The Role of Trio, a Rho Guanine Nucleotide Exchange Factor, in Glomerular Podocytes.

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The Role of Trio, a Rho Guanine Nucleotide Exchange Factor, in Glomerular Podocytes.

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2018 nî lūn-bûn

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2018年の論文

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年學術文章

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2018年學術文章

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The Role of Trio, a Rho Guanine Nucleotide Exchange Factor, in Glomerular Podocytes.

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The Role of Trio, a Rho Guanine Nucleotide Exchange Factor, in Glomerular Podocytes.

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The Role of Trio, a Rho Guanine Nucleotide Exchange Factor, in Glomerular Podocytes.

@en

The Role of Trio, a Rho Guanine Nucleotide Exchange Factor, in Glomerular Podocytes.

@nl

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The Role of Trio, a Rho Guanine Nucleotide Exchange Factor, in Glomerular Podocytes.

@en

The Role of Trio, a Rho Guanine Nucleotide Exchange Factor, in Glomerular Podocytes.

@nl

P1476

The Role of Trio, a Rho Guanine Nucleotide Exchange Factor, in Glomerular Podocytes.

@en

P2093

Cindy Baldwin

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

Lamine Aoudjit

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

Mirela Maier

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

Tomoko Takano

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P2860

Tara, a novel F-actin binding protein, associates with the Trio guanine nucleotide exchange factor and regulates actin cytoskeletal organization

The multidomain protein Trio binds the LAR transmembrane tyrosine phosphatase, contains a protein kinase domain, and has separate rac-specific and rho-specific guanine nucleotide exchange factor domains

Function and regulation of the Rho guanine nucleotide exchange factor Trio

Ras superfamily GEFs and GAPs: validated and tractable targets for cancer therapy?

Rho GTPases in cell biology

Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia

Arhgap24 inactivates Rac1 in mouse podocytes, and a mutant form is associated with familial focal segmental glomerulosclerosis

The N-terminal DH-PH domain of Trio induces cell spreading and migration by regulating lamellipodia dynamics in a Rac1-dependent fashion.

Trio amino-terminal guanine nucleotide exchange factor domain expression promotes actin cytoskeleton reorganization, cell migration and anchorage-independent cell growth.

The Rac-specific exchange factors Dock1 and Dock5 are dispensable for the establishment of the glomerular filtration barrier in vivo.

P31

scholarly article

P356

10.3390/IJMS19020479

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P407

English

P433

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

P478

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

P577

2018-02-06T00:00:00Z

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P698

29415466

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P932

5855701

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