Structure of a serine protease poised to resynthesize a peptide bond
about
Determinants of Affinity and Proteolytic Stability in Interactions of Kunitz Family Protease Inhibitors with MesotrypsinThe catalytic aspartate is protonated in the Michaelis complex formed between trypsin and an in vitro evolved substrate-like inhibitor: a refined mechanism of serine protease actionThe P 2 ′ residue is a key determinant of mesotrypsin specificity: engineering a high-affinity inhibitor with anticancer activityPresence versus absence of hydrogen bond donor Tyr-39 influences interactions of cationic trypsin and mesotrypsin with protein protease inhibitorsBiochemical identification and crystal structure of kynurenine formamidase from Drosophila melanogasterMastering the canonical loop of serine protease inhibitors: enhancing potency by optimising the internal hydrogen bond networkSequence and conformational specificity in substrate recognition: several human Kunitz protease inhibitor domains are specific substrates of mesotrypsin.Mesotrypsin Has Evolved Four Unique Residues to Cleave Trypsin Inhibitors as SubstratesAn Acrobatic Substrate Metamorphosis Reveals a Requirement for Substrate Conformational Dynamics in Trypsin Proteolysis.Progressive dry-core-wet-rim hydration trend in a nested-ring topology of protein binding interfaces.Contribution of explicit solvent effects to the binding affinity of small-molecule inhibitors in blood coagulation factor serine proteases.Serine protease acylation proceeds with a subtle re-orientation of the histidine ring at the tetrahedral intermediate.Zymogen activation confers thermodynamic stability on a key peptide bond and protects human cationic trypsin from degradation.Hepatocyte growth factor activator (HGFA): molecular structure and interactions with HGFA inhibitor-1 (HAI-1).Mechanisms of macromolecular protease inhibitorsNatural and engineered plasmin inhibitors: applications and design strategies.Recent advances on plasmin inhibitors for the treatment of fibrinolysis-related disorders.A novel subtilase inhibitor in plants shows structural and functional similarities to protease propeptides.Visualization of a substrate-induced productive conformation of the catalytic triad of the Neisseria meningitidis peptidoglycan O-acetylesterase reveals mechanistic conservation in SGNH esterase family members.Enzyme-specific activation versus leaving group ability.Molecular dynamics simulations on pars intercerebralis major peptide-C (PMP-C) reveal the role of glycosylation and disulfide bonds in its enhanced structural stability and function.Development of a Solid-Phase Approach to the Natural Product Class of Ahp-Containing CyclodepsipeptidesIdentification and pharmaceutical evaluation of novel frog skin-derived serine proteinase inhibitor peptide-PE-BBI (Pelophylax esculentus Bowman-Birk inhibitor) for the potential treatment of cancer
P2860
Q27664637-2BAA6383-1870-4A7D-95F8-2BFB4EF2C939Q27666029-B05442D2-0045-4400-B144-0C7BBF82A2BAQ27671330-323CFD90-C38C-4270-908D-838997105A8BQ27679201-CC24619E-68F6-4953-A858-CEC30F9EB358Q27681115-B9045B18-791C-44F0-B0EC-960AA40900DAQ28740672-34C79CDD-00FB-4281-B179-4E8FCA2519E0Q30367678-A29783A2-6E2A-458D-BE76-86283AA31BBEQ30376720-32E753CD-A678-4304-8421-D30175484A08Q30394859-6C6043A1-7068-4473-8114-0E97FE50D319Q31053281-72C24FCE-0A02-4187-B3A3-F38CF5AF5C2FQ33877415-FD167E92-7E0A-4219-9ABB-A8453FEC2C49Q35543143-5E3B8FD3-8E36-49E4-978C-9477CA054B74Q37596314-14AC7957-BE72-4241-AE93-96BC241FD9BEQ37733686-76423D06-377E-4E9C-9D0B-FE5557FF45C6Q37807358-F10684A6-698B-4DB9-A2F5-DB5B2A64849FQ37975189-0CAA3F54-EA2C-4109-8118-F8890ACA928AQ38198582-AACB00B8-9D66-452A-9096-80CA77549888Q38949308-7E04D1A1-BFB9-4A9A-B0D7-079B77F1279EQ41714298-5CF10E35-8A86-45A6-8D10-A27C266FF7BCQ43242803-910640EB-6ADE-4FC3-B0E1-34CBE6F301E5Q52733608-64F83782-2FB3-4A5F-B49D-2BA9014B6F05Q57833371-1613C5AF-419A-4E7C-9390-88FC8D06D467Q59126350-8F82EF5F-6188-4B2B-A695-EC7BE92D30D7
P2860
Structure of a serine protease poised to resynthesize a peptide bond
description
2009 nî lūn-bûn
@nan
2009 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Structure of a serine protease poised to resynthesize a peptide bond
@ast
Structure of a serine protease poised to resynthesize a peptide bond
@en
Structure of a serine protease poised to resynthesize a peptide bond
@nl
type
label
Structure of a serine protease poised to resynthesize a peptide bond
@ast
Structure of a serine protease poised to resynthesize a peptide bond
@en
Structure of a serine protease poised to resynthesize a peptide bond
@nl
prefLabel
Structure of a serine protease poised to resynthesize a peptide bond
@ast
Structure of a serine protease poised to resynthesize a peptide bond
@en
Structure of a serine protease poised to resynthesize a peptide bond
@nl
P2093
P2860
P356
P1476
Structure of a serine protease poised to resynthesize a peptide bond
@en
P2093
David P Goldenberg
Elena Zakharova
Martin P Horvath
P2860
P304
P356
10.1073/PNAS.0902463106
P407
P577
2009-07-07T00:00:00Z