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Showing drug card for Primaquine (DB01087)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-06-23 18:07:20
Primary Accession Number DB01087
Secondary Accession Number
  • APRD00604
Name Primaquine
Drug Type
  • Approved
  • Small Molecule
Description An aminoquinoline that is given by mouth to produce a radical cure and prevent relapse of vivax and ovale malarias following treatment with a blood schizontocide. It has also been used to prevent transmission of falciparum malaria by those returning to areas where there is a potential for re-introduction of malaria. Adverse effects include anemias and GI disturbances. (From Martindale, The Extra Pharmacopeia, 30th ed, p404)
Synonyms Not Available
Brand Names
  1. Neo-Quipenyl
  2. Primachin
Brand Mixtures Not Available
Chemical IUPAC Name N-(6-methoxyquinolin-8-yl)pentane-1,4-diamine
Chemical Formula C15H21N3O
Chemical Structure Structure
CAS Registry Number 90-34-6
InChI Identifier InChI=1/C15H21N3O/c1-11(5-3-7-16)18-14-10-13(19-2)9-12-6-4-8-17-15(12)14/h4,6,8-11,18H,3,5,7,16H2,1-2H3
InChI Key INDBQLZJXZLFIT-UHFFFAOYAU
KEGG Drug Not Available
KEGG Compound C07627 Link Image
PubChem Compound 4908 Link Image
PubChem Substance 9829 Link Image
ChEBI ID Not Available
PharmGKB ID Not Available
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 02017776 Link Image
RxList Link Not Available
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Primaquine Link Image
FDA Label
Material Safety Data Sheet (MSDS) Not Available
Synthesis Reference Not Available
Average Molecular Weight 259.3467
Monoisotopic Molecular Weight 259.1685
State Solid
Melting Point < 25 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 5.64e-02 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 2.1 Source: PhysProp
Predicted LogP 2.77 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -3.66 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 1Y01 Link Image
Experimental PDB File Show
Experimental PDB Structure
Isomeric SMILES COC1=CC(N[C@H](C)CCCN)=C2N=CC=CC2=C1
Canonical SMILES COC1=CC(NC(C)CCCN)=C2N=CC=CC2=C1
Drug Category
  • Antimalarial Agents
  • Antimalarials
  • Antiprotozoal Agents
ATC Codes
AHFS Codes
  • 08:30.08
Indication For the treatment of malaria.
Pharmacology Primaquine is an antimalarial agent and is the essential co-drug with chloroquine in treating all cases of malaria. In the blood, malaria parasites break down a part of the red blood cells known as haemoglobin. When this happens haemoglobin is divided into two parts; haem and globin. Haem is toxic to the malaria parasite. To prevent it from being damaged, the malaria parasite produces an chemical which converts the toxic haem into a non-toxic product. Primaquine acts by interfering with a part of the parasite (mitochondria) that is responsible for supplying it with energy. Without energy the parasite dies. This stops the infection from continuing and allows the person to recover. Primaquine kills the intrahepatic form of Plasmodium vivax and Plasmodium ovale, and thereby prevents the development of the erythrocytic forms that are responsible for relapses (it also kills gametocytes). Primaquine is not used in the prevention of malaria, only in the treatment. It has insignificant activity against the asexual blood forms of the parasite and therefore it is always used in conjunction with a blood schizonticide and never as a single agent. Primaquine has gametocytocidal activity against all plasmodia, including P. falciparum.
Mechanism of Action Primaquine's mechanism of action is not well understood. It may be acting by generating reactive oxygen species or by interfering with the electron transport in the parasite.
Absorption Not Available
Toxicity Not Available
Protein Binding Not Available
Biotransformation Not Available
Half Life 3.7-7.4 hours
Dosage Forms
Form Route
Tablet Oral
Patient Information Not Available
Contraindications Not Available
Interactions Not Available
Drug Interactions
Drug Interaction
Atomoxetine The CYP2D6 inhibitor could increases the effect and toxicity of atomoxetine
Food Interactions
  • Take with food to decrease dyspepsia.
