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PDGFRA (platelet-derived growth factor receptor, alpha polypeptide)

Identity

Other namesCD140A
PDGFR-2
PDGFR2
RHEPDGFRA
HGNC (Hugo) PDGFRA
LocusID (NCBI) 5156
Location 4q12
Location_base_pair Starts at 55095264 and ends at 55164412 bp from pter ( according to hg19-Feb_2009)  [Mapping]
Note Size: 69151 bases; Orientation: plus strand.

DNA/RNA

Description The gene encoding the α-subunit of the PDGFRA maps to band q12 of chromosome 4. The gene contains 23 exons spanning about 65 kb. The first noncoding exon is followed by a large intron of approximately 23 kb (Gronwald et al., 1990; Kawagishi et al., 1995). An important paralog of PDGFRA is FLT4.
Transcription 6.4-kb transcript; coexpressed with the 5.3-kb PDGF receptor mRNA.

Protein

Description Size: 1089 amino acids; molecular weight: 122670 Da.
Subunit: Interacts with dimeric PDGFA, PDGFB and/or PDGFC; heterodimers with PDGFRB. Present in an inactive conformation as a monomer in the absence of bound ligand.
Expression PDGFR expression is characteristic of various mesodermal derivatives; specially expressed in the urinary tracts and in male and female genitals.
Localisation Subcellular location: cell membrane.
Function Member of the type III class of tyrosine kinase receptors which also includes c-KIT, FLT3 and the macrophage-colony-stimulating factor receptor; characterized by five immunoglobuline-like extracellular domains; a single-spanning transmembrane domain and an intracellular split kinase domain, connected by a flexible polypeptide insert; structurally homologous to c-KIT. PDGFA has transmembrane receptor protein tyrosine kinase activity and acts as a cell-surface receptor for members of the platelet-derived growth factor family: PDGFA, PDGFB and PDGFC, which are mitogens for fibroblasts and cells of mesenchymal origin origin. It plays an essential role in the regulation of many biological processes including cell proliferation, survival, differentiation and cell migration. Plays an important role in embryonic development, in the adult control tissue homeostasis in various organs including kidney, epidydimis, lung and pancreas; required for normal development of intestinal villi in the gastrointestinal tract, plays a role in platelet activation, wound healing and angiogenesis (Demoulin et al., 2012; Heldin et al., 2013).
Regulation: Function as homo- and/or heterodimers depending on the cell type; activated by ligand-induced dimerization and autophosphorylation on specific tyrosine residues upon binding. Activation of the intracellular kinase activity of the receptor leads to creation of docking sites for signal transduction molecules. Subsequent phosphorylation of its substrates initiates a variety of signal transduction cascades that promotes cell proliferation, survival and migration through the PI3K-AKT-mTOR and RAS-MAPK pathways as well as promotes activation of STAT family members (JAK/STAT) (Demoulin et al., 2012).

Mutations

Note Mutations in the PDGFRA gene contribute to the pathophysiology of various diseases such as atherosclerosis, abnormalities of the tubal neural development and fibrotic diseases. In cancer, activating point mutations, gene amplifications and chromosomal rearrangements including gene fusions and chromosomal deletions have been found in certain malignancies. These include hematological malignancies such as acute myeloid leukemia, atypical chronic myelogenous leukemia, chronic myelomonocytic leukemia, eosinophilic disorders and mastocytosis (Gotlib et al., 2008). PDGFRA mutations also have been described in somatic and familial gastrointestinal stromal tumors, synovial sarcomas, glioblastoma, malignant peripheral nerve sheath tumors, melanoma and a in a variety of other cancers (Chompret et al., 2004; Heinrich et al., 2003).

Implicated in

Entity Gastrointestinal stromal tumor (GIST)
Note Activating mutations of PDGFRA are found in 5-8% of patients with gastrointestinal stromal tumors (GISTs) but their frequency increases to 30% to 40% in gastric GISTs lacking KIT mutations (Corless et al., 2005; Lasota et al., 2008). The majority of these mutations are "substitution missense", that can arise by various mechanisms (Figure 1). These include mutation hot spots in exon 18 of the PDGFRA gene such as the Asp-to-Val substitution at codon 842 (D842V) encoding the activation loop. Other activating mutations are less frequent such as mutations in exons 12 encoding the juxtamembrane domain and in exon 14 encoding the tyrosine kinase 1 domain of PDGFRA (Chompret et al., 2004; Heinrich et al., 2003). PDGFRA mutations except for D842V in exon 18 are sensitive to imatinib inhibition. However, despite initial clinical responses to tyrosine kinase inhibitors (imatinib, nilotinib, sorafenib and sunatinib), the majority of these patient develops resistance to the drug limiting the long-term benefit of tyrosine kinase inhibitors in this group of patients (Gramza et al., 2009; Pierotti et al., 2011).
The D842V mutation results in an amino acid substitution at position 842 in PDGFRA, from an aspartic acid (D) to a valine (V). This mutation occurs within the TK2 domain (Figure 1).
PDGFRA D842V mutation has been found in a distinct subset of GIST, typically from the stomach. The D842V mutation is known to be associated with tyrosine kinase inhibitor resistance.
 
