Mannosylphosphodolichol synthase overexpression supports angiogenesis.

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http://www.wikidata.org/entity/Q41967901

description

2010 nî lūn-bûn

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2010年の論文

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2010年論文

@yue

2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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2010年论文

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2010年论文

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name

Mannosylphosphodolichol synthase overexpression supports angiogenesis.

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type

Item

label

Mannosylphosphodolichol synthase overexpression supports angiogenesis.

@en

prefLabel

Mannosylphosphodolichol synthase overexpression supports angiogenesis.

@en

P1476

Mannosylphosphodolichol synthase overexpression supports angiogenesis.

@en

P2093

Aditi Banerjee

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

Dipak K Banerjee

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

Krishna Baksi

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

Zhenbo Zhang

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P2860

Dolichol phosphate mannose synthase (DPM1) mutations define congenital disorder of glycosylation Ie (CDG-Ie)

Dolichol phosphate mannose synthase is required in vivo for glycosyl phosphatidylinositol membrane anchoring, O mannosylation, and N glycosylation of protein in Saccharomyces cerevisiae

Cloning and sequencing of the yeast gene for dolichol phosphate mannose synthase, an essential protein.

Assembly of asparagine-linked oligosaccharides

Congenital disorders of glycosylation: review of their molecular bases, clinical presentations and specific therapies

Requirement of protein kinase type I for cAMP-mediated up-regulation of lipid-linked oligosaccharide for asparagine-linked protein glycosylation.

Biosynthesis of glycosyl-phosphatidylinositol lipids in Trypanosoma brucei: involvement of mannosyl-phosphoryldolichol as the mannose donor

cAMP-mediated protein phosphorylation of microsomal membranes increases mannosylphosphodolichol synthase activity

Topography of glycosylation reactions in the endoplasmic reticulum.

Protein C-mannosylation is enzyme-catalysed and uses dolichyl-phosphate-mannose as a precursor.

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90-98

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scholarly article

P356

10.3109/10242420903411629

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P478

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P577

2010-01-01T00:00:00Z

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45272582

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20640223

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overexpression

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2903885

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