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Showing drug card for Erlotinib (DB00530)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-02-19 16:04:59
Primary Accession Number DB00530
Secondary Accession Number
  • APRD00951
Name Erlotinib
Drug Type
  • Approved
  • Investigational
  • Small Molecule
Description Erlotinib hydrochloride (trade name Tarceva, Genentech/OSIP, originally coded as OSI-774) is a drug used to treat non-small cell lung cancer, pancreatic cancer and several other types of cancer. Similar to gefitinib, erlotinib specifically targets the epidermal growth factor receptor (EGFR) tyrosine kinase. It binds in a reversible fashion to the adenosine triphosphate (ATP) binding site of the receptor. Erlotinib has recently been shown to be a potent inhibitor of JAK2V617F activity. JAK2V617F is a mutant of tyrosine kinase JAK2, is found in most patients with polycythemia vera (PV) and a substantial proportion of patients with idiopathic myelofibrosis or essential thrombocythemia. The study suggests that erlotinib may be used for treatment of JAK2V617F-positive PV and other myeloproliferative disorders.
Synonyms
  1. OSI-774
  2. erlotinib
Brand Names
  1. Tarceva
Brand Mixtures Not Available
Chemical IUPAC Name N-(3-ethynylphenyl)-6,7-bis(2-methoxyethoxy)quinazolin-4-amine
Chemical Formula C22H23N3O4
Chemical Structure Structure
CAS Registry Number 183321-74-6
InChI Identifier InChI=1/C22H23N3O4/c1-4-16-6-5-7-17(12-16)25-22-18-13-20(28-10-8-26-2)21(29-11-9-27-3)14-19(18)23-15-24-22/h1,5-7,12-15H,8-11H2,2-3H3,(H,23,24,25)/f/h25H
InChI Key AAKJLRGGTJKAMG-LNNLXFCOCG
KEGG Drug Not Available
KEGG Compound Not Available
PubChem Compound 176870 Link Image
PubChem Substance 7885946 Link Image
ChEBI ID Not Available
PharmGKB ID PA13468792 Link Image
HET ID AQ4 Link Image
GenBank ID Not Available
Drug ID Number [DIN] 02269023 Link Image
RxList Link http://www.rxlist.com/cgi/generic4/tarceva.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Erlotinib Link Image
FDA Label
Material Safety Data Sheet (MSDS) Not Available
Synthesis Reference Not Available
Average Molecular Weight 393.4357
Monoisotopic Molecular Weight 393.1689
State Solid
Melting Point Not Available
Experimental Water Solubility Very slightly soluble (hydrochloride salt - maximal solubility of approximately 0.4 mg/mL occurs at a pH of approximately 2) Source: PhysProp
Predicted Water Solubility 8.91e-03 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 2.7 Source: PhysProp
Predicted LogP 3.13 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -4.64 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point Not Available
Mass Spectrum Not Available
MOL File Show Link Image | Download Link Image
SDF File Show Link Image | Download Link Image
PDB File Show Link Image | Download Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Isomeric SMILES COCCOC1=C(OCCOC)C=C2C(NC3=CC=CC(=C3)C#C)=NC=NC2=C1
Canonical SMILES COCCOC1=C(OCCOC)C=C2C(NC3=CC=CC(=C3)C#C)=NC=NC2=C1
Drug Category
  • Protein Kinase Inhibitors
ATC Codes
AHFS Codes
  • 10:00.00
Indication For the treatment of patients with locally advanced or metastatic non-small cell lung cancer after failure of at least one prior chemotherapy regimen. Also for use, in combination with gemcitabine, as the first-line treatment of patients with locally advanced, unresectable or metastatic pancreatic cancer.
Pharmacology Erlotinib is a Human Epidermal Growth Factor Receptor Type 1/Epidermal Growth Factor Receptor (HER1/EGFR) tyrosine kinase inhibitor.
Mechanism of Action The mechanism of clinical antitumor action of erlotinib is not fully characterized. Erlotinib inhibits the intracellular phosphorylation of tyrosine kinase associated with the epidermal growth factor receptor (EGFR). Specificity of inhibition with regard to other tyrosine kinase receptors has not been fully characterized. EGFR is expressed on the cell surface of normal cells and cancer cells.
