Atlas of Genetics and Cytogenetics in Oncology and Haematology


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RAF1 (v-raf-1 murine leukemia viral oncogene homolog 1)

Identity

Other namesCRAF
Raf-1
c-Raf
HGNC (Hugo) RAF1
LocusID (NCBI) 5894
Location 3p25.2
Location_base_pair Starts at 12625100 and ends at 12705700 bp from pter ( according to hg19-Feb_2009)  [Mapping]

DNA/RNA

Note History and Nomenclature:
c-Raf-1 was the first successfully cloned functional human homolog of the v-Raf gene, and thus the gene product of c-Raf-1 has historically been referred to in the literature simply as Raf-1. Subsequently, B-Raf and A-Raf-1 paralogues ( BRAF, located in Xq13 and ARAF, located in Xp11) were discovered. A suitable nomenclature is as follows: A-RAF, B-RAF, and C-RAF for the functional human proteins and A-RAF, B-RAF, and C-RAF for the corresponding genes; a-raf, b-raf, and c-raf for the murine proteins and A-Raf, B-Raf, and C-Raf for the corresponding genes. Raf-1 (or RAF-1) is generally taken to mean C-RAF-1 but could apply to A-RAF-1 equally. Here, RAF-1 will be taken to mean C-RAF-1 (RAF-1 = C-RAF-1, etc.).
Description C-RAF (RAF-1, C-RAF-1) encompasses 80,570 bp of DNA; 17 Exons.
Transcription RAF-1 transcribed mRNA contains 3212-3216 nucleotides.

Protein

Description The RAF proteins share three conserved domains: two (CR1 and CR2) in the N terminus and a third (CR3-encoding for the serine/threonine kinase domain) in the C terminus. The RAF proteins exhibit complex regulation involving numerous phosphorylation sites throughout the proteins. Despite constitutional similarity, the Raf isoforms have been shown to carry out non-redundant functions, implying that they are distinct.
RAF-1 (C-RAF-1): 72-74 kDa.
Note: A-RAF: about 68 kDa.
Note: B-RAF (which undergoes alternate splicing): ranges from 75 to 100 kDa.
Expression C-RAF (RAF-1) and A-RAF mRNA is expressed ubiquitously. A-RAF mRNA is highly expressed in urogenital organs. B-RAF is expressed in a wide range of tissues, but most substantially in neuronal tissues.
Localisation Cytosolic.
Function RAF proteins are part of the conserved MAPK (mitogen-activated protein kinase)/ERK (extracellular signal-regulated kinase) signaling cascade between the cell surface and the nucleus. RAF is regulated by the upstream RAS family of small G proteins. RAS is predominantly located on the inner leaflet of the plasma membrane and is functionally activated by GTP-binding. Binding of various extracellular ligands such as growth factors and hormones activates RAS and subsequently RAF proteins. RAS binds directly to the N-terminal regulatory domain or RAF (the RAS binding domain (RBD)). RAS interacts secondarily with the cysteine-rich domain (CRD) on CR1 of RAF. RAS-RAF binding can be affected by 14-3-3 proteins and other scaffold/adaptor proteins kinase suppressor of RAS (KSR), the multidomain protein connector-enhancer of KSR (CNK), and the leucine-rich-repeat protein suppressor of RAS mutations-8 (SUR8), which cause formation of various homo- and heterodimers and subsequently affect signal transduction. RAF activation leads to activation of the protein kinases MEK1 and MEK2 and subsequently the MAPK proteins ERK1 and ERK2. The downstream effects of MEK1/2-ERK1/2 activation are varied, complex, and depend on the cellular context. Resultant effects include activation of transcription factors involved in tumorigenesis, cell growth, survival, differentiation, metabolism, and cytoskeletal rearrangements. RAF-1 (C-RAF-1), A-RAF, and B-RAF are all capable of activating the MEK1/2-ERK1/2 signaling pathway.
RAF-1 is capable of activating the NF-kB transcription factor through an unknown mechanism that does not seem to involve direct phosphorylation of NF-kB and is independent of MEK1/2-ERK1/2 signaling.
RAF-1 is known to directly affect cell survival through phosphorylation of BAG1 (BCL2-associated athanogene-1), an anti-apoptotic protein that binds to BCL2, a second anti-apoptotic factor, also the prototype for a family of mammalian genes involved in mitochondrial outer membrane permeability (MOMP), thus restoring its function. BCL2 also targets RAF-1 to the mitochondrial membrane, where it is able to more readily phosphorylate substrates. The RAF-1/BAG1/BCL2 interaction allows RAF-1 to phosphorylate the pro-apoptotic protein BAD at the mitochondrial membrane, promoting cell survival.
Other known substrates of RAF-1 include the phosphatase CDC25C, the apoptosis signal-regulating kinase-1 (ASK1), and the tumor-suppressor protein retinoblastoma (Rb).
RAF-1 is tightly regulated by the AKT/PKB pathway through phosphorylation at S259.

Mutations

Somatic It has been widely established that RAF-1 over activity, typically via ras-activating mutations, is central to tumorigenesis and cell proliferation in numerous cancers (about 30% of all human cancers). However, it has come to the fore that oncogenesis may be due to ras/RAF-1 dysregulation (either increased or decreased expression) rather than increases in ras/RAF-1 activity exclusively.

Implicated in

Entity Medullary Thyroid Cancer (MTC)
Disease A neuroendocrine tumor derived from parafollicular C cells of the thyroid gland, MTC is the third most common form of thyroid cancer, accounting for 3-5% of all cases. MTC cells secrete hormones and tumor markers such as calcitonin, chromogranin A (CgA), and carcinoembryonic antigen (CEA).
Symptoms are related to either direct invasion or metastasis (neck mass, dyspnea, dysphagia, voice changes, pain) or tumor secretion of bioactive amines and peptides (diarrhea, flushing).
Prognosis Currently, surgery is the only potentially curative therapy for patients with MTC. The recommended operation is total thyroidectomy with lymph node dissection. However, 50% of patients treated with surgery suffer persistent or recurrent disease.
Oncogenesis 20% of patients with medullary thyroid cancer have an autosomal dominant inherited form of the disease, which is the result of well-characterized point mutations in the RET proto-oncogene. RAF-1 is conserved but not expressed at baseline in MTC. Pre-clinical studies have shown that activation of RAF-1 in MTC (TT) cells by means of RAF-1 gene transfection or RAF-1 activating small molecules (ZM336372) results in tumor cell growth inhibition in vitro and in vivo.
  
