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Showing drug card for Ethionamide (DB00609)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-06-23 18:07:50
Primary Accession Number DB00609
Secondary Accession Number
  • APRD00961
Name Ethionamide
Drug Type
  • Approved
  • Small Molecule
Description A second-line antitubercular agent that inhibits mycolic acid synthesis. It also may be used for treatment of leprosy. (From Smith and Reynard, Textbook of Pharmacology, 1992, p868)
Synonyms
  1. ET
  2. ETH
  3. ETP
  4. Ethinamide
  5. Ethionamid prothionamid
  6. Ethionamidum [INN-Latin]
  7. Ethioniamide
  8. Ethylisothiamide
  9. Ethyonomide
  10. Etionamid
  11. Etionamida [INN-Spanish]
  12. Etionamide [DCIT]
  13. Etioniamid
Brand Names
  1. Aethionamidum
  2. Aetina
  3. Aetiva
  4. Amidazin
  5. Amidazine
  6. Atina
  7. Bayer 5312
  8. Ethimide
  9. Ethina
  10. Etimid
  11. Etiocidan
  12. Etionid
  13. Etionizin
  14. Etionizina
  15. Etionizine
  16. Fatoliamid
  17. Iridocin
  18. Iridozin
  19. Isothin
  20. Isotiamida
  21. Itiocide
  22. Nicotion
  23. Nisotin
  24. Nizotin
  25. Rigenicid
  26. Sertinon
  27. Teberus
  28. Thianid
  29. Thianide
  30. Thioamide
  31. Thiomid
  32. Thioniden
  33. Tianid
  34. Tio-Mid
  35. Tiomid
  36. Trecator
  37. Trecator-SC
  38. Trekator
  39. Trescatyl
  40. Trescazide
  41. Tubenamide
  42. Tubermin
  43. Tuberoid
  44. Tuberoson
Brand Mixtures Not Available
Chemical IUPAC Name 2-ethylpyridine-4-carbothioamide
Chemical Formula C8H10N2S
Chemical Structure Structure
CAS Registry Number 536-33-4
InChI Identifier InChI=1/C8H10N2S/c1-2-7-5-6(8(9)11)3-4-10-7/h3-5H,2H2,1H3,(H2,9,11)/f/h9H2
InChI Key AEOCXXJPGCBFJA-JSGPKCTECX
KEGG Drug D00591 Link Image
KEGG Compound C07665 Link Image
PubChem Compound 2761171 Link Image
PubChem Substance 9867 Link Image
ChEBI ID Not Available
PharmGKB ID PA449528 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] Not Available
RxList Link http://www.rxlist.com/cgi/generic2/ethionamide.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Ethionamide Link Image
FDA Label
Material Safety Data Sheet (MSDS)
Synthesis Reference Not Available
Average Molecular Weight 166.2430
Monoisotopic Molecular Weight 166.0565
State Solid
Melting Point 163 oC
Experimental Water Solubility Practically insoluble Source: PhysProp
Predicted Water Solubility 8.39e-01 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity 0.5 Source: PhysProp
Predicted LogP 1.88 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -2.30 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 CCC1=NC=CC(=C1)C(N)=S
Canonical SMILES CCC1=NC=CC(=C1)C(N)=S
Drug Category
  • Antitubercular Agents
  • Fatty Acid Synthesis Inhibitors
  • Leprostatic Agents
ATC Codes
AHFS Codes Not Available
Indication For use in the treatment of pulmonary and extrapulmonary tuberculosis when other antitubercular drugs have failed.
Pharmacology Ethinamate is bacteriostatic against M. tuberculosis. In a study examining ethionamide resistance, ethionamide administered orally initially decreased the number of culturable Mycobacterium tuberculosis organisms from the lungs of H37Rv infected mice. Drug resistance developed with continued ethionamide monotherapy, but did not occur when mice received ethionamide in combination with streptomycin or isoniazid.
