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Showing drug card for Pegfilgrastim (DB00019)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-02-19 16:03:15
Primary Accession Number DB00019
Secondary Accession Number
  • BIOD00094
  • BTD00094
Name Pegfilgrastim
Drug Type
  • Approved
  • Biotech
Description PEGylated (at N terminus) form of human G-CSF (Granulocyte colony stimulating factor), 175 residues, produced from E. coli via bacterial fermentation.
Synonyms
  1. G-CSF
  2. Granulocyte colony-stimulating factor precursor
  3. Lenograstim
  4. Pluripoietin
Brand Names
  1. Neulasta (Amgen Inc.)
Brand Mixtures Not Available
Chemical IUPAC Name PEGylated human granulocyte colony stimulating factor
Chemical Formula C845H1343N223O243S9
Chemical Structure Structure
Protein Sequence(s) >DB00019 sequence 
MTPLGPASSLPQSFLLKCLEQVRKIQGDGAALQEKLCATYKLCHPEELVLLGHSLGIPWA
PLSSCPSQALQLAGCLSQLHSGLFLYQGLLQALEGISPELGPTLDTLQLDVADFATTIWQ
QMEELGMAPALQPTQGAMPAFASAFQRRAGGVLVASHLQSFLEVSYRVLRHLAQP
CAS Registry Number 208265-92-3
InChI Identifier Not Available
InChI Key Not Available
KEGG Drug Not Available
KEGG Compound Not Available
PubChem Compound Not Available
PubChem Substance Not Available
ChEBI ID Not Available
PharmGKB ID PA10809 Link Image
HET ID Not Available
GenBank ID X03438 Link Image
Drug ID Number [DIN] 02249790 Link Image
RxList Link http://www.rxlist.com/cgi/generic3/neulasta.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Pegfilgrastim Link Image
FDA Label
Material Safety Data Sheet (MSDS) Not Available
Synthesis Reference Not Available
Average Molecular Weight 18802.8000
Monoisotopic Molecular Weight Not Available
State Liquid
Melting Point 60 oC (Luo, P., Protein Science 11:1218-1226 (2002))
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility Not Available Calculated using ALOGPS
Experimental LogP/Hydrophobicity 0.209 Source: PhysProp
Predicted LogP Not Available Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS Not Available Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point 5.65
Mass Spectrum Not Available
MOL File Not Available
SDF File Not Available
PDB File Not Available
Experimental PDB ID 1RHG Link Image
Experimental PDB File Show
Experimental PDB Structure
Isomeric SMILES Not Available
Canonical SMILES Not Available
Drug Category
  • Anti-Infective Agents
  • Antineutropenic Agents
  • Immunomodulatory Agents
ATC Codes
AHFS Codes
  • 20:16.00
Indication Increases leukocyte production, for treatment in non-myeloid cancer, neutropenia and bone marrow transplant
Pharmacology Used in the treatment of chemotherapy-induced neutropenia by enhancing the production of neutrophils. Pegfilgrastim acts on hematopoietic cells by binding to specific cell surface receptors thereby stimulating proliferation, differentiation, commitment, and end cell functional activation. Pegfilgrastim has reduced renal clearance and prolonged persistence in vivo as compared to Filgrastim.