Entity Carcinoid Tumors
Disease Carcinoids are tumors that arise from the diffuse neuroendocrine cell system of the gut, lungs, and other organs. The incidence is 1-5 per 100,000 individuals. Carcinoids frequently metastasize to the liver and are the second most common source of isolated liver metastases. Carcinoids secrete various bioactive hormones such as 5-HT (5-hydroxy tryptophan, also known as serotonin) and chromogranin A.
Prognosis Patients with hepatic metastases suffer debilitating symptoms such as abdominal pain, flushing, bronchoconstriction, and diarrhea. Palliative treatment for these hormone-induced symptoms includes somatostatin analogs (such as octeotride). Conventional anticancer treatments such as chemotherapy and external beam radiation is largely ineffective for carcinoid tumors.
Oncogenesis RAF-1 activation is detrimental to tumorigenesis in carcinoid cells. Marked reduction in neuroendocrine phenotypic markers such as human achaete-scute complex like-1 (ASCL-1) and bioactive hormones 5-HT, chromogranin A, and synaptophysin has been noted upon RAF-1 activation using an estrogen-inducible RAF-1 construct in human GI (BON) and pulmonary carcinoid cell lines (NCI-H727) .
Treatment of GI carcinoid cells with RAF-1 activator ZM336372 led to a decrease in bioactive hormone levels, a suppression of cellular proliferation, an increase in cell cycle inhibitors p21 and p18, as well as a decrease in the neuroendocrine phenotypic marker ASCL-1. ZM336372 treatments also led to progressive phosphorylation (activation) of MEK1/2, ERK1/2, and RAF-1.
  
Entity Small Cell Lung Cancer (SCLC)
Disease SCLC tends to present with metastatic and regional spread. Carcinoids rarely metastasize, arise from major bronchi, and express neuron-specific enolase, chromogranin, and synaptophysin. Neuroendocrine carcinoids or atypical carcinoids have a more aggressive course.
Oncogenesis Human small-cell lung cancer (SCLC) cell lines rarely harbor ras-activating mutations. In one cell line of SCLC, DMS53, it was shown that by RAF-1 induction using an estrogen-inducible RAF-1 construct SCLC cells underwent differentiation and G1-specific growth arrest in conjunction with MEK/ERK1/2 pathway activation.
  
Entity Non-Small Cell Lung Cancer (NSCLC).
Disease Adenocarcinoma is the most common type of NSCLC accounting for about 40% of cases. Lesions are generally located peripherally and develop systemic metastases despite small primary tumors. 25% of NSCLC are squamous cell carcinomas which often remain localized.
Oncogenesis RAF-1 is over-expressed due to oncogenic ras mutations in about 35% of NSCLC.
The majority of NSCLC exhibits EGFR over-expression leading to upregulation of RAF-1 activity. NSCLC has been shown to be mediated by a TGF-a/EGFR-mediated autocrine loop activated by signaling involving RAF-1 and PI3K-Akt.
  
Entity Pheochromocytoma.
Disease Pheochromocytomas are neuroectodermal in origin and arise from the chromaffin cells of the adrenal medulla. 10% of tumors are bilateral. Typical symptoms such as hypertension, headaches, diaphoresis, palpitations, diarrhea, and skin rashes, are related to tumor production of catecholamines, especially in patients with metastases. Pheochromocytoma is potentially fatal, but relatively uncommon (2-8 cases per million people annually). Curative therapy is surgery, usually accomplished by laparoscopic adrenalectomy.
Oncogenesis Activation of MEK1/2-ERK1/2 is necessary for differentiation of pheochromocytoma (PC12) cells and leads to decreased cell proliferation. RAF-1 activation in pheochromocytoma cells using ZM336372 led to cellular differentiation, growth arrest, and a decrease in the neuroendocrine marker chromogranin A.
  
Entity Non-Neuroendocrine Cancers with ras-activating Mutations.
Oncogenesis About 30% of all human cancers express ras-activating mutations. More than 85% of pancreatic adenocarcinomas, and 50% of colonic adenocarcinomas harbor K-ras mutations. K-ras is an upstream effector of RAF-1 in the RAF-1/MEK/ERK1/2 signaling pathway. Ras mutations have also been linked to tumorigenesis of cholangiocarcinoma, adenocarcinoma of the lung, squamous cell cancer, gastric adenocarcinoma, small bowel adenocarcinoma, and malignant melanoma.
  
Entity Colorectal Cancer.
Oncogenesis RAF-1 is over-activated due to oncogenic ras mutations in about 50% of colon cancers. These mutations are associated with poor prognosis, and are necessary for maintenance of the malignant phenotype.
RAF-1 inhibition in response to interaction with RAF kinase inhibitor protein (RKIP) (up-regulated in conjunction with the nuclear factor kappa B signaling pathway) has been linked with overall and disease-free survival in patients with colorectal cancers. RKIP has been identified as potentially useful for identifying early-stage CRC patients at risk for relapse.
  
Entity Pancreatic Carcinoma.
Oncogenesis RAF-1 is overactivated due to oncogenic ras mutations in about 90% of pancreatic carcinomas (Panc-1 and Mia-PaCa2). It has been shown that malignancy of these cells is reduced using k-ras RNAi. Pharmacological inhibition of the RAF/MEK/ERK pathway in pancreatic cancer cell lines (via MEK inhibition) results in reduction in cellular proliferation and an increase in cell cycle arrest.
  
Entity Hepatocellular Carcinoma (HCC)
Oncogenesis RAF-1 is over-activated in about 50% of biopsies while the RAF-1 protein is over-expressed in nearly 100% of all HCC's. Angiogenesis and other functions essential to tumorigenesis in HCC have been reported to depend on the RAF/MEK/ERK signaling pathway. RAF-1 inhibitor Sorafenib has been reported (in-vitro and in-vivo) to inhibit RAF-1 activity, leading to decreased MEK/ERK activity, reduced cellular proliferation, and apoptosis in several HCC cell lines including HepG2 and PLC/PRF/5.
  