Pathways Not Available
General References
  1. ALVING AS, ARNOLD J, HOCKWALD RS, CLAYMAN CB, DERN RJ, BEUTLER E, FLANAGAN CL: Potentiation of the curative action of primaquine in vivax malaria by quinine and chloroquine. J Lab Clin Med. 1955 Aug;46(2):301-6. [PubMed Link Image]
  2. Hill DR, Baird JK, Parise ME, Lewis LS, Ryan ET, Magill AJ: Primaquine: report from CDC expert meeting on malaria chemoprophylaxis I. Am J Trop Med Hyg. 2006 Sep;75(3):402-15. [PubMed Link Image]
  3. Mihaly GW, Ward SA, Edwards G, Nicholl DD, Orme ML, Breckenridge AM: Pharmacokinetics of primaquine in man. I. Studies of the absolute bioavailability and effects of dose size. Br J Clin Pharmacol. 1985 Jun;19(6):745-50. [PubMed Link Image]
  4. Cohen RJ, Sachs JR, Wicker DJ, Conrad ME: Methemoglobinemia provoked by malarial chemoprophylaxis in Vietnam. N Engl J Med. 1968 Nov 21;279(21):1127-31. [PubMed Link Image]
  5. Coleman MD, Coleman NA: Drug-induced methaemoglobinaemia. Treatment issues. Drug Saf. 1996 Jun;14(6):394-405. [PubMed Link Image]
  6. Drugs.com Link Image
  7. Wikipedia Link Image
Organisms Affected
  • Plasmodium
Phase 1 Metabolizing Enzymes
  1. Cytochrome P450 1A1 (CYP1A1)
Targets
  1. Hemoglobin subunit alpha
Phase 1 Metabolizing Enzyme 1 [top]
Enzyme 1 Name Cytochrome P450 1A1 (CYP1A1)
Enzyme 1 Gene Name CYP1A1
Enzyme 1 SwissProt ID P04798 Link Image
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 Protein Sequence >sp|P04798|CP1A1_HUMAN Cytochrome P450 1A1 (EC 1.14.14.1) 
MLFPISMSATEFLLASVIFCLVFWVIRASRPQVPKGLKNPPGPWGWPLIGHMLTLGKNPH
LALSRMSQQYGDVLQIRIGSTPVVVLSGLDTIRQALVRQGDDFKGRPDLYTFTLISNGQS
MSFSPDSGPVWAARRRLAQNGLKSFSIASDPASSTSCYLEEHVSKEAEVLISTLQELMAG
PGHFNPYRYVVVSVTNVICAICFGRRYDHNHQELLSLVNLNNNFGEVVGSGNPADFIPIL
RYLPNPSLNAFKDLNEKFYSFMQKMVKEHYKTFEKGHIRDITDSLIEHCQEKQLDENANV
QLSDEKIINIVLDLFGAGFDTVTTAISWSLMYLVMNPRVQRKIQEELDTVIGRSRRPRLS
DRSHLPYMEAFILETFRHSSFVPFTIPHSTTRDTSLKGFYIPKGRCVFVNQWQINHDQKL
WVNPSEFLPERFLTPDGAIDKVLSEKVIIFGMGKRKCIGETIARWEVFLFLAILLQRVEF
SVPLGVKVDMTPIYGLTMKHACCEHFQMQLRS
Drug Target 1 [top]
Target 1 ID 144
Target 1 Name Hemoglobin subunit alpha
Target 1 Synonyms
  1. Alpha-globin
  2. Hemoglobin alpha chain
Target 1 Gene Name HBA1
Target 1 Protein Sequence >Hemoglobin subunit alpha 
VLSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFPHFDLSHGSAQVKGHGK
KVADALTNAVAHVDDMPNALSALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPA
VHASLDKFLASVSTVLTSKYR
Target 1 Number of Residues 143
Target 1 Molecular Weight 15126
Target 1 Theoretical pI 9.09
Target 1 GO Classification
Function
tetrapyrrole binding
heme binding
binding
oxygen binding
Process
physiological process
cellular physiological process
transport
gas transport
oxygen transport
Component
protein complex
hemoglobin complex
Target 1 General Function Involved in iron ion binding
Target 1 Specific Function Involved in oxygen transport from the lung to the various peripheral tissues
Target 1 Pathways Not Available
Target 1 Reactions Not Available
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 386764 Link Image