Mechanism of Action Pegfilgrastim binds to the G-CSF receptor. As a G-CSF analog, it controls proliferation of committed progenitor cells and influences their maturation into mature neutrophils. Pegfilgrastim also stimulates the release of neutrophils from bone marrow storage pools and reduces their maturation time. Pegfilgrastim acts to increase the phagocytic activity of mature neutrophils. In patients receiving cytotoxic chemotherapy, pegfilgrastim can accelerate neutrophil recovery, leading to a reduction in duration of the neutropenic phase
Absorption Not Available
Toxicity Not Available
Protein Binding Not Available
Biotransformation Not Available
Half Life 15-80 hrs
Dosage Forms
Form Route
Solution Subcutaneous
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions Not Available
Food Interactions Not Available
Pathways Not Available
General References
  1. Drugs.com Link Image
  2. Wikipedia Link Image
  3. RxList Link Image
Organisms Affected Not Available
Targets
  1. Leukocyte elastase
  2. Granulocyte colony-stimulating factor receptor
Drug Target 1 [top]
Target 1 ID 437
Target 1 Name Leukocyte elastase
Target 1 Synonyms
  1. Bone marrow serine protease
  2. EC 3.4.21.37
  3. Elastase-2
  4. HLE
  5. Human leukocyte elastase
  6. Leukocyte elastase precursor
  7. Medullasin
  8. Neutrophil elastase
  9. PMN elastase
Target 1 Gene Name ELA2
Target 1 Protein Sequence >Leukocyte elastase precursor 
MTLGRRLACLFLACVLPALLLGGTALASEIVGGRRARPHAWPFMVSLQLRGGHFCGATLI
APNFVMSAAHCVANVNVRAVRVVLGAHNLSRREPTRQVFAVQRIFENGYDPVNLLNDIVI
LQLNGSATINANVQVAQLPAQGRRLGNGVQCLAMGWGLLGRNRGIASVLQELNVTVVTSL
CRRSNVCTLVRGRQAGVCFGDSGSPLVCNGLIHGIASFVRGGCASGLYPDAFAPVAQFVN
WIDSIIQRSEDNPCPHPRDPDPASRTH
Target 1 Number of Residues 271
Target 1 Molecular Weight 28518
Target 1 Theoretical pI 9.41
Target 1 GO Classification
Function
catalytic activity
hydrolase activity
peptidase activity
endopeptidase activity
serine-type endopeptidase activity
Process
physiological process
metabolism
macromolecule metabolism
protein metabolism
cellular protein metabolism
proteolysis
Component
Not Available
Target 1 General Function Involved in elastase activity and cytokine binding
Target 1 Specific Function Modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis
Target 1 Pathways Not Available
Target 1 Reactions
  • Hydrolysis of proteins, including elastin. Preferential cleavage Val! > Ala!
Target 1 Pfam Domain Function
Target 1 Signals
  • 1-27
Target 1 Transmembrane Regions
  • 7-26
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 296665 Link Image
Target 1 UniProtKB/Swiss-Prot ID P08246 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name ELNE_HUMAN Link Image
Target 1 PDB ID 1H1B Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location
  • Cytoplasmic
Target 1 Gene Sequence >804 bp 
ATGACCCTCGGCCGCCGACTCGCGTGTCTTTTCCTCGCCTGTGTCCTGCCGGCCTTGCTG
CTGGGGGGCACCGCGCTGGCCTCGGAGATTGTGGGGGGCCGGCGAGCGCGGCCCCACGCG
TGGCCCTTCATGGTGTCCCTGCAGCTGCGCGGAGGCCACTTCTGCGGCGCCACCCTGATT
GCGCCCAACTTCGTCATGTCGGCCGCGCACTGCGTGGCGAATGTAAACGTCCGCGCGGTG
CGGGTGGTCCTGGGAGCCCATAACCTCTCGCGGCGGGAGCCCACCCGGCAGGTGTTCGCC
GTGCAGCGCATCTTCGAAAACGGCTACGACCCCGTAAACTTGCTCAACGACATCGTGATT
CTCCAGCTCAACGGGTCGGCCACCATCAACGCCAACGTGCAGGTGGCCCAGCTGCCGGCT
CAGGGACGCCGCCTGGGCAACGGGGTGCAGTGCCTGGCCATGGGCTGGGGCCTTCTGGGC