Mechanism of Action Ethionamide may be bacteriostatic or bactericidal in action, depending on the concentration of the drug attained at the site of infection and the susceptibility of the infecting organism. Ethionamide, like prothionamide and pyrazinamide, is a nicotinic acid derivative related to isoniazid. It is thought that ethionamide undergoes intracellular modification and acts in a similar fashion to isoniazid. Isoniazid inhibits the synthesis of mycoloic acids, an essential component of the bacterial cell wall. Specifically isoniazid inhibits InhA, the enoyl reductase from Mycobacterium tuberculosis, by forming a covalent adduct with the NAD cofactor. It is the INH-NAD adduct that acts as a slow, tight-binding competitive inhibitor of InhA.
Absorption Essentially completely absorbed following oral administration and not subjected to any appreciable first pass metabolism. Bioavailability approximately 100%.
Toxicity Symptoms of overdose include convulsions, nausea, and vomiting.
Protein Binding Approximately 30% bound to proteins.
Biotransformation Hepatic and extensive. Metabolized to the active metabolite sulfoxide, and several inactive metabolites. The sulphoxide metabolite has been demonstrated to have antimicrobial activity against Mycobacterium tuberculosis.
Half Life 2 to 3 hours
Dosage Forms
Form Route
Tablet, film coated Oral
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
  • Mycobacteria
Targets
  1. Enoyl-[acyl-carrier-protein] reductase [NADH]
  2. Peroxidase/catalase T
Drug Target 1 [top]
Target 1 ID 368
Target 1 Name Enoyl-[acyl-carrier-protein] reductase [NADH]
Target 1 Synonyms
  1. EC 1.3.1.9
  2. NADH- dependent enoyl-ACP reductase
Target 1 Gene Name inhA
Target 1 Protein Sequence >Enoyl-[acyl-carrier-protein] reductase [NADH] 
MTGLLDGKRILVSGIITDSSIAFHIARVAQEQGAQLVLTGFDRLRLIQRITDRLPAKAPL
LELDVQNEEHLASLAGRVTEAIGAGNKLDGVVHSIGFMPQTGMGINPFFDAPYADVSKGI
HISAYSYASMAKALLPIMNPGGSIVGMDFDPSRAMPAYNWMTVAKSALESVNRFVAREAG
KYGVRSNLVAAGPIRTLAMSAIVGGALGEEAGAQIQLLEEGWDQRAPIGWNMKDATPVAK
TVCALLSDWLPATTGDIIYADGGAHTQLL
Target 1 Number of Residues 273
Target 1 Molecular Weight 28528
Target 1 Theoretical pI 6.02
Target 1 GO Classification
Function
catalytic activity
oxidoreductase activity
Process
physiological process
metabolism
Component
Not Available
Target 1 General Function Lipid transport and metabolism
Target 1 Specific Function Involved in the resistance against the antituberculosis drugs isoniazid and ethionamide
Target 1 Pathways
Name SMPDB Link KEGG Link
Fatty acid biosynthesis (path 1) map00061 Link Image
Target 1 Reactions
  • acyl-[acyl-carrier-protein] + NAD+ = trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADH + H+
Target 1 Pfam Domain Function Not Available
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Essential
Target 1 GenBank ID Protein 1524230 Link Image
Target 1 UniProtKB/Swiss-Prot ID P0A5Y6 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name INHA_MYCTU Link Image
Target 1 PDB ID 1P45 Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location Not Available
