Electrostatic influence on the kinetics of ligand binding to acetylcholinesterase. Distinctions between active center ligands and fasciculin.
about
A structural snapshot of an intermediate on the streptavidin-biotin dissociation pathwayDual GPCR and GAG mimicry by the M3 chemokine decoy receptorAccelerating the Association of the Most Stable Protein-Ligand Complex by More than Two Orders of MagnitudeElectrostatic interactions in the binding pathway of a transient protein complex studied by NMR and isothermal titration calorimetry.qPIPSA: relating enzymatic kinetic parameters and interaction fields.Association of aminoglycosidic antibiotics with the ribosomal A-site studied with Brownian dynamicsThe use of thermodynamic and kinetic data in drug discovery: decisive insight or increasing the puzzlement?Gated Diffusion-controlled ReactionsPredicting Protein-protein Association Rates using Coarse-grained Simulation and Machine Learning.Kinetics of diffusion-controlled enzymatic reactions with charged substratesFundamental aspects of protein-protein association kineticsThe dynamics of ligand barrier crossing inside the acetylcholinesterase gorgeFinite element solution of the steady-state Smoluchowski equation for rate constant calculationsContinuum diffusion reaction rate calculations of wild-type and mutant mouse acetylcholinesterase: adaptive finite element analysis.Tetrameric mouse acetylcholinesterase: continuum diffusion rate calculations by solving the steady-state Smoluchowski equation using finite element methods.Slow, reversible, coupled folding and binding of the spectrin tetramerization domain.Conformational transitions in protein-protein association: binding of fasciculin-2 to acetylcholinesterase.Electrostatic steering at acetylcholine binding sitesOrder N algorithm for computation of electrostatic interactions in biomolecular systemsNumerical calculation of protein-ligand binding rates through solution of the Smoluchowski equation using smoothed particle hydrodynamicsFinite element analysis of the time-dependent Smoluchowski equation for acetylcholinesterase reaction rate calculations.Poisson-Boltzmann calculations of nonspecific salt effects on protein-protein binding free energies.Quantitative analysis of multisite protein-ligand interactions by NMR: binding of intrinsically disordered p53 transactivation subdomains with the TAZ2 domain of CBP.Conformation gating as a mechanism for enzyme specificity.Prediction of salt and mutational effects on the association rate of U1A protein and U1 small nuclear RNA stem/loop II.Rate theories for biologistsMulti-Scale Continuum Modeling of Biological Processes: From Molecular Electro-Diffusion to Sub-Cellular Signaling TransductionComputational methods for biomolecular electrostatics.Darwinian biophysics: electrostatics and evolution in the kinetics of molecular binding.Quaternary benzyltriethylammonium ion binding to the Na,K-ATPase: a tool to investigate extracellular K+ binding reactions.The role of protonation states in ligand-receptor recognition and binding.Neuronal AChE splice variants and their non-hydrolytic functions: redefining a target of AChE inhibitors?Predicting affinity- and specificity-enhancing mutations at protein-protein interfaces.Computer applications for prediction