AGGAACCGTGGGATCGCCAGCGTCCTGCAGGAGCTCAACGTGACGGTGGTGACGTCCCTC
TGCCGTCGCAGCAACGTCTGCACTCTCGTGAGGGGCCGGCAGGCCGGCGTCTGTTTCGGG
GACTCCGGCAGCCCCTTGGTCTGCAACGGGCTAATCCACGGAATTGCCTCCTTCGTCCGG
GGAGGCTGCGCCTCAGGGCTCTACCCCGATGCCTTTGCCCCGGTGGCACAGTTTGTAAAC
TGGATCGACTCTATCATCCAACGCTCCGAGGACAACCCCTGTCCCCACCCCCGGGACCCG
GACCCGGCCAGCAGGACCCACTGA
Target 1 GenBank Gene ID
Target 1 GeneCard ID ELA2 Link Image
Target 1 GenAtlas ID ELA2 Link Image
Target 1 HGNC ID HGNC:3309 Link Image
Target 1 Chromosome Location 19
Target 1 Locus 19p13.3
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Horwitz M, Benson KF, Person RE, Aprikyan AG, Dale DC: Mutations in ELA2, encoding neutrophil elastase, define a 21-day biological clock in cyclic haematopoiesis. Nat Genet. 1999 Dec;23(4):433-6. [PubMed Link Image]
  2. Aoki Y, Hase T: The primary structure and elastinolytic activity of medullasin (a serine protease of bone marrow). Biochem Biophys Res Commun. 1991 Jul 31;178(2):501-6. [PubMed Link Image]
  3. Okano K, Aoki Y, Shimizu H, Naruto M: Functional expression of human leukocyte elastase (HLE)/medullasin in eukaryotic cells. Biochem Biophys Res Commun. 1990 Mar 30;167(3):1326-32. [PubMed Link Image]
  4. Farley D, Salvesen G, Travis J: Molecular cloning of human neutrophil elastase. Biol Chem Hoppe Seyler. 1988 May;369 Suppl:3-7. [PubMed Link Image]
  5. Gabay JE, Scott RW, Campanelli D, Griffith J, Wilde C, Marra MN, Seeger M, Nathan CF: Antibiotic proteins of human polymorphonuclear leukocytes. Proc Natl Acad Sci U S A. 1989 Jul;86(14):5610-4. [PubMed Link Image]
  6. Farley D, Travis J, Salvesen G: The human neutrophil elastase gene. Analysis of the nucleotide sequence reveals three distinct classes of repetitive DNA. Biol Chem Hoppe Seyler. 1989 Jul;370(7):737-44. [PubMed Link Image]
  7. Okano K, Aoki Y, Sakurai T, Kajitani M, Kanai S, Shimazu T, Shimizu H, Naruto M: Molecular cloning of complementary DNA for human medullasin: an inflammatory serine protease in bone marrow cells. J Biochem (Tokyo). 1987 Jul;102(1):13-6. [PubMed Link Image]
  8. Takahashi H, Nukiwa T, Yoshimura K, Quick CD, States DJ, Holmes MD, Whang-Peng J, Knutsen T, Crystal RG: Structure of the human neutrophil elastase gene. J Biol Chem. 1988 Oct 15;263(29):14739-47. [PubMed Link Image]
  9. Navia MA, McKeever BM, Springer JP, Lin TY, Williams HR, Fluder EM, Dorn CP, Hoogsteen K: Structure of human neutrophil elastase in complex with a peptide chloromethyl ketone inhibitor at 1.84-A resolution. Proc Natl Acad Sci U S A. 1989 Jan;86(1):7-11. [PubMed Link Image]
  10. Wei AZ, Mayr I, Bode W: The refined 2.3 A crystal structure of human leukocyte elastase in a complex with a valine chloromethyl ketone inhibitor. FEBS Lett. 1988 Jul 18;234(2):367-73. [PubMed Link Image]
  11. 3422232 Takahashi H, Nukiwa T, Basset P, Crystal RG: Myelomonocytic cell lineage expression of the neutrophil elastase gene. J Biol Chem. 1988 Feb 15;263(5):2543-7.
  12. 3479752 Nakamura H, Okano K, Aoki Y, Shimizu H, Naruto M: Nucleotide sequence of human bone marrow serine protease (medullasin) gene. Nucleic Acids Res. 1987 Nov 25;15(22):9601-2.
  13. 3550808 Sinha S, Watorek W, Karr S, Giles J, Bode W, Travis J: Primary structure of human neutrophil elastase. Proc Natl Acad Sci U S A. 1987 Apr;84(8):2228-32.
