Cytoplasmic translocation of the retinoblastoma protein disrupts sarcomeric organization. - Wikidata - awgldk - TriplyDB

Cytoplasmic translocation of the retinoblastoma protein disrupts sarcomeric organization.

Cytoplasmic translocation of the retinoblastoma protein disrupts sarcomeric organization.

http://www.wikidata.org/entity/Q37350607

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SMYD proteins: key regulators in skeletal and cardiac muscle development and function Association between tensin 1 and p130Cas at focal adhesions links actin inward flux to cell migration.Disruptive influence.A retinoblastoma allele that is mutated at its common E2F interaction site inhibits cell proliferation in gene-targeted mice Functions of the Tumor Suppressors p53 and Rb in Actin Cytoskeleton Remodeling Towards precision medicine: discovering novel gynecological cancer biomarkers and pathways using linked data.Inhibition of Rb Phosphorylation Leads to mTORC2-Mediated Activation of Akt.

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Cytoplasmic translocation of the retinoblastoma protein disrupts sarcomeric organization.

http://www.wikidata.org/entity/Q37350607

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 03 December 2013

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Cytoplasmic translocation of the retinoblastoma protein disrupts sarcomeric organization.

@en

Cytoplasmic translocation of the retinoblastoma protein disrupts sarcomeric organization.

@nl

type

label

Cytoplasmic translocation of the retinoblastoma protein disrupts sarcomeric organization.

@en

Cytoplasmic translocation of the retinoblastoma protein disrupts sarcomeric organization.

@nl

prefLabel

Cytoplasmic translocation of the retinoblastoma protein disrupts sarcomeric organization.

@en

Cytoplasmic translocation of the retinoblastoma protein disrupts sarcomeric organization.

@nl

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Cytoplasmic translocation of the retinoblastoma protein disrupts sarcomeric organization.

@en

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Keigo Araki

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

Keiko Kawauchi

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

Mie Yamamoto

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

Yoichi Taya

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

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Functional interactions between phosphatase POPX2 and mDia modulate RhoA pathways

Cell cycle, CDKs and cancer: a changing paradigm

Formin follows function: a muscle-specific isoform of FHOD3 is regulated by CK2 phosphorylation and promotes myofibril maintenance

p140mDia, a mammalian homolog of Drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for profilin.

A Suv39h-dependent mechanism for silencing S-phase genes in differentiating but not in cycling cells.

Lamin A/C binding protein LAP2alpha is required for nuclear anchorage of retinoblastoma protein

The consensus motif for phosphorylation by cyclin D1-Cdk4 is different from that for phosphorylation by cyclin A/E-Cdk2

Molecular mechanisms underlying RB protein function

Leiomodin is an actin filament nucleator in muscle cells.

Differential regulation of retinoblastoma protein function by specific Cdk phosphorylation sites

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e01228

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scholarly article

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10.7554/ELIFE.01228

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2

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2013-12-03T00:00:00Z

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24302570

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