Target 1 UniProtKB/Swiss-Prot ID P69905 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name HBA_HUMAN Link Image
Target 1 PDB ID 1Y01 Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location Not Available
Target 1 Gene Sequence >429 bp 
ATGGTGCTGTCTCCTGCCGACAAGACCAACGTCAAGGCCGCCTGGGGTAAGGTCGGCGCG
CACGCTGGCGAGTATGGTGCGGAGGCCCTGGAGAGGATGTTCCTGTCCTTCCCCACCACC
AAGACCTACTTCCCGCACTTCGACCTGAGCCACGGCTCTGCCCAGGTTAAGGGCCACGGC
AAGAAGGTGGCCGACGCCCTGACCAACGCCGTGGCGCACGTGGACGACATGCCCAACGCG
CTGTCCGCCCTGAGCGACCTGCACGCGCACAAGCTTCGGGTGGACCCGGTCAACTTCAAG
CTCCTAAGCCACTGCCTGCTGGTGACCCTGGCCGCCCACCTCCCCGCCGAGTTCACCCCT
GCGGTGCACGCCTCCCTGGACAAGTTCCTGGCTTCTGTGAGCACCGTGCTGACCTCCAAA
TACCGTTAA
Target 1 GenBank Gene ID
Target 1 GeneCard ID HBA1 Link Image
Target 1 GenAtlas ID HBA1 Link Image
Target 1 HGNC ID HGNC:4823 Link Image
Target 1 Chromosome Location 16
Target 1 Locus 16p13.3
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed Link Image]
  2. Brimhall B, Jones RT, Schneider RG, Hosty TS, Tomlin G, Atkins R: Two new hemoglobins. Hemoglobin Alabama (beta39(C5)Gln leads to Lys) and hemoglobin Montgomery (alpha 48(CD 6) Leu leads to Arg). Biochim Biophys Acta. 1975 Jan 30;379(1):28-32. [PubMed Link Image]
  3. Zhao Y, Zhong M, Liu Z, Xu X: [Rapid detection of the common alpha-thalassemia-2 determinants by PCR assay] Zhonghua Yi Xue Yi Chuan Xue Za Zhi. 2001 Jun;18(3):216-8. [PubMed Link Image]
  4. Zhao Y, Xu X: Alpha2(CD31 AGG-->AAG, Arg-->Lys) causing non-deletional alpha-thalassemia in a Chinese family with HbH disease. Haematologica. 2001 May;86(5):541-2. [PubMed Link Image]
  5. Fermi G: Three-dimensional fourier synthesis of human deoxyhaemoglobin at 2-5 A resolution: refinement of the atomic model. J Mol Biol. 1975 Sep 15;97(2):237-56. [PubMed Link Image]
  6. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  7. Abbes S, M'Rad A, Fitzgerald PA, Dormer P, Blouquit Y, Kister J, Galacteros F, Wajcman H: HB Al-Ain Abu Dhabi [alpha 18(A16)Gly----Asp]: a new hemoglobin variant discovered in an Emiratee family. Hemoglobin. 1992;16(5):355-62. [PubMed Link Image]
  8. Fujisawa K, Hattori Y, Ohba Y, Ando S: Hb Yuda or alpha 130(H13)Ala----Asp; a new alpha chain variant with low oxygen affinity. Hemoglobin. 1992;16(5):435-9. [PubMed Link Image]
  9. Wajcman H, Blouquit Y, Vasseur C, Le Querrec A, Laniece M, Melevendi C, Rasore A, Galacteros F: Two new human hemoglobin variants caused by unusual mutational events: Hb Zaire contains a five residue repetition within the alpha-chain and Hb Duino has two residues substituted in the beta-chain. Hum Genet. 1992 Aug;89(6):676-80. [PubMed Link Image]
  10. Silva MM, Rogers PH, Arnone A: A third quaternary structure of human hemoglobin A at 1.7-A resolution. J Biol Chem. 1992 Aug 25;267(24):17248-56. [PubMed Link Image]
  11. 1618774 Vasseur C, Blouquit Y, Kister J, Prome D, Kavanaugh JS, Rogers PH, Guillemin C, Arnone A, Galacteros F, Poyart C, et al.: Hemoglobin Thionville. An alpha-chain variant with a substitution of a glutamate for valine at NA-1 and having an acetylated methionine NH2 terminus. J Biol Chem. 1992 Jun 25;267(18):12682-91.
