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Improving the catalytic activity of hyperthermophilic Pyrococcus horikoshii prolidase for detoxification of organophosphorus nerve agents over a broad range of temperaturesStructure of human cytosolic X-prolyl aminopeptidase: a double Mn(II)-dependent dimeric enzyme with a novel three-domain subunitStructural and functional analysis of the Spt16p N-terminal domain reveals overlapping roles of yFACT subunitsThe FACT Spt16 “peptidase” domain is a histone H3–H4 binding moduleInfluence of intermolecular contacts on the structure of recombinant prolidase fromThermococcus sibiricusOrganophosphorus acid anhydrolase fromAlteromonas macleodii: structural study and functional relationship to prolidasesProlidase function in proline metabolism and its medical and biotechnological applicationsKinetic and structural evidences on human prolidase pathological mutants suggest strategies for enzyme functional rescueCrystal Structural and Functional Analysis of the Putative Dipeptidase from Pyrococcus horikoshii OT3Prolidase directly binds and activates epidermal growth factor receptor and stimulates downstream signalingMolecular characterisation of six patients with prolidase deficiency: identification of the first small duplication in the prolidase gene and of a mutation generating symptomatic and asymptomatic outcomes within the same family.Analyzing the catalytic role of Asp97 in the methionine aminopeptidase from Escherichia coli.Model organisms for genetics in the domain Archaea: methanogens, halophiles, Thermococcales and Sulfolobales.Organophosphorus hydrolase as an in vivo catalytic nerve agent bioscavenger.Current and emerging strategies for organophosphate decontamination: special focus on hyperstable enzymes.A plasma proteolysis pathway comprising blood coagulation proteasesStructure of recombinant prolidase from Thermococcus sibiricus in space group P21221.Osmoprotection of Bacillus subtilis through import and proteolysis of proline-containing peptides.Structural basis of substrate selectivity of E. coli prolidaseFE(II) is the native cofactor for Escherichia coli methionine aminopeptidase.Crystallization and preliminary X-ray diffraction analysis of Xaa-Pro dipeptidase from Xanthomonas campestris.Characterization of the dinuclear metal center of Pyrococcus furiosus prolidase by analysis of targeted mutants.Crystal structure of a dodecameric tetrahedral-shaped aminopeptidase.PEPD is a pivotal regulator of p53 tumor suppressor.Crystal structure of a novel prolidase from Deinococcus radiodurans identifies new subfamily of bacterial prolidases.Characterization of recombinant prolidase from Lactococcus lactis- changes in substrate specificity by metal cations, and allosteric behavior of the peptidase.Aminopeptidase p mediated detoxification of organophosphonate analogues of sarin: mechanistic and stereochemical study at the phosphorus atom of the substrate.Substrate specificity and reaction mechanism of human prolidase.Comprehensive in-silico prediction of damage associated SNPs in Human Prolidase gene.High-level expression and molecular characterization of a recombinant prolidase from NovaBlue
P2860
Q21296775-085E8492-79CF-46E9-AED7-0E605A6FDD88Q24318414-11292C45-C2A2-40F4-A5E0-488C43133681Q27649362-BAC6C087-3AFC-4D24-B9B2-07BDEC4D0A0BQ27650951-9941B7E6-A755-4C96-9C39-C0FDF11ED859Q27675063-1CD6DBCB-172C-497B-97E5-B34E3C2523BAQ27677152-1E9943A6-493E-4199-A689-142232126F84Q28264745-471CA28C-772E-49D5-9197-806A89E03CFAQ28487971-2CF9AE84-CF7B-4735-9F5F-5A68BDC75404Q33621760-2FF75241-098B-48DF-9F40-6DEC9AA9811FQ36561975-96CE2E87-A572-4C6D-BC4F-18F183A9C039Q36927164-710CDF7F-64A6-491E-9FD5-21A7F43D0D16Q37234265-317C7B16-BDC7-4229-BF66-8BC9B0E3178FQ37832278-1658C6AF-CC7E-4C1A-951B-D010A8BAEE18Q37989116-89CF54C1-1364-442E-8AD2-30C454F94449Q38718707-9DB67FE7-13B8-428D-9710-BFC10694B894Q39539762-D65B498D-89EF-4B76-B419-3AFBB8D659D8Q40652040-43F51AA4-7106-42CE-B535-6813E33E0702Q41843133-BE67E70A-639E-4309-85E4-CDFF91DFB4BFQ42066132-8726A366-D81E-4267-B740-DEFE674387B8Q42077475-56546F64-8CE9-45EE-BFE6-C5F14177FDC6Q42868305-35ED6C64-7BBF-4BF8-B641-E23A37A5413BQ44863708-CDC8A07A-3405-465F-BE73-B2704D11A27BQ45064158-282DFD3B-ED44-440D-8E26-7C182F78A181Q46242652-8B23AC84-3584-439B-8AA1-312E200D2CF8Q46304080-2B6B049E-BB3A-4E02-8FE0-24AD2448C57DQ46857629-9FA832FB-78DF-4F09-8BF3-57C729673292Q46938105-A92728EB-ADB0-4BC3-8300-B5236EB6B883Q50907640-4D08EC5D-CBE8-4A4E-BE01-D5B8632A425EQ55334221-AFF5CC13-4E02-4260-9B9A-8B7B371E7517Q58587291-A6160FB0-875E-4E2E-9C61-45EE5EDB75BB
P2860
description
2004 nî lūn-bûn
@nan
2004 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի մարտին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Structure of the prolidase from Pyrococcus furiosus
@ast
Structure of the prolidase from Pyrococcus furiosus
@en
Structure of the prolidase from Pyrococcus furiosus
@nl
type
label
Structure of the prolidase from Pyrococcus furiosus
@ast
Structure of the prolidase from Pyrococcus furiosus
@en
Structure of the prolidase from Pyrococcus furiosus
@nl
prefLabel
Structure of the prolidase from Pyrococcus furiosus
@ast
Structure of the prolidase from Pyrococcus furiosus
@en
Structure of the prolidase from Pyrococcus furiosus
@nl
P2093
P356
P1433
P1476
Structure of the prolidase from Pyrococcus furiosus
@en
P2093
Amy M Grunden
Angeli L Menon
Hans C Freeman
J Mitchell Guss
Megan J Maher
Michael W W Adams
Mousumi Ghosh
P304
P356
10.1021/BI0356451
P407
P50
P577
2004-03-16T00:00:00Z