About: Interaction between serine (pro)enzymes, and kazal and kunitz inhibitors

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About: Interaction between serine (pro)enzymes, and kazal and kunitz inhibitors Goto Sponge NotDistinct Permalink

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scientific article published on 01 April 1983

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована у квітні 1983 (uk) im April 1983 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu n'abril de 1983 (ast) scientific article published on 01 April 1983 (en)
publication date	wds:Q56877767-9285E6ED-1D93-4A93-BB15-5AE36A14DAAF
publication date	1983-04-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q56877767-6E72B8B2-9214-44D5-846A-1DB450953A49
language of work or name	English
cites work	wds:Q56877767-05158E97-95CF-4934-B209-F4690380F27D wds:Q56877767-073AAF7D-291C-4842-A443-76534A6ACC63 wds:Q56877767-08242FBE-D9E7-4670-B841-97F7AB78F5CE wds:Q56877767-094717E3-9216-4F78-9DE0-EF311D01A120 wds:Q56877767-0E98A7C3-F350-4B60-949C-70813DF1B436 wds:Q56877767-16BC5E61-BF81-401D-A493-E894ECB96079 wds:Q56877767-173C489F-1C05-4B2D-97C6-34B0C85C5754 wds:Q56877767-1BB55F32-A716-4A86-A86D-D4656D37CBD7 wds:Q56877767-249205E9-7217-4135-AB48-DCF7D30BF98C wds:Q56877767-32370AF8-C557-4207-AF9D-10097A86F796 wds:Q56877767-3802AAB8-FCEC-4713-A464-6D07E7C16B57 wds:Q56877767-3CCB295A-0C1A-4F9C-B112-85CC9058A218 wds:Q56877767-3DD4B769-1692-47DF-9C77-AE490C97372B wds:Q56877767-4C3239B5-5098-462F-ADEB-A86DA4A30CC7 wds:Q56877767-5525908C-3FB4-4855-9B8E-BC587EB78631 wds:Q56877767-5871712B-D8FA-4A01-A665-3B815673F776 wds:Q56877767-5B7616A6-5A09-4B3B-BD68-2953B4EA5E64 wds:Q56877767-60EA978B-A58A-4916-A85D-DB83A322F596 wds:Q56877767-6AFBF0D1-DD09-4D9B-B944-ED48A90A238A wds:Q56877767-7A43FFBA-3F4E-4E6A-B85E-FC623DBB860E wds:Q56877767-7BE5E451-C122-4481-8501-9ADE45ADF480 wds:Q56877767-97C82440-52F0-4CA6-B974-8CCAFC052879 wds:Q56877767-9A4571E4-2EFA-4BA2-9CBF-84F0C1EF0315 wds:Q56877767-9AF68B65-259A-4C95-AA18-489E7458CA3C wds:Q56877767-A1443267-642B-4EE6-A923-184FF73FDF6F wds:Q56877767-AF5BB3CC-2D32-447A-8038-0F78EE4EB414 wds:Q56877767-B1E8C811-79AD-477C-BF2F-5FB88A4A5142 wds:Q56877767-B459ECB6-F1DF-4170-8B8B-5B377B83188F wds:Q56877767-D1E38388-FF32-4202-991A-65E3BD75E9DA wds:Q56877767-D5427DC9-FEEA-4ACF-9FD7-DBD107B0BE5C wds:Q56877767-DF0D4130-F6CA-450E-AB1B-932FBC534A30 wds:Q56877767-E3E40364-5589-426B-A64C-EB5729BEF86D wds:Q56877767-F0EA2100-031F-458F-8CBB-D75B53F91922 wds:Q56877767-F222E165-01F5-400A-A3F8-5CAB915E45CB wds:Q56877767-F9561012-5C6F-45C3-90BE-847BC23D546F
cites work	Trypsin--pancreatic secretory inhibitor (Kazal inhibitor) interaction. Kinetic and thermodynamic properties. Crystal structure of a bacterial protein proteinase inhibitor (Streptomyces subtilisin inhibitor) at 2·6 Å resolution Crystallization, crystal structure analysis and molecular model of the third domain of Japanese quail ovomucoid, a Kazal type inhibitor Three-dimensional structure of the complex between pancreatic secretory trypsin inhibitor (Kazal type) and trypsinogen at 1.8 A resolution. Structure solution, crystallographic refinement and preliminary structural interpretation The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. II. The binding of the pancreatic trypsin inhibitor and of isoleucine-valine and of sequentially related peptides to trypsinogen and to p-guanidinobenzoate-tryp Structural basis of the activation and action of trypsin Structure of crystalline -chymotrypsin. V. The atomic structure of tosyl- -chymotrypsin at 2 A resolution Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. Crystal structure determination and stereochemistry of the contact region Trypsin-pancreatic trypsin inhibitor association. Dynamics of the interaction and role of disulfide bridges Induction of the bovine trypsinogen-trypsin transition by peptides