Absorption Erlotinib is about 60% absorbed after oral administration and its bioavailability is substantially increased by food to almost 100%.
Toxicity Symptoms of overdose include diarrhea, rash, and liver transaminase elevation.
Protein Binding 93% protein bound to albumin and alpha-1 acid glycoprotein (AAG)
Biotransformation In vitro assays of cytochrome P450 metabolism showed that erlotinib is metabolized primarily by CYP3A4 and to a lesser extent by CYP1A2, and the extrahepatic isoform CYP1A1.
Half Life Median half-life of 36.2 hours.
Dosage Forms
Form Route
Tablet Oral
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Atazanavir This CYP3A4 inhibitor increases levels/toxicity of erlotinib
Clarithromycin This CYP3A4 inhibitor increases levels/toxicity of erlotinib
Erythromycin This CYP3A4 inhibitor increases levels/toxicity of erlotinib
Indinavir This CYP3A4 inhibitor increases levels/toxicity of erlotinib
Itraconazole This CYP3A4 inhibitor increases levels/toxicity of erlotinib
Ketoconazole This CYP3A4 inhibitor increases levels/toxicity of erlotinib
Nefazodone This CYP3A4 inhibitor increases levels/toxicity of erlotinib
Nelfinavir This CYP3A4 inhibitor increases levels/toxicity of erlotinib
Rifabutin Decreased levels/effect of erlotinib
Rifampin Decreased levels/effect of erlotinib
Rifapentine Decreased levels/effect of erlotinib
Ritonavir This CYP3A4 inhibitor increases levels/toxicity of erlotinib
Saquinavir This CYP3A4 inhibitor increases levels/toxicity of erlotinib
St. John's Wort Decreased levels/effect of erlotinib
Telithromycin This CYP3A4 inhibitor increases levels/toxicity of erlotinib
Troleandomycin This CYP3A4 inhibitor increases levels/toxicity of erlotinib
Voriconazole This CYP3A4 inhibitor increases levels/toxicity of erlotinib
Food Interactions
  • Take at least 1 hour before or 2 hours after any food.
  • Take with a glass of water.
Pathways Not Available
General References
  1. Blum G, Gazit A, Levitzki A: Substrate competitive inhibitors of IGF-1 receptor kinase. Biochemistry. 2000 Dec 26;39(51):15705-12. [PubMed Link Image]
  2. Raymond E, Faivre S, Armand JP: Epidermal growth factor receptor tyrosine kinase as a target for anticancer therapy. Drugs. 2000;60 Suppl 1:15-23; discussion 41-2. [PubMed Link Image]
  3. Jones HE, Goddard L, Gee JM, Hiscox S, Rubini M, Barrow D, Knowlden JM, Williams S, Wakeling AE, Nicholson RI: Insulin-like growth factor-I receptor signalling and acquired resistance to gefitinib (ZD1839; Iressa) in human breast and prostate cancer cells. Endocr Relat Cancer. 2004 Dec;11(4):793-814. [PubMed Link Image]
  4. Dudek AZ, Kmak KL, Koopmeiners J, Keshtgarpour M: Skin rash and bronchoalveolar histology correlates with clinical benefit in patients treated with gefitinib as a therapy for previously treated advanced or metastatic non-small cell lung cancer. Lung Cancer. 2006 Jan;51(1):89-96. Epub 2005 Nov 14. [PubMed Link Image]