  14. 3640709 Bode W, Wei AZ, Huber R, Meyer E, Travis J, Neumann S: X-ray crystal structure of the complex of human leukocyte elastase (PMN elastase) and the third domain of the turkey ovomucoid inhibitor. EMBO J. 1986 Oct;5(10):2453-8.
Target 1 Drug References
  1. Pelus LM, Bian H, King AG, Fukuda S: Neutrophil-derived MMP-9 mediates synergistic mobilization of hematopoietic stem and progenitor cells by the combination of G-CSF and the chemokines GRObeta/CXCL2 and GRObetaT/CXCL2delta4. Blood. 2004 Jan 1;103(1):110-9. Epub 2003 Sep 4. [PubMed Link Image]
  2. Carter CR, Whitmore KM, Thorpe R: The significance of carbohydrates on G-CSF: differential sensitivity of G-CSFs to human neutrophil elastase degradation. J Leukoc Biol. 2004 Mar;75(3):515-22. Epub 2003 Dec 4. [PubMed Link Image]
  3. Druhan LJ, Ai J, Massullo P, Kindwall-Keller T, Ranalli MA, Avalos BR: Novel mechanism of G-CSF refractoriness in patients with severe congenital neutropenia. Blood. 2005 Jan 15;105(2):584-91. Epub 2004 Sep 7. [PubMed Link Image]
  4. Jian MY, Koizumi T, Tsushima K, Fujimoto K, Kubo K: Effects of granulocyte colony-stimulating factor (G-CSF) and neutrophil elastase inhibitor (ONO-5046) on acid-induced lung injury in rats. Inflammation. 2004 Dec;28(6):327-36. [PubMed Link Image]
  5. Schepers H, Wierenga AT, van Gosliga D, Eggen BJ, Vellenga E, Schuringa JJ: Reintroduction of C/EBPalpha in leukemic CD34+ stem/progenitor cells impairs self-renewal and partially restores myelopoiesis. Blood. 2007 Aug 15;110(4):1317-25. Epub 2007 May 2. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 870
Target 2 Name Granulocyte colony-stimulating factor receptor
Target 2 Synonyms
  1. CD114 antigen
  2. G-CSF-R
  3. Granulocyte colony-stimulating factor receptor precursor
Target 2 Gene Name CSF3R
Target 2 Protein Sequence >Granulocyte colony-stimulating factor receptor precursor 
MARLGNCSLTWAALIILLLPGSLEECGHISVSAPIVHLGDPITASCIIKQNCSHLDPEPQ
ILWRLGAELQPGGRQQRLSDGTQESIITLPHLNHTQAFLSCCLNWGNSLQILDQVELRAG
YPPAIPHNLSCLMNLTTSSLICQWEPGPETHLPTSFTLKSFKSRGNCQTQGDSILDCVPK
DGQSHCCIPRKHLLLYQNMGIWVQAENALGTSMSPQLCLDPMDVVKLEPPMLRTMDPSPE
AAPPQAGCLQLCWEPWQPGLHINQKCELRHKPQRGEASWALVGPLPLEALQYELCGLLPA
TAYTLQIRCIRWPLPGHWSDWSPSLELRTTERAPTVRLDTWWRQRQLDPRTVQLFWKPVP
LEEDSGRIQGYVVSWRPSGQAGAILPLCNTTELSCTFHLPSEAQEVALVAYNSAGTSRPT
PVVFSESRGPALTRLHAMARDPHSLWVGWEPPNPWPQGYVIEWGLGPPSASNSNKTWRME
QNGRATGFLLKENIRPFQLYEIIVTPLYQDTMGPSQHVYAYSQEMAPSHAPELHLKHIGK
TWAQLEWVPEPPELGKSPLTHYTIFWTNAQNQSFSAILNASSRGFVLHGLEPASLYHIHL
MAASQAGATNSTVLTLMTLTPEGSELHIILGLFGLLLLLTCLCGTAWLCCSPNRKNPLWP
