopenalex-snapshot
Origins of Enhanced Proton Transport in the Y7F Mutant of Human Carbonic Anhydrase II
inferred← citeshttps://doi.org/10.1021/ja8091938openalex-snapshot
Elucidation of the Proton Transport Mechanism in Human Carbonic Anhydrase II
inferred← citeshttps://doi.org/10.1021/jp0757309openalex-snapshot
A Theoretical Study on the Detection of Proton Transfer Pathways in Some Mutants of Human Carbonic Anhydrase II
inferred← citeshttps://doi.org/10.1021/jp101515hopenalex-snapshot
Role of Second Coordination Sphere Amino Acid Residues on the Proton Transfer Mechanism of Human Carbonic Anhydrase II (HCA II)
inferred← citeshttps://doi.org/10.1021/jp808606bopenalex-snapshot
Proton Affinities of Some Amino Acid Side Chains in a Restricted Environment
inferred← citeshttps://doi.org/10.1021/jp8102047openalex-snapshot
Mapping Proton Wires in Proteins: Carbonic Anhydrase and GFP Chromophore Biosynthesis
inferred← citeshttps://doi.org/10.1021/jp9010982openalex-snapshot
Transition Path Sampling Study of the Conformational Fluctuation of His-64 in Human Carbonic Anhydrase II
inferred← citeshttps://doi.org/10.1039/c7cp00887bopenalex-snapshot
Kinetics of CO 2 diffusion in human carbonic anhydrase: a study using molecular dynamics simulations and the Markov-state model
inferred← citeshttps://doi.org/10.1039/d0cp03652hopenalex-snapshot
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inferred← citeshttps://doi.org/10.1039/d0nj03544kopenalex-snapshot
The crystal structures of 2-(4-benzhydrylpiperazin-1-yl)- N -(4-sulfamoylphenyl)acetamide in complex with human carbonic anhydrase II and VII provide insights into selective CA inhibitor development
inferred← citeshttps://doi.org/10.1073/pnas.1520786113openalex-snapshot
Tracking solvent and protein movement during CO 2 release in carbonic anhydrase II crystals
inferred← citeshttps://doi.org/10.1074/jbc.m802134200openalex-snapshot
Nonenzymatic Proton Handling by Carbonic Anhydrase II during H+-Lactate Cotransport via Monocarboxylate Transporter 1
inferred← citeshttps://doi.org/10.1074/jbc.m805353200openalex-snapshot
Entrapment of Carbon Dioxide in the Active Site of Carbonic Anhydrase II
inferred← citeshttps://doi.org/10.1080/07391102.2022.2048075openalex-snapshot
In the footsteps of an inhibitor unbinding from the active site of human carbonic anhydrase II
inferred← citeshttps://doi.org/10.1080/14756366.2016.1225046openalex-snapshot
Insights into the role of reactive sulfhydryl groups of Carbonic Anhydrase III and VII during oxidative damage
inferred← citeshttps://doi.org/10.1107/s0907444913007208openalex-snapshot
X-ray structure of the first `extremo-α-carbonic anhydrase', a dimeric enzyme from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1
inferred← citeshttps://doi.org/10.1107/s2052252514004096openalex-snapshot
Structural insight into activity enhancement and inhibition of H64A carbonic anhydrase II by imidazoles
inferred← citeshttps://doi.org/10.1107/s2052252517017626openalex-snapshot
Active-site solvent replenishment observed during human carbonic anhydrase II catalysis.
inferred← citeshttps://doi.org/10.1517/13543776.2012.707646openalex-snapshot
Update on carbonic anhydrase inhibitors: a patent review (2008 – 2011)
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