The ActA protein of Listeria monocytogenes acts as a nucleator inducing reorganization of the actin cytoskeleton.
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The tumor suppressor Scrib interacts with the zyxin-related protein LPP, which shuttles between cell adhesion sites and the nucleusMitochondrial BCL-2 inhibits AMBRA1-induced autophagyAMBRA1 is able to induce mitophagy via LC3 binding, regardless of PARKIN and p62/SQSTM1RabGEFs are a major determinant for specific Rab membrane targetingA novel proline-rich motif present in ActA of Listeria monocytogenes and cytoskeletal proteins is the ligand for the EVH1 domain, a protein module present in the Ena/VASP family.LPP, an actin cytoskeleton protein related to zyxin, harbors a nuclear export signal and transcriptional activation capacityActin-based motility of intracellular microbial pathogensThe proline-rich focal adhesion and microfilament protein VASP is a ligand for profilinsDual epitope recognition by the VASP EVH1 domain modulates polyproline ligand specificity and binding affinityExploitation of eukaryotic subcellular targeting mechanisms by bacterial effectorsCommon themes in microbial pathogenicity revisitedBicaudal D induces selective dynein-mediated microtubule minus end-directed transportEmergence of large-scale cell morphology and movement from local actin filament growth dynamicsMicrotubules as platforms for assaying actin polymerization in vivoDystroglycan, Tks5 and Src mediated assembly of podosomes in myoblastsThe herpesvirus VP1/2 protein is an effector of dynein-mediated capsid transport and neuroinvasion.PACSIN2 regulates cell adhesion during gastrulation in Xenopus laevis.The microtubule-binding protein ensconsin is an essential cofactor of kinesin-1Modification of the Creator recombination system for proteomics applications--improved expression by addition of splice sites.The Key Events Dose-Response Framework: its potential for application to foodborne pathogenic microorganismsDeletion of the central proline-rich repeat domain results in altered antigenicity and lack of surface expression of the Streptococcus mutans P1 adhesin molecule.Identification of two regions in the N-terminal domain of ActA involved in the actin comet tail formation by Listeria monocytogenes.Listeria pathogenesis and molecular virulence determinantsA Bacillus subtilis secreted protein with a role in endospore coat assembly and function.Significance of host cell kinesin in the development of Chlamydia psittaci.Biology under construction: in vitro reconstitution of cellular function.Yogi Berra, Forrest Gump, and the discovery of Listeria actin comet tails.Protocadherin FAT1 binds Ena/VASP proteins and is necessary for actin dynamics and cell polarization.Mechanism of actin-based motility: a dynamic state diagram.How the bacterial pathogen Listeria monocytogenes mediates the switch from environmental Dr. Jekyll to pathogenic Mr. HydeClose packing of Listeria monocytogenes ActA, a natively unfolded protein, enhances F-actin assembly without dimerization.Bacterial subversion of host actin dynamics at the plasma membrane.Cotranslational transport of ABP140 mRNA to the distal pole of S. cerevisiae.iactA of Listeria ivanovii, although distantly related to Listeria monocytogenes actA, restores actin tail formation in an L. monocytogenes actA mutant.Detection and characterization by differential PCR of host eukaryotic cell genes differentially transcribed following uptake of intracellular bacteria.Regulation of Wnt signaling by the tumor suppressor adenomatous polyposis coli does not require the ability to enter the nucleus or a particular cytoplasmic localization.The tandem repeat domain in the Listeria monocytogenes ActA protein controls the rate of actin-based motility, the percentage of moving bacteria, and the localization of vasodilator-stimulated phosphoprotein and profilinThe PET and LIM1-2 domains of testin contribute to intramolecular and homodimeric interactions.Actin-based movement of Listeria monocytogenes: actin assembly results from the local maintenance of uncapped filament barbed ends at the bacterium surface.Collapsin Response Mediator Protein-1 Regulates Arp2/3-dependent Actin Assembly
P2860
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P2860
The ActA protein of Listeria monocytogenes acts as a nucleator inducing reorganization of the actin cytoskeleton.
description
1994 nî lūn-bûn
@nan
1994 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
The ActA protein of Listeria m ...... ion of the actin cytoskeleton.
@ast
The ActA protein of Listeria m ...... ion of the actin cytoskeleton.
@en
The ActA protein of Listeria m ...... ion of the actin cytoskeleton.
@nl
type
label
The ActA protein of Listeria m ...... ion of the actin cytoskeleton.
@ast
The ActA protein of Listeria m ...... ion of the actin cytoskeleton.
@en
The ActA protein of Listeria m ...... ion of the actin cytoskeleton.
@nl
prefLabel
The ActA protein of Listeria m ...... ion of the actin cytoskeleton.
@ast
The ActA protein of Listeria m ...... ion of the actin cytoskeleton.
@en
The ActA protein of Listeria m ...... ion of the actin cytoskeleton.
@nl
P2093
P2860
P1433
P1476
The ActA protein of Listeria m ...... tion of the actin cytoskeleton
@en
P2093
P2860
P304
P356
10.1002/J.1460-2075.1994.TB06318.X
P407
P577
1994-02-01T00:00:00Z