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Human RAF1 Protein expressed in Wheat germ - ABIN1317314
Rodríguez-Muñoz, de la Torre-Madrid, Sánchez-Blázquez, Garzón: NO-released zinc supports the simultaneous binding of Raf-1 and PKC? cysteine-rich domains to HINT1 protein at the mu-opioid receptor. in Antioxidants & redox signaling 2011
RAF1 may have a role in survival in hepatocellular carcinoma, and indicate whether sorafenib should be used as a postoperative adjuvant
Mutational activation of Kit-, Ras/Raf/Erk (show EPHB2 Proteins)- and Akt (show AKT1 Proteins)- pathways indicate the biological importance of these pathways and their components as potential targets for therapy.
Results indicate that des (show DES Proteins)-gamma-carboxy prothrombin (show F2 Proteins) (DCP (show ACE Proteins)) antagonizes the inhibitory effects of Sorafenib on hepatocellular carcinoma (HCC (show FAM126A Proteins)) through activation of the Raf/MEK (show MAP2K1 Proteins)/ERK (show EPHB2 Proteins) and PI3K (show PIK3CA Proteins)/Akt (show AKT1 Proteins)/mTOR (show FRAP1 Proteins) signaling pathways.
DiRas3 (show DIRAS3 Proteins) binds to KSR1 (show KSR1 Proteins) independently of its interaction with activated Ras and RAF.
RhoA (show RHOA Proteins)/ROCK and Raf-1/CK2 (show CSNK2A1 Proteins) pathway are responsible for TNF-alpha (show TNF Proteins)-mediated endothelial cytotoxicity via regulation of the vimentin (show VIM Proteins) cytoskeleton.
Although Raf-1 gene is not mutated, an abnormality of Raf-1 kinase feedback regulation enhances its antiapoptotic function, and Raf-1 can still be a pharmaceutical target to increase chemotherapy or radiotherapy sensitivity in these cancer cells.
RAF1 plays a critical role in maintaining the transformed phenotype of CRC cells, including those with mutated KRAS.
This finding suggests that stringent assemblage of Hsp90 (show HSP90 Proteins) keeps CRAF kinase equipped for participating in the MAPK (show MAPK1 Proteins) pathway. Thus, the role of Hsp90 (show HSP90 Proteins) in CRAF maturation and activation acts as a limiting factor to maintain the function of a strong client like CRAF kinase.
Oncogenic NFIA:RAF1 fusion activation of the MAPK (show MAPK1 Proteins) pathway is associated with pilocytic astrocytoma.
IGF2BP2 (show IGF2BP2 Proteins) as a post-transcriptional regulatory mRNA-binding factor, interfering with Raf-1 degradation by miR (show MLXIP Proteins)-195, that contributes to Colorectal carcinogenesis.
cdk10 (show CDK10 Proteins) has roles in vertebrate development and a critical function in neurogenesis by modulation of raf1a expression
Our results indicate that Rb-Raf-1 interaction plays an important role in spontaneous hair cell regeneration in zebrafish
Zebrafish embryos with morpholino knockdown of raf1 demonstrated the need for raf1 for the development of normal myocardial structure and function.
analysis of the roles of Raf- and PI3K-signalling pathways in melanoma
data suggest that G alpha(i3), Shc (show SHC1 Proteins), Grb2 (show GRB2 Proteins), Ras, and Raf-1 link Src (show SRC Proteins) to activation of MAPK (show MAPK1 Proteins) and to the AT(2)-dependent increase in eNOS (show NOS3 Proteins) expression in PAECs
BRAF (show BRAF Proteins) and ROKalpha (show ROCK2 Proteins) form independent RAF1 complexes in embryonic fibroblasts (MEFs) treated with epidermal growth factor (EGF (show EGF Proteins)).
Mechanistically, BRAF (show BRAF Proteins) and RAF1 operate independently to balance MAPK (show MAPK1 Proteins) signaling: BRAF (show BRAF Proteins) promotes ERK (show EPHB2 Proteins) activation, while RAF1 dims stress kinase activation.
Neuroprotective (arylthio)cyclopentenone prostaglandins directly bind to c-Raf protein and protect cells from down-regulation of the c-Raf protein itself, resulting in protection against oxidative stress.
A- and B-Raf (show SNRPE Proteins) ablation in chondrocytes does not alter skeletal development, whereas ablation of C-Raf decreases hypertrophic chondrocyte apoptosis and impairs vascularization of the growth plate. However, ablation of C-Raf does not impair phosphate-induced ERK1/2 phosphorylation in vitro, but leads to rickets by decreasing VEGF (show VEGFA Proteins) protein stability.
We confirmed that Raf1(L613V) knock-in confers a NS-like phenotype, including cardiac hypertrophy. Active RSK3 (show RPS6KA2 Proteins) was increased in Raf1(L613V) mice. Constitutive RSK3 (show RPS6KA2 Proteins) gene deletion prevented the Raf1(L613V)-dependent concentric growth in width of the cardiac myocyte and attenuated cardiac hypertrophy in female mice.
C-Raf involves in osteoblast survival in response to mechanical stress.
Dual inhibition of c-Raf and soluble epoxide hydrolase (show EPHX2 Proteins) by t-CUPM prevents mutant KrasG12D-initiated murine pancreatic carcinoma growth.
Simultaneous inhibition of sEH (show EPHX2 Proteins) and c-RAF prevents chronic pancreatitis and murine pancreatic intraepithelial neoplasia in LSL-KrasG(1)(2)D/Pdx-1 (show PDX1 Proteins)-Cre mice.
under normal physiological conditions, PTEN suppresses AKT (show AKT1 Proteins) activity to maintain activation of the RAF1/ERK (show EPHB2 Proteins) signaling pathway, which in turn maintains normal function of the initial segment and therefore, normal sperm maturation.
these data indicate that B-RAF (show SNRPE Proteins) is an important factor in oncogenic C-RAF-mediated tumorigenesis.
Both c-Raf and B-Raf (show BRAF Proteins) are required for Ras-induced MEK1 (show MAP2K1 Proteins) and p42 (show EPB42 Proteins) MAP kinase (show MAPK1 Proteins) activation.
This gene is the cellular homolog of viral raf gene (v-raf). The encoded protein is a MAP kinase kinase kinase (MAP3K), which functions downstream of the Ras family of membrane associated GTPases to which it binds directly. Once activated, the cellular RAF1 protein can phosphorylate to activate the dual specificity protein kinases MEK1 and MEK2, which in turn phosphorylate to activate the serine/threonine specific protein kinases, ERK1 and ERK2. Activated ERKs are pleiotropic effectors of cell physiology and play an important role in the control of gene expression involved in the cell division cycle, apoptosis, cell differentiation and cell migration. Mutations in this gene are associated with Noonan syndrome 5 and LEOPARD syndrome 2.
, RAF proto-oncogene serine/threonine-protein kinase
, proto-oncogene c-RAF
, raf proto-oncogene serine/threonine protein kinase
, murine leukemia viral (v-raf-1) oncogene homolog 1 (3611-MSV)
, v-raf-1 murine leukemia viral oncogene homolog 1
, murine leukemia viral oncogene homolog
, serine/threonine protein kinase RAF1
, MIL proto-oncogene serine/threonine-protein kinase
, c-mil protein
, murine leukemia viral (v-raf-1) oncogene homolog 1
, RAF proto-oncogene serine/threonine-protein kinase-like
, Craf1 transforming
, murine sarcoma 3611 oncogene 1
, sarcoma 3611 oncogene
, v-raf-1 leukemia viral oncogene 1
, Proto-oncogene c-RAF