Lipids: architects and regulators of membrane dynamics and trafficking.

about

Links between lipid homeostasis, organelle morphodynamics and protein trafficking in eukaryotic and plant secretory pathways.

P2860

Q37814211-9C6FEB8A-AECB-4791-96C3-0395CC531D4E

P2860

Lipids: architects and regulators of membrane dynamics and trafficking.

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description

2007 nî lūn-bûn

@nan

2007年の論文

@ja

2007年論文

@yue

2007年論文

@zh-hant

2007年論文

@zh-hk

2007年論文

@zh-mo

2007年論文

@zh-tw

2007年论文

@wuu

2007年论文

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2007年论文

@zh-cn

name

Lipids: architects and regulators of membrane dynamics and trafficking.

@en

Lipids: architects and regulators of membrane dynamics and trafficking.

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type

Item

label

Lipids: architects and regulators of membrane dynamics and trafficking.

@en

Lipids: architects and regulators of membrane dynamics and trafficking.

@nl

prefLabel

Lipids: architects and regulators of membrane dynamics and trafficking.

@en

Lipids: architects and regulators of membrane dynamics and trafficking.

@nl

P1476

Lipids: architects and regulators of membrane dynamics and trafficking.

@en

P2093

Patrick Moreau

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

P2860

Analysis of oxysterol binding protein homologue Kes1p function in regulation of Sec14p-dependent protein transport from the yeast Golgi complex.

Phospholipase D2 is localized to the rims of the Golgi apparatus in mammalian cells

Lipid raft association of SNARE proteins regulates exocytosis in PC12 cells

Evidence that phospholipase A2 activity is required for Golgi complex and trans Golgi network membrane tubulation

COPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes

Golgi fragmentation is associated with ceramide-induced cellular effects.

Sterol structure determines the separation of phases and the curvature of the liquid-ordered phase in model membranes.

Vesicle-associated membrane protein-associated protein-A (VAP-A) interacts with the oxysterol-binding protein to modify export from the endoplasmic reticulum.

Two tail-anchored protein variants, differing in transmembrane domain length and intracellular sorting, interact differently with lipids.

p125 is localized in endoplasmic reticulum exit sites and involved in their organization.

P304

157-159

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P31

scholarly article

P356

10.4161/PSB.2.3.3686

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P433

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

P478

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

P577

2007-05-01T00:00:00Z

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P5875

26764858

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P698

19704742

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P932

2634043

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Lipids: architects and regulators of membrane dynamics and trafficking.

about

P2860

P2860

Lipids: architects and regulators of membrane dynamics and trafficking.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P5875

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P5875

P698

P932