1.8-A crystal structure of the catalytic domain of human neutrophil collagenase (matrix metalloproteinase-8) complexed with a peptidomimetic hydroxamate primed-side inhibitor with a distinct selectivity profile

1.8-A crystal structure of the catalytic domain of human neutrophil collagenase (matrix metalloproteinase-8) complexed with a peptidomimetic hydroxamate primed-side inhibitor with a distinct selectivity profile

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http://www.wikidata.org/entity/Q27741275
The 1.8-A crystal structure of a matrix metalloproteinase 8-barbiturate inhibitor complex reveals a previously unobserved mechanism for collagenase substrate recognitionThe structure of the catalytic domain of Tannerella forsythia karilysin reveals it is a bacterial xenologue of animal matrix metalloproteinasesStructural Basis for Matrix Metalloproteinase-2 (MMP-2)-selective Inhibitory Action of  -Amyloid Precursor Protein-derived InhibitorStructural differences of matrix metalloproteinases. Homology modeling and energy minimization of enzyme-substrate complexesMatrix metalloproteinases as novel biomarkers and potential therapeutic targets in human cancer.Matrix metalloproteinases in the pathophysiology and progression of gynecological malignancies: could their inhibition be an effective therapeutic approach?Targeting the tumor microenvironment by immunotherapy: part 2.Targeting angiogenesis for treatment of human cancerPharmacodynamic considerations in the use of matrix metalloproteinase inhibitors in cancer treatment.Intricate Functions of Matrix Metalloproteinases in Physiological and Pathological Conditions.Molecular design of a highly selective and strong protein inhibitor against matrix metalloproteinase-2 (MMP-2).Computational insights into the selectivity mechanism of APP-IP over matrix metalloproteinases.Identification of a region of beta-amyloid precursor protein essential for its gelatinase A inhibitory activity.Binding of active matrilysin to cell surface cholesterol sulfate is essential for its membrane-associated proteolytic action and induction of homotypic cell adhesion.Effect of species differences on stromelysin-1 (MMP-3) inhibitor potency. An explanation of inhibitor selectivity using homology modeling and chimeric proteins.
P2860

1.8-A crystal structure of the catalytic domain of human neutrophil collagenase (matrix metalloproteinase-8) complexed with a peptidomimetic hydroxamate primed-side inhibitor with a distinct selectivity profile

Item
http://www.wikidata.org/entity/Q27741275
description
1997 nî lūn-bûn
@nan
1997 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի հուլիսին հրատարակված գիտական հոդված
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1997年の論文
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1997年論文
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1997年論文
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1997年論文
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1997年論文
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1997年論文
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1997年论文
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1.8-A crystal structure of the ...... a distinct selectivity profile
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1.8-A crystal structure of the ...... a distinct selectivity profile
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1.8-A crystal structure of the ...... a distinct selectivity profile
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10.1111/J.1432-1033.1997.00356.X
P407
P433
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P577
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P921