of protein-protein interactions and rational drug design.Ion binding to biological macromolecules.Interaction of acetylcholinesterase with neurexin-1β regulates glutamatergic synaptic stability in hippocampal neurons.Computational Studies on Acetylcholinesterases.Estimation of kinetic and thermodynamic ligand-binding parameters using computational strategies.Electrostatic attraction of weak monoacid anions increases probability for protonation and passage through aquaporins.Kinetic Insights into the Binding between the nSH3 Domain of CrkII and Proline-Rich Motifs in cAbl
P2860
Q27619071-744EF0C4-D8BE-4C77-97AF-9EB33D22C547Q27649259-184BAF49-2B1E-4D4D-A32C-1C2C9D2C6686Q27714406-701101D8-15A0-44C9-AADB-66D65C1548B7Q30009332-FA3E9A4C-F7F3-4432-9483-5B52C243F5EEQ30365015-AA3BCF2A-7764-48EA-A0CB-A2E361B6E395Q30485247-5328F83C-9D54-420C-8A7C-D4D7970D6C8AQ30881748-CA5015DC-70AD-4111-8DD3-98365AABE0ECQ31011573-CB014F75-1A41-4F97-A198-402DED8F097EQ33572785-7E3B7B2F-56DA-4342-BB0D-0932CD28CC07Q33650706-576F7A04-AF41-4EC9-A153-0BC23915D8B9Q33893739-7870A593-2770-4BA8-8D1A-F0184A80235EQ34183070-70D22C1A-2BE7-429B-8162-72091F77D258Q34185206-A45C9756-F70D-438C-BCBB-2DBDBA763DBFQ34187003-00C43B1E-E0E4-4214-9CA8-A050E150ACEAQ34189318-F676B4E0-5EC9-4A26-9B35-6BAB9786C7ADQ34314714-513CFF82-4769-4C56-B28A-E47C45198395Q34524776-0A5965A6-544D-4C5A-923F-9F9A1F37CE32Q34829773-2C232A73-D393-4746-8D6B-83120DC902BDQ35539942-590DE94D-F2E8-4D62-B4A6-6CE04EDFBA57Q35626805-589AD19E-53C0-4F56-BE48-A6A886132716Q35753783-784769E1-B4A0-47EA-BA7D-43E9632F6D87Q35774389-5976F9AF-A8D0-4462-9B2C-3F2831473A5FQ35791163-20EA3993-0DA3-4A5C-9731-5988F6C67211Q36255724-05523309-A5B1-480E-B16B-C4E3B8FFAC88Q36479185-E92150C3-5602-46C6-A743-949BA465CF7AQ36520904-E76908B8-EEEF-41B1-81A3-F1B38CFB67E6Q36682460-7CE8B950-351F-424A-8671-17ECDB6910E9Q36712976-ABED8111-8B3D-4481-88CC-7CAE09D9E0A5Q37194791-5E2DD964-5714-4C53-81D3-C70B3826EF16Q37416960-17078C64-C626-49B2-A5AC-15D72CDCDE3CQ38061449-BD4794A4-02FA-47FB-8569-F62D0BFE4183Q38132755-EF41A404-407D-461D-880C-6B80F857BD22Q38141059-1B2EEFC3-A6E0-49CB-91F5-F8F77310860CQ38364115-0ABFD519-9E80-40B9-9770-D449CFCC108AQ38379384-8637FA21-2587-4A73-96C0-5E645A1E9B6FQ38599650-2C15D781-4DD1-449D-A765-EA56A3664189Q38630724-F9E74E73-55DE-4DE9-92FC-76E246843AAAQ38737287-22A91A1A-10B4-455B-9972-B67E2AB83D3BQ38866290-D241C199-F3EE-4192-989A-3C299A67367AQ39223642-C1B178DD-DD6A-47D6-B53E-F787C4F9F882
P2860
Electrostatic influence on the kinetics of ligand binding to acetylcholinesterase. Distinctions between active center ligands and fasciculin.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
1997年學術文章
@zh-hant
name
Electrostatic influence on the ...... center ligands and fasciculin.
@en
Electrostatic influence on the ...... center ligands and fasciculin.
@nl
type
label
Electrostatic influence on the ...... center ligands and fasciculin.
@en
Electrostatic influence on the ...... center ligands and fasciculin.
@nl
prefLabel
Electrostatic influence on the ...... center ligands and fasciculin.
@en
Electrostatic influence on the ...... center ligands and fasciculin.
@nl
P2093
P2860
P356
P1476
Electrostatic influence on the ...... center ligands and fasciculin.
@en
P2093
P2860
P304
23265-23277
P356
10.1074/JBC.272.37.23265
P407
P577
1997-09-01T00:00:00Z