Entity Prostate Cancer.
Oncogenesis RAF kinase inhibitor protein (RKIP) coding mRNAs have been observed to activate interferon-inducible 2',5'-oligoadenylate synthetases (OAS). OAS activity is characteristically increased (via these mRNAs) in prostate cancer cell lines PC3, LNCaP and DU145. RKIP expression is detectable in primary prostate cancer sections but not in metastases. This suggests RKIP's characterization as an anti-metastasis gene using the RAF/MEK/ERK signaling pathway is appropriate.
RAF-1 inhibition using systemically delivered novel cationic cardiolipin liposomes (NeoPhectin-AT) containing a small interfering RNA (siRNA) against RAF-1 causes tumor growth inhibition in a xenograft model of human prostate cancer.
RAF/MEK/ERK signaling pathway activation via a biologically active peptide called a prosaptide (TX14A) stimulates cell proliferation/survival, migration, and invasion in human prostate cancer cells.
NSC 95397 and NSC 672121, cdc25 inhibitors, were shown to activate the RAF/MEK/ERK pathway in prostate cancer cells.
RAF-1 activation in LNCaP prostate cancer cells using an estrogen-inducible construct led to growth inhibition.
  
Entity Breast Cancer.
Oncogenesis Growth hormone releasing hormone (GHRH) has been shown to regulate breast cancer cell proliferation and differentiation. In MDA-231 breast cancer cells, exogenous GHRH stimulated dose-dependent proliferation. RAF-1 inhibition using the agent PD98059 caused prevention of MAPK phosphorylation by GHRH as well as reduced cellular proliferation.
Proliferative effects of steroid hormone estradiol on MCF-7 breast cancer cells have been linked with increased expression of RAF-1, possibly due to direct activation of RAF-1 by estradiol.
RAF kinase inhibitor protein (RKIP) is associated with metastasis suppression. RKIP expression is lost in lymph node metastases. This suggests RKIP is a metastasis inhibitor gene and that RAF-1 expression enables metastasis.
The PTK inhibitor AG 879 inhibits proliferation of human breast cancer cells through inhibition of MAP kinase activation through inhibition of expression of the RAF-1 gene.
RAF-1 down-regulation is associated with paclitaxel drug resistance in human breast cancer cell line MCF-7/Adr.
  
Entity Renal Cell Carcinoma.
Oncogenesis RAF-1 is overactivated in conjunction with loss of function of the VHL ( von Hippel-Lindau) tumor-suppressor gene.
  
Entity Glioma .
Oncogenesis RAF-1 inhibitor AAL881 inhibited growth of glioma cell xenografts.
  
Entity Cervical Cancer.
Oncogenesis Low RAF-1 kinase activity is significantly associated with paclitaxel sensitivity in cervical cancers.
  
Entity Ovarian Cancer.
Oncogenesis RAF-1 dysregulation is associated with poor prognosis and possibly carcinogenesis. RAF-1 inhibition using RNAi reduces cellular proliferatin and inhibits ovarian tumor cell growth in vitro and in vivo. Similar results were observed using antisense oligonucleotide (ASO) therapy (ISIS 5132 and ISIS 13650).
RAF-1 inhibition by the Akt pathway sensitizes human ovarian cancer cells to the drug paclitaxel.
  
Entity Gastric Cancer.
Oncogenesis RAF-1 inactivation using RNAi in gastric cancer cell line SGC7901 led to dramatic reductions in angiogenesis, increased apoptosis, and decreased cellular proliferation.
  
Entity Bladder Cancer.
Oncogenesis RAF-1 gene amplification was detected in 4% of bladder cancer samples. Deletions at the RAF-1 locus were detected in 2.2% of these samples. Both amplifications and deletions were heavily correlated with high tumor grade (P < 0.00001), advanced stage (P < 0.0001), and poor survival (P<0.05).
  
Entity Lymphoma.
Oncogenesis RAF-1 is typically over-expressed in thymic lymphomas from TCR transgenic mice.
  

Other Leukemias implicated (Data extracted from papers in the Atlas)

Leukemias 11q23ChildAMLID1615

Other Solid tumors implicated (Data extracted from papers in the Atlas)