Figure 1. Schematic representation of the most frequent activating mutations of the homologous platelet-derived growth factor receptor alpha (PDGFRA) kinase in patients with gastrointestinal stromal tumors. Most common mutations are in exon 18, such as the D842V substitution that shows resistance to imatinib. Mutations in the juxtamembrane domain (exon 12; V561D most common) and in exon 14 tyrosine kinase 1 (TK1) domain (e.g., N659K) are less common. Abbreviations: JM, juxtamembrane; TK, tyrosine kinase. Adopted and modified from Pierott et al., 2011).
  
Entity Hematologic disorders with primary eosinophilia
Note Several chromosomal rearrangements generating fusion genes causing PDGFRA activation have been described in a variety of uncommon hematologic disorders that are often accompanied with a related condition called hypereosinophilic syndrome. These rearrangements activate PDGFRA by fusion to various partner genes: STRN (2p24) in the t(2;4)(p22;q12), FIP1L1 (interstitial 4q12 deletion), CDK5RAP2 (9q33) in the ins(9;4)(q33;q12q25), KIF5B (10p11) in the t(4;10)(q12;p11), ETV6 (12p13) in the t(4;12)(q12;p13), and BCR (22q11) in the t(4;22)(q12;q11). In each of these rearrangements, the breakpoints in PDGFRA partner genes are variable, but the breakpoints in PDGFRA invariably involve exon 12 encoding a portion of the juxtamembrane domain with autoinhibitory function (Baxter et al., 2002; Gotlib et al., 2008); the disruption of which activates the fusion protein (Figure 2).
The most investigated of these fusion genes is FIP1L1-PDGFRA that arise as a result of a cryptic interstitial deletion on chromosome 4q12. FIP1L1-PDGFRA fusion protein is involved in the pathogenesis of uncommon hematologic disorders with primary eosinophilia like chronic eosinophilic leukemia (CEL) hyperseosinophilic syndrome (HES) and systemic mastocytosis (SM). Similar to other fusion tyrosine kinases, FIP1L1-PDGFRA is a constitutively active tyrosine kinase that was shown to be sensitive to kinase inhibitors (Cools et al., 2003; Jain et al., 2013).
 
Figure 2. The structure and mechanism of activation of PDGFRA fusions in hematological disorders. In the fusion oncogene, the partner gene always replaces the 5 part of exon 12 of PDGFRA creating an in frame fusion. As the 5 part of exon 12 of PDGFRA containing the inhibitory domain is truncated, its expression is controlled by the partner gene promoter resulting in constitutive activation of the PDGFRA kinase domain. NH2: N-terminal site; COOH: C-terminal site; TM: transmembrane domain; JM: juxtamembrane domain. Adopted and modified from Cools et al., 2003 and Gotlib et al., 2008).
  
Entity Lung adenocarcinoma
Cytogenetics A t(4;12)(q12;q12) was found in a case of lung adenocarcinoma (Seo et al., 2012).
Hybrid/Mutated Gene SCAF11/PDGFRA
  

Breakpoints

 

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

Leukemias 11q23ChildAMLID1615 11q23ID1030 11q23secondLeukID1131 t1119ELLID1029 t0812q24q22ID2057
t0814ID1050 8p11inMPDID1091 inv8p11q13ID1189 PrimarCutanALCLID2118 t0708q34p11ID1409
t0809p12q33ID1129 t0811p11p15ID1200 t0811p12p15ID1521