  5. Li Z, Xu M, Xing S, Ho WT, Ishii T, Li Q, Fu X, Zhao ZJ: Erlotinib effectively inhibits JAK2V617F activity and polycythemia vera cell growth. J Biol Chem. 2007 Feb 9;282(6):3428-32. Epub 2006 Dec 18. [PubMed Link Image]
  6. Wikipedia Link Image
  7. RxList Link Image
Organisms Affected
  • Humans and other mammals
Phase 1 Metabolizing Enzymes
  1. Cytochrome P450 3A4 (CYP3A4)
Targets
  1. Epidermal growth factor receptor
Phase 1 Metabolizing Enzyme 1 [top]
Enzyme 1 Name Cytochrome P450 3A4 (CYP3A4)
Enzyme 1 Gene Name CYP3A4
Enzyme 1 SwissProt ID P08684 Link Image
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 Protein Sequence >sp|P08684|CP3A4_HUMAN Cytochrome P450 3A4 (EC 1.14.13.67) 
ALIPDLAMETWLLLAVSLVLLYLYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMFD
MECHKKYGKVWGFYDGQQPVLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKSAISIA
EDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKDVFGAYSM
DVITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICVF
PREVTNFLRKSVKRMKESRLEDTQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSII
FIFAGYETTSSVLSFIMYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVLQMEYLDMVVN
ETLRLFPIAMRLERVCKKDVEINGMFIPKGWVVMIPSYALHRDPKYWTEPEKFLPERFSK
KNKDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLGG
LLQPEKPVVLKVESRDGTVSGA
Drug Target 1 [top]
Target 1 ID 844
Target 1 Name Epidermal growth factor receptor
Target 1 Synonyms
  1. EC 2.7.10.1
  2. Epidermal growth factor receptor precursor
  3. Receptor tyrosine-protein kinase ErbB-1
Target 1 Gene Name EGFR
Target 1 Protein Sequence >Epidermal growth factor receptor precursor 
MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEV
VLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALA
VLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDF
QNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGC
TGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYV
VTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFK
NCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAF
ENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKL
FGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCN
LLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVM
GENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPSIATGMVGALLLLLVV
ALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLRILKETEFKKIKVLGS
GAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGI
CLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAA
RNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSY
GVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPK
FRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQ
QGFFSSPSTSRTPLLSSLSATSNNSTVACIDRNGLQSCPIKEDSFLQRYSSDPTGALTED
SIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLNPAPSRDPHYQDPHSTAVGNPEYLN
TVQPTCVNSTFDSPAHWAQKGSHQISLDNPDYQQDFFPKEAKPNGIFKGSTAENAEYLRV
APQSSEFIGA
Target 1 Number of Residues 1230
Target 1 Molecular Weight 134279
