Identification of specific hemopexin-like domain residues that facilitate matrix metalloproteinase collagenolytic activity. - Test2 - elhamkhani - TriplyDB

Identification of specific hemopexin-like domain residues that facilitate matrix metalloproteinase collagenolytic activity.

Identification of specific hemopexin-like domain residues that facilitate matrix metalloproteinase collagenolytic activity.

http://www.wikidata.org/entity/Q37433262

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Biophysical studies of matrix metalloproteinase/triple-helix complexes Matrix metalloproteinase interactions with collagen and elastin Collagenolytic Matrix Metalloproteinase Activities toward Peptomeric Triple-Helical Substrates Structural insights into triple-helical collagen cleavage by matrix metalloproteinase 1 Structural basis for matrix metalloproteinase 1-catalyzed collagenolysis.Cheminformatics-based drug design approach for identification of inhibitors targeting the characteristic residues of MMP-13 hemopexin domain Limitations in bonding to dentin and experimental strategies to prevent bond degradation Matrix metalloproteinase-induced epithelial-mesenchymal transition in breast cancer.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 Development of a Förster resonance energy transfer assay for monitoring bacterial collagenase triple-helical peptidase activity.FRET-based and other fluorescent proteinase probes.Inhibition of matrix metalloproteinase 14 (MMP-14)-mediated cancer cell migration.Exosite interactions impact matrix metalloproteinase collagen specificities.New strategies for targeting matrix metalloproteinases Matrix metalloproteinase inhibition by heterotrimeric triple-helical Peptide transition state analogues The interface between catalytic and hemopexin domains in matrix metalloproteinase-1 conceals a collagen binding exosite.Comparison of metalloproteinase protein and activity profiling.Matrix metalloproteinases as breast cancer drivers and therapeutic targets.Defining requirements for collagenase cleavage in collagen type III using a bacterial collagen system.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 Interstitial collagen catabolism.Examination of matrix metalloproteinase-1 in solution: a preference for the pre-collagenolysis state.Effects of Mutations on Structure-Function Relationships of Matrix Metalloproteinase-1.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.Determining the Substrate Specificity of Matrix Metalloproteases using Fluorogenic Peptide Substrates.Importance of the Linker Region in Matrix Metalloproteinase-1 Domain Interactions.Identification of novel, exosite-binding matrix metalloproteinase-13 inhibitor scaffolds.Dynamics of the beta2-adrenergic G-protein coupled receptor revealed by hydrogen-deuterium exchange Peptide from the C-terminal domain of tissue inhibitor of matrix metalloproteinases-2 (TIMP-2) inhibits membrane activation of matrix metalloproteinase-2 (MMP-2).Modified platelet deposition on matrix metalloproteinase 13 digested collagen I.Transient collagen triple helix binding to a key metalloproteinase in invasion and development.Functional characterization of selective exosite-binding inhibitors of matrix metalloproteinase-13 (MMP-13) - experimental validation in human breast and colon cancer.Tricine as a convenient scaffold for the synthesis of C-terminally branched collagen-model peptides.

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P2860

Identification of specific hemopexin-like domain residues that facilitate matrix metalloproteinase collagenolytic activity.

http://www.wikidata.org/entity/Q37433262

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on July 2009

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Identification of specific hem ...... inase collagenolytic activity.

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Identification of specific hem ...... inase collagenolytic activity.

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type

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Identification of specific hem ...... inase collagenolytic activity.

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Identification of specific hem ...... inase collagenolytic activity.

@nl

prefLabel

Identification of specific hem ...... inase collagenolytic activity.

@en

Identification of specific hem ...... inase collagenolytic activity.

@nl

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JBC.M109.016873

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Journal of Biological Chemistry

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Identification of specific hem ...... einase collagenolytic activity

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Gregg B Fields

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

Janelle L Lauer-Fields

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Michael J Chalmers

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Patrick R Griffin

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Scott A Busby

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P2860

Alternate binding modes for a ubiquitin-SH3 domain interaction studied by NMR spectroscopy

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

Collagen fibril architecture, domain organization, and triple-helical conformation govern its proteolysis

NMR structure of tissue inhibitor of metalloproteinases-1 implicates localized induced fit in recognition of matrix metalloproteinases

Evidence of reciprocal reorientation of the catalytic and hemopexin-like domains of full-length MMP-12

Prediction of the tissue-specificity of selective estrogen receptor modulators by using a single biochemical method

Structure of full-length porcine synovial collagenase reveals a C-terminal domain containing a calcium-linked, four-bladed beta-propeller

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Hydrolysis of triple-helical collagen peptide models by matrix metalloproteinases

Primary structure effects on peptide group hydrogen exchange

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24017-24024

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scholarly article

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10.1074/JBC.M109.016873

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36

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2009-07-01T00:00:00Z

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19574232

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2781996

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