Solid Tumors AmeloblastomID5945 MedulloblastomaID5065

External links

Nomenclature
HGNC (Hugo)RAF1   9829
Cards
AtlasRAF1ID42032ch3p25
Entrez_Gene (NCBI)RAF1  5894  Raf-1 proto-oncogene, serine/threonine kinase
GeneCards (Weizmann)RAF1
Ensembl (Hinxton)ENSG00000132155 [Gene_View]  chr3:12625100-12705700 [Contig_View]  RAF1 [Vega]
ICGC DataPortalENSG00000132155
AceView (NCBI)RAF1
Genatlas (Paris)RAF1
WikiGenes5894
SOURCE (Princeton)NM_002880
Genomic and cartography
GoldenPath (UCSC)RAF1  -  3p25.2   chr3:12625100-12705700 -  3p25   [Description]    (hg19-Feb_2009)
EnsemblRAF1 - 3p25 [CytoView]
Mapping of homologs : NCBIRAF1 [Mapview]
OMIM164760   611553   611554   
Gene and transcription
Genbank (Entrez)AK226028 AK303561 AK303920 AK312248 BC018119
RefSeq transcript (Entrez)NM_002880
RefSeq genomic (Entrez)AC_000135 NC_000003 NC_018914 NG_007467 NT_022517 NW_001838877 NW_004929309
Consensus coding sequences : CCDS (NCBI)RAF1
Cluster EST : UnigeneHs.159130 [ NCBI ]
CGAP (NCI)Hs.159130
Alternative Splicing : Fast-db (Paris)GSHG0021524
Alternative Splicing GalleryENSG00000132155
Gene ExpressionRAF1 [ NCBI-GEO ]     RAF1 [ SEEK ]   RAF1 [ MEM ]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP04049 (Uniprot)
NextProtP04049  [Medical]
With graphics : InterProP04049
Splice isoforms : SwissVarP04049 (Swissvar)
Catalytic activity : Enzyme2.7.11.1 [ Enzyme-Expasy ]   2.7.11.12.7.11.1 [ IntEnz-EBI ]   2.7.11.1 [ BRENDA ]   2.7.11.1 [ KEGG ]   
Domaine pattern : Prosite (Expaxy)PROTEIN_KINASE_ATP (PS00107)    PROTEIN_KINASE_DOM (PS50011)    PROTEIN_KINASE_ST (PS00108)    RBD (PS50898)    ZF_DAG_PE_1 (PS00479)    ZF_DAG_PE_2 (PS50081)   
Domains : Interpro (EBI)DAG/PE-bd    Kinase-like_dom    Prot_Kinase_C-like_PE/DAG-bd    Prot_kinase_dom    Protein_kinase_ATP_BS    Raf-like_ras-bd    Ser-Thr/Tyr_kinase_cat_dom    Ser/Thr_kinase_AS    Ubiquitin-rel_dom   
Related proteins : CluSTrP04049
Domain families : Pfam (Sanger)C1_1 (PF00130)    Pkinase_Tyr (PF07714)    RBD (PF02196)   
Domain families : Pfam (NCBI)pfam00130    pfam07714    pfam02196   
Domain families : Smart (EMBL)C1 (SM00109)  RBD (SM00455)  
DMDM Disease mutations5894
Blocks (Seattle)P04049
PDB (SRS)1C1Y    1FAQ    1FAR    1GUA    1RFA    3CU8    3IQJ    3IQU    3IQV    3KUC    3KUD    3NKX    3O8I    3OMV    4FJ3    4G0N    4G3X    4IEA    4IHL   
PDB (PDBSum)1C1Y    1FAQ    1FAR    1GUA    1RFA    3CU8    3IQJ    3IQU    3IQV    3KUC    3KUD    3NKX    3O8I    3OMV    4FJ3    4G0N    4G3X    4IEA    4IHL   
PDB (IMB)1C1Y    1FAQ    1FAR    1GUA    1RFA    3CU8    3IQJ    3IQU    3IQV    3KUC    3KUD    3NKX    3O8I    3OMV    4FJ3    4G0N    4G3X    4IEA    4IHL   
PDB (RSDB)1C1Y    1FAQ    1FAR    1GUA    1RFA    3CU8    3IQJ    3IQU    3IQV    3KUC    3KUD    3NKX    3O8I    3OMV    4FJ3    4G0N    4G3X    4IEA    4IHL   
Human Protein AtlasENSG00000132155
Peptide AtlasP04049
HPRD01265
IPIIPI00021786   IPI00900312   IPI01015603   IPI00788857   IPI00925565   
Protein Interaction databases
DIP (DOE-UCLA)P04049
IntAct (EBI)P04049
FunCoupENSG00000132155
BioGRIDRAF1
IntegromeDBRAF1
STRING (EMBL)RAF1
Ontologies - Pathways
QuickGOP04049
Ontology : AmiGOMAPK cascade  activation of MAPKK activity  response to hypoxia  protein kinase activity  protein serine/threonine kinase activity  MAP kinase kinase kinase activity  protein binding  ATP binding  nucleus  cytoplasm  cytoplasm  mitochondrial outer membrane  Golgi apparatus  cytosol  plasma membrane  plasma membrane  protein phosphorylation  apoptotic process  signal transduction  epidermal growth factor receptor signaling pathway  activation of adenylate cyclase activity  small GTPase mediated signal transduction  Ras protein signal transduction  synaptic transmission  axon guidance  heart development  blood coagulation  cell proliferation  negative regulation of cell proliferation  insulin receptor signaling pathway  fibroblast growth factor receptor signaling pathway  platelet activation  pseudopodium  small GTPase binding  negative regulation of protein complex assembly  mitogen-activated protein kinase kinase binding  positive regulation of peptidyl-serine phosphorylation  ion transmembrane transport  regulation of Rho protein signal transduction  Fc-epsilon receptor signaling pathway  wound healing  identical protein binding  regulation of apoptotic process  negative regulation of apoptotic process  negative regulation of cysteine-type endopeptidase activity involved in apoptotic process  innate immune response  intermediate filament cytoskeleton organization  regulation of cell differentiation  metal ion binding  protein heterodimerization activity  neurotrophin TRK receptor signaling pathway  transmembrane transport  death-inducing signaling complex assembly  negative regulation of extrinsic apoptotic signaling pathway via death domain receptors  regulation of cell motility  
Ontology : EGO-EBIMAPK cascade  activation of MAPKK activity  response to hypoxia  protein kinase activity  protein serine/threonine kinase activity  MAP kinase kinase kinase activity  protein binding  ATP binding  nucleus  cytoplasm  cytoplasm  mitochondrial outer membrane  Golgi apparatus  cytosol  plasma membrane  plasma membrane  protein phosphorylation  apoptotic process  signal transduction  epidermal growth factor receptor signaling pathway  activation of adenylate cyclase activity  small GTPase mediated signal transduction  Ras protein signal transduction  synaptic transmission  axon guidance  heart development  blood coagulation  cell proliferation  negative regulation of cell proliferation  insulin receptor signaling pathway  fibroblast growth factor receptor signaling pathway  platelet activation  pseudopodium  small GTPase binding  negative regulation of protein complex assembly  mitogen-activated protein kinase kinase binding  positive regulation of peptidyl-serine phosphorylation  ion transmembrane transport  regulation of Rho protein signal transduction  Fc-epsilon receptor signaling pathway  wound healing  identical protein binding  regulation of apoptotic process  negative regulation of apoptotic process  negative regulation of cysteine-type endopeptidase activity involved in apoptotic process  innate immune response  intermediate filament cytoskeleton organization  regulation of cell differentiation  metal ion binding  protein heterodimerization activity  neurotrophin TRK receptor signaling pathway  transmembrane transport  death-inducing signaling complex assembly  negative regulation of extrinsic apoptotic signaling pathway via death domain receptors  regulation of cell motility  
Pathways : BIOCARTASignaling Pathway from G-Protein Families [Genes]    Role of MAL in Rho-Mediated Activation of SRF [Genes]    EGF Signaling Pathway [Genes]    EPO Signaling Pathway [Genes]    Role of ERBB2 in Signal Transduction and Oncology [Genes]    IL 6 signaling pathway [Genes]    T Cell Receptor Signaling Pathway [Genes]    Roles of ?-arrestin-dependent Recruitment of Src Kinases in GPCR Signaling [Genes]    BCR Signaling Pathway [Genes]    Bioactive Peptide Induced Signaling Pathway [Genes]    Phosphorylation of MEK1 by cdk5/p35 down regulates the MAP kinase pathway [Genes]    fMLP induced chemokine gene expression in HMC-1 cells [Genes]    Nerve growth factor pathway (NGF) [Genes]    Aspirin Blocks Signaling Pathway Involved in Platelet Activation [Genes]    TPO Signaling Pathway [Genes]    Erk and PI-3 Kinase Are Necessary for Collagen Binding in Corneal Epithelia [Genes]    Erk1/Erk2 Mapk Signaling pathway [Genes]    Insulin Signaling Pathway [Genes]    MAPKinase Signaling Pathway [Genes]    Signaling of Hepatocyte Growth Factor Receptor [Genes]    CCR3 signaling in Eosinophils [Genes]    Fc Epsilon Receptor I Signaling in Mast Cells [Genes]    Multiple antiapoptotic pathways from IGF-1R signaling lead to BAD phosphorylation [Genes]    IL 3 signaling pathway [Genes]    Keratinocyte Differentiation [Genes]    PDGF Signaling Pathway [Genes]    Links between Pyk2 and Map Kinases [Genes]    Ras Signaling Pathway [Genes]    Ceramide Signaling Pathway [Genes]    IL 2 signaling pathway [Genes]    IL-2 Receptor Beta Chain in T cell Activation [Genes]    Integrin Signaling Pathway [Genes]    Sprouty regulation of tyrosine kinase signals [Genes]    Influence of Ras and Rho proteins on G1 to S Transition [Genes]    CXCR4 Signaling Pathway [Genes]    Inhibition of Cellular Proliferation by Gleevec [Genes]    Angiotensin II mediated activation of JNK Pathway via Pyk2 dependent signaling [Genes]    Role of ?-arrestins in the activation and targeting of MAP kinases [Genes]    Cadmium induces DNA synthesis and proliferation in macrophages [Genes]    Growth Hormone Signaling Pathway [Genes]    IGF-1 Signaling Pathway [Genes]    NFAT and Hypertrophy of the heart (Transcription in the broken heart) [Genes]   
Pathways : KEGGMAPK signaling pathway    ErbB signaling pathway    Ras signaling pathway    Rap1 signaling pathway    Chemokine signaling pathway    FoxO signaling pathway    PI3K-Akt signaling pathway    Vascular smooth muscle contraction    VEGF signaling pathway    Focal adhesion    Gap junction    Natural killer cell mediated cytotoxicity    T cell receptor signaling pathway    B cell receptor signaling pathway    Fc epsilon RI signaling pathway    Fc gamma R-mediated phagocytosis    Long-term potentiation    Neurotrophin signaling pathway    Serotonergic synapse    Long-term depression    Regulation of actin cytoskeleton    Insulin signaling pathway    GnRH signaling pathway    Progesterone-mediated oocyte maturation    Estrogen signaling pathway    Melanogenesis    Prolactin signaling pathway    Thyroid hormone signaling pathway    Alcoholism    Tuberculosis    Hepatitis C    Hepatitis B    Influenza A    Pathways in cancer    Proteoglycans in cancer    MicroRNAs in cancer    Colorectal cancer    Renal cell carcinoma    Pancreatic cancer    Endometrial cancer    Glioma    Prostate cancer    Melanoma    Bladder cancer    Chronic myeloid leukemia    Acute myeloid leukemia    Non-small cell lung cancer   
REACTOMEP04049 [protein]
REACTOME PathwaysREACT_111045 Developmental Biology [pathway]
REACTOME PathwaysREACT_116125 Disease [pathway]
REACTOME PathwaysREACT_604 Hemostasis [pathway]
REACTOME PathwaysREACT_6900 Immune System [pathway]
REACTOME PathwaysREACT_13685 Neuronal System [pathway]
REACTOME PathwaysREACT_111102 Signal Transduction [pathway]
REACTOME PathwaysREACT_15518 Transmembrane transport of small molecules [pathway]
Protein Interaction DatabaseRAF1
Wikipedia pathwaysRAF1
Gene fusion - rearrangments
Rearrangement : COSMICSRGAP3 [3p25.3]  -  RAF1 [3p25.2]
Rearrangement : TICdbESRP1 [8q22.1]  -  RAF1 [1p36.32]
Rearrangement : TICdbSRGAP3 [3p25.3]  -  RAF1 [11p13]
Polymorphisms : SNP, mutations, diseases
SNP Single Nucleotide Polymorphism (NCBI)RAF1
SNP (GeneSNP Utah)RAF1
SNP : HGBaseRAF1
Genetic variants : HAPMAPRAF1
1000_GenomesRAF1 
ICGC programENSG00000132155 
Cancer Gene: CensusRAF1 
CONAN: Copy Number AnalysisRAF1 
Somatic Mutations in Cancer : COSMICRAF1 
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
DECIPHER (Syndromes)3:12625100-12705700
Mutations and Diseases : HGMDRAF1
OMIM164760    611553    611554   
MedgenRAF1
GENETestsRAF1
Disease Genetic AssociationRAF1
Huge Navigator RAF1 [HugePedia]  RAF1 [HugeCancerGEM]
Genomic VariantsRAF1  RAF1 [DGVbeta]
Exome VariantRAF1
dbVarRAF1
ClinVarRAF1
snp3D : Map Gene to Disease5894
DGIdb (Curated mutations)RAF1
DGIdb (Drug Gene Interaction db)RAF1
General knowledge
Homologs : HomoloGeneRAF1
Homology/Alignments : Family Browser (UCSC)RAF1
Phylogenetic Trees/Animal Genes : TreeFamRAF1
Chemical/Protein Interactions : CTD5894
Chemical/Pharm GKB GenePA34183
Clinical trialRAF1
Cancer Resource (Charite)ENSG00000132155
Other databases
Probes
Litterature
PubMed431 Pubmed reference(s) in Entrez
CoreMineRAF1
GoPubMedRAF1
iHOPRAF1

