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The protein encoded by LIMS1 is an adaptor protein which contains five LIM domains, or double zinc fingers. Zusätzlich bieten wir Ihnen LIM and Senescent Cell Antigen-Like Domains 1 Antikörper (69) und LIM and Senescent Cell Antigen-Like Domains 1 Kits (1) und viele weitere Produktgruppen zu diesem Protein an.
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that PINCH-1 may be playing an important role in etiopathogenesis of both subtypes breast cancer
Mammalian cells have two functional PINCH proteins, PINCH1 and PINCH2 (zeige LIMS2 Proteine). PINCH not only binds to Nck2 (zeige NCK2 Proteine) and engages in the signaling of growth factor receptors, but also forms a ternary complex with ILK (zeige ILK Proteine) and parvin (zeige PARVA Proteine) (IPP (zeige IPP Proteine) complex).
our data suggest an essential role of PINCH1, ILK (zeige ILK Proteine) and ILKAP (zeige ILKAP Proteine) for the radioresistance of p53 (zeige TP53 Proteine)-wildtype glioblastoma multiforme cells
Data suggest that PINCH1 and Nck2 (zeige NCK2 Proteine) critically participate in the regulation of cellular radiosensitivity and EGFR (zeige EGFR Proteine) 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 (zeige CSF2 Proteine) levels of PINCH appear to correlate with changes in blood CD4 (zeige CD4 Proteine) count and with changes in CSF (zeige CSF2 Proteine) hyperphosphorylated Tau levels
two novel genes, galectin 9 (zeige LGALS9 Proteine) 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 (zeige BCL11A Proteine) bone marrow stromal cells compared to normal bone marrow stromal cells (p<0.01).
findings suggest that PINCH-1 regulates integrin-mediated adhesion of keratinocytes through the interactions with ILK (zeige ILK Proteine) as well as EPLIN (zeige LIMA1 Proteine).
Rsu-1 (zeige RSU1 Proteine) expression is dramatically decreased in PINCH double knockout mouse livers.
PINCH-1 inhibits JNK (zeige MAPK8 Proteine)-mediated apoptosis by stabilising the PINCH-1 binding protein RSU-1 (zeige RSU1 Proteine) and promotes Bcl-2 (zeige BCL2 Proteine)-dependent pro-survival signalling downstream of integrins.
Data suggest that the adapter protein (zeige GRB10 Proteine) 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 (zeige ILK Proteine)-alpha-parvin (zeige PARVA Proteine) complex in the control of podocyte adhesion, morphology, and survival.
LIM (zeige PDLIM5 Proteine) 5 domain of PINCH1 interacts with Rsu-1 (zeige RSU1 Proteine) 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 (zeige ILK Proteine) and alpha-parvin (zeige PARVA Proteine) 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