Target 1 Theoretical pI 6.67
Target 1 GO Classification
Function
binding
nucleotide binding
purine nucleotide binding
adenyl nucleotide binding
ATP binding
epidermal growth factor receptor activity
catalytic activity
transferase activity
transferase activity, transferring phosphorus-containing groups
kinase activity
protein kinase activity
protein-tyrosine kinase activity
transmembrane receptor protein tyrosine kinase activity
Process
cellular process
cell communication
signal transduction
cell surface receptor linked signal transduction
enzyme linked receptor protein signaling pathway
transmembrane receptor protein tyrosine kinase signaling pathway
physiological process
metabolism
macromolecule metabolism
biopolymer metabolism
biopolymer modification
protein modification
protein amino acid phosphorylation
Component
cell
membrane
Target 1 General Function Involved in transmembrane receptor protein tyrosine kinase activity
Target 1 Specific Function Isoform 2/truncated isoform may act as an antagonist
Target 1 Pathways Not Available
Target 1 Reactions
  • ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Target 1 Pfam Domain Function
Target 1 Signals
  • 1-24
Target 1 Transmembrane Regions
  • 646-668
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 757924 Link Image
Target 1 UniProtKB/Swiss-Prot ID P00533 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name EGFR_HUMAN Link Image
Target 1 PDB ID 1IVO Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location
  • Cell membrane
  • single-pass type I membrane protein. Isoform 2:Secreted protein
Target 1 Gene Sequence >3633 bp 
ATGCGACCCTCCGGGACGGCCGGGGCAGCGCTCCTGGCGCTGCTGGCTGCGCTCTGCCCG
GCGAGTCGGGCTCTGGAGGAAAAGAAAGTTTGCCAAGGCACGAGTAACAAGCTCACGCAG
TTGGGCACTTTTGAAGATCATTTTCTCAGCCTCCAGAGGATGTTCAATAACTGTGAGGTG
GTCCTTGGGAATTTGGAAATTACCTATGTGCAGAGGAATTATGATCTTTCCTTCTTAAAG
ACCATCCAGGAGGTGGCTGGTTATGTCCTCATTGCCCTCAACACAGTGGAGCGAATTCCT
TTGGAAAACCTGCAGATCATCAGAGGAAATATGTACTACGAAAATTCCTATGCCTTAGCA
GTCTTATCTAACTATGATGCAAATAAAACCGGACTGAAGGAGCTGCCCATGAGAAATTTA
CAGGAAATCCTGCATGGCGCCGTGCGGTTCAGCAACAACCCTGCCCTGTGCAACGTGGAG
AGCATCCAGTGGCGGGACATAGTCAGCAGTGACTTTCTCAGCAACATGTCGATGGACTTC
CAGAACCACCTGGGCAGCTGCCAAAAGTGTGATCCAAGCTGTCCCAATGGGAGCTGCTGG
GGTGCAGGAGAGGAGAACTGCCAGAAACTGACCAAAATCATCTGTGCCCAGCAGTGCTCC
GGGCGCTGCCGTGGCAAGTCCCCCAGTGACTGCTGCCACAACCAGTGTGCTGCAGGCTGC
ACAGGCCCCCGGGAGAGCGACTGCCTGGTCTGCCGCAAATTCCGAGACGAAGCCACGTGC
AAGGACACCTGCCCCCCACTCATGCTCTACAACCCCACCACGTACCAGATGGATGTGAAC
CCCGAGGGCAAATACAGCTTTGGTGCCACCTGCGTGAAGAAGTGTCCCCGTAATTATGTG
GTGACAGATCACGGCTCGTGCGTCCGAGCCTGTGGGGCCGACAGCTATGAGATGGAGGAA
GACGGCGTCCGCAAGTGTAAGAAGTGCGAAGGGCCTTGCCGCAAAGTGTGTAACGGAATA
GGTATTGGTGAATTTAAAGACTCACTCTCCATAAATGCTACGAATATTAAACACTTCAAA
AACTGCACCTCCATCAGTGGCGATCTCCACATCCTGCCGGTGGCATTTAGGGGTGACTCC
TTCACACATACTCCTCCTCTGGATCCACAGGAACTGGATATTCTGAAAACCGTAAAGGAA
ATCACAGGGTTTTTGCTGATTCAGGCTTGGCCTGAAAACAGGACGGACCTCCATGCCTTT