Bibliography

Structure and biological activity of human homologs of the raf/mil oncogene.
Bonner TI, Kerby SB, Sutrave P, Gunnell MA, Mark G, Rapp UR
Molecular and cellular biology. 1985 ; 5 (6) : 1400-1407.
PMID 2993863
 
Actively transcribed genes in the raf oncogene group, located on the X chromosome in mouse and human.
Huebner K, ar-Rushdi A, Griffin CA, Isobe M, Kozak C, Emanuel BS, Nagarajan L, Cleveland JL, Bonner TI, Goldsborough MD
Proceedings of the National Academy of Sciences of the United States of America. 1986 ; 83 (11) : 3934-3938.
PMID 3520560
 
The complete coding sequence of the human A-raf-1 oncogene and transforming activity of a human A-raf carrying retrovirus.
Beck TW, Huleihel M, Gunnell M, Bonner TI, Rapp UR
Nucleic acids research. 1987 ; 15 (2) : 595-609.
PMID 3029685
 
Expression of raf family proto-oncogenes in normal mouse tissues.
Storm SM, Cleveland JL, Rapp UR
Oncogene. 1990 ; 5 (3) : 345-351.
PMID 1690378
 
MAP kinases ERK1 and ERK2: pleiotropic enzymes in a ubiquitous signaling network.
Robbins DJ, Zhen E, Cheng M, Xu S, Ebert D, Cobb MH
Advances in cancer research. 1994 ; 63 : 93-116.
PMID 8036991
 