SVPDPAHSSLGSWVPTIMEEDAFQLPGLGTPPITKLTVLEEDEKKPVPWESHNSSETCGL
PTLVQTYVLQGDPRAVSTQPQSQSGTSDQVLYGQLLGSPTSPGPGHYLRCDSTQPLLAGL
TPSPKSYENLWFQASPLGTLVTPAPSQEDDCVFGPLLNFPLLQGIRVHGMEALGSF
Target 2 Number of Residues 849
Target 2 Molecular Weight 92157
Target 2 Theoretical pI 6.14
Target 2 GO Classification
Function
signal transducer activity
receptor activity
transmembrane receptor activity
hematopoietin/interferon-class (D200-domain) cytokine receptor activity
Process
Not Available
Component
cell
membrane
Target 2 General Function Involved in hematopoietin/interferon-class (D200-domain) cytokine receptor activity
Target 2 Specific Function Receptor for granulocyte colony-stimulating factor. In addition it may function in some adhesion or recognition events at the cell surface
Target 2 Pathways Not Available
Target 2 Reactions Not Available
Target 2 Pfam Domain Function
Target 2 Signals
  • 1-24
Target 2 Transmembrane Regions
  • 628-650
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 31697 Link Image
Target 2 UniProtKB/Swiss-Prot ID Q99062 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name CSF3R_HUMAN Link Image
Target 2 PDB ID Not Available
Target 2 Cellular Location
  • Cell membrane
  • single-pass type I membrane protein. Isoform GCSFR2:Secreted protein (Probable). Isof
Target 2 Gene Sequence >2511 bp 
ATGGCAAGGCTGGGAAACTGCAGCCTGACTTGGGCTGCCCTGATCATCCTGCTGCTCCCC
GGAAGTCTGGAGGAGTGCGGGCACATCAGTGTCTCAGCCCCCATCGTCCACCTGGGGGAT
CCCATCACAGCCTCCTGCATCATCAAGCAGAACTGCAGCCATCTGGACCCGGAGCCACAG
ATTCTGTGGAGACTGGGAGCAGAGCTTCAGCCCGGGGGCAGGCAGCAGCGTCTGTCTGAT
GGGACCCAGGAATCTATCATCACCCTGCCCCACCTCAACCACACTCAGGCCTTTCTCTCC
TGCTGCCTGAACTGGGGCAACAGCCTGCAGATCCTGGACCAGGTTGAGCTGCGCGCAGGC
TACCCTCCAGCCATACCCCACAACCTCTCCTGCCTCATGAACCTCACAACCAGCAGCCTC
ATCTGCCAGTGGGAGCCAGGACCTGAGACCCACCTACCCACCAGCTTCACTCTGAAGAGT
TTCAAGAGCCGGGGCAACTGTCAGACCCAAGGGGACTCCATCCTGGACTGCGTGCCCAAG
GACGGGCAGAGCCACTGCTGCATCCCACGCAAACACCTGCTGTTGTACCAGAATATGGGC
ATCTGGGTGCAGGCAGAGAATGCGCTGGGGACCAGCATGTCCCCACAACTGTGTCTTGAT
CCCATGGATGTTGTGAAACTGGAGCCCCCCATGCTGCGGACCATGGACCCCAGCCCTGAA
GCGGCCCCTCCCCAGGCAGGCTGCCTACAGCTGTGCTGGGAGCCATGGCAGCCAGGCCTG
CACATAAATCAGAAGTGTGAGCTGCGCCACAAGCCGCAGCGTGGAGAAGCCAGCTGGGCA
CTGGTGGGCCCCCTCCCCTTGGAGGCCCTTCAGTATGAGCTCTGCGGGCTCCTCCCAGCC
ACGGCCTACACCCTGCAGATACGCTGCATCCGCTGGCCCCTGCCTGGCCACTGGAGCGAC
TGGAGCCCCAGCCTGGAGCTGAGAACTACCGAACGGGCCCCCACTGTCAGACTGGACACA
TGGTGGCGGCAGAGGCAGCTGGACCCCAGGACAGTGCAGCTGTTCTGGAAGCCAGTGCCC
CTGGAGGAAGACAGCGGACGGATCCAAGGTTATGTGGTTTCTTGGAGACCCTCAGGCCAG
GCTGGGGCCATCCTGCCCCTCTGCAACACCACAGAGCTCAGCTGCACCTTCCACCTGCCT