GAGAACCTAGAAATCATACGCGGCAGGACCAAGCAACATGGTCAGTTTTCTCTTGCAGTC
GTCAGCCTGAACATAACATCCTTGGGATTACGCTCCCTCAAGGAGATAAGTGATGGAGAT
GTGATAATTTCAGGAAACAAAAATTTGTGCTATGCAAATACAATAAACTGGAAAAAACTG
TTTGGGACCTCCGGTCAGAAAACCAAAATTATAAGCAACAGAGGTGAAAACAGCTGCAAG
GCCACAGGCCAGGTCTGCCATGCCTTGTGCTCCCCCGAGGGCTGCTGGGGCCCGGAGCCC
AGGGACTGCGTCTCTTGCCGGAATGTCAGCCGAGGCAGGGAATGCGTGGACAAGTGCAAG
CTTCTGGAGGGTGAGCCAAGGGAGTTTGTGGAGAACTCTGAGTGCATACAGTGCCACCCA
GAGTGCCTGCCTCAGGCCATGAACATCACCTGCACAGGACGGGGACCAGACAACTGTATC
CAGTGTGCCCACTACATTGACGGCCCCCACTGCGTCAAGACCTGCCCGGCAGGAGTCATG
GGAGAAAACAACACCCTGGTCTGGAAGTACGCAGACGCCGGCCATGTGTGCCACCTGTGC
CATCCAAACTGCACCTACGGATGCACTGGGCCAGGTCTTGAAGGCTGTCCAACGAATGGG
CCTAAGATCCCGTCCATCGCCACTGGGATGGTGGGGGCCCTCCTCTTGCTGCTGGTGGTG
GCCCTGGGGATCGGCCTCTTCATGCGAAGGCGCCACATCGTTCGGAAGCGCACGCTGCGG
AGGCTGCTGCAGGAGAGGGAGCTTGTGGAGCCTCTTACACCCAGTGGAGAAGCTCCCAAC
CAAGCTCTCTTGAGGATCTTGAAGGAAACTGAATTCAAAAAGATCAAAGTGCTGGGCTCC
GGTGCGTTCGGCACGGTGTATAAGGGACTCTGGATCCCAGAAGGTGAGAAAGTTAAAATT
CCCGTCGCTATCAAGGAATTAAGAGAAGCAACATCTCCGAAAGCCAACAAGGAAATCCTC
GATGAAGCCTACGTGATGGCCAGCGTGGACAACCCCCACGTGTGCCGCCTGCTGGGCATC
TGCCTCACCTCCACCGTGCAACTCATCACGCAGCTCATGCCCTTCGGCTGCCTCCTGGAC
TATGTCCGGGAACACAAAGACAATATTGGCTCCCAGTACCTGCTCAACTGGTGTGTGCAG
ATCGCAAAGGGCATGAACTACTTGGAGGACCGTCGCTTGGTGCACCGCGACCTGGCAGCC
AGGAACGTACTGGTGAAAACACCGCAGCATGTCAAGATCACAGATTTTGGGCTGGCCAAA
CTGCTGGGTGCGGAAGAGAAAGAATACCATGCAGAAGGAGGCAAAGTGCCTATCAAGTGG
ATGGCATTGGAATCAATTTTACACAGAATCTATACCCACCAGAGTGATGTCTGGAGCTAC
GGGGTGACCGTTTGGGAGTTGATGACCTTTGGATCCAAGCCATATGACGGAATCCCTGCC
AGCGAGATCTCCTCCATCCTGGAGAAAGGAGAACGCCTCCCTCAGCCACCCATATGTACC
ATCGATGTCTACATGATCATGGTCAAGTGCTGGATGATAGACGCAGATAGTCGCCCAAAG
TTCCGTGAGTTGATCATCGAATTCTCCAAAATGGCCCGAGACCCCCAGCGCTACCTTGTC
ATTCAGGGGGATGAAAGAATGCATTTGCCAAGTCCTACAGACTCCAACTTCTACCGTGCC
CTGATGGATGAAGAAGACATGGACGACGTGGTGGATGCCGACGAGTACCTCATCCCACAG
CAGGGCTTCTTCAGCAGCCCCTCCACGTCACGGACTCCCCTCCTGAGCTCTCTGAGTGCA
ACCAGCAACAATTCCACCGTGGCTTGCATTGATAGAAATGGGCTGCAAAGCTGTCCCATC
AAGGAAGACAGCTTCTTGCAGCGATACAGCTCAGACCCCACAGGCGCCTTGACTGAGGAC
AGCATAGACGACACCTTCCTCCCAGTGCCTGAATACATAAACCAGTCCGTTCCCAAAAGG
CCCGCTGGCTCTGTGCAGAATCCTGTCTATCACAATCAGCCTCTGAACCCCGCGCCCAGC
AGAGACCCACACTACCAGGACCCCCACAGCACTGCAGTGGGCAACCCCGAGTATCTCAAC
ACTGTCCAGCCCACCTGTGTCAACAGCACATTCGACAGCCCTGCCCACTGGGCCCAGAAA
GGCAGCCACCAAATTAGCCTGGACAACCCTGACTACCAGCAGGACTTCTTTCCCAAGGAA
GCCAAGCCAAATGGCATCTTTAAGGGCTCCACAGCTGAAAATGCAGAATACCTAAGGGTC
GCGCCACAAAGCAGTGAATTTATTGGAGCATGA
Target 1 GenBank Gene ID
Target 1 GeneCard ID EGFR Link Image
Target 1 GenAtlas ID EGFR Link Image
Target 1 HGNC ID HGNC:3236 Link Image
Target 1 Chromosome Location 7
Target 1 Locus 7p12
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Sato C, Kim JH, Abe Y, Saito K, Yokoyama S, Kohda D: Characterization of the N-oligosaccharides attached to the atypical Asn-X-Cys sequence of recombinant human epidermal growth factor receptor. J Biochem (Tokyo). 2000 Jan;127(1):65-72. [PubMed Link Image]