  12. 1634355 Miyashita H, Hashimoto K, Mohri H, Ohokubo T, Harano T, Harano K, Imai K: Hb Kanagawa [alpha 40(C5)Lys----Met]: a new alpha chain variant with an increased oxygen affinity. Hemoglobin. 1992;16(1-2):1-10.
  13. 1634357 Langdown JV, Davidson RJ, Williamson D: A new alpha chain variant, Hb Turriff [alpha 99(G6)Lys----Glu]: the interference of abnormal hemoglobins in Hb A1c determination. Hemoglobin. 1992;16(1-2):11-7.
  14. 1634363 Orisaka M, Tajima T, Harano T, Harano K, Kushida Y, Imai K: A new alpha chain variant, Hb Hanamaki or alpha 2(139)(HC1)Lys----Glu beta 2, found in a Japanese family. Hemoglobin. 1992;16(1-2):67-71.
  15. 1686260 Jiang NH, Liang S, Wen XJ, Liang R, Su C, Tang Z: Hb Westmead: an alpha 2-globin gene mutation detected by polymerase chain reaction and Stu I cleavage. Hemoglobin. 1991;15(4):291-5.
  16. 1802882 Zwerdling T, Williams S, Nasr SA, Rucknagel DL: Hb Port Huron [alpha 56 (E5)Lys----ARG]: a new alpha chain variant. Hemoglobin. 1991;15(5):381-91.
  17. 2079430 Harkness M, Harkness DR, Kutlar F, Kutlar A, Wilson JB, Webber BB, Codrington JF, Huisman TH: Hb Sun Prairie or alpha(2)130(H13)Ala----Pro beta 2, a new unstable variant occurring in low quantities. Hemoglobin. 1990;14(5):479-89.
  18. 2101836 Wilson JB, Webber BB, Plaseska D, de Alarcon PA, McMillan SK, Huisman TH: Hb Davenport or alpha 2(78)(EF7)Asn----His beta 2. Hemoglobin. 1990;14(6):599-605.
  19. 2606724 Wilson JB, Webber BB, Kutlar A, Reese AL, McKie VC, Lutcher CL, Felice AE, Huisman TH: Hb Evans or alpha 262(E11)Val----Met beta 2; an unstable hemoglobin causing a mild hemolytic anemia. Hemoglobin. 1989;13(6):557-66.
  20. 2752146 Cash FE, Monplaisir N, Goossens M, Liebhaber SA: Locus assignment of two alpha-globin structural mutants from the Caribbean basin: alpha Fort de France (alpha 45 Arg) and alpha Spanish Town (alpha 27 Val). Blood. 1989 Aug 1;74(2):833-5.
  21. 3654264 Fleming PJ, Sumner DR, Wyatt K, Hughes WG, Melrose WD, Jupe DM, Baikie MJ: Hemoglobin Hobart or alpha 20(Bl)His----Arg: a new alpha chain hemoglobin variant. Hemoglobin. 1987;11(3):211-20.
