Chymotrypsinogen: 2.5-angstrom crystal structure, comparison with alpha-chymotrypsin, and implications for zymogen activation
about
Crystal structure of the HGF beta-chain in complex with the Sema domain of the Met receptorGaussian-weighted RMSD superposition of proteins: a structural comparison for flexible proteins and predicted protein structures.The structure of the human betaII-tryptase tetramer: fo(u)r better or worseMolecular mechanisms for the conversion of zymogens to active proteolytic enzymesStructural basis of profactor D activation: from a highly flexible zymogen to a novel self-inhibited serine protease, complement factor DThe crystal structure of the zymogen catalytic domain of complement protease C1r reveals that a disruptive mechanical stress is required to trigger activation of the C1 complex.The refined 1.9-Å X-ray crystal structure of d-Phe-Pro-Arg chloromethylketone-inhibited human α-thrombin: Structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationshipsThree-dimensional structure of porcine procarboxypeptidase B: a structural basis of its inactivityCrystal Structures of Prethrombin-2 Reveal Alternative Conformations under Identical Solution Conditions and the Mechanism of Zymogen ActivationA Molecular Switch Governs the Interaction between the Human Complement Protease C1s and Its Substrate, Complement C4Biochemical and structural characterization of SplD protease from Staphylococcus aureusStaphylococcal SplB Serine Protease Utilizes a Novel Molecular Mechanism of ActivationComparative studies of the specificities of -chymotrypsin and subtilisin BPN'. Studies with flexible substratesBiophysical highlights from 54 years of macromolecular crystallographySAS-Pro: simultaneous residue assignment and structure superposition for protein structure alignment.Discovery of an allosteric site in the caspasesA mesoscopic model for protein-protein interactions in solution.Lyophilization-induced reversible changes in the secondary structure of proteins.Role of proteolytic enzymes in biological regulation (a review).Using the water signal to detect invisible exchanging protons in the catalytic triad of a serine protease.Sequence organisation and transcriptional regulation of the mouse elastase II and trypsin genesAllostery in trypsin-like proteases suggests new therapeutic strategies.Conformational selection in trypsin-like proteases.Models of the serine protease domain of the human antithrombotic plasma factor activated protein C and its zymogen.Structure and function of microplasminogen: I. Methionine shuffling, chemical proteolysis, and proenzyme activation.The co-crystal structure of unliganded bovine alpha-thrombin and prethrombin-2: movement of the Tyr-Pro-Pro-Trp segment and active site residues upon ligand bindingThe insect immune protein scolexin is a novel serine proteinase homologPartial sequence of human complement component factor B: novel type of serine protease.A novel heparin-dependent processing pathway for human tryptase. Autocatalysis followed by activation with dipeptidyl peptidase I.Theoretical aspects of orbital steering.Inactivation of bovine trypsinogen and chymotrypsinogen by diisopropylphosphorofluoridate.A general method to assess similarity of protein structures, with applications to T4 bacteriophage lysozyme.Stable conformations of aliphatic disulfides: influence of 1,4 interactions involving sulfur atoms.The conformational switch from the factor X zymogen to protease state mediates exosite expression and prothrombinase assembly.Chemical modification of amino groups and guanidino groups of trypsin. Preparation of stable and soluble derivatives.Properties of the histidine residues of indole-chymotrypsin. Implications for the activation process and catalytic mechanism.Hyperconjugation-mediated solvent effects in phosphoanhydride bonds.The reactivity of functional groups as a probe for investigating the topography of tobacco mosaic virus. The use of mutants with additional lysine residues in the coat protein.Protein flexibility, not disorder, is intrinsic to molecular recognition.A competitive labelling method for determining the ionization constants and reactivity of individual histidine residues in proteins. The histidines of -chymotrypsin.
P2860
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P2860
Chymotrypsinogen: 2.5-angstrom crystal structure, comparison with alpha-chymotrypsin, and implications for zymogen activation
description
1970 nî lūn-bûn
@nan
1970 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1970 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1970年の論文
@ja
1970年学术文章
@wuu
1970年学术文章
@zh-cn
1970年学术文章
@zh-hans
1970年学术文章
@zh-my
1970年学术文章
@zh-sg
1970年學術文章
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name
Chymotrypsinogen: 2.5-angstrom ...... cations for zymogen activation
@ast
Chymotrypsinogen: 2.5-angstrom ...... cations for zymogen activation
@en
Chymotrypsinogen: 2.5-angstrom ...... cations for zymogen activation
@nl
type
label
Chymotrypsinogen: 2.5-angstrom ...... cations for zymogen activation
@ast
Chymotrypsinogen: 2.5-angstrom ...... cations for zymogen activation
@en
Chymotrypsinogen: 2.5-angstrom ...... cations for zymogen activation
@nl
prefLabel
Chymotrypsinogen: 2.5-angstrom ...... cations for zymogen activation
@ast
Chymotrypsinogen: 2.5-angstrom ...... cations for zymogen activation
@en
Chymotrypsinogen: 2.5-angstrom ...... cations for zymogen activation
@nl
P2093
P1433
P1476
Chymotrypsinogen: 2.5-angstrom ...... cations for zymogen activation
@en
P2093
P304
P407
P577
1970-04-28T00:00:00Z