about
Proteopedia - a scientific 'wiki' bridging the rift between three-dimensional structure and function of biomacromoleculesFunction and structure of inherently disordered proteinsThe synaptic acetylcholinesterase tetramer assembles around a polyproline II helixStructure and evolution of the serum paraoxonase family of detoxifying and anti-atherosclerotic enzymesDirected evolution of mammalian paraoxonases PON1 and PON3 for bacterial expression and catalytic specializationMolecular basis of reduced glucosylceramidase activity in the most common Gaucher disease mutant, N370SAn idea whose time has comeA neutral molecule in a cation-binding site: specific binding of a PEG-SH to acetylcholinesterase from Torpedo californicaStructure of a complex of the potent and specific inhibitor BW284C51 with Torpedo californica acetylcholinesteraseAcetylcholinesterase complexed with bivalent ligands related to huperzine a: experimental evidence for species-dependent protein-ligand complementarityX-ray structure of human acid-β-glucosidase, the defective enzyme in Gaucher diseaseProduction of glucocerebrosidase with terminal mannose glycans for enzyme replacement therapy of Gaucher's disease using a plant cell systemCrystal structures of complexes of N-butyl- and N-nonyl-deoxynojirimycin bound to acid beta-glucosidase: insights into the mechanism of chemical chaperone action in Gaucher diseaseUse of a 'caged' analogue to study the traffic of choline within acetylcholinesterase by kinetic crystallographyCrystal 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 SiteShoot-and-Trap: Use of specific x-ray damage to study structural protein dynamics by temperature-controlled cryo-crystallographyAcid beta-glucosidase: insights from structural analysis and relevance to Gaucher disease therapyThe crystal structure of a complex of acetylcholinesterase with a bis-(-)-nor-meptazinol derivative reveals disruption of the catalytic triadCrystallographic snapshots of nonaged and aged conjugates of soman with acetylcholinesterase, and of a ternary complex of the aged conjugate with pralidoximeCharacterization of gene-activated human acid- -glucosidase: Crystal structure, glycan composition, and internalization into macrophagesAcetylcholinesterase: From 3D structure to functionCyclodextrin-mediated crystallization of acid β-glucosidase in complex with amphiphilic bicyclic nojirimycin analoguesBackdoor opening mechanism in acetylcholinesterase based on X-ray crystallography and molecular dynamics simulationsFlexibility of the flap in the active site of BACE1 as revealed by crystal structures and molecular dynamics simulationsComputational redesign of a mononuclear zinc metalloenzyme for organophosphate hydrolysisCatalytic versatility and backups in enzyme active sites: the case of serum paraoxonase 1Catalytic metal ion rearrangements underline promiscuity and evolvability of a metalloenzyme
P50
Q21183903-82219CF6-C93C-4033-A5B1-78DE80DEFA2DQ22061740-7D286BC6-8DDD-47C5-BC2F-E551906274C8Q24311587-E240AF4B-FC7D-49DB-A377-ADAC3BB22BEBQ24337370-5F6A9BBF-697F-4D30-81FF-597E5F7FED6DQ24598027-F39A2A00-AD54-45F2-AC33-C3F639A8BA54Q24621867-CBA3BD8F-3390-403D-BDB6-FBA72FC1CB76Q24642388-2CC92714-03A6-4D14-A8A8-D681A0CB750DQ27639318-C05FB168-6F56-4A07-90FC-B5D8D105E6BCQ27639706-D72D9E72-26AC-43BB-9B53-1CF39A51F2BEQ27640280-07B58D7D-0CF6-40AF-9666-C96DD373DFA6Q27641402-0BD853D1-D752-45EE-88FA-7477E1BB631BQ27644895-713FEB45-EFC7-456A-8F46-E690239EFA9DQ27646926-00D07A6F-E7F5-4037-B964-A02A655E4C74Q27649071-0DD33BB1-68BB-4989-92BB-0503B4E0CE9BQ27650721-425F4899-78B8-4ACC-99AF-917AD57ABA9BQ27651567-B4B1E6EA-D357-495A-AD25-39577CC9FFADQ27652072-3FC1B8F8-5413-4010-80E5-7FE2593264E0Q27654472-848C27C2-FAEB-4CE2-947D-A9F19C084D66Q27656774-391BBFBE-A264-4DAF-B82D-A9F6C45EF5FAQ27657379-9F95E2F5-8E6C-45AC-9CEC-ACF657FCEE3DQ27659614-94BA0FFA-4558-4A7D-9D19-CEFBD3B142A4Q27667205-46DB01D9-E186-45EC-8478-5D45DEABC803Q27667894-1B5609CC-995E-4809-86DC-338937710FB7Q27676370-1D6C5A39-E346-4993-B846-85F845D4CB7CQ27677060-A371DBAA-6DA7-45D0-ACCD-CF61BD23B54EQ27677812-49CCFB5A-F8BD-425C-80A7-219BC3B50C23Q27683778-FEC1351D-C410-4996-AF56-91A07D6A92C4
P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Israel Silman
@ast
Israel Silman
@en
Israel Silman
@es
Israel Silman
@nl
Israel Silman
@sl
type
label
Israel Silman
@ast
Israel Silman
@en
Israel Silman
@es
Israel Silman
@nl
Israel Silman
@sl
prefLabel
Israel Silman
@ast
Israel Silman
@en
Israel Silman
@es
Israel Silman
@nl
Israel Silman
@sl