about
Modeling and structural analysis of PA clan serine proteasesThe midgut of Aedes albopictus females expresses active trypsin-like serine peptidasesIntrinsic evolutionary constraints on protease structure, enzyme acylation, and the identity of the catalytic triadThe structural basis for catalysis and substrate specificity of a rhomboid proteaseStructure and Catalysis of Acylaminoacyl Peptidase: CLOSED AND OPEN SUBUNITS OF A DIMER OLIGOPEPTIDASEStructure and Function of Allophanate HydrolaseStructural Insights into the Effector – Immunity System Tae4/Tai4 from Salmonella typhimuriumS46 Peptidases are the First Exopeptidases to be Members of Clan PAThe crystal structure of the amidohydrolase VinJ shows a unique hydrophobic tunnel for its interaction with polyketide substratesStructure of the nisin leader peptidase NisP revealing a C-terminal autocleavage activityA thermo-responsive protein treatment for dry eyes.Food Value of Mealworm Grown on Acrocomia aculeata Pulp FlourChemical Composition and Food Potential of Pachymerus nucleorum Larvae Parasitizing Acrocomia aculeata KernelsStructural and mutational analyses of dipeptidyl peptidase 11 from Porphyromonas gingivalis reveal the molecular basis for strict substrate specificity.Site-Specific Zwitterionic Polymer Conjugates of a Protein Have Long Plasma Circulation.A simple method for finding a protein's ligand-binding pockets.The intrinsic disorder alphabet. III. Dual personality of serine.Estimating the evidence of selection and the reliability of inference in unigenic evolution.Mechanism of Orlistat Hydrolysis by the Thioesterase of Human Fatty Acid Synthase.Alignment of non-covalent interactions at protein-protein interfaces.The proteolytic system of lactic acid bacteria revisited: a genomic comparisonIdentification of the main venom protein components of Aphidius ervi, a parasitoid wasp of the aphid model Acyrthosiphon pisum.Active site prediction using evolutionary and structural information.Molecular Cloning and Optimization for High Level Expression of Cold-Adapted Serine Protease from Antarctic Yeast Glaciozyma antarctica PI12A trypsin homolog in amphioxus: expression, enzymatic activity and evolution.Using the water signal to detect invisible exchanging protons in the catalytic triad of a serine protease.Neutrophil elastase, proteinase 3, and cathepsin G as therapeutic targets in human diseases.Histidine biosynthesis, its regulation and biotechnological application in Corynebacterium glutamicum.Remarkable diversity in the enzymes catalyzing the last step in synthesis of the pimelate moiety of biotin.Handicap-Recover Evolution Leads to a Chemically Versatile, Nucleophile-Permissive Protease.The channel-activating protease CAP1/Prss8 is required for placental labyrinth maturation.Diversity-enhancing selection acts on a female reproductive protease family in four subspecies of Drosophila mojavensisDecoupled roles for the atypical, bifurcated binding pocket of the ybfF hydrolase.Molecular intercommunication between the complement and coagulation systemsTaking the plunge: integrating structural, enzymatic and computational insights into a unified model for membrane-immersed rhomboid proteolysisCharacterisation of divergent flavivirus NS3 and NS5 protein sequences detected in Rhipicephalus microplus ticks from BrazilWhy Ser and not Thr brokers catalysis in the trypsin foldRole of Corynebacterium glutamicum sprA encoding a serine protease in glxR-mediated global gene regulation.Identification and characterization of a novel serine protease, VvpS, that contains two functional domains and is essential for autolysis of Vibrio vulnificusSerine protease acylation proceeds with a subtle re-orientation of the histidine ring at the tetrahedral intermediate.
P2860
Q21199586-0CA8BDA2-1C51-4BA1-B024-58BBA8623CB1Q24288906-1BCE2F10-278A-404C-A440-2157F79EEB05Q26781998-660B6B9E-CC3B-4C93-A2D2-F2A48E4C5828Q27664874-8171A78B-50CB-4F2D-BD64-C35DC3E39779Q27665946-FD6009C5-FBD5-4FBF-BCD3-E6C9619292FDQ27678562-AA72F745-F77F-49B8-BAB5-D8EE644CDD74Q27678922-8A44EE5D-A991-41C5-A6A1-D1D7E9D69FE5Q27683781-C00B32AE-0E34-4981-9273-0E40E7D71C14Q27689072-3CBB71D8-9A8A-4A85-B3A9-A68D8267B607Q27690679-41FBDDAB-8DB9-47D7-B5EE-5B8ACA47F634Q28115093-B9CA90A4-BA46-45CE-AF4A-6B9486CC8260Q28551010-837EE633-1336-40D6-B4E0-56C748A04330Q28551090-CFD3A8B2-E5CC-4C14-AA87-85C442E0FFC9Q30152912-4D6222F2-90D0-4A0C-8584-34795093A42DQ30278501-29F47CE9-E053-4B2A-940D-5FE29C095434Q30364865-58679657-DD68-4327-A026-E193EBE15331Q30399038-52C14FED-9AE3-426D-A843-F646E9C52936Q30497513-199FB4EF-FC17-4937-B439-A63605263273Q30589786-4E2582AE-0BD3-455A-A454-C7CDE82F3423Q33326651-2120BA36-574C-4327-AC92-38AF10148C86Q33524556-876C49B5-5F8C-47D1-B8AD-05A592CBCAD3Q33669359-06952A9B-0213-450F-9706-ED0EBFACCCEDQ33686362-CBA27FE2-43C0-46E2-86E3-951264080AA9Q33908295-1B8F51FC-DEEF-42DA-889F-12CC2CAFC558Q33916916-DD318E0B-F44E-49D8-B0BD-9A7F2DDE176AQ33978526-8FFD5D61-3678-4A3F-A49C-84F342D6C41FQ34149948-33ECFFA9-7793-4EE3-80D9-30F243DFE579Q34341218-D1243157-E694-4847-87E2-554BAAE73160Q34478005-4DEFF2F2-5B62-4B48-BC56-6A50BDA3963AQ34481684-23F3002B-DF90-4D6F-A571-DA9F6F476E77Q34584498-4886B5EC-8B7E-4ED1-B981-FF96A1A40942Q34715010-F80553C5-C043-4274-8D5D-769AD3450FF0Q34720119-3D864817-6A56-4E70-A5D0-54D7E86D3670Q35067949-536D3AE4-336E-4187-BAB8-17DD202F07C8Q35090253-38BCE860-A926-4640-9E84-E3FC1C762224Q35120221-D971CA44-9E08-49FC-B87C-4F7C141F547BQ35127936-23EFDCBD-2CA3-4410-A55D-64E7FDC82785Q35137740-A01F32E5-8D38-4F8B-B69D-1BA0847AED02Q35139144-02903608-A39F-4750-ACA1-FBA87272AAD7Q35543143-24181479-C0E6-4608-A543-5535E5026C9A
P2860
description
2005 nî lūn-bûn
@nan
2005 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
The catalytic triad of serine peptidases.
@ast
The catalytic triad of serine peptidases.
@en
The catalytic triad of serine peptidases.
@nl
type
label
The catalytic triad of serine peptidases.
@ast
The catalytic triad of serine peptidases.
@en
The catalytic triad of serine peptidases.
@nl
prefLabel
The catalytic triad of serine peptidases.
@ast
The catalytic triad of serine peptidases.
@en
The catalytic triad of serine peptidases.
@nl
P1476
The catalytic triad of serine peptidases.
@en
P2093
P2888
P304
P356
10.1007/S00018-005-5160-X
P577
2005-10-01T00:00:00Z