Heparinoids activate a protease, secreted by mucosa and tumors, via tethering supplemented by allostery. - sprookjes - yvandenbroek - TriplyDB

Heparinoids activate a protease, secreted by mucosa and tumors, via tethering supplemented by allostery.

Heparinoids activate a protease, secreted by mucosa and tumors, via tethering supplemented by allostery.

http://www.wikidata.org/entity/Q33777230

about

Charge-Triggered Membrane Insertion of Matrix Metalloproteinase-7, Supporter of Innate Immunity and Tumors SPR Biosensor Probing the Interactions between TIMP-3 and Heparin/GAGs.Peripheral membrane associations of matrix metalloproteinases.Glycan Activation of a Sheddase: Electrostatic Recognition between Heparin and proMMP-7.Transient collagen triple helix binding to a key metalloproteinase in invasion and development.The Hessian Blob Algorithm: Precise Particle Detection in Atomic Force Microscopy Imagery.Mapping Lipid Bilayer Recognition Sites of Metalloproteinases and Other Prospective Peripheral Membrane Proteins.

P2860

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P2860

Heparinoids activate a protease, secreted by mucosa and tumors, via tethering supplemented by allostery.

http://www.wikidata.org/entity/Q33777230

description

2014 nî lūn-bûn

@nan

2014 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2014年の論文

@ja

2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

name

Heparinoids activate a proteas ...... ing supplemented by allostery.

@ast

Heparinoids activate a proteas ...... ing supplemented by allostery.

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type

label

Heparinoids activate a proteas ...... ing supplemented by allostery.

@ast

Heparinoids activate a proteas ...... ing supplemented by allostery.

@en

prefLabel

Heparinoids activate a proteas ...... ing supplemented by allostery.

@ast

Heparinoids activate a proteas ...... ing supplemented by allostery.

@en

P1433

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P1433

ACS Chemical Biology

P1476

Heparinoids activate a proteas ...... ring supplemented by allostery

@en

P2093

Fuming Zhang

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

Gavin M King

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

Raghavendar Reddy Sanganna Gari

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Robert J Linhardt

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

Yan G Fulcher

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

P2860

N.m.r. and molecular-modelling studies of the solution conformation of heparin

MMP7 shedding of syndecan-1 facilitates re-epithelialization by affecting alpha(2)beta(1) integrin activation

The crystal and molecular structures of a cathepsin K:chondroitin sulfate complex

Semi-rigid solution structures of heparin by constrained X-ray scattering modelling: new insight into heparin-protein complexes

Regulation of intestinal alpha-defensin activation by the metalloproteinase matrilysin in innate host defense

Heparan sulfate proteoglycans as extracellular docking molecules for matrilysin (matrix metalloproteinase 7)

The TIMP2 membrane type 1 metalloproteinase "receptor" regulates the concentration and efficient activation of progelatinase A. A kinetic study

Heparin activates beta-secretase (BACE1) of Alzheimer's disease and increases autocatalysis of the enzyme.

Predominant contribution of surface approximation to the mechanism of heparin acceleration of the antithrombin-thrombin reaction. Elucidation from salt concentration effects.

Kinetics of the heparin-enhanced antithrombin III/thrombin reaction. Evidence for a template model for the mechanism of action of heparin.

P304

957-966

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scholarly article

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10.1021/CB400898T

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4

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9

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P50

Steven R Van Doren

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2014-02-10T00:00:00Z

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260093093

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24495220

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4063349

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