  2. Habib AA, Chatterjee S, Park SK, Ratan RR, Lefebvre S, Vartanian T: The epidermal growth factor receptor engages receptor interacting protein and nuclear factor-kappa B (NF-kappa B)-inducing kinase to activate NF-kappa B. Identification of a novel receptor-tyrosine kinase signalosome. J Biol Chem. 2001 Mar 23;276(12):8865-74. Epub 2000 Dec 14. [PubMed Link Image]
  3. Reiter JL, Threadgill DW, Eley GD, Strunk KE, Danielsen AJ, Sinclair CS, Pearsall RS, Green PJ, Yee D, Lampland AL, Balasubramaniam S, Crossley TD, Magnuson TR, James CD, Maihle NJ: Comparative genomic sequence analysis and isolation of human and mouse alternative EGFR transcripts encoding truncated receptor isoforms. Genomics. 2001 Jan 1;71(1):1-20. [PubMed Link Image]
  4. Haley JD, Waterfield MD: Contributory effects of de novo transcription and premature transcript termination in the regulation of human epidermal growth factor receptor proto-oncogene RNA synthesis. J Biol Chem. 1991 Jan 25;266(3):1746-53. [PubMed Link Image]
  5. Margolis BL, Lax I, Kris R, Dombalagian M, Honegger AM, Howk R, Givol D, Ullrich A, Schlessinger J: All autophosphorylation sites of epidermal growth factor (EGF) receptor and HER2/neu are located in their carboxyl-terminal tails. Identification of a novel site in EGF receptor. J Biol Chem. 1989 Jun 25;264(18):10667-71. [PubMed Link Image]
  6. Chen WS, Lazar CS, Lund KA, Welsh JB, Chang CP, Walton GM, Der CJ, Wiley HS, Gill GN, Rosenfeld MG: Functional independence of the epidermal growth factor receptor from a domain required for ligand-induced internalization and calcium regulation. Cell. 1989 Oct 6;59(1):33-43. [PubMed Link Image]
  7. Russo MW, Lukas TJ, Cohen S, Staros JV: Identification of residues in the nucleotide binding site of the epidermal growth factor receptor/kinase. J Biol Chem. 1985 May 10;260(9):5205-8. [PubMed Link Image]
  8. Ishii S, Xu YH, Stratton RH, Roe BA, Merlino GT, Pastan I: Characterization and sequence of the promoter region of the human epidermal growth factor receptor gene. Proc Natl Acad Sci U S A. 1985 Aug;82(15):4920-4. [PubMed Link Image]
  9. Carpenter G: Receptors for epidermal growth factor and other polypeptide mitogens. Annu Rev Biochem. 1987;56:881-914. [PubMed Link Image]
  10. Heisermann GJ, Gill GN: Epidermal growth factor receptor threonine and serine residues phosphorylated in vivo. J Biol Chem. 1988 Sep 15;263(26):13152-8. [PubMed Link Image]
  11. 3329716 Haley J, Whittle N, Bennet P, Kinchington D, Ullrich A, Waterfield M: The human EGF receptor gene: structure of the 110 kb locus and identification of sequences regulating its transcription. Oncogene Res. 1987 Sep-Oct;1(4):375-96.
  12. 6093780 Simmen FA, Gope ML, Schulz TZ, Wright DA, Carpenter G, O'Malley BW: Isolation of an evolutionarily conserved epidermal growth factor receptor cDNA from human A431 carcinoma cells. Biochem Biophys Res Commun. 1984 Oct 15;124(1):125-32.
