Targeting of Listeria monocytogenes ActA protein to the plasma membrane as a tool to dissect both actin-based cell morphogenesis and ActA function.
about
LPP, an actin cytoskeleton protein related to zyxin, harbors a nuclear export signal and transcriptional activation capacityVillin-like actin-binding proteins are expressed ubiquitously in ArabidopsisgC1q-R/p32, a C1q-binding protein, is a receptor for the InlB invasion protein of Listeria monocytogenesCommon themes in microbial pathogenicity revisitedPivotal role of VASP in Arp2/3 complex-mediated actin nucleation, actin branch-formation, and Listeria monocytogenes motilityVillin enhances hepatocyte growth factor-induced actin cytoskeleton remodeling in epithelial cellsThe actin-based nanomachine at the leading edge of migrating cells.The stress-induced virulence protein InlH controls interleukin-6 production during murine listeriosisIdentification 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 determinantsYogi Berra, Forrest Gump, and the discovery of Listeria actin comet tails.Morphology of the lamellipodium and organization of actin filaments at the leading edge of crawling cells.ActA promotes Listeria monocytogenes aggregation, intestinal colonization and carriageDifferences in virulence and in expression of PrfA and PrfA-regulated virulence genes of Listeria monocytogenes strains belonging to serogroup 4.Ribotypes and virulence gene polymorphisms suggest three distinct Listeria monocytogenes lineages with differences in pathogenic potentialThe 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 Listeria monocytogenes virulence factor InlJ is specifically expressed in vivo and behaves as an adhesin.ActA is a dimer.Polymerizing microtubules activate site-directed F-actin assembly in nerve growth cones.The ActA polypeptides of Listeria ivanovii and Listeria monocytogenes harbor related binding sites for host microfilament proteins.Host cell heparan sulfate proteoglycans mediate attachment and entry of Listeria monocytogenes, and the listerial surface protein ActA is involved in heparan sulfate receptor recognition.Growing an actin gel on spherical surfaces.Interactions of Listeria monocytogenes with mammalian cells during entry and actin-based movement: bacterial factors, cellular ligands and signaling
P2860
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P2860
Targeting of Listeria monocytogenes ActA protein to the plasma membrane as a tool to dissect both actin-based cell morphogenesis and ActA function.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on June 1995
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Targeting of Listeria monocyto ...... rphogenesis and ActA function.
@en
Targeting of Listeria monocyto ...... rphogenesis and ActA function.
@nl
type
label
Targeting of Listeria monocyto ...... rphogenesis and ActA function.
@en
Targeting of Listeria monocyto ...... rphogenesis and ActA function.
@nl
prefLabel
Targeting of Listeria monocyto ...... rphogenesis and ActA function.
@en
Targeting of Listeria monocyto ...... rphogenesis and ActA function.
@nl
P2093
P2860
P1433
P1476
Targeting of Listeria monocyto ...... orphogenesis and ActA function
@en
P2093
P2860
P304
P356
10.1002/J.1460-2075.1995.TB07274.X
P407
P577
1995-06-01T00:00:00Z