About: Structural implications for the role of the N terminus in the ‘superactivation’ of collagenases

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About: Structural implications for the role of the N terminus in the ‘superactivation’ of collagenases Goto Sponge NotDistinct Permalink

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description	article (en) ലേഖനം (ml) artículu científicu (ast) wetenschappelijk artikel (nl) наукова стаття, опублікована в січні 1994 (uk) im Januar 1994 veröffentlichter wissenschaftlicher Artikel (de)
publication date	wds:Q56603117-67BA171E-52A1-493F-9AF3-4896C2AEF5E5
publication date	1994-01-31 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q56603117-AD8C855B-1931-42B8-8D75-127246D1BD66
language of work or name	English
cites work	wds:Q56603117-11048455-5644-42FC-BCA0-174E1B351760 wds:Q56603117-170057C6-BC02-4669-86A7-525479A34C8F wds:Q56603117-2E7D59EF-B622-46EA-AF40-3F69D99B33DA wds:Q56603117-31C35C56-561B-41B4-8396-C0B858F02886 wds:Q56603117-3E3EA862-97E7-4A75-9B40-33C1592C600B wds:Q56603117-5405E509-4877-4410-8826-7BB86707C298 wds:Q56603117-5F291187-841B-4217-B56D-6606D143EA55 wds:Q56603117-77285396-BAC7-4B82-A8FD-91F83EEFA776 wds:Q56603117-79B77E93-A65F-4233-B84B-784F85691867 wds:Q56603117-83C04511-60B2-46F6-B9B8-399DB5AC5E23 wds:Q56603117-851C9D99-9F1B-487B-8CDF-021A9470F662 wds:Q56603117-95E25B39-22BE-4EE0-B248-FAAF948D9FBD wds:Q56603117-A507DADA-E09B-4E6A-B6F4-EF14442C6367 wds:Q56603117-BE7C60D5-2A31-48AF-88C2-C6505CBF0550 wds:Q56603117-D97C9D54-4FEA-4F6E-931B-3D669F69C335 wds:Q56603117-DEB6479F-6CBF-4792-AE80-CD200F318AB2 wds:Q56603117-E491AFE3-CF32-42CF-86E8-E4F8F54F937C wds:Q56603117-E7F75A90-C0ED-40C8-82F7-BEAA97CAA53B
cites work	Structure of astacin and implications for activation of astacins and zinc-ligation of collagenases Refined 1.8 A X-ray crystal structure of astacin, a zinc-endopeptidase from the crayfish Astacus astacus L. Structure determination, refinement, molecular structure and comparison with thermolysin Mechanisms of activation of tissue procollagenase by matrix metalloproteinase 3 (stromelysin) Characterization of 58-kilodalton human neutrophil collagenase: comparison with human fibroblast collagenase Mercurial activation of human polymorphonuclear leucocyte procollagenase Collagenase is a component of the specific granules of human neutrophil leucocytes Fragmentation of human polymorphonuclear-leucocyte collagenase Purification of human collagenases with a hydroxamic acid affinity column The recombinant catalytic domain of human neutrophil collagenase lacks type I collagen substrate specificity Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features Stromelysin is an activator of procollagenase. A study with natural and recombinant enzymes Direct activation of human neutrophil procollagenase by recombinant stromelysin Tissue cooperation in a proteolytic cascade activating human interstitial collagenase Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins' Matrix metalloproteinases: a review Characterization and activation of procollagenase from human polymorphonuclear leucocytes. N-terminal sequence determination of the proenzyme and various proteolytically activated forms Accurate bond and angle parameters for X-ray protein structure refinement Biosynthesis and secretion of procollagenase by rabbit synovial fibroblasts. Inhibition of procollagenase secretion by monensin and evidence for glycosylation of procollagenase
author name string	wds:Q56603117-0B939BB9-A117-431D-A367-CDFD99DC30AF wds:Q56603117-32162D8E-C13D-4DD3-9A93-423B2C2CD3B2 wds:Q56603117-4A9D2740-D69B-49C3-A649-E92E1B3646D2 wds:Q56603117-5FBD5F9F-2645-4D45-B3A8-5F61FDBEB252 wds:Q56603117-966DA5BF-7040-4E2E-85B2-688EEAD9F7DC wds:Q56603117-FEB33AE7-907D-4E10-833A-D77785EB1AEE
author name string	Michael Piper Harald Tschesche Peter Reinemer Thomas Kleine Frank Grams Susanne Schnierer
rdfs:label	Structural implications for the role of the N terminus in the ‘superactivation’ of collagenases (en) Structural implications for the role of the N terminus in the ‘superactivation’ of collagenases (nl)
skos:prefLabel	Structural implications for the role of the N terminus in the ‘superactivation’ of collagenases (en) Structural implications for the role of the N terminus in the ‘superactivation’ of collagenases (nl)
name	Structural implications for the role of the N terminus in the ‘superactivation’ of collagenases (en) Structural implications for the role of the N terminus in the ‘superactivation’ of collagenases (nl)
author	wds:Q56603117-1F0426A0-25D0-4FDA-A15E-C829D11D843F wds:Q56603117-CFC98B34-C03A-41B5-857F-5B6DBEEEA9B0
author	Wolfram Bode Robert Huber
title	wds:Q56603117-5EBDDD24-405A-47BE-9A4E-4ED17CF05F5C
title	Structural implications for the role of the N terminus in the ‘superactivation’ of collagenases (en)
page(s)	wds:Q56603117-80F57BF2-2FC3-401F-AC16-30605A36F78E
page(s)	227-233
instance of	wds:Q56603117-F4BF0132-9417-491F-9443-2DA11E3BEAEB
instance of	scholarly article
main subject	wds:Q56603117-0864CC60-B2BA-4950-BE49-3D9746DAB662 wds:Q56603117-2BC6096D-14A7-4E32-B8CA-1F9CB1A7E3B8 wds:Q56603117-373DC938-7A6C-4A56-9608-BB772D1321B4 wds:Q56603117-DDC10CA4-AAA7-49ED-B156-7182E45035F5
main subject	cell biology biophysics molecular biology structural biology
published in	wds:Q56603117-11206BA3-DED4-4200-9B50-7062BA2F2B09
published in	FEBS Letters
issue	wds:Q56603117-0693931F-C13A-4E57-B179-B9ED7C7659B8
volume	wds:Q56603117-4C945712-A643-4DCA-9DFB-A684D59032A3
issue	2
volume	338
DOI	wds:Q56603117-2D47B41B-D47C-4533-886E-23508576DB04
DOI	http://dx.doi.org/10.1016/0014-5793(94)80370-6
DOI	10.1016/0014-5793(94)80370-6
ResearchGate publication ID	wds:Q56603117-74851DDC-09E5-4D28-A378-E1C5843252D2
ResearchGate publication ID	14892484
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q56603117
is cites work of	Identification of Peptide Substrates for Human MMP-11 (Stromelysin-3) Using Phage Display X-ray structure of a hydroxamate inhibitor complex of stromelysin catalytic domain and its comparison with members of the zinc metalloproteinase superfamily Activation mechanism of meprins, members of the astacin metalloendopeptidase family Crystal structure of full-length human collagenase 3 (MMP-13) with peptides in the active site defines exosites in the catalytic domain X-ray structures of human neutrophil collagenase complexed with peptide hydroxamate and peptide thiol inhibitors. Implications for substrate binding and rational drug design

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