Artemin crystal structure reveals insights into heparan sulfate binding - Wikidata - wikimedia - TriplyDB

Artemin crystal structure reveals insights into heparan sulfate binding

Artemin crystal structure reveals insights into heparan sulfate binding

http://www.wikidata.org/entity/Q28242882

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The DAN family: modulators of TGF-β signaling and beyond An automatic refolding apparatus for preparative-scale protein production The Structure of the Glial Cell Line-derived Neurotrophic Factor-Coreceptor Complex: INSIGHTS INTO RET SIGNALING AND HEPARIN BINDING Comparison of GFL–GFRα complexes: further evidence relating GFL bend angle to RET signalling Structure of Protein Related to Dan and Cerberus: Insights into the Mechanism of Bone Morphogenetic Protein Antagonism Engineering potent long-acting variants of the Wnt inhibitor DKK2 Topographically specific regeneration of sensory axons in the spinal cord Human-protein-derived peptides for intracellular delivery of biomolecules.Heparan sulfate proteoglycan syndecan-3 is a novel receptor for GDNF, neurturin, and artemin Artemin promotes functional long-distance axonal regeneration to the brainstem after dorsal root crush PDB_REDO: constructive validation, more than just looking for errors.Neurotrophic factor receptor RET: structure, cell biology, and inherited diseases.Glial cell line-derived neurotrophic factor: characterization of mammalian posttranslational modifications.Exceptional stability of artemin neurotrophic factor dimers: effects of temperature, pH, buffer and storage conditions on protein integrity and activity.Investigating the Role of Artemin Glycosylation.The major determinant of the heparin binding of glial cell-line-derived neurotrophic factor is near the N-terminus and is dispensable for receptor binding.Quantitative analysis of the activation mechanism of the multicomponent growth-factor receptor Ret.The GDNF Family: A Role in Cancer?The Fractional Occupation Number Weighted Density as a Versatile Analysis Tool for Molecules with a Complicated Electronic Structure.Structure and biophysical characterisation of the human full-length Neurturin-GFRa2 complex - a role for heparan sulfate in signalling.

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Artemin crystal structure reveals insights into heparan sulfate binding

http://www.wikidata.org/entity/Q28242882

description

2006 nî lūn-bûn

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2006 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի հունիսին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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name

Artemin crystal structure reveals insights into heparan sulfate binding

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Artemin crystal structure reveals insights into heparan sulfate binding

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Artemin crystal structure reveals insights into heparan sulfate binding

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type

label

Artemin crystal structure reveals insights into heparan sulfate binding

@ast

Artemin crystal structure reveals insights into heparan sulfate binding

@en

Artemin crystal structure reveals insights into heparan sulfate binding

@nl

prefLabel

Artemin crystal structure reveals insights into heparan sulfate binding

@ast

Artemin crystal structure reveals insights into heparan sulfate binding

@en

Artemin crystal structure reveals insights into heparan sulfate binding

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Artemin crystal structure reveals insights into heparan sulfate binding

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Anthony Rossomando

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

BangJian Gong

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

Blake Pepinsky

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

Carolyn Pelletier

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Dinah Sah

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

Mia Rushe

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P Ann Boriack-Sjodin

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Paul Carmillo

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Ping Jin

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6801-6812

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scholarly article

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10.1021/BI060035X

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22

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45

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crystal structure