The mouse B-raf gene encodes multiple protein isoforms with tissue-specific expression.
Barnier JV, Papin C, Eychˆ®ne A, Lecoq O, Calothy G
The Journal of biological chemistry. 1995 ; 270 (40) : 23381-23389.
PMID 7559496
 
Raf1 interaction with Cdc25 phosphatase ties mitogenic signal transduction to cell cycle activation.
Galaktionov K, Jessus C, Beach D
Genes & development. 1995 ; 9 (9) : 1046-1058.
PMID 7744247
 
Post-natal lethality and neurological and gastrointestinal defects in mice with targeted disruption of the A-Raf protein kinase gene.
Pritchard CA, Bolin L, Slattery R, Murray R, McMahon M
Current biology : CB. 1996 ; 6 (5) : 614-617.
PMID 8805280
 
Bcl-2 targets the protein kinase Raf-1 to mitochondria.
Wang HG, Rapp UR, Reed JC
Cell. 1996 ; 87 (4) : 629-638.
PMID 8929532
 
Bcl-2 interacting protein, BAG-1, binds to and activates the kinase Raf-1.
Wang HG, Takayama S, Rapp UR, Reed JC
Proceedings of the National Academy of Sciences of the United States of America. 1996 ; 93 (14) : 7063-7068.
PMID 8692945
 
How Ras-related proteins talk to their effectors.
Wittinghofer A, Nassar N
Trends in biochemical sciences. 1996 ; 21 (12) : 488-491.
PMID 9009833
 
Endothelial apoptosis in Braf-deficient mice.
Wojnowski L, Zimmer AM, Beck TW, Hahn H, Bernal R, Rapp UR, Zimmer A
Nature genetics. 1997 ; 16 (3) : 293-297.
PMID 9207797
 
Paclitaxel is preferentially cytotoxic to human cervical tumor cells with low Raf-1 kinase activity: implications for paclitaxel-based chemoradiation regimens.
Britten RA, Perdue S, Opoku J, Craighead P
Radiotherapy and oncology : journal of the European Society for Therapeutic Radiology and Oncology. 1998 ; 48 (3) : 329-334.
PMID 9925253
 
Murine Ksr interacts with MEK and inhibits Ras-induced transformation.
Denouel-Galy A, Douville EM, Warne PH, Papin C, Laugier D, Calothy G, Downward J, Eychˆ®ne A
Current biology : CB. 1998 ; 8 (1) : 46-55.
PMID 9427625
 
Estrogen activates raf-1 kinase and induces expression of Egr-1 in MCF-7 breast cancer cells.
Pratt MA, Satkunaratnam A, Novosad DM
Molecular and cellular biochemistry. 1998 ; 189 (1-2) : 119-125.
PMID 9879662
 
Craf-1 protein kinase is essential for mouse development.
Wojnowski L, Stancato LF, Zimmer AM, Hahn H, Beck TW, Larner AC, Rapp UR, Zimmer A
Mechanisms of development. 1998 ; 76 (1-2) : 141-149.
PMID 9767153
 
Raf-1 physically interacts with Rb and regulates its function: a link between mitogenic signaling and cell cycle regulation.
Wang S, Ghosh RN, Chellappan SP
Molecular and cellular biology. 1998 ; 18 (12) : 7487-7498.
PMID 9819434
 
Raf-1-induced cell cycle arrest in LNCaP human prostate cancer cells.
Ravi RK, McMahon M, Yangang Z, Williams JR, Dillehay LE, Nelkin BD, Mabry M
Journal of cellular biochemistry. 1999 ; 72 (4) : 458-469.
PMID 10022606
 
Phosphorylation and regulation of Raf by Akt (protein kinase B).
Zimmermann S, Moelling K
Science (New York, N.Y.). 1999 ; 286 (5445) : 1741-1744.
PMID 10576742
 
Raf induces NF-kappaB by membrane shuttle kinase MEKK1, a signaling pathway critical for transformation.
Baumann B, Weber CK, Troppmair J, Whiteside S, Israel A, Rapp UR, Wirth T
Proceedings of the National Academy of Sciences of the United States of America. 2000 ; 97 (9) : 4615-4620.
PMID 10758165
 
Overexpression of Ras, Raf and L-myc but not Bcl-2 family proteins is linked with resistance to TCR-mediated apoptosis and tumorigenesis in thymic lymphomas from TCR transgenic mice.
Kobzdej M, Matuszyk J, Strzadala L
Leukemia research. 2000 ; 24 (1) : 33-38.
PMID 10634643
 
The leucine-rich repeat protein SUR-8 enhances MAP kinase activation and forms a complex with Ras and Raf.
Li W, Han M, Guan KL
Genes & development. 2000 ; 14 (8) : 895-900.
PMID 10783161
 
Expression of the A-raf proto-oncogene in the normal adult and embryonic mouse.
Luckett JC, Hˆºser MB, Giagtzoglou N, Brown JE, Pritchard CA
Cell growth & differentiation : the molecular biology journal of the American Association for Cancer Research. 2000 ; 11 (3) : 163-171.
PMID 10768864
 
Raf-1 promotes cell survival by antagonizing apoptosis signal-regulating kinase 1 through a MEK-ERK independent mechanism.
Chen J, Fujii K, Zhang L, Roberts T, Fu H
Proceedings of the National Academy of Sciences of the United States of America. 2001 ; 98 (14) : 7783-7788.
PMID 11427728
 
KSR: a MAPK scaffold of the Ras pathway?
Morrison DK
Journal of cell science. 2001 ; 114 (Pt 9) : 1609-1612.
PMID 11309192
 
MEK kinase activity is not necessary for Raf-1 function.
Hˆºser M, Luckett J, Chiloeches A, Mercer K, Iwobi M, Giblett S, Sun XM, Brown J, Marais R, Pritchard C
The EMBO journal. 2001 ; 20 (8) : 1940-1951.
PMID 11296227
 
Association of c-Raf expression with survival and its targeting with antisense oligonucleotides in ovarian cancer.
McPhillips F, Mullen P, Monia BP, Ritchie AA, Dorr FA, Smyth JF, Langdon SP
British journal of cancer. 2001 ; 85 (11) : 1753-1758.
PMID 11742498
 
Embryonic lethality and fetal liver apoptosis in mice lacking the c-raf-1 gene.
Mikula M, Schreiber M, Husak Z, Kucerova L, Rˆºth J, Wieser R, Zatloukal K, Beug H, Wagner EF, Baccarini M
The EMBO journal. 2001 ; 20 (8) : 1952-1962.
PMID 11296228
 