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

Solid Tumors AmeloblastomID5945 MedulloblastomaID5065 rhab5004

External links

Nomenclature
HGNC (Hugo)PDGFRA   8803
Cards
AtlasPDGFRAID143ch4q12
Entrez_Gene (NCBI)PDGFRA  5156  platelet-derived growth factor receptor, alpha polypeptide
GeneCards (Weizmann)PDGFRA
Ensembl (Hinxton)ENSG00000134853 [Gene_View]  chr4:55095264-55164412 [Contig_View]  PDGFRA [Vega]
ICGC DataPortalENSG00000134853
AceView (NCBI)PDGFRA
Genatlas (Paris)PDGFRA
WikiGenes5156
SOURCE (Princeton)NM_006206
Genomic and cartography
GoldenPath (UCSC)PDGFRA  -  4q12   chr4:55095264-55164412 +  4q12   [Description]    (hg19-Feb_2009)
EnsemblPDGFRA - 4q12 [CytoView]
Mapping of homologs : NCBIPDGFRA [Mapview]
OMIM173490   606764   607685   
Gene and transcription
Genbank (Entrez)AA599881 AA625689 AK308353 AK311006 AK316578
RefSeq transcript (Entrez)NM_006206
RefSeq genomic (Entrez)AC_000136 NC_000004 NC_018915 NG_009250 NT_022853 NW_001838913 NW_004929319
Consensus coding sequences : CCDS (NCBI)PDGFRA
Cluster EST : UnigeneHs.74615 [ NCBI ]
CGAP (NCI)Hs.74615
Alternative Splicing : Fast-db (Paris)GSHG0033967
Alternative Splicing GalleryENSG00000134853
Gene ExpressionPDGFRA [ NCBI-GEO ]     PDGFRA [ SEEK ]   PDGFRA [ MEM ]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP16234 (Uniprot)
NextProtP16234  [Medical]
With graphics : InterProP16234
Splice isoforms : SwissVarP16234 (Swissvar)
Catalytic activity : Enzyme2.7.10.1 [ Enzyme-Expasy ]   2.7.10.12.7.10.1 [ IntEnz-EBI ]   2.7.10.1 [ BRENDA ]   2.7.10.1 [ KEGG ]   
Domaine pattern : Prosite (Expaxy)IG_LIKE (PS50835)    PROTEIN_KINASE_ATP (PS00107)    PROTEIN_KINASE_DOM (PS50011)    PROTEIN_KINASE_TYR (PS00109)    RECEPTOR_TYR_KIN_III (PS00240)   
Domains : Interpro (EBI)Ig-like_dom    Ig-like_fold    Ig_I-set    Ig_sub    Ig_sub2    Kinase-like_dom    PDGFRA    Prot_kinase_dom    Protein_kinase_ATP_BS    Ser-Thr/Tyr_kinase_cat_dom    Tyr_kinase_AS    Tyr_kinase_cat_dom    Tyr_kinase_CSF1/PDGF_rcpt    Tyr_kinase_rcpt_3_CS   
Related proteins : CluSTrP16234
Domain families : Pfam (Sanger)I-set (PF07679)    Pkinase_Tyr (PF07714)   
Domain families : Pfam (NCBI)pfam07679    pfam07714   
Domain families : Smart (EMBL)IG (SM00409)  IGc2 (SM00408)  TyrKc (SM00219)  
DMDM Disease mutations5156
Blocks (Seattle)P16234
PDB (SRS)1GQ5   
PDB (PDBSum)1GQ5   
PDB (IMB)1GQ5   
PDB (RSDB)1GQ5   
Human Protein AtlasENSG00000134853
Peptide AtlasP16234
HPRD01429
IPIIPI00027721   IPI00336178   IPI00967402   IPI00967879   IPI00967081   IPI00967704   IPI00966241   
Protein Interaction databases
DIP (DOE-UCLA)P16234
IntAct (EBI)P16234
FunCoupENSG00000134853
BioGRIDPDGFRA
IntegromeDBPDGFRA
STRING (EMBL)PDGFRA
Ontologies - Pathways
QuickGOP16234
Ontology : AmiGOluteinization  in utero embryonic development  cell activation  transmembrane receptor protein tyrosine kinase activity  platelet-derived growth factor alpha-receptor activity  platelet-derived growth factor alpha-receptor activity  vascular endothelial growth factor-activated receptor activity  platelet-derived growth factor receptor binding  protein binding  ATP binding  nucleus  cytoplasm  plasma membrane  integral component of plasma membrane  epidermal growth factor receptor signaling pathway  positive regulation of cytosolic calcium ion concentration  estrogen metabolic process  positive regulation of cell proliferation  fibroblast growth factor receptor signaling pathway  external side of plasma membrane  negative regulation of platelet activation  positive regulation of phospholipase C activity  positive regulation of phosphatidylinositol 3-kinase signaling  membrane  viral process  peptidyl-tyrosine phosphorylation  signal transduction involved in regulation of gene expression  extracellular matrix organization  lung development  adrenal gland development  positive regulation of cell migration  positive regulation of cell migration  male genitalia development  intrinsic component of plasma membrane  Leydig cell differentiation  platelet-derived growth factor receptor-alpha signaling pathway  vascular endothelial growth factor binding  positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway  Fc-epsilon receptor signaling pathway  wound healing  odontogenesis of dentin-containing tooth  protein homodimerization activity  positive regulation of phosphatidylinositol 3-kinase activity  innate immune response  positive regulation of DNA replication  protein autophosphorylation  platelet-derived growth factor receptor signaling pathway  neurotrophin TRK receptor signaling pathway  phosphatidylinositol-mediated signaling  phosphatidylinositol-mediated signaling  positive regulation of fibroblast proliferation  platelet-derived growth factor binding  platelet-derived growth factor binding  embryonic digestive tract morphogenesis  embryonic cranial skeleton morphogenesis  embryonic skeletal system morphogenesis  regulation of chemotaxis  cardiac myofibril assembly  palate development  face morphogenesis  cell chemotaxis  retina vasculature development in camera-type eye  positive regulation of ERK1 and ERK2 cascade  platelet aggregation  cellular response to amino acid stimulus  metanephric glomerular capillary formation  regulation of actin cytoskeleton reorganization  regulation of mesenchymal stem cell differentiation  