  22. 3754246 Como PF, Barber S, Sage RE, Trent RJ, Kronenberg H: Hemoglobin Woodville: alpha (2)6(A4) aspartic acid----tyrosine. Hemoglobin. 1986;10(2):135-41.
  23. 4212045 Reed RE, Winter WP, Rucknagel DL: Haemoglobin inkster (alpha2 85aspartic acid leads to valine beta2) coexisting with beta-thalassaemia in a Caucasian family. Br J Haematol. 1974 Mar;26(3):475-84.
  24. 4528583 Huisman TH, Wilson JB, Gravely M, Hubbard M: Hemoglobin Grady: the first example of a variant with elongated chains due to an insertion of residues. Proc Natl Acad Sci U S A. 1974 Aug;71(8):3270-3.
  25. 4744335 Sumida I, Ota Y, Imamura T, Yanase T: Hemoglobin Sawara: alpha 6(A4) aspartic acid leads to alanine. Biochim Biophys Acta. 1973 Sep 21;322(1):23-6.
  26. 478977 Sanguansermsri T, Matragoon S, Changloah L, Flatz G: Hemoglobin Suan-Dok (alpha 2 109 (G16) Leu replaced by Arg beta 2): an unstable variant associated with alpha-thalassemia. Hemoglobin. 1979;3(2-3):161-74.
  27. 5115619 Fujiwara N, Maekawa T, Matsuda G: Hemoglobin Atago (alpha2-85Tyr beta-2) a new abnormal human hemoglobin found in Nagasaki. Biochemical studies on hemoglobins and myoglobins. VI. Int J Protein Res. 1971;3(1):35-9.
  28. 5780195 Charache S, Mondzac AM, Gessner U: Hemoglobin Hasharon (alpha-2-47 his(CD5)beta-2): a hemoglobin found in low concentration. J Clin Invest. 1969 May;48(5):834-47.
  29. 6244294 Wilson JT, Wilson LB, Reddy VB, Cavallesco C, Ghosh PK, deRiel JK, Forget BG, Weissman SM: Nucleotide sequence of the coding portion of human alpha globin messenger RNA. J Biol Chem. 1980 Apr 10;255(7):2807-15.
  30. 6452630 Liebhaber SA, Goossens MJ, Kan YW: Cloning and complete nucleotide sequence of human 5'-alpha-globin gene. Proc Natl Acad Sci U S A. 1980 Dec;77(12):7054-8.
  31. 6526652 Zeng YT, Huang SZ, Qiu XK, Cheng GC, Ren ZR, Jin QC, Chen CY, Jiao CT, Tang ZG, Liu RH, et al.: Hemoglobin Chongqing [alpha 2(NA2)Leu----Arg] and hemoglobin Harbin [alpha 16(A14)Lys----Met] found in China. Hemoglobin. 1984;8(6):569-81.
  32. 6815131 Harano T, Harano K, Shibata S, Ueda S, Imai K, Seki M: HB Handa [alpha 90 (FG 2) Lys replaced by Met]: structure and biosynthesis of a new slightly higher oxygen affinity variant. Hemoglobin. 1982;6(4):379-89.
  33. 7161109 Zeng YT, Huang SZ, Zhou XD, Qiu XK, Dong QY, Li MY, Bai JH: Hb Shenyang (alpha 26 (B7) Ala replaced by Glu): a new unstable variant found in China. Hemoglobin. 1982;6(6):625-8.
  34. 7448866 Michelson AM, Orkin SH: The 3' untranslated regions of the duplicated human alpha-globin genes are unexpectedly divergent. Cell. 1980 Nov;22(2 Pt 2):371-7.
  35. 7470621 Honig GR, Shamsuddin M, Zaizov R, Steinherz M, Solar I, Kirschmann C: Hemoglobin Petah Tikva (alpha 110 ala replaced by asp): a new unstable variant with alpha-thalassemia-like expression. Blood. 1981 Apr;57(4):705-11.