High-throughput tissue microarray analysis of 3p25 (RAF1) and 8p12 (FGFR1) copy number alterations in urinary bladder cancer.
Simon R, Richter J, Wagner U, Fijan A, Bruderer J, Schmid U, Ackermann D, Maurer R, Alund G, Knˆnagel H, Rist M, Wilber K, Anabitarte M, Hering F, Hardmeier T, Schˆnenberger A, Flury R, Jˆ§ger P, Fehr JL, Schraml P, Moch H, Mihatsch MJ, Gasser T, Sauter G
Cancer research. 2001 ; 61 (11) : 4514-4519.
PMID 11389083
 
Critical contribution of linker proteins to Raf kinase activation.
Anselmo AN, Bumeister R, Thomas JM, White MA
The Journal of biological chemistry. 2002 ; 277 (8) : 5940-5943.
PMID 11741918
 
Inhibition of phosphorylation of BAD and Raf-1 by Akt sensitizes human ovarian cancer cells to paclitaxel.
Mabuchi S, Ohmichi M, Kimura A, Hisamoto K, Hayakawa J, Nishio Y, Adachi K, Takahashi K, Arimoto-Ishida E, Nakatsuji Y, Tasaka K, Murata Y
The Journal of biological chemistry. 2002 ; 277 (36) : 33490-33500.
PMID 12087097
 
Fidelity and spatio-temporal control in MAP kinase (ERKs) signalling.
Pouyssˆ©gur J, Volmat V, Lenormand P
Biochemical pharmacology. 2002 ; 64 (5-6) : 755-763.
PMID 12213567
 
Activation of the ras/raf-1 signal transduction pathway in carcinoid tumor cells results in morphologic transdifferentiation.
Sippel RS, Chen H
Surgery. 2002 ; 132 (6) : 1035-1039.
PMID 12490852
 
14-3-3 proteins: active cofactors in cellular regulation by serine/threonine phosphorylation.
Tzivion G, Avruch J
The Journal of biological chemistry. 2002 ; 277 (5) : 3061-3064.
PMID 11709560
 
The effects of beta-estradiol on Raf activity, cell cycle progression and growth factor synthesis in the MCF-7 breast cancer cell line.
Weinstein-Oppenheimer CR, Burrows C, Steelman LS, McCubrey JA
Cancer biology & therapy. 2002 ; 1 (3) : 256-262.
PMID 12432273
 
Raf-1 and Bcl-2 induce distinct and common pathways that contribute to breast cancer drug resistance.
Davis JM, Navolanic PM, Weinstein-Oppenheimer CR, Steelman LS, Hu W, Konopleva M, Blagosklonny MV, McCubrey JA
Clinical cancer research : an official journal of the American Association for Cancer Research. 2003 ; 9 (3) : 1161-1170.
PMID 12631622
 
Effects of raf kinase inhibitor protein expression on suppression of prostate cancer metastasis.
Fu Z, Smith PC, Zhang L, Rubin MA, Dunn RL, Yao Z, Keller ET
Journal of the National Cancer Institute. 2003 ; 95 (12) : 878-889.
PMID 12813171
 
Ras proteins: different signals from different locations.
Hancock JF
Nature reviews. Molecular cell biology. 2003 ; 4 (5) : 373-384.
PMID 12728271
 
Down-regulation of Raf-1 kinase is associated with paclitaxel resistance in human breast cancer MCF-7/Adr cells.
Lee M, Koh WS, Han SS
Cancer letters. 2003 ; 193 (1) : 57-64.
PMID 12691824
 
Human homologue of Drosophila CNK interacts with Ras effector proteins Raf and Rlf.
Lanigan TM, Liu A, Huang YZ, Mei L, Margolis B, Guan KL
The FASEB journal : official publication of the Federation of American Societies for Experimental Biology. 2003 ; 17 (14) : 2048-2060.
PMID 14597674
 
Regulation of MAP kinase signaling modules by scaffold proteins in mammals.
Morrison DK, Davis RJ
Annual review of cell and developmental biology. 2003 ; 19 : 91-118.
PMID 14570565
 
Raf-1 activation suppresses neuroendocrine marker and hormone levels in human gastrointestinal carcinoid cells.
Sippel RS, Carpenter JE, Kunnimalaiyaan M, Lagerholm S, Chen H
American journal of physiology. Gastrointestinal and liver physiology. 2003 ; 285 (2) : G245-G254.
PMID 12851216
 
Raf and the road to cell survival: a tale of bad spells, ring bearers and detours.
Troppmair J, Rapp UR
Biochemical pharmacology. 2003 ; 66 (8) : 1341-1345.
PMID 14555207
 
Raf kinase inhibitor protein: a prostate cancer metastasis suppressor gene.
Keller ET, Fu Z, Yeung K, Brennan M
Cancer letters. 2004 ; 207 (2) : 131-137.
PMID 15151133
 
Prosaptide TX14A stimulates growth, migration, and invasion and activates the Raf-MEK-ERK-RSK-Elk-1 signaling pathway in prostate cancer cells.
Koochekpour S, Sartor O, Lee TJ, Zieske A, Patten DY, Hiraiwa M, Sandhoff K, Remmel N, Minokadeh A
The Prostate. 2004 ; 61 (2) : 114-123.
PMID 15305334
 
Novel actions of tyrphostin AG 879: inhibition of RAF-1 and HER-2 expression combined with strong antitumoral effects on breast cancer cells.
Larsson LI
Cellular and molecular life sciences : CMLS. 2004 ; 61 (19-20) : 2624-2631.
PMID 15526167
 
Antisense oligonucleotide targeting of Raf-1: importance of raf-1 mRNA expression levels and raf-1-dependent signaling in determining growth response in ovarian cancer.
Mullen P, McPhillips F, MacLeod K, Monia B, Smyth JF, Langdon SP
Clinical cancer research : an official journal of the American Association for Cancer Research. 2004 ; 10 (6) : 2100-2108.
PMID 15041731
 
Activation of the Raf-1/MEK/Erk kinase pathway by a novel Cdc25 inhibitor in human prostate cancer cells.
Nemoto K, Vogt A, Oguri T, Lazo JS
The Prostate. 2004 ; 58 (1) : 95-102.
PMID 14673957
 
The RAF proteins take centre stage.
Wellbrock C, Karasarides M, Marais R
Nature reviews. Molecular cell biology. 2004 ; 5 (11) : 875-885.
PMID 15520807
 