Ontology : EGO-EBIluteinization  in utero embryonic development  cell activation  transmembrane receptor protein tyrosine kinase activity  platelet-derived growth factor alpha-receptor activity  platelet-derived growth factor alpha-receptor activity  vascular endothelial growth factor-activated receptor activity  platelet-derived growth factor receptor binding  protein binding  ATP binding  nucleus  cytoplasm  plasma membrane  integral component of plasma membrane  epidermal growth factor receptor signaling pathway  positive regulation of cytosolic calcium ion concentration  estrogen metabolic process  positive regulation of cell proliferation  fibroblast growth factor receptor signaling pathway  external side of plasma membrane  negative regulation of platelet activation  positive regulation of phospholipase C activity  positive regulation of phosphatidylinositol 3-kinase signaling  membrane  viral process  peptidyl-tyrosine phosphorylation  signal transduction involved in regulation of gene expression  extracellular matrix organization  lung development  adrenal gland development  positive regulation of cell migration  positive regulation of cell migration  male genitalia development  intrinsic component of plasma membrane  Leydig cell differentiation  platelet-derived growth factor receptor-alpha signaling pathway  vascular endothelial growth factor binding  positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway  Fc-epsilon receptor signaling pathway  wound healing  odontogenesis of dentin-containing tooth  protein homodimerization activity  positive regulation of phosphatidylinositol 3-kinase activity  innate immune response  positive regulation of DNA replication  protein autophosphorylation  platelet-derived growth factor receptor signaling pathway  neurotrophin TRK receptor signaling pathway  phosphatidylinositol-mediated signaling  phosphatidylinositol-mediated signaling  positive regulation of fibroblast proliferation  platelet-derived growth factor binding  platelet-derived growth factor binding  embryonic digestive tract morphogenesis  embryonic cranial skeleton morphogenesis  embryonic skeletal system morphogenesis  regulation of chemotaxis  cardiac myofibril assembly  palate development  face morphogenesis  cell chemotaxis  retina vasculature development in camera-type eye  positive regulation of ERK1 and ERK2 cascade  platelet aggregation  cellular response to amino acid stimulus  metanephric glomerular capillary formation  regulation of actin cytoskeleton reorganization  regulation of mesenchymal stem cell differentiation  
Pathways : BIOCARTARac 1 cell motility signaling pathway [Genes]    Erk1/Erk2 Mapk Signaling pathway [Genes]    PDGF Signaling Pathway [Genes]    CBL mediated ligand-induced downregulation of EGF receptors [Genes]    Phospholipids as signalling intermediaries [Genes]    Role of PI3K subunit p85 in regulation of Actin Organization and Cell Migration [Genes]   
Pathways : KEGGMAPK signaling pathway    Ras signaling pathway    Rap1 signaling pathway    Calcium signaling pathway    Cytokine-cytokine receptor interaction    Endocytosis    PI3K-Akt signaling pathway    Focal adhesion    Gap junction    Regulation of actin cytoskeleton    HTLV-I infection    Pathways in cancer    MicroRNAs in cancer    Glioma    Prostate cancer    Melanoma   
REACTOMEP16234 [protein]
REACTOME PathwaysREACT_116125 Disease [pathway]
REACTOME PathwaysREACT_6900 Immune System [pathway]
REACTOME PathwaysREACT_111102 Signal Transduction [pathway]
Protein Interaction DatabasePDGFRA
Wikipedia pathwaysPDGFRA
Gene fusion - rearrangments
Rearrangement : TICdbBCR [22q11.23]  -  PDGFRA [2p23.2]
Rearrangement : TICdbCDK5RAP2 [9q33.2]  -  PDGFRA [9q34.12]
Rearrangement : TICdbETV6 [12p13.2]  -  PDGFRA [2q31.1]
Rearrangement : TICdbFIP1L1 [4q12]  -  PDGFRA [7q22.3]
Rearrangement : TICdbKIF5B [10p11.22]  -  PDGFRA [1p32.3]
Rearrangement : TICdbSTRN [2p22.2]  -  PDGFRA [21q22.2]
Polymorphisms : SNP, mutations, diseases
SNP Single Nucleotide Polymorphism (NCBI)PDGFRA
SNP (GeneSNP Utah)PDGFRA
SNP : HGBasePDGFRA
Genetic variants : HAPMAPPDGFRA
1000_GenomesPDGFRA 
ICGC programENSG00000134853 
Cancer Gene: CensusPDGFRA 
CONAN: Copy Number AnalysisPDGFRA 
Somatic Mutations in Cancer : COSMICPDGFRA 
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
LOVD (Leiden Open Variation Database)Zhejiang University Center for Genetic and Genomic Medicine (ZJU-CGGM)
DECIPHER (Syndromes)4:55095264-55164412
Mutations and Diseases : HGMDPDGFRA
OMIM173490    606764    607685   
MedgenPDGFRA
GENETestsPDGFRA
Disease Genetic AssociationPDGFRA
Huge Navigator PDGFRA [HugePedia]  PDGFRA [HugeCancerGEM]
Genomic VariantsPDGFRA  PDGFRA [DGVbeta]
Exome VariantPDGFRA
dbVarPDGFRA
ClinVarPDGFRA
snp3D : Map Gene to Disease5156
DGIdb (Curated mutations)PDGFRA
DGIdb (Drug Gene Interaction db)PDGFRA
General knowledge
Homologs : HomoloGenePDGFRA
Homology/Alignments : Family Browser (UCSC)PDGFRA
Phylogenetic Trees/Animal Genes : TreeFamPDGFRA
Chemical/Protein Interactions : CTD5156
Chemical/Pharm GKB GenePA33147
Drug Sensitivity PDGFRA
Clinical trialPDGFRA
Cancer Resource (Charite)ENSG00000134853
Other databases
Probes
Litterature
PubMed349 Pubmed reference(s) in Entrez
CoreMinePDGFRA
GoPubMedPDGFRA
iHOPPDGFRA