TCAGAAGCCCAGGAGGTGGCCCTTGTGGCCTATAACTCAGCCGGGACCTCTCGCCCCACC
CCGGTGGTCTTCTCAGAAAGCAGAGGCCCAGCTCTGACCAGACTCCATGCCATGGCCCGA
GACCCTCACAGCCTCTGGGTAGGCTGGGAGCCCCCCAATCCATGGCCTCAGGGCTATGTG
ATTGAGTGGGGCCTGGGCCCCCCCAGCGCGAGCAATAGCAACAAGACCTGGAGGATGGAA
CAGAATGGGAGAGCCACGGGGTTTCTGCTGAAGGAGAACATCAGGCCCTTTCAGCTCTAT
GAGATCATCGTGACTCCCTTGTACCAGGACACCATGGGACCCTCCCAGCATGTCTATGCC
TACTCTCAAGAAATGGCTCCCTCCCATGCCCCAGAGCTGCATCTAAAGCACATTGGCAAG
ACCTGGGCACAGCTGGAGTGGGTGCCTGAGCCCCCTGAGCTGGGGAAGAGCCCCCTTACC
CACTACACCATCTTCTGGACCAACGCTCAGAACCAGTCCTTCTCCGCCATCCTGAATGCC
TCCTCCCGTGGCTTTGTCCTCCATGGCCTGGAGCCCGCCAGTCTGTATCACATCCACCTC
ATGGCTGCCAGCCAGGCTGGGGCCACCAACAGTACAGTCCTCACCCTGATGACCTTGACC
CCAGAGGGGTCGGAGCTACACATCATCCTGGGCCTGTTCGGCCTCCTGCTGTTGCTCACC
TGCCTCTGTGGAACTGCCTGGCTCTGTTGCAGCCCCAACAGGAAGAATCCCCTCTGGCCA
AGTGTCCCAGACCCAGCTCACAGCAGCCTGGGCTCCTGGGTGCCCACAATCATGGAGGAG
GATGCCTTCCAGCTGCCCGGCCTTGGCACGCCACCCATCACCAAGCTCACAGTGCTGGAG
GAGGATGAAAAGAAGCCGGTGCCCTGGGAGTCCCATAACAGCTCAGAGACCTGTGGCCTC
CCCACTCTGGTCCAGACCTATGTGCTCCAGGGGGACCCAAGAGCAGTTTCCACCCAGCCC
CAATCCCAGTCTGGCACCAGCGATCAGGTCCTTTATGGGCAGCTGCTGGGCAGCCCCACA
AGCCCAGGGCCAGGGCACTATCTCCGCTGTGACTCCACTCAGCCCCTCTTGGCGGGCCTC
ACCCCCAGCCCCAAGTCCTATGAGAACCTCTGGTTCCAGGCCAGCCCCTTGGGGACCCTG
GTAACCCCAGCCCCAAGCCAGGAGGACGACTGTGTCTTTGGGCCACTGCTCAACTTCCCC
CTCCTGCAGGGGATCCGGGTCCATGGGATGGAGGCGCTGGGGAGCTTCTAG
Target 2 GenBank Gene ID
Target 2 GeneCard ID CSF3R Link Image
Target 2 GenAtlas ID CSF3R Link Image
Target 2 HGNC ID HGNC:2439 Link Image
Target 2 Chromosome Location 1
Target 2 Locus 1p35-p34.3
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Seto Y, Fukunaga R, Nagata S: Chromosomal gene organization of the human granulocyte colony-stimulating factor receptor. J Immunol. 1992 Jan 1;148(1):259-66. [PubMed Link Image]
  2. Fukunaga R, Seto Y, Mizushima S, Nagata S: Three different mRNAs encoding human granulocyte colony-stimulating factor receptor. Proc Natl Acad Sci U S A. 1990 Nov;87(22):8702-6. [PubMed Link Image]
  3. Fukunaga R, Ishizaka-Ikeda E, Pan CX, Seto Y, Nagata S: Functional domains of the granulocyte colony-stimulating factor receptor. EMBO J. 1991 Oct;10(10):2855-65. [PubMed Link Image]
  4. Larsen A, Davis T, Curtis BM, Gimpel S, Sims JE, Cosman D, Park L, Sorensen E, March CJ, Smith CA: Expression cloning of a human granulocyte colony-stimulating factor receptor: a structural mosaic of hematopoietin receptor, immunoglobulin, and fibronectin domains. J Exp Med. 1990 Dec 1;172(6):1559-70. [PubMed Link Image]
