Structural basis for the sheddase function of human meprin metalloproteinase at the plasma membrane
about
A Novel Family of Soluble Minimal Scaffolds Provides Structural Insight into the Catalytic Domains of Integral Membrane MetallopeptidasesLaminin L4 domain structure resembles adhesion modules in ephrin receptor and other transmembrane glycoproteinsCrystal Structure of the Neuropilin-1 MAM Domain: Completing the Neuropilin-1 Ectodomain PictureEffects of Glycosylation on the Enzymatic Activity and Mechanisms of ProteasesTargeting Neuroblastoma Cell Surface Proteins: Recommendations for Homology Modeling of hNET, ALK, and TrkBDevelopment of high throughput screening assays and pilot screen for inhibitors of metalloproteases meprin α and β.Origin and Diversification of Meprin Proteases.Structural Basis for Latency and Function of Immune Inhibitor A Metallopeptidase, a Modulator of the Bacillus anthracis SecretomeThe metalloproteases meprin α and meprin β: unique enzymes in inflammation, neurodegeneration, cancer and fibrosis.Sequence Requirements for Neuropilin-2 Recognition by ST8SiaIV and Polysialylation of Its O-Glycans.Crystal structure of TRAF1 TRAF domain and its implications in the TRAF1-mediated intracellular signaling pathway.Meprin Metalloproteases Generate Biologically Active Soluble Interleukin-6 Receptor to Induce Trans-Signaling.Mapping orphan proteases by proteomics: meprin metalloproteases deciphered as potential therapeutic targets.Handling Metalloproteinases.The Metalloprotease Meprin β Is an Alternative β-Secretase of APP.Metalloproteinase meprin α regulates migration and invasion of human hepatocarcinoma cells and is a mediator of the oncoprotein Reptin.Intracellular activation of ovastacin mediates pre-fertilization hardening of the zona pellucida.Trafficking in Alzheimer's Disease: Modulation of APP Transport and Processing by the Transmembrane Proteins LRP1, SorLA, SorCS1c, Sortilin, and Calsyntenin.Shedding light on designing potential meprin β inhibitors through ligand-based robust validated computational approaches: A proposal to chemists!Structure of the TRAF4 TRAF domain with a coiled-coil domain and its implications for the TRAF4 signalling pathway.Myroilysin Is a New Bacterial Member of the M12A Family of Metzincin Metallopeptidases and Is Activated by a Cysteine Switch Mechanism.
P2860
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P2860
Structural basis for the sheddase function of human meprin metalloproteinase at the plasma membrane
description
2012 nî lūn-bûn
@nan
2012 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Structural basis for the shedd ...... teinase at the plasma membrane
@ast
Structural basis for the shedd ...... teinase at the plasma membrane
@en
Structural basis for the shedd ...... teinase at the plasma membrane
@nl
type
label
Structural basis for the shedd ...... teinase at the plasma membrane
@ast
Structural basis for the shedd ...... teinase at the plasma membrane
@en
Structural basis for the shedd ...... teinase at the plasma membrane
@nl
prefLabel
Structural basis for the shedd ...... teinase at the plasma membrane
@ast
Structural basis for the shedd ...... teinase at the plasma membrane
@en
Structural basis for the shedd ...... teinase at the plasma membrane
@nl
P2093
P2860
P50
P3181
P356
P1476
Structural basis for the shedd ...... teinase at the plasma membrane
@en
P2093
Christoph Becker-Pauly
Claudia Broder
Erwin E Sterchi
F Xavier Gomis-Rüth
Joan L Arolas
Tamara Jefferson
Tibisay Guevara
Walter Stöcker
P2860
P304
P3181
P356
10.1073/PNAS.1211076109
P407
P577
2012-10-02T00:00:00Z