Bibliography

The human PDGF receptor alpha-subunit gene maps to chromosome 4 in close proximity to c-kit.
Gronwald RG, Adler DA, Kelly JD, Disteche CM, Bowen-Pope DF.
Hum Genet. 1990 Aug;85(3):383-5.
PMID 1697560
 
Structure, organization, and transcription units of the human alpha-platelet-derived growth factor receptor gene, PDGFRA.
Kawagishi J, Kumabe T, Yoshimoto T, Yamamoto T.
Genomics. 1995 Nov 20;30(2):224-32.
PMID 8586421
 
The t(4;22)(q12;q11) in atypical chronic myeloid leukaemia fuses BCR to PDGFRA.
Baxter EJ, Hochhaus A, Bolufer P, Reiter A, Fernandez JM, Senent L, Cervera J, Moscardo F, Sanz MA, Cross NC.
Hum Mol Genet. 2002 Jun 1;11(12):1391-7.
PMID 12023981
 
A tyrosine kinase created by fusion of the PDGFRA and FIP1L1 genes as a therapeutic target of imatinib in idiopathic hypereosinophilic syndrome.
Cools J, DeAngelo DJ, Gotlib J, Stover EH, Legare RD, Cortes J, Kutok J, Clark J, Galinsky I, Griffin JD, Cross NC, Tefferi A, Malone J, Alam R, Schrier SL, Schmid J, Rose M, Vandenberghe P, Verhoef G, Boogaerts M, Wlodarska I, Kantarjian H, Marynen P, Coutre SE, Stone R, Gilliland DG.
N Engl J Med. 2003 Mar 27;348(13):1201-14.
PMID 12660384
 
