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http://hub.abes.fr/acs/periodical/bichaw/2002/volume_41/issue_11/101021bi020016x/authorship/7
http://hub.abes.fr/acs/periodical/bichaw/1991/volume_30/issue_21/101021bi00235a015/authorship/4
http://hub.abes.fr/acs/periodical/bichaw/1992/volume_31/issue_48/101021bi00163a039/authorship/3
http://hub.abes.fr/acs/periodical/bichaw/1978/volume_17/issue_6/101021bi00599a029/authorship/2
http://hub.abes.fr/oup/periodical/bioinformatics/2005/volume_21/issue_16/101093bioinformaticsbti537/authorship/7
http://hub.abes.fr/acs/periodical/jacsat/1992/volume_114/issue_10/101021ja00036a043/authorship/9
http://hub.abes.fr/acs/periodical/bichaw/2002/volume_41/issue_9/101021bi011652i/authorship/10
http://hub.abes.fr/acs/periodical/jpcafh/2002/volume_106/issue_1/101021jp0113275/authorship/9
http://hub.abes.fr/acs/periodical/bichaw/2002/volume_41/issue_35/101021bi020151/authorship/10
http://hub.abes.fr/oup/periodical/nar/2007/volume_35/issue_suppl2/101093nargkm307/authorship/3
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http://hub.abes.fr/oup/periodical/proeng/2009/volume_22/issue_10/101093proteingzp045/authorship/6
http://hub.abes.fr/acs/periodical/jmcmar/2006/volume_49/issue_18/101021jm060164b/authorship/9
http://hub.abes.fr/acs/periodical/jpcafh/2001/volume_105/issue_8/101021jp002933n/authorship/5
http://hub.abes.fr/acs/periodical/jpcbfk/2005/volume_109/issue_49/101021jp0552877/authorship/6
http://hub.abes.fr/acs/periodical/bichaw/2001/volume_40/issue_35/101021bi0101392/authorship/5
http://hub.abes.fr/acs/periodical/jmcmar/2001/volume_44/issue_20/101021jm010826r/authorship/11
http://hub.abes.fr/acs/periodical/jacsat/2003/volume_125/issue_37/101021ja029775t/authorship/4
http://hub.abes.fr/acs/periodical/jacsat/2003/volume_125/issue_2/101021ja021111w/authorship/7
http://hub.abes.fr/acs/periodical/jpcafh/2004/volume_108/issue_43/101021jp0476850/authorship/8
http://hub.abes.fr/acs/periodical/jacsat/2008/volume_130/issue_25/101021ja7109822/authorship/3
http://hub.abes.fr/acs/periodical/jpcafh/2000/volume_104/issue_42/101021jp001306v/authorship/8
http://hub.abes.fr/acs/periodical/jacsat/2004/volume_126/issue_47/101021ja0466154/authorship/8
http://hub.abes.fr/acs/periodical/jacsat/2005/volume_127/issue_31/101021ja051765f/authorship/6
http://hub.abes.fr/acs/periodical/jpcafh/2001/volume_105/issue_22/101021jp003098c/authorship/9
http://hub.abes.fr/acs/periodical/bichaw/1977/volume_16/issue_12/101021bi00631a018/authorship/2
http://hub.abes.fr/acs/periodical/bichaw/1982/volume_21/issue_9/101021bi00538a013/authorship/4
http://hub.abes.fr/acs/periodical/bichaw/1994/volume_33/issue_48/101021bi00252a006/authorship/5
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.gamma.-Chymotrypsin is a complex of .alpha.-chymotrypsin with its own autolysis products
Simple general acid-base catalysis of physiological acetylcholinesterase reactions
Novel pyrene-containing organophosphates as fluorescent probes for studying aging-induced conformational changes in organophosphate-inhibited acetylcholinesterase
Characterization of gene-activated human acid-β-glucosidase: Crystal structure, glycan composition, and internalization into macrophages
Acetylcholinesterase Complexed with Bivalent LigandsRelated to Huperzine A: Experimental Evidence forSpecies-Dependent Protein−Ligand Complementarity
Crystal Packing Mediates Enantioselective LigandRecognition at the Peripheral Site of Acetylcholinesterase
A Structure-Based Design Approach to the Development of Novel, ReversibleAChE Inhibitors
Theoretical Insight into the Interactions of TMA-Benzene and TMA-Pyrrole with B3LYPDensity-Functional Theory (DFT) and ab Initio Second Order Møller−Plesset PerturbationTheory (MP2) Calculations
FoldIndex©: a simple tool to predict whether a given protein sequence is intrinsically unfolded
Design, expression and characterization of mutants of fasciculin optimized for interaction with its target, acetylcholinesterase
How Does Huperzine A Enter and Leave the Binding Gorge ofAcetylcholinesterase? Steered Molecular DynamicsSimulations
Quantum/Classical Mechanical Comparison of Cation−π Interactions betweenTetramethylammonium and Benzene
A Structural Motif of Acetylcholinesterase That Promotes Amyloid β-Peptide FibrilFormation
3D Structure of Torpedo californica Acetylcholinesterase Complexed with HuprineX at 2.1 Å Resolution: Kinetic and Molecular Dynamic Correlates,
A server and database for dipole moments of proteins
The Relationship between Binding Models of TMA with Furan and Imidazole and theMolecular Electrostatic Potentials: DFT and MP2 Computational Studies
How Does Ammonium Interact with Aromatic Groups? A Density Functional Theory(DFT/B3LYP) Investigation
The Complex of a Bivalent Derivative of Galanthamine withTorpedo Acetylcholinesterase Displays Drastic Deformation ofthe Active-Site Gorge: Implications for Structure-Based DrugDesign
Kinetic and Structural Studies on the Interaction of Cholinesterases with theAnti-Alzheimer Drug Rivastigmine,
X-ray Structures of Torpedo californica Acetylcholinesterase Complexed with(+)-Huperzine A and (−)-Huperzine B: Structural Evidence for an Active SiteRearrangement,
Complexes of Alkylene-Linked Tacrine Dimers with Torpedo californica Acetylcholinesterase: Binding of Bis(5)-tacrine Produces a Dramatic Rearrangement in the Active-Site Gorge
Crystal Structure of Thioflavin T Bound to the Peripheral Site of Torpedo californica Acetylcholinesterase Reveals How Thioflavin T Acts as a Sensitive Fluorescent Reporter of Ligand Binding to the Acylation Site
Additivity of Cation−π Interactions: An ab Initio Computational Study on π−Cation−πSandwich Complexes
Dynamic Mechanism of E2020 Binding to Acetylcholinesterase: A Steered MolecularDynamics Simulation
Inactivation of electric eel acetylcholinesterase by acylation with N-hydroxysuccinimide esters of amino acid derivatives
Effects of quaternary ligands on the inhibition of acetylcholinesterase by arsenite
A Metastable State of Torpedo californica Acetylcholinesterase Generated by Modification with Organomercurials
Chemical modification of Torpedo acetylcholinesterase by disulfides: appearance of a "molten globule" state
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