Mechanical load induces a 100-fold increase in the rate of collagen proteolysis by MMP-1. - Test2 - elhamkhani - TriplyDB

Mechanical load induces a 100-fold increase in the rate of collagen proteolysis by MMP-1.

Mechanical load induces a 100-fold increase in the rate of collagen proteolysis by MMP-1.

http://www.wikidata.org/entity/Q35873741

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Physical, Spatial, and Molecular Aspects of Extracellular Matrix of In Vivo Niches and Artificial Scaffolds Relevant to Stem Cells Research Approaches to manipulating the dimensionality and physicochemical properties of common cellular scaffolds Internal strain drives spontaneous periodic buckling in collagen and regulates remodeling.Structure of collagenase G reveals a chew-and-digest mechanism of bacterial collagenolysis Structural basis for matrix metalloproteinase 1-catalyzed collagenolysis.Introduction to cell-hydrogel mechanosensing Strain tunes proteolytic degradation and diffusive transport in fibrin networks Systems mechanobiology: tension-inhibited protein turnover is sufficient to physically control gene circuits.3D traction stresses activate protease-dependent invasion of cancer cells Stress sensitivity and mechanotransduction during heart development Small-angle light scattering to detect strain-directed collagen degradation in native tissue.The physics of cancer: the role of physical interactions and mechanical forces in metastasis.Single-molecule tracking of collagenase on native type I collagen fibrils reveals degradation mechanism.Multiplexed single-molecule force proteolysis measurements using magnetic tweezers Fibers with integrated mechanochemical switches: minimalistic design principles derived from fibronectin In-vivo stretch of term human fetal membranes.Interstitial collagen catabolism.Homeostatic maintenance via degradation and repair of elastic fibers under tension Mechanical Forces Accelerate Collagen Digestion by Bacterial Collagenase in Lung Tissue Strips.Involvement of eIF6 in external mechanical stretch-mediated murine dermal fibroblast function via TGF-β1 pathway.Matrix mechanics and regulation of the fibroblast phenotype.Advances in magnetic tweezers for single molecule and cell biophysics.How to Measure Molecular Forces in Cells: A Guide to Evaluating Genetically-Encoded FRET-Based Tension Sensors.MMP-14 in skeletal muscle repair.Mitral valve leaflet remodelling during pregnancy: insights into cell-mediated recovery of tissue homeostasis.Conformational dynamics accompanying the proteolytic degradation of trimeric collagen I by collagenases.Molecular level detection and localization of mechanical damage in collagen enabled by collagen hybridizing peptides.Highly sensitive single-fibril erosion assay demonstrates mechanochemical switch in native collagen fibrils.Chain registry and load-dependent conformational dynamics of collagen Molecular mechanism of force induced stabilization of collagen against enzymatic breakdown.Intrinsic fluctuations lead to broad range of transduced forces in tethered-bead single-molecule experiments.Effects of fluoride on expression of bone-specific genes in developing Xenopus laevis larvae.Manipulating motions of targeted single cells in solution by an integrated double-ring magnetic tweezers imaging microscope.Potential roles of metalloproteinases of endometrium-derived exosomes in embryo-maternal crosstalk during implantation.Single-Molecule Assay for Proteolytic Susceptibility: Force-Induced Collagen Destabilization.A biochemo-mechano coupled, computational model combining membrane transport and pericellular proteolysis in tissue mechanics.Engineering Tissues without the Use of a Synthetic Scaffold: A Twenty-Year History of the Self-Assembly Method.Joining forces: integrating the mechanical and optical single molecule toolkits A Guide to Magnetic Tweezers and Their Applications Genetically modified human type II collagen for N- and C-terminal covalent tagging

P2860

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P2860

Mechanical load induces a 100-fold increase in the rate of collagen proteolysis by MMP-1.

http://www.wikidata.org/entity/Q35873741

description

2011 nî lūn-bûn

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2011年の論文

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2011年学术文章

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2011年学术文章

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2011年学术文章

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2011年学术文章

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2011年學術文章

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2011年學術文章

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name

Mechanical load induces a 100-fold increase in the rate of collagen proteolysis by MMP-1.

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Mechanical load induces a 100-fold increase in the rate of collagen proteolysis by MMP-1.

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type

label

Mechanical load induces a 100-fold increase in the rate of collagen proteolysis by MMP-1.

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Mechanical load induces a 100-fold increase in the rate of collagen proteolysis by MMP-1.

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prefLabel

Mechanical load induces a 100-fold increase in the rate of collagen proteolysis by MMP-1.

@ast

Mechanical load induces a 100-fold increase in the rate of collagen proteolysis by MMP-1.

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Journal of the American Chemical Society

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Mechanical load induces a 100-fold increase in the rate of collagen proteolysis by MMP-1.

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P2093

Alexander R Dunn

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

Arjun S Adhikari

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

Jack Chai

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

P2860

Mechanical strain stabilizes reconstituted collagen fibrils against enzymatic degradation by mammalian collagenase matrix metalloproteinase 8 (MMP-8)

Collagen stabilization at atomic level: crystal structure of designed (GlyProPro)10foldon

Matrix metalloproteinases: regulators of the tumor microenvironment

Contour length and refolding rate of a small protein controlled by engineered disulfide bonds.

Mechanotransduction in vascular physiology and atherogenesis.

Mapping local matrix remodeling induced by a migrating tumor cell using three-dimensional multiple-particle tracking.

Collagen fibrils: nanoscale ropes.

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

Direct visualization of protease action on collagen triple helical structure.

Mechanical strain enhances survivability of collagen micronetworks in the presence of collagenase: implications for load-bearing matrix growth and stability

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1686-1689

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10.1021/JA109972P

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21247159

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