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TRIP6 gene
Known as:
MGC4423
, MGC29959
, MGC10556
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National Institutes of Health
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Related topics
Related topics
1 relation
TRIP11 gene
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2009
Highly Cited
2009
TRIP6, a novel molecular partner of the MAGI‐1 scaffolding molecule, promotes invasiveness
E. Chastre
,
Mahmoud Abdessamad
,
+6 authors
L. Kotelevets
The FASEB Journal
2009
Corpus ID: 37788635
We recently established the critical role of the PTEN/MAGI‐lb signalosome in stabilization of cell‐cell contacts and suppression…
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Highly Cited
2006
Highly Cited
2006
Salmonella typhimurium disseminates within its host by manipulating the motility of infected cells
M. Worley
,
George S. Nieman
,
Kaoru Geddes
,
Fred Heffron
Proceedings of the National Academy of Sciences…
2006
Corpus ID: 7835286
The mammalian host has a number of innate immune mechanisms designed to limit the spread of infection, yet many bacteria…
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Highly Cited
2006
Highly Cited
2006
Supervillin modulation of focal adhesions involving TRIP6/ZRP-1
N. Takizawa
,
Tara C. Smith
,
+7 authors
E. Luna
Journal of Cell Biology
2006
Corpus ID: 970822
Cell–substrate contacts, called focal adhesions (FAs), are dynamic in rapidly moving cells. We show that supervillin (SV)—a…
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Highly Cited
2005
Highly Cited
2005
The tumor suppressor Scrib interacts with the zyxin-related protein LPP, which shuttles between cell adhesion sites and the nucleus
Marleen M. R. Petit
,
S. Meulemans
,
P. Alen
,
T. Ayoubi
,
E. Jansen
,
W. V. D. Van de Ven
BMC Cell Biology
2005
Corpus ID: 17429529
BackgroundAt sites of cell adhesion, proteins exist that not only perform structural tasks but also have a signaling function…
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Highly Cited
2004
Highly Cited
2004
Endoglin Regulates Cytoskeletal Organization through Binding to ZRP-1, a Member of the Lim Family of Proteins*
F. Sanz‐Rodríguez
,
M. Guerrero-Esteo
,
L. Botella
,
D. Banville
,
C. Vary
,
C. Bernabéu
Journal of Biological Chemistry
2004
Corpus ID: 25140502
Endoglin is a component of the transforming growth factor-β receptor complex abundantly expressed at the surface of endothelial…
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Highly Cited
2004
Highly Cited
2004
TRIP6 Enhances Lysophosphatidic Acid-induced Cell Migration by Interacting with the Lysophosphatidic Acid 2 Receptor*
Jun Xu
,
Yun-Ju Lai
,
Weei-Chin Lin
,
F. Lin
Journal of Biological Chemistry
2004
Corpus ID: 9144267
Lysophosphatidic acid (LPA) induces actin rearrangement, focal adhesion assembly, and cell migration through the activation of…
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Highly Cited
2004
Highly Cited
2004
A nuclear isoform of the focal adhesion LIM-domain protein Trip6 integrates activating and repressing signals at AP-1- and NF-kappaB-regulated promoters.
O. Kassel
,
S. Schneider
,
Christine Heilbock
,
M. Litfin
,
M. Göttlicher
,
P. Herrlich
Genes & Development
2004
Corpus ID: 26801389
Glucocorticoid receptor (GR)-mediated transrepression of the transcription factors AP-1 and NF-kappaB, responsible for most of…
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Highly Cited
2002
Highly Cited
2002
Members of the Zyxin Family of LIM Proteins Interact with Members of the p130Cas Family of Signal Transducers*
J. Yi
,
S. Kloeker
,
+4 authors
M. Beckerle
Journal of Biological Chemistry
2002
Corpus ID: 31721200
Integrin binding to extracellular matrix proteins induces formation of signaling complexes at focal adhesions. Zyxin co-localizes…
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Highly Cited
2000
Highly Cited
2000
The zyxin-related protein TRIP6 interacts with PDZ motifs in the adaptor protein RIL and the protein tyrosine phosphatase PTP-BL.
Edwin Cuppen
,
M.A.P.C. van Ham
,
D. G. Wansink
,
A.L.M. de Leeuw
,
Bé Wieringa
,
Wiljan Hendriks
European Journal of Cell Biology
2000
Corpus ID: 30720237
The small adaptor protein RIL consists of two segments, the C-terminal LIM and the N-terminal PDZ domain, which mediate multiple…
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Highly Cited
1998
Highly Cited
1998
The human TRIP6 gene encodes a LIM domain protein and maps to chromosome 7q22, a region associated with tumorigenesis.
Jinseong Yi
,
M. Beckerle
Genomics
1998
Corpus ID: 35199624
The thyroid receptor interacting protein-6 (TRIP6) was first identified as a ligand-dependent binding partner for the thyroid…
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