MMP-12 catalytic domain recognizes triple helical peptide models of collagen V with exosites and high activity. - Wikidata - wikimedia - TriplyDB

MMP-12 catalytic domain recognizes triple helical peptide models of collagen V with exosites and high activity.

MMP-12 catalytic domain recognizes triple helical peptide models of collagen V with exosites and high activity.

http://www.wikidata.org/entity/Q41176062

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Characterization of a New S8 serine Protease from Marine Sedimentary Photobacterium sp. A5-7 and the Function of Its Protease-Associated Domain Remote exosites of the catalytic domain of matrix metalloproteinase-12 enhance elastin degradation.Path to Collagenolysis: COLLAGEN V TRIPLE-HELIX MODEL BOUND PRODUCTIVELY AND IN ENCOUNTERS BY MATRIX METALLOPROTEINASE-12.Apparent tradeoff of higher activity in MMP-12 for enhanced stability and flexibility in MMP-3.NMR and bioinformatics discovery of exosites that tune metalloelastase specificity for solubilized elastin and collagen triple helices.Basis for substrate recognition and distinction by matrix metalloproteinases Ambidextrous binding of cell and membrane bilayers by soluble matrix metalloproteinase-12.Enzymatic turnover of macromolecules generates long-lasting protein-water-coupled motions beyond reaction steady state Using fluorogenic peptide substrates to assay matrix metalloproteinases.Exosite interactions impact matrix metalloproteinase collagen specificities.Mechanical load induces a 100-fold increase in the rate of collagen proteolysis by MMP-1.Matrix metalloproteinases as breast cancer drivers and therapeutic targets.Severe Infection With Avian Influenza A Virus is Associated With Delayed Immune Recovery in Survivors Interstitial collagen catabolism.Identification of specific hemopexin-like domain residues that facilitate matrix metalloproteinase collagenolytic activity.Analysis of flavonoid-based pharmacophores that inhibit aggrecanases (ADAMTS-4 and ADAMTS-5) and matrix metalloproteinases through the use of topologically constrained peptide substrates.The role of collagen charge clusters in the modulation of matrix metalloproteinase activity.Chemical biology for understanding matrix metalloproteinase function.Studying the structure and dynamics of biomolecules by using soluble paramagnetic probes Determining the Substrate Specificity of Matrix Metalloproteases using Fluorogenic Peptide Substrates.Interdomain flexibility in full-length matrix metalloproteinase-1 (MMP-1).Structural requirements for the collagenase and elastase activity of cathepsin K and its selective inhibition by an exosite inhibitor.

P2860

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P2860

MMP-12 catalytic domain recognizes triple helical peptide models of collagen V with exosites and high activity.

http://www.wikidata.org/entity/Q41176062

description

2008 nî lūn-bûn

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

@zh-tw

2008年论文

@wuu

2008年论文

@zh

2008年论文

@zh-cn

name

MMP-12 catalytic domain recogn ...... th exosites and high activity.

@en

type

label

MMP-12 catalytic domain recogn ...... th exosites and high activity.

@en

prefLabel

MMP-12 catalytic domain recogn ...... th exosites and high activity.

@en

P1433

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P1433

Journal of Biological Chemistry

P1476

MMP-12 catalytic domain recogn ...... th exosites and high activity.

@en

P2093

Gregg B Fields

http://www.w3.org/2001/XMLSchema#string

Janelle L Lauer-Fields

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Mark O Palmier

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Rajagopalan Bhaskaran

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Steven R Van Doren

http://www.w3.org/2001/XMLSchema#string

P2860

Identification and characterization of human endometase (Matrix metalloproteinase-26) from endometrial tumor

Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages

Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

Sequence dependent conformational variations of collagen triple-helical structure

Substrate specificity determinants of human macrophage elastase (MMP-12) based on the 1.1 A crystal structure

Crystal structure of human macrophage elastase (MMP-12) in complex with a hydroxamic acid inhibitor

Structure of the C-terminally truncated human ProMMP9, a gelatin-binding matrix metalloproteinase

Solution structure of the 40,000 Mr phosphoryl transfer complex between the N-terminal domain of enzyme I and HPr

X-ray structures of binary and ternary enzyme-product-inhibitor complexes of matrix metalloproteinases

Global orientation of bound MMP-3 and N-TIMP-1 in solution via residual dipolar couplings

P304

21779-21788

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scholarly article

P356

10.1074/JBC.M709966200

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31

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P478

283

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2008-06-06T00:00:00Z

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5317079

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18539597

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2490773

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