PDGFRA activating mutations in gastrointestinal stromal tumors.
Heinrich MC, Corless CL, Duensing A, McGreevey L, Chen CJ, Joseph N, Singer S, Griffith DJ, Haley A, Town A, Demetri GD, Fletcher CD, Fletcher JA.
Science. 2003 Jan 31;299(5607):708-10. Epub 2003 Jan 9.
PMID 12522257
 
PDGFRA germline mutation in a family with multiple cases of gastrointestinal stromal tumor.
Chompret A, Kannengiesser C, Barrois M, Terrier P, Dahan P, Tursz T, Lenoir GM, Bressac-De Paillerets B.
Gastroenterology. 2004 Jan;126(1):318-21.
PMID 14699510
 
PDGFRA mutations in gastrointestinal stromal tumors: frequency, spectrum and in vitro sensitivity to imatinib.
Corless CL, Schroeder A, Griffith D, Town A, McGreevey L, Harrell P, Shiraga S, Bainbridge T, Morich J, Heinrich MC.
J Clin Oncol. 2005 Aug 10;23(23):5357-64. Epub 2005 May 31. (REVIEW)
PMID 15928335
 
Five years since the discovery of FIP1L1-PDGFRA: what we have learned about the fusion and other molecularly defined eosinophilias.
Gotlib J, Cools J.
Leukemia. 2008 Nov;22(11):1999-2010. doi: 10.1038/leu.2008.287. Epub 2008 Oct 9. (REVIEW)
PMID 18843283
 
Clinical significance of oncogenic KIT and PDGFRA mutations in gastrointestinal stromal tumours.
Lasota J, Miettinen M.
Histopathology. 2008 Sep;53(3):245-66. doi: 10.1111/j.1365-2559.2008.02977.x. Epub 2008 Feb 28. (REVIEW)
PMID 18312355
 
Resistance to Tyrosine Kinase Inhibitors in Gastrointestinal Stromal Tumors.
Gramza AW, Corless CL, Heinrich MC.
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PMID 20008851
 
Targeted therapy in GIST: in silico modeling for prediction of resistance.
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PMID 21364689
 
Platelet-derived growth factors and their receptors in normal and malignant hematopoiesis.
Demoulin JB, Montano-Almendras CP.
Am J Blood Res. 2012;2(1):44-56. Epub 2012 Jan 1.
PMID 22432087
 
The transcriptional landscape and mutational profile of lung adenocarcinoma.
Seo JS, Ju YS, Lee WC, Shin JY, Lee JK, Bleazard T, Lee J, Jung YJ, Kim JO, Shin JY, Yu SB, Kim J, Lee ER, Kang CH, Park IK, Rhee H, Lee SH, Kim JI, Kang JH, Kim YT.
Genome Res. 2012 Nov;22(11):2109-19.
PMID 22975805
 
Structural and functional properties of platelet-derived growth factor and stem cell factor receptors.
Heldin CH, Lennartsson J.
Cold Spring Harb Perspect Biol. 2013 Aug 1;5(8):a009100. doi: 10.1101/cshperspect.a009100. (REVIEW)
PMID 23906712
 
Imatinib therapy in a patient with suspected chronic neutrophilic leukemia and FIP1L1-PDGFRA rearrangement.
Jain N, Khoury JD, Pemmaraju N, Kollipara P, Kantarjian H, Verstovsek S.
Blood. 2013 Nov 7;122(19):3387-8. doi: 10.1182/blood-2013-07-516500.
PMID 24203930
 
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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Contributor(s)

Written06-2014Adriana Zamecnikova, Soad Al Bahar
Kuwait Cancer Control Center, Department of Hematology, Laboratory of Cancer Genetics, Kuwait

Citation

This paper should be referenced as such :
Zamecnikova A, Al Bahar S
PDGFRA (platelet-derived growth factor receptor, alpha polypeptide);
Atlas Genet Cytogenet Oncol Haematol. June 2014
Free online version   Free pdf version   [Bibliographic record ]
URL : http://AtlasGeneticsOncology.org/Genes/PDGFRAID143ch4q12.html

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indexed on : Thu Dec 4 15:18:49 CET 2014

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