Physiology and pathophysiology of type 3 deiodinase in humans.
Huang SA
Thyroid : official journal of the American Thyroid Association. 2005 ; 15 (8) : 875-881.
PMID 16131330
 
Pharmacologic inhibition of RAF-->MEK-->ERK signaling elicits pancreatic cancer cell cycle arrest through induced expression of p27Kip1.
Gysin S, Lee SH, Dean NM, McMahon M
Cancer research. 2005 ; 65 (11) : 4870-4880.
PMID 15930308
 
Reduction of Raf-1 kinase inhibitor protein expression correlates with breast cancer metastasis.
Hagan S, Al-Mulla F, Mallon E, Oien K, Ferrier R, Gusterson B, Garcˆ‚a JJ, Kolch W
Clinical cancer research : an official journal of the American Association for Cancer Research. 2005 ; 11 (20) : 7392-7397.
PMID 16243812
 
Inhibition of gastric cancer angiogenesis by vector-based RNA interference for Raf-1.
Meng F, Ding J, Liu N, Zhang J, Shao X, Shen H, Xue Y, Xie H, Fan D
Cancer biology & therapy. 2005 ; 4 (1) : 113-117.
PMID 15662129
 
Systemic delivery of RafsiRNA using cationic cardiolipin liposomes silences Raf-1 expression and inhibits tumor growth in xenograft model of human prostate cancer.
Pal A, Ahmad A, Khan S, Sakabe I, Zhang C, Kasid UN, Ahmad I
International journal of oncology. 2005 ; 26 (4) : 1087-1091.
PMID 15754006
 
ZM336372, a Raf-1 activator, suppresses growth and neuroendocrine hormone levels in carcinoid tumor cells.
Van Gompel JJ, Kunnimalaiyaan M, Holen K, Chen H
Molecular cancer therapeutics. 2005 ; 4 (6) : 910-917.
PMID 15956248
 
Raf kinase inhibitor protein expression in a survival analysis of colorectal cancer patients.
Al-Mulla F, Hagan S, Behbehani AI, Bitar MS, George SS, Going JJ, Garcˆ‚a JJ, Scott L, Fyfe N, Murray GI, Kolch W
Journal of clinical oncology : official journal of the American Society of Clinical Oncology. 2006 ; 24 (36) : 5672-5679.
PMID 17179102
 
Metastasis suppressor gene Raf kinase inhibitor protein (RKIP) is a novel prognostic marker in prostate cancer.
Fu Z, Kitagawa Y, Shen R, Shah R, Mehra R, Rhodes D, Keller PJ, Mizokami A, Dunn R, Chinnaiyan AM, Yao Z, Keller ET
The Prostate. 2006 ; 66 (3) : 248-256.
PMID 16175585
 
Role of Raf kinase in cancer: therapeutic potential of targeting the Raf/MEK/ERK signal transduction pathway.
Gollob JA, Wilhelm S, Carter C, Kelley SL
Seminars in oncology. 2006 ; 33 (4) : 392-406.
PMID 16890795
 
ZM336372, a Raf-1 activator, inhibits growth of pheochromocytoma cells.
Kappes A, Vaccaro A, Kunnimalaiyaan M, Chen H
The Journal of surgical research. 2006 ; 133 (1) : 42-45.
PMID 16603190
 
The Raf-1 pathway: a molecular target for treatment of select neuroendocrine tumors?
Kunnimalaiyaan M, Chen H
Anti-cancer drugs. 2006 ; 17 (2) : 139-142.
PMID 16428931
 
Transforming growth factor-beta1 sensitivity is altered in Abl-Myc- and Raf-Myc-induced mouse pre-B-cell tumors.
Letterio J, Rudikoff E, Voong N, Bauer SR
Stem cells (Dayton, Ohio). 2006 ; 24 (12) : 2611-2617.
PMID 16945999
 
Sorafenib blocks the RAF/MEK/ERK pathway, inhibits tumor angiogenesis, and induces tumor cell apoptosis in hepatocellular carcinoma model PLC/PRF/5.
Liu L, Cao Y, Chen C, Zhang X, McNabola A, Wilkie D, Wilhelm S, Lynch M, Carter C
Cancer research. 2006 ; 66 (24) : 11851-11858.
PMID 17178882
 
Selection and cloning of poly(rC)-binding protein 2 and Raf kinase inhibitor protein RNA activators of 2',5'-oligoadenylate synthetase from prostate cancer cells.
Molinaro RJ, Jha BK, Malathi K, Varambally S, Chinnaiyan AM, Silverman RH
Nucleic acids research. 2006 ; 34 (22) : 6684-6695.
PMID 17145707
 
Comparison of strategies targeting Raf-1 mRNA in ovarian cancer.
Mullen P, McPhillips F, Monia BP, Smyth JF, Langdon SP
International journal of cancer. Journal international du cancer. 2006 ; 118 (6) : 1565-1571.
PMID 16184551
 
AAL881, a novel small molecule inhibitor of RAF and vascular endothelial growth factor receptor activities, blocks the growth of malignant glioma.
Sathornsumetee S, Hjelmeland AB, Keir ST, McLendon RE, Batt D, Ramsey T, Yusuff N, Rasheed BK, Kieran MW, Laforme A, Bigner DD, Friedman HS, Rich JN
Cancer research. 2006 ; 66 (17) : 8722-8730.
PMID 16951188
 
Autocrine/paracrine regulation of breast cancer cell proliferation by growth hormone releasing hormone via Ras, Raf, and mitogen-activated protein kinase.
Siriwardana G, Bradford A, Coy D, Zeitler P
Molecular endocrinology (Baltimore, Md.). 2006 ; 20 (9) : 2010-2019.
PMID 16613992
 
In-vivo activation of Raf-1 inhibits tumor growth and development in a xenograft model of human medullary thyroid cancer.
Vaccaro A, Chen H, Kunnimalaiyaan M
Anti-cancer drugs. 2006 ; 17 (7) : 849-853.
PMID 16926634
 
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Written03-2007Max Cayo, David Yu Greentblatt, Muthusamy Kunnimalaiyaan, Herbert Chen

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This paper should be referenced as such :
Chen, H ; Kunnimalaiyaan, M ; Greentblatt, DY ; Cayo, M
RAF1 (v-raf-1 murine leukemia viral oncogene homolog 1)
Atlas Genet Cytogenet Oncol Haematol. 2007;11(3):239-244.
Free online version   Free pdf version   [Bibliographic record ]
URL : http://AtlasGeneticsOncology.org/Genes/RAF1ID42032ch3p25.html

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