sequentially similar to the N-terminus of trypsin The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. The refined crystal structures of the bovine trypsinogen-pancreatic trypsin inhibitor complex and of its ternary complex with Ile-Val at 1.9 A resolution Protein inhibitors of proteinases Pancreatic trypsin inhibitor. II. Reaction with trypsin Conformational equilibria in -and -chymotrypsin. The energetics and importance of the salt bridge LINKED FUNCTIONS AND RECIPROCAL EFFECTS IN HEMOGLOBIN: A SECOND LOOK. The Use of Esters of N-Hydroxysuccinimide in Peptide Synthesis Binding of benzoamidine and protons to trypsin as measured by difference spectra Pre-existence of the active site in zymogens, the interaction of trypsinogen with the basic pancreatic trypsin inhibitor (Kunitz) Investigation of serum trypsin and related substances. I. The quantitative demonstration of trypsinlike activity in human blood serum by a micromethod The reliability of Michaelis constants and maximum velocities estimated by using the integrated Michaelis–Menten equation Catalytic properties of human urinary kallikrein Catalytic properties of serine proteases. 2. Comparison between human urinary kallikrein and human urokinase, bovine beta-trypsin, bovine thrombin, and bovine alpha-chymotrypsin The Interaction between alpha-Chymotrypsin and Pancreatic Trypsin Inhibitor (Kunitz Inhibitor). Kinetic and Thermodynamic Properties Differential titration of trypsin-like enzymes Hydrolysis of Amino-Acid Esters by Pig-Pancreatic Kallikrein Kinetics of the interaction of bovine pancreatic trypsin inhibitor (Kunitz) with alpha-chymotrypsin. Stopped-flow kinetics of the resynthesis of the reactive site peptide bond in kallikrein inhibitor (Kunitz) by β-trypsin Inhibition of porcine glandular kallikreins by structurally homologous proteinase inhibitors of the Kunitz (Trasylol) type. Significance of the basic nature of amino acid residues in subside positions for kallikrein inhibition Isolation and characterization of a new form of the porcine pancreatic secretory trypsin inhibitor. Biochemical studies and high-resolution 1H-NMR Isolation and characterization of human urinary kallikrein The hydrolysis of alpha-CBZ-L-lysine-p-nitrophenyl ester by two forms of human urokinase “Subunit-exchange” chromatography of proteins: Behavior of α-chymotrypsin Active site in zymogens. Proton magnetic resonance pH titration curves of histidine-57 in porcine and bovine trypsinogens and in their complexes with bovine pancreatic trypsin inhibitor (Kunitz) On the reaction of acetamidomethanol with native and reduced bovine pancreatic trypsin inhibtor (Kunitz inhibitor) Benzyloxycarbonylarginine nitrophenyl ester salts: 1-hydroxybenzotriazole catalyzed acylations of amines
author name string	wds:Q56877767-09C9E146-6DC2-4330-9648-D4897E3B80D3 wds:Q56877767-1F48047A-83CE-45D5-8654-CF8C53A62011 wds:Q56877767-35C7C94E-FEF7-4E7A-AA89-FD22B24B125F wds:Q56877767-67E8381A-B797-484F-AC80-2A8A83C042BB wds:Q56877767-72415091-8B13-4BC7-80F5-2BA8886191BE
author name string	G Gatti P Ascenzi E Antonini E Menegatti M Guarneri
rdfs:label	Interaction between serine (pro)enzymes, and kazal and kunitz inhibitors (en) Interaction between serine (pro)enzymes, and kazal and kunitz inhibitors (nl)
skos:prefLabel	Interaction between serine (pro)enzymes, and kazal and kunitz inhibitors (en) Interaction between serine (pro)enzymes, and kazal and kunitz inhibitors (nl)
name	Interaction between serine (pro)enzymes, and kazal and kunitz inhibitors (en) Interaction between serine (pro)enzymes, and kazal and kunitz inhibitors (nl)
author	wds:Q56877767-E7CC0A23-49D8-401E-8421-026533993138
author	Martino Bolognesi
title	wds:Q56877767-C3A8E63A-B7C6-4F4F-8482-253CDE7F92DD
title	Interaction between serine (pro)enzymes, and Kazal and Kunitz inhibitors (en)

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