Human beta-tryptase is a ring-like tetramer with active sites facing a central pore
about
Identification of a new member of the tryptase family of mouse and human mast cell proteases which possesses a novel COOH-terminal hydrophobic extensionCellular localization of membrane-type serine protease 1 and identification of protease-activated receptor-2 and single-chain urokinase-type plasminogen activator as substratesCrystal structures of the FXIa catalytic domain in complex with ecotin mutants reveal substrate-like interactionsFormation of active monomers from tetrameric human beta-tryptaseThe structure of the human betaII-tryptase tetramer: fo(u)r better or worseActive monomers of human beta-tryptase have expanded substrate specificitiesHuman subjects are protected from mast cell tryptase deficiency despite frequent inheritance of loss-of-function mutationsUrokinase-type plasminogen activator is a preferred substrate of the human epithelium serine protease tryptase epsilon/PRSS22The B12 anti-tryptase monoclonal antibody disrupts the tetrameric structure of heparin-stabilized beta-tryptase to form monomers that are inactive at neutral pH and active at acidic pHProtease signalling: the cutting edgeMast cell proteoglycansNew structural motifs on the chymotrypsin fold and their potential roles in complement factor BCatalytic domain structures of MT-SP1/matriptase, a matrix-degrading transmembrane serine proteinaseStructure of human dipeptidyl peptidase I (cathepsin C): exclusion domain added to an endopeptidase framework creates the machine for activation of granular serine proteasesIsolation, Cloning and Structural Characterisation of Boophilin, a Multifunctional Kunitz-Type Proteinase Inhibitor from the Cattle TickActive site conformational changes of prostasin provide a new mechanism of protease regulation by divalent cationsGlycosylation and the activation of proteinase-activated receptor 2 (PAR(2)) by human mast cell tryptaseSelective inhibition of trypsin by (2R,4R)-4-phenyl-1-[Nalpha-(7- methoxy-2-naphthalenesulfonyl)-L-arginyl]-2-piperidinecarboxylic acidStructural requirements and mechanism for heparin-induced activation of a recombinant mouse mast cell tryptase, mouse mast cell protease-6: formation of active tryptase monomers in the presence of low molecular weight heparinMouse chromosome 17A3.3 contains 13 genes that encode functional tryptic-like serine proteases with distinct tissue and cell expression patternsMutational tail loss is an evolutionary mechanism for liberating marapsins and other type I serine proteases from transmembrane anchors.Tryptase 4, a new member of the chromosome 17 family of mouse serine proteases.Human tryptase epsilon (PRSS22), a new member of the chromosome 16p13.3 family of human serine proteases expressed in airway epithelial cells.Promiscuous processing of human alphabeta-protryptases by cathepsins L, B, and CGeneration of anaphylatoxins by human beta-tryptase from C3, C4, and C5Definition of the extended substrate specificity determinants for beta-tryptases I and II.Structural and energetic determinants of the S1-site specificity in serine proteases.Reversible and noncompetitive inhibition of beta-tryptase by protein surface binding of tetravalent peptide ligands identified from a combinatorial split-mix library.Mast cell peptidases: chameleons of innate immunity and host defense.The bronchial epithelium as a key regulator of airway inflammation and remodelling in asthma.Effect of tryptase inhibition on joint inflammation: a pharmacological and lentivirus-mediated gene transfer study.Human tryptases alpha and beta/II are functionally distinct due, in part, to a single amino acid difference in one of the surface loops that forms the substrate-binding cleft.Structural basis of the resistance of an insect carboxypeptidase to plant protease inhibitorsBiochemical and functional characterization of human transmembrane tryptase (TMT)/tryptase gamma. TMT is an exocytosed mast cell protease that induces airway hyperresponsiveness in vivo via an interleukin-13/interleukin-4 receptor alpha/signal transNatural and synthetic inhibitors of kallikrein-related peptidases (KLKs).Mast cell proteases as pharmacological targetsTryptase: potential role in airway inflammation and remodeling.Tissue-specific expression of mast cell granule serine proteinases and their role in inflammation in the lung and gut.Allostery in trypsin-like proteases suggests new therapeutic strategies.A simple, sensitive and safe method to determine the human α/β-tryptase genotype
P2860
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P2860
Human beta-tryptase is a ring-like tetramer with active sites facing a central pore
description
1998 nî lūn-bûn
@nan
1998 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի մարտին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
name
Human beta-tryptase is a ring-like tetramer with active sites facing a central pore
@ast
Human beta-tryptase is a ring-like tetramer with active sites facing a central pore
@en
Human beta-tryptase is a ring-like tetramer with active sites facing a central pore
@nl
type
label
Human beta-tryptase is a ring-like tetramer with active sites facing a central pore
@ast
Human beta-tryptase is a ring-like tetramer with active sites facing a central pore
@en
Human beta-tryptase is a ring-like tetramer with active sites facing a central pore
@nl
prefLabel
Human beta-tryptase is a ring-like tetramer with active sites facing a central pore
@ast
Human beta-tryptase is a ring-like tetramer with active sites facing a central pore
@en
Human beta-tryptase is a ring-like tetramer with active sites facing a central pore
@nl
P2093
P2860
P356
P1433
P1476
Human beta-tryptase is a ring-like tetramer with active sites facing a central pore
@en
P2093
P2860
P2888
P304
P356
10.1038/32703
P407
P577
1998-03-01T00:00:00Z
P6179
1043336259