  13. 6324343 Weber W, Gill GN, Spiess J: Production of an epidermal growth factor receptor-related protein. Science. 1984 Apr 20;224(4646):294-7.
  14. 6325948 Mroczkowski B, Mosig G, Cohen S: ATP-stimulated interaction between epidermal growth factor receptor and supercoiled DNA. Nature. 1984 May 17-23;309(5965):270-3.
  15. 6326261 Lin CR, Chen WS, Kruiger W, Stolarsky LS, Weber W, Evans RM, Verma IM, Gill GN, Rosenfeld MG: Expression cloning of human EGF receptor complementary DNA: gene amplification and three related messenger RNA products in A431 cells. Science. 1984 May 25;224(4651):843-8.
  16. 6328312 Ullrich A, Coussens L, Hayflick JS, Dull TJ, Gray A, Tam AW, Lee J, Yarden Y, Libermann TA, Schlessinger J, et al.: Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cells. Nature. 1984 May 31-Jun 6;309(5967):418-25.
  17. 6330563 Xu YH, Ishii S, Clark AJ, Sullivan M, Wilson RK, Ma DP, Roe BA, Merlino GT, Pastan I: Human epidermal growth factor receptor cDNA is homologous to a variety of RNAs overproduced in A431 carcinoma cells. Nature. 1984 Jun 28-Jul 4;309(5971):806-10.
  18. 7654368 Ilekis JV, Stark BC, Scoccia B: Possible role of variant RNA transcripts in the regulation of epidermal growth factor receptor expression in human placenta. Mol Reprod Dev. 1995 Jun;41(2):149-56.
  19. 8918811 Reiter JL, Maihle NJ: A 1.8 kb alternative transcript from the human epidermal growth factor receptor gene encodes a truncated form of the receptor. Nucleic Acids Res. 1996 Oct 15;24(20):4050-6.
  20. 8962717 Smith KD, Davies MJ, Bailey D, Renouf DV, Hounsell EF: Analysis of the glycosylation patterns of the extracellular domain of the epidermal growth factor receptor expressed in Chinese hamster ovary fibroblasts. Growth Factors. 1996;13(1-2):121-32.
  21. 9103388 Ilekis JV, Gariti J, Niederberger C, Scoccia B: Expression of a truncated epidermal growth factor receptor-like protein (TEGFR) in ovarian cancer. Gynecol Oncol. 1997 Apr;65(1):36-41.
  22. 9556602 Abe Y, Odaka M, Inagaki F, Lax I, Schlessinger J, Kohda D: Disulfide bond structure of human epidermal growth factor receptor. J Biol Chem. 1998 May 1;273(18):11150-7.
Target 1 Drug References
  1. Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. [PubMed Link Image]
  2. Kim TE, Murren JR: Erlotinib OSI/Roche/Genentech. Curr Opin Investig Drugs. 2002 Sep;3(9):1385-95. [PubMed Link Image]
  3. Laird AD, Cherrington JM: Small molecule tyrosine kinase inhibitors: clinical development of anticancer agents. Expert Opin Investig Drugs. 2003 Jan;12(1):51-64. [PubMed Link Image]
  4. Delbaldo C, Faivre S, Raymond E: [Epidermal growth factor inhibitors] Rev Med Interne. 2003 Jun;24(6):372-83. [PubMed Link Image]
  5. Bulgaru AM, Mani S, Goel S, Perez-Soler R: Erlotinib (Tarceva): a promising drug targeting epidermal growth factor receptor tyrosine kinase. Expert Rev Anticancer Ther. 2003 Jun;3(3):269-79. [PubMed Link Image]
  6. Akita RW, Sliwkowski MX: Preclinical studies with Erlotinib (Tarceva). Semin Oncol. 2003 Jun;30(3 Suppl 7):15-24. [PubMed Link Image]

This project is supported by Genome Alberta & Genome Canada, a not-for-profit organization that is leading Canada's national genomics strategy with $600 million in funding from the federal government. This project is also supported in part by GenomeQuest, Inc., an enterprise genomic information company serving the life science community.