  36. 7558876 Harano T, Harano K, Imai K, Murakami T, Matsubara H: Hb Kurosaki [alpha 7(A5)Lys-->Glu]: a new alpha chain variant found in a Japanese woman. Hemoglobin. 1995 May-Jul;19(3-4):197-201.
  37. 7713747 Yalcin A, Avcu F, Beyan C, Gurgey A, Ural AU: A case of HB J-Meerut (or Hb J-Birmingham) [alpha 120(H3)Ala-->Glu] Hemoglobin. 1994 Nov;18(6):433-5.
  38. 7786798 Darbellay R, Mach-Pascual S, Rose K, Graf J, Beris P: Haemoglobin Tunis-Bizerte: a new alpha 1 globin 129 Leu-->Pro unstable variant with thalassaemic phenotype. Br J Haematol. 1995 May;90(1):71-6.
  39. 8195005 Giordano PC, Harteveld CL, Streng H, Oosterwijk JC, Heister JG, Amons R, Bernini LF: Hb Kurdistan [alpha 47(CE5)Asp-->Tyr], a new alpha chain variant in combination with beta (0)-thalassemia. Hemoglobin. 1994 Jan;18(1):11-8.
  40. 8294199 Wajcman H, Kalmes G, Groff P, Prome D, Riou J, Galacteros F: Hb Melusine [alpha 114(GH2)Pro-->Ser]: a new neutral hemoglobin variant. Hemoglobin. 1993 Oct;17(5):397-405.
  41. 8294200 Wajcman H, Kister J, M'Rad A, Marden MC, Riou J, Galacteros F: Hb Val de Marne [alpha 133(H16)Ser-->Arg]: a new hemoglobin variant with moderate increase in oxygen affinity. Hemoglobin. 1993 Oct;17(5):407-17.
  42. 8448109 Kavanaugh JS, Moo-Penn WF, Arnone A: Accommodation of insertions in helices: the mutation in hemoglobin Catonsville (Pro 37 alpha-Glu-Thr 38 alpha) generates a 3(10)-->alpha bulge. Biochemistry. 1993 Mar 16;32(10):2509-13.
  43. 8745434 Harano T, Harano K, Imai K, Terunuma S: HB Swan River [alpha 6(A4)ASP-->Gly] observed in a Japanese man. Hemoglobin. 1996 Feb;20(1):75-8.
  44. 9322075 Brennan SO, Matthews JR: Hb Auckland [alpha 87(F8) His-->Asn]: a new mutation of the proximal histidine identified by electrospray mass spectrometry. Hemoglobin. 1997 Sep;21(5):393-403.
  45. 9452028 Wajcman H, Prehu MO, Prehu C, Blouquit Y, Prome D, Galacteros F: Hemoglobin Phnom Penh [alpha117Phe(H1)-Ile-alpha118Thr(H2)]; evidence for a hotspot for insertion of residues in the third exon of the alpha1-globin gene. Hum Mutat. 1998;Suppl 1:S20-2.
  46. 9494044 Wajcman H, Kister J, Riou J, Galacteros F, Girot R, Maier-Redelsperger M, Nayudu NV, Giordano PC: Hb Godavari [alpha 95(G2)Pro-->Thr]: a neutral amino acid substitution in the alpha 1 beta 2 interface that modifies the electrophoretic mobility of hemoglobin. Hemoglobin. 1998 Jan;22(1):11-22.
  47. 9665850 Sutherland-Smith AJ, Baker HM, Hofmann OM, Brittain T, Baker EN: Crystal structure of a human embryonic haemoglobin: the carbonmonoxy form of gower II (alpha2 epsilon2) haemoglobin at 2.9 A resolution. J Mol Biol. 1998 Jul 17;280(3):475-84.
Target 1 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [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.