Target 1 Gene Sequence >810 bp 
ATGACAGGACTGCTGGACGGCAAACGGATTCTGGTTAGCGGAATCATCACCGACTCGTCG
ATCGCGTTTCACATCGCACGGGTAGCCCAGGAGCAGGGCGCCCAGCTGGTGCTCACCGGG
TTCGACCGGCTGCGGCTGATTCAGCGCATCACCGACCGGCTGCCGGCAAAGGCCCCGCTG
CTCGAACTCGACGTGCAAAACGAGGAGCACCTGGCCAGCTTGGCCGGCCGGGTGACCGAG
GCGATCGGGGCGGGCAACAAGCTCGACGGGGTGGTGCATTCGATTGGGTTCATGCCGCAG
ACCGGGATGGGCATCAACCCGTTCTTCGACGCGCCCTACGCGGATGTGTCCAAGGGCATC
CACATCTCGGCGTATTCGTATGCTTCGATGGCCAAGGCGCTGCTGCCGATCATGAACCCC
GGAGGTTCCATCGTCGGCATGGACTTCGACCCGAGCCGGGCGATGCCGGCCTACAACTGG
ATGACGGTCGCCAAGAGCGCGTTGGAGTCGGTCAACAGGTTCGTGGCGCGCGAGGCCGGC
AAGTACGGTGTGCGTTCGAATCTCGTTGCCGCAGGCCCTATCCGGACGCTGGCGATGAGT
GCGATCGTCGGCGGTGCGCTCGGCGAGGAGGCCGGCGCCCAGATCCAGCTGCTCGAGGAG
GGCTGGGATCAGCGCGCTCCGATCGGCTGGAACATGAAGGATGCGACGCCGGTCGCCAAG
ACGGTGTGCGCGCTGCTGTCTGACTGGCTGCCGGCGACCACGGGTGACATCATCTACGCC
GACGGCGGCGCGCACACCCAATTGCTCTAG
Target 1 GenBank Gene ID
Target 1 GeneCard ID Not Available
Target 1 GenAtlas ID Not Available
Target 1 HGNC ID Not Available
Target 1 Chromosome Location Not Available
Target 1 Locus Not Available
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Rozwarski DA, Vilcheze C, Sugantino M, Bittman R, Sacchettini JC: Crystal structure of the Mycobacterium tuberculosis enoyl-ACP reductase, InhA, in complex with NAD+ and a C16 fatty acyl substrate. J Biol Chem. 1999 May 28;274(22):15582-9. [PubMed Link Image]
  2. Fleischmann RD, Alland D, Eisen JA, Carpenter L, White O, Peterson J, DeBoy R, Dodson R, Gwinn M, Haft D, Hickey E, Kolonay JF, Nelson WC, Umayam LA, Ermolaeva M, Salzberg SL, Delcher A, Utterback T, Weidman J, Khouri H, Gill J, Mikula A, Bishai W, Jacobs Jr WR Jr, Venter JC, Fraser CM: Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains. J Bacteriol. 2002 Oct;184(19):5479-90. [PubMed Link Image]
  3. Dessen A, Quemard A, Blanchard JS, Jacobs WR Jr, Sacchettini JC: Crystal structure and function of the isoniazid target of Mycobacterium tuberculosis. Science. 1995 Mar 17;267(5204):1638-41. [PubMed Link Image]
  4. Banerjee A, Dubnau E, Quemard A, Balasubramanian V, Um KS, Wilson T, Collins D, de Lisle G, Jacobs WR Jr: inhA, a gene encoding a target for isoniazid and ethionamide in Mycobacterium tuberculosis. Science. 1994 Jan 14;263(5144):227-30. [PubMed Link Image]
  5. Rozwarski DA, Grant GA, Barton DH, Jacobs WR Jr, Sacchettini JC: Modification of the NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis. Science. 1998 Jan 2;279(5347):98-102. [PubMed Link Image]
  6. Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE 3rd, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Krogh A, McLean J, Moule S, Murphy L, Oliver K, Osborne J, Quail MA, Rajandream MA, Rogers J, Rutter S, Seeger K, Skelton J, Squares R, Squares S, Sulston JE, Taylor K, Whitehead S, Barrell BG: Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 1998 Jun 11;393(6685):537-44. [PubMed Link Image]
Target 1 Drug References
