Mapping wild-type and R345W fibulin-3 intracellular interactomes.

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Mapping wild-type and R345W fibulin-3 intracellular interactomes.

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2016 nî lūn-bûn

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2016年の論文

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年學術文章

@yue

2016年學術文章

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2016年學術文章

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Mapping wild-type and R345W fibulin-3 intracellular interactomes.

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Mapping wild-type and R345W fibulin-3 intracellular interactomes.

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Mapping wild-type and R345W fibulin-3 intracellular interactomes.

@en

P1476

Mapping wild-type and R345W fibulin-3 intracellular interactomes.

@en

P2093

Annie Nguyen

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

John D Hulleman

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

Joseph C Genereux

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P2860

A single EFEMP1 mutation associated with both Malattia Leventinese and Doyne honeycomb retinal dystrophy

Gene ontology: tool for the unification of biology

ERdj5 is the ER reductase that catalyzes the removal of non-native disulfides and correct folding of the LDL receptor

ECM1 interacts with fibulin-3 and the beta 3 chain of laminin 332 through its serum albumin subdomain-like 2 domain

ERp57 is essential for efficient folding of glycoproteins sharing common structural domains

Aberrant accumulation of EFEMP1 underlies drusen formation in Malattia Leventinese and age-related macular degeneration

A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins.

Tissue inhibitor of metalloproteinases-3 (TIMP-3) is a binding partner of epithelial growth factor-containing fibulin-like extracellular matrix protein 1 (EFEMP1). Implications for macular degenerations

The MIntAct project--IntAct as a common curation platform for 11 molecular interaction databases

Gene Ontology Consortium: going forward

P304

165-169

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P31

scholarly article

P356

10.1016/J.EXER.2016.10.017

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P478

153

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P577

2016-10-21T00:00:00Z

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P698

27777122

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P932

5433432

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