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The protein encoded by LIMS1 is an adaptor protein which contains five LIM domains, or double zinc fingers.
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Mammalian cells have two functional PINCH proteins, PINCH1 and PINCH2 (Montrer LIMS2 Protéines). PINCH not only binds to Nck2 (Montrer NCK2 Protéines) and engages in the signaling of growth factor receptors, but also forms a ternary complex with ILK (Montrer ILK Protéines) and parvin (Montrer PARVA Protéines) (IPP (Montrer IPP Protéines) complex).
our data suggest an essential role of PINCH1, ILK (Montrer ILK Protéines) and ILKAP (Montrer ILKAP Protéines) for the radioresistance of p53 (Montrer TP53 Protéines)-wildtype glioblastoma multiforme cells
Data suggest that PINCH1 and Nck2 (Montrer NCK2 Protéines) critically participate in the regulation of cellular radiosensitivity and EGFR (Montrer EGFR Protéines) function and downstream signaling in a cellular model of human squamous cell carcinoma.
Downregulation of PINCH1 is associated with metastatic breast cancer.
changes in CSF (Montrer CSF2 Protéines) levels of PINCH appear to correlate with changes in blood CD4 (Montrer CD4 Protéines) count and with changes in CSF (Montrer CSF2 Protéines) hyperphosphorylated Tau levels
two novel genes, galectin 9 (Montrer LGALS9 Protéines) and PINCH, were expressed at much higher levels in cancerous lesions than in normal tissues in all the patients with clear-cell carcinoma who were examined
PINCH predicts survival in rectal cancer patients with RT, but not in patients without RT. The expression of PINCH may be regulated by radiation and by environmental factors surrounding the cells.
PINCH is increased and binds to hp-Tau. These studies address a new mechanism by which AD and HIV may intersect and identify PINCH as a contributing factor to the accumulation of hyperphosphorylated Tau.
Pinch-1 mRNA and protein were significantly up-regulated in acute lymphoblastic leukemia and acute myeloid leukemia (Montrer BCL11A Protéines) bone marrow stromal cells compared to normal bone marrow stromal cells (p<0.01).
PINCH protein might play an important role in the tumourigenesis and metastasis of gastric adenocarcinoma.
findings suggest that PINCH-1 regulates integrin-mediated adhesion of keratinocytes through the interactions with ILK (Montrer ILK Protéines) as well as EPLIN (Montrer LIMA1 Protéines).
Rsu-1 (Montrer RSU1 Protéines) expression is dramatically decreased in PINCH double knockout mouse livers.
PINCH-1 inhibits JNK (Montrer MAPK8 Protéines)-mediated apoptosis by stabilising the PINCH-1 binding protein RSU-1 (Montrer RSU1 Protéines) and promotes Bcl-2 (Montrer BCL2 Protéines)-dependent pro-survival signalling downstream of integrins.
Data suggest that the adapter protein (Montrer GRB10 Protéines) PINCH1 critically participates in the regulation of the cellular radiosensitivity of normal and malignant cells similarly under adhesion and suspension conditions.
PINCH1 plays an essential role in early murine embryonic development but is dispensable in ventricular cardiomyocytes.
These results provide important evidence for a crucial role of the PINCH-1-ILK (Montrer ILK Protéines)-alpha-parvin (Montrer PARVA Protéines) complex in the control of podocyte adhesion, morphology, and survival.
LIM (Montrer PDLIM5 Protéines) 5 domain of PINCH1 interacts with Rsu-1 (Montrer RSU1 Protéines) in mammalian cells and functions, in part, by altering cell adhesion.
The PINCH1 is composed of 5 LIM domains, binds ILK and locates to integrin-mediated adhesion sites, and PINCH1 is for integrin function, actin organization, cell-cell adhesion and endodermal cell survival during the implanting of mouse embryos.
PICH1, Ilk (Montrer ILK Protéines) and alpha-parvin (Montrer PARVA Protéines) form a complex to costameres in neonatal mouse ventricular myocytes. This complex is stimulated by fibronectins and phenylephrine, and by both by drug synergism, to regulate cardiac myocyte hypertrophy.
The protein encoded by this gene is an adaptor protein which contains five LIM domains, or double zinc fingers. The protein is likely involved in integrin signaling through its LIM domain-mediated interaction with integrin-linked kinase, found in focal adhesion plaques. It is also thought to act as a bridge linking integrin-linked kinase to NCK adaptor protein 2, which is involved in growth factor receptor kinase signaling pathways. Its localization to the periphery of spreading cells also suggests that this protein may play a role in integrin-mediated cell adhesion or spreading. Several transcript variants encoding different isoforms have been found for this gene.
LIM and senescent cell antigen-like-containing domain protein 1
, particularly interesting new Cys-His protein 1
, renal carcinoma antigen NY-REN-48