  1. Larsen MH, Vilcheze C, Kremer L, Besra GS, Parsons L, Salfinger M, Heifets L, Hazbon MH, Alland D, Sacchettini JC, Jacobs WR Jr: Overexpression of inhA, but not kasA, confers resistance to isoniazid and ethionamide in Mycobacterium smegmatis, M. bovis BCG and M. tuberculosis. Mol Microbiol. 2002 Oct;46(2):453-66. [PubMed Link Image]
  2. Morlock GP, Metchock B, Sikes D, Crawford JT, Cooksey RC: ethA, inhA, and katG loci of ethionamide-resistant clinical Mycobacterium tuberculosis isolates. Antimicrob Agents Chemother. 2003 Dec;47(12):3799-805. [PubMed Link Image]
  3. 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]
  4. 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]
  5. Banerjee A, Dubnau E, Quemard A, Balasubramanian V, Um KS, Wilson T, Collins D, de Lisle G, Jacobs WR Jr: inhA, a gene encoding a target for isoniazid and ethionamide in Mycobacterium tuberculosis. Science. 1994 Jan 14;263(5144):227-30. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 518
Target 2 Name Peroxidase/catalase T
Target 2 Synonyms
  1. Catalase-peroxidase T
  2. EC 1.11.1.6
Target 2 Gene Name katG
Target 2 Protein Sequence >Peroxidase/catalase T 
MPEQHPPITETTTGAASNGCPVVGHMKYPVEGGGNQDWWPNRLNLKVLHQNPAVADPMGA
AFDYAAEVATIDVDALTRDIEEVMTTSQPWWPADYGHYGPLFIRMAWHAAGTYRIHDGRG
GAGGGMQRFAPLNSWPDNASLDKARRLLWPVKKKYGKKLSWADLIVFAGNCALESMGFKT
FGFGFGRVDQWEPDEVYWGKEATWLGDERYSGKRDLENPLAAVQMGLIYVNPEGPNGNPD
PMAAAVDIRETFRRMAMNDVETAALIVGGHTFGKTHGAGPADLVGPEPEAAPLEQMGLGW
KSSYGTGTGKDAITSGIEVVWTNTPTKWDNSFLEILYGYEWELTKSPAGAWQYTAKDGAG
AGTIPDPFGGPGRSPTMLATDLSLRVDPIYERITRRWLEHPEELADEFAKAWYKLIHRDM
GPVARYLGPLVPKQTLLWQDPVPAVSHDLVGEAEIASLKSQIRASGLTVSQLVSTAWAAA
SSFRGSDKRGGANGGRIRLQPQVGWEVNDPDGDLRKVIRTLEEIQESFNSAAPGNIKVSF
ADLVVLGGCAAIEKAAKAAGHNITVPFTPGRTDASQEQTDVESFAVLEPKADGFRNYLGK
GNPLPAEYMLLDKANLLTLSAPEMTVLVGGLRVLGANYKRLPLGVFTEASESLTNDFFVN
LLDMGITWEPSPADDGTYQGKDGSGKVKWTGSRVDLVFGSNSELRALVEVYGADDAQPKF
VQDFVAAWDKVMNLDRFDVR
Target 2 Number of Residues 752
Target 2 Molecular Weight 80605
Target 2 Theoretical pI 4.87
Target 2 GO Classification
Function
antioxidant activity
peroxidase activity
catalase activity
Process
oxygen and reactive oxygen species metabolism
response to oxidative stress
physiological process
metabolism
cellular metabolism
generation of precursor metabolites and energy
electron transport
Component
Not Available
Target 2 General Function Inorganic ion transport and metabolism
Target 2 Specific Function Bifunctional, exhibiting both a catalase and broad- spectrum peroxidase activities. May play a role in the intracellular survival of mycobacteria
Target 2 Pathways
Name SMPDB Link KEGG Link
Methane metabolism map00680 Link Image
Tryptophan metabolism SMP00063 Link Image map00380 Link Image
Target 2 Reactions
  • 2 H2O2 = O2 + 2 H2O
Target 2 Pfam Domain Function
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • None
Target 2 Essentiality Essential
Target 2 GenBank ID Protein 581368 Link Image
Target 2 UniProtKB/Swiss-Prot ID Q08129 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name CATA_MYCTU Link Image
Target 2 PDB ID 1SJ2 Link Image
Target 2 PDB File Show
Target 2 3D Structure
Target 2 Cellular Location Not Available
Target 2 Gene Sequence >2223 bp 
GTGCCCGAGCAACACCCACCCATTACