Drebrin at Junctional Plaques. - Wikidata - awgldk - TriplyDB

Drebrin at Junctional Plaques.

Drebrin at Junctional Plaques.

http://www.wikidata.org/entity/Q42514367

about

Drebrin at Junctional Plaques.

http://www.wikidata.org/entity/Q42514367

description

2017 nî lūn-bûn

@nan

2017年の論文

@ja

2017年学术文章

@wuu

2017年学术文章

@zh-cn

2017年学术文章

@zh-hans

2017年学术文章

@zh-my

2017年学术文章

@zh-sg

2017年學術文章

@yue

2017年學術文章

@zh

2017年學術文章

@zh-hant

name

Drebrin at Junctional Plaques.

@en

Drebrin at Junctional Plaques.

@nl

type

label

Drebrin at Junctional Plaques.

@en

Drebrin at Junctional Plaques.

@nl

prefLabel

Drebrin at Junctional Plaques.

@en

Drebrin at Junctional Plaques.

@nl

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978-4-431-56550-5_18

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Advances in Experimental Medicine and Biology

P1476

Drebrin at Junctional Plaques.

@en

P2093

Wiebke K Ludwig-Peitsch

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

P2860

Drebrin preserves endothelial integrity by stabilizing nectin at adherens junctions

A novel role for drebrin in regulating progranulin bioactivity in bladder cancer

Drebrin is a widespread actin-associating protein enriched at junctional plaques, defining a specific microfilament anchorage system in polar epithelial cells

Cloning of drebrin A and induction of neurite-like processes in drebrin-transfected cells

Drebrin is a novel connexin-43 binding partner that links gap junctions to the submembrane cytoskeleton

Drebrin, an actin-binding, cell-type characteristic protein: induction and localization in epithelial skin tumors and cultured keratinocytes.

iTRAQ analysis of colorectal cancer cell lines suggests Drebrin (DBN1) is overexpressed during liver metastasis.

Laminin-111 stimulates proliferation of mouse embryonic stem cells through a reduction of gap junctional intercellular communication via RhoA-mediated Cx43 phosphorylation and dissociation of Cx43/ZO-1/drebrin complex.

Many faces of drebrin: from building dendritic spines and stabilizing gap junctions to shaping neurite-like cell processes.

Dynamic contacts: rearranging adherens junctions to drive epithelial remodelling.

P304

313-328

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scholarly article

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10.1007/978-4-431-56550-5_18

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P407

P478

1006

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P577

2017-01-01T00:00:00Z

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28865028

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