A unique substrate recognition profile for matrix metalloproteinase-2. - Wikidata - awgldk - TriplyDB

A unique substrate recognition profile for matrix metalloproteinase-2.

A unique substrate recognition profile for matrix metalloproteinase-2.

http://www.wikidata.org/entity/Q30761477

about

Novel proteolytic processing of the ectodomain of the zinc transporter ZIP4 (SLC39A4) during zinc deficiency is inhibited by acrodermatitis enteropathica mutations Peptide substrate specificities and protein cleavage sites of human endometase/matrilysin-2/matrix metalloproteinase-26 Engineering exosite peptides for complete inhibition of factor VIIa using a protease switch with substrate phage.Directed evolution of retroviruses activatable by tumour-associated matrix metalloproteases.Phage display substrate: a blind method for determining protease specificity.Library-based selection of retroviruses selectively spreading through matrix metalloprotease-positive cells.MMP-20 is predominately a tooth-specific enzyme with a deep catalytic pocket that hydrolyzes type V collagen Mapping protease substrates by using a biotinylated phage substrate library.Kinetic and binding effects in peptide substrate selectivity of matrix metalloproteinase-2: Molecular dynamics and QM/MM calculations.Directed evolution of protease beacons that enable sensitive detection of endogenous MT1-MMP activity in tumor cell lines.Inflammation and pancreatic cancer: molecular and functional interactions between S100A8, S100A9, NT-S100A8 and TGFβ1 Using fluorogenic peptide substrates to assay matrix metalloproteinases.Sequential Amyloid-β Degradation by the Matrix Metalloproteases MMP-2 and MMP-9.Massively parallel enzyme kinetics reveals the substrate recognition landscape of the metalloprotease ADAMTS13.High-Throughput Multiplexed Peptide-Centric Profiling Illustrates Both Substrate Cleavage Redundancy and Specificity in the MMP Family.Protease substrate profiling using bacterial display of self-blocking affinity proteins and flow-cytometric sorting.Mapping the Substrate Recognition Landscapes of Metalloproteases Using Comprehensive Mutagenesis.Constraining specificity in the N-domain of tissue inhibitor of metalloproteinases-1; gelatinase-selective inhibitors.Chemical biology for understanding matrix metalloproteinase function.Intracellular substrate cleavage: a novel dimension in the biochemistry, biology and pathology of matrix metalloproteinases.Proteolytic Activity Matrix Analysis (PrAMA) for simultaneous determination of multiple protease activities Determining the Substrate Specificity of Matrix Metalloproteases using Fluorogenic Peptide Substrates.Matrix metalloproteinase-2 (MMP-2) generates soluble HLA-G1 by cell surface proteolytic shedding.Selective modulation of matrix metalloproteinase 9 (MMP-9) functions via exosite inhibition.Direct Loading of iTEP-Delivered CTL Epitope onto MHC Class I Complexes on the Dendritic Cell Surface.Targeting an MMP-9-activated prodrug to multiple myeloma-diseased bone marrow: a proof of principle in the 5T33MM mouse model.Gelatinase A (MMP-2) is necessary and sufficient for renal tubular cell epithelial-mesenchymal transformation.A residue in the S2 subsite controls substrate selectivity of matrix metalloproteinase-2 and matrix metalloproteinase-9.Triphasic mixture model of cell-mediated enzymatic degradation of hydrogels.Development of a novel fluorogenic proteolytic beacon for in vivo detection and imaging of tumour-associated matrix metalloproteinase-7 activity.Protease degradable tethers for controlled and cell-mediated release of nanoparticles in 2- and 3-dimensions Mathematical model of the role of degradation on matrix development in hydrogel scaffold.Synthesis of tri-functionalized MMP2 FRET probes using a chemo-selective and late-stage modification of unprotected peptides.High throughput protease profiling comprehensively defines active site specificity for thrombin and ADAMTS13.Towards an MMP-2-activated molecular agent for cancer imaging.Prostate specific membrane antigen produces pro-angiogenic laminin peptides downstream of matrix metalloprotease-2.Molecular dynamics simulation study on the interaction of collagen-like peptides with gelatinase-A (MMP-2).MMP-9 triggered micelle-to-fibre transitions for slow release of doxorubicin.Novel Gd(III)-based probes for MR molecular imaging of matrix metalloproteinases.Development of an attenuated interleukin-2 fusion protein that can be activated by tumour-expressed proteases.

P2860

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P2860

A unique substrate recognition profile for matrix metalloproteinase-2.

http://www.wikidata.org/entity/Q30761477

description

2001 nî lūn-bûn

@nan

2001 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2001 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2001年の論文

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2001年論文

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2001年論文

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2001年論文

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2001年論文

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2001年論文

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2001年论文

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name

A unique substrate recognition profile for matrix metalloproteinase-2.

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A unique substrate recognition profile for matrix metalloproteinase-2.

@en

type

label

A unique substrate recognition profile for matrix metalloproteinase-2.

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A unique substrate recognition profile for matrix metalloproteinase-2.

@en

prefLabel

A unique substrate recognition profile for matrix metalloproteinase-2.

@ast

A unique substrate recognition profile for matrix metalloproteinase-2.

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Journal of Biological Chemistry

P1476

A unique substrate recognition profile for matrix metalloproteinase-2.

@en

P2093

Emily I Chen

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

Eric W Howard

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

Jeffrey W Smith

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Steven J Kridel

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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

The metzincins--topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases

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

X-ray structures of human neutrophil collagenase complexed with peptide hydroxamate and peptide thiol inhibitors. Implications for substrate binding and rational drug design

Structure of the catalytic domain of fibroblast collagenase complexed with an inhibitor

X-ray structure of active site-inhibited clotting factor Xa. Implications for drug design and substrate recognition

Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1

On the size of the active site in proteases. I. Papain

Comparative protein modelling by satisfaction of spatial restraints

Matrix metalloproteinase-9 triggers the angiogenic switch during carcinogenesis

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4485-4491

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scholarly article

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10.1074/JBC.M109469200

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6

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277

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11694539

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