  5. Dong F, Hoefsloot LH, Schelen AM, Broeders CA, Meijer Y, Veerman AJ, Touw IP, Lowenberg B: Identification of a nonsense mutation in the granulocyte-colony-stimulating factor receptor in severe congenital neutropenia. Proc Natl Acad Sci U S A. 1994 May 10;91(10):4480-4. [PubMed Link Image]
  6. Haniu M, Horan T, Arakawa T, Le J, Katta V, Rohde MF: Extracellular domain of granulocyte-colony stimulating factor receptor. Interaction with its ligand and identification of a domain in close proximity of ligand-binding region. Arch Biochem Biophys. 1995 Dec 20;324(2):344-56. [PubMed Link Image]
  7. Yamasaki K, Naito S, Anaguchi H, Ohkubo T, Ota Y: Solution structure of an extracellular domain containing the WSxWS motif of the granulocyte colony-stimulating factor receptor and its interaction with ligand. Nat Struct Biol. 1997 Jun;4(6):498-504. [PubMed Link Image]
  8. Layton JE, Iaria J, Smith DK, Treutlein HR: Identification of a ligand-binding site on the granulocyte colony-stimulating factor receptor by molecular modeling and mutagenesis. J Biol Chem. 1997 Nov 21;272(47):29735-41. [PubMed Link Image]
Target 2 Drug References
  1. Elsasser A, Franzen M, Kohlmann A, Weisser M, Schnittger S, Schoch C, Reddy VA, Burel S, Zhang DE, Ueffing M, Tenen DG, Hiddemann W, Behre G: The fusion protein AML1-ETO in acute myeloid leukemia with translocation t(8;21) induces c-jun protein expression via the proximal AP-1 site of the c-jun promoter in an indirect, JNK-dependent manner. Oncogene. 2003 Aug 28;22(36):5646-57. [PubMed Link Image]
  2. Cao YR, Shao ZH, Liu H, Shi J, Bai J, Tu MF, Wang HQ, Xing LM, Cui ZZ, Sun J, Jia HR, Yang TY: [The response of bone marrow hematopoietic cells to G-CSF in paroxysmal nocturnal hemoglobinuria patients] Zhonghua Xue Ye Xue Za Zhi. 2005 Apr;26(4):235-8. [PubMed Link Image]
  3. Zhuang D, Qiu Y, Haque SJ, Dong F: Tyrosine 729 of the G-CSF receptor controls the duration of receptor signaling: involvement of SOCS3 and SOCS1. J Leukoc Biol. 2005 Oct;78(4):1008-15. Epub 2005 Jul 20. [PubMed Link Image]
  4. Erkeland SJ, Aarts LH, Irandoust M, Roovers O, Klomp A, Valkhof M, Gits J, Eyckerman S, Tavernier J, Touw IP: Novel role of WD40 and SOCS box protein-2 in steady-state distribution of granulocyte colony-stimulating factor receptor and G-CSF-controlled proliferation and differentiation signaling. Oncogene. 2007 Mar 29;26(14):1985-94. Epub 2006 Sep 25. [PubMed Link Image]
  5. Ward AC: The role of the granulocyte colony-stimulating factor receptor (G-CSF-R) in disease. Front Biosci. 2007 Jan 1;12:608-18. [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.