Selective modulation of matrix metalloproteinase 9 (MMP-9) functions via exosite inhibition. - Wikidata - wikimedia - TriplyDB

Selective modulation of matrix metalloproteinase 9 (MMP-9) functions via exosite inhibition.

Selective modulation of matrix metalloproteinase 9 (MMP-9) functions via exosite inhibition.

http://www.wikidata.org/entity/Q40089357

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Heart failure with preserved ejection fraction: emerging drug strategies Collagenolytic Matrix Metalloproteinase Activities toward Peptomeric Triple-Helical Substrates Biochemistry and molecular biology of gelatinase B or matrix metalloproteinase-9 (MMP-9): the next decade Tumor cell-produced matrix metalloproteinase 9 (MMP-9) drives malignant progression and metastasis of basal-like triple negative breast cancer.NMR and bioinformatics discovery of exosites that tune metalloelastase specificity for solubilized elastin and collagen triple helices.Matrix metalloproteinases in tumorigenesis: an evolving paradigm.Identification of exosite-targeting inhibitors of anthrax lethal factor by high-throughput screening Citrate synthase is a novel in vivo matrix metalloproteinase-9 substrate that regulates mitochondrial function in the postmyocardial infarction left ventricle.Development of a Förster resonance energy transfer assay for monitoring bacterial collagenase triple-helical peptidase activity.FRET-based and other fluorescent proteinase probes.Exosite interactions impact matrix metalloproteinase collagen specificities.New strategies for targeting matrix metalloproteinases Matrix metalloproteinase inhibition by heterotrimeric triple-helical Peptide transition state analogues Recruitment of Matrix Metalloproteinase-9 (MMP-9) to the Fibroblast Cell Surface by Lysyl Hydroxylase 3 (LH3) Triggers Transforming Growth Factor-β (TGF-β) Activation and Fibroblast Differentiation Comparison of metalloproteinase protein and activity profiling.Matrix metalloproteinases as breast cancer drivers and therapeutic targets.The history of matrix metalloproteinases: milestones, myths, and misperceptions.Identification of collagen binding domain residues that govern catalytic activities of matrix metalloproteinase-2 (MMP-2).Synthesis of Fmoc-Gly-Ile Phosphinic Pseudodipeptide: Residue Specific Conditions for Construction of Matrix Metalloproteinase Inhibitor Building Blocks Matrix metalloproteinases as input and output signals for post-myocardial infarction remodeling Interstitial collagen catabolism.Matrix metalloproteinase (MMP)-9: a proximal biomarker for cardiac remodeling and a distal biomarker for inflammation.Peptide-based selective inhibitors of matrix metalloproteinase-mediated activities MMP-9 signaling in the left ventricle following myocardial infarction.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.Synthesis and biological applications of collagen-model triple-helical peptides.Temporal and spatial expression of matrix metalloproteinases and tissue inhibitors of metalloproteinases following myocardial infarction.Spinal cord injury induced neuropathic pain: Molecular targets and therapeutic approaches.Determining the Substrate Specificity of Matrix Metalloproteases using Fluorogenic Peptide Substrates.Peptide from the C-terminal domain of tissue inhibitor of matrix metalloproteinases-2 (TIMP-2) inhibits membrane activation of matrix metalloproteinase-2 (MMP-2).Matrix Metalloproteinases in Myocardial Infarction and Heart Failure.Efficient synthesis of Fmoc-protected phosphinic pseudodipeptides: Building blocks for the synthesis of matrix metalloproteinase inhibitors.Hydroxyproline-containing collagen analogs trigger the release and activation of collagen-sequestered proMMP-2 by competition with prodomain-derived peptide P33-42.Therapeutic Potential of Matrix Metalloproteinase Inhibition in Breast Cancer.Early matrix metalloproteinase-9 inhibition post-myocardial infarction worsens cardiac dysfunction by delaying inflammation resolution.Functional characterization of selective exosite-binding inhibitors of matrix metalloproteinase-13 (MMP-13) - experimental validation in human breast and colon cancer.Matrix Metalloproteinase-9 (MMP-9) as a Cancer Biomarker and MMP-9 Biosensors: Recent Advances

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P2860

Selective modulation of matrix metalloproteinase 9 (MMP-9) functions via exosite inhibition.

http://www.wikidata.org/entity/Q40089357

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年论文

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2008年论文

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2008年论文

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name

Selective modulation of matrix ...... ctions via exosite inhibition.

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type

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Selective modulation of matrix ...... ctions via exosite inhibition.

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Selective modulation of matrix ...... ctions via exosite inhibition.

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Journal of Biological Chemistry

P1476

Selective modulation of matrix ...... ctions via exosite inhibition.

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P2093

Gregg B Fields

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Janelle L Lauer-Fields

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John K Whitehead

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Keith Brew

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Robert P Hammer

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Shunzi Li

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P2860

The role of the C-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagenase-3, substrate specificity, and tissue inhibitor of metalloproteinase interaction

Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed

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

Identification of the (183)RWTNNFREY(191) region as a critical segment of matrix metalloproteinase 1 for the expression of collagenolytic activity

Hydrolysis of triple-helical collagen peptide models by matrix metalloproteinases

New functions for the matrix metalloproteinases in cancer progression

Structural stability of binding sites: consequences for binding affinity and allosteric effects.

A unique substrate recognition profile for matrix metalloproteinase-2.

Amino acid propensities for the collagen triple-helix.

The roles of substrate thermal stability and P2 and P1' subsite identity on matrix metalloproteinase triple-helical peptidase activity and collagen specificity.

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20087-20095

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scholarly article

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10.1074/JBC.M801438200

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29

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283

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2008-05-22T00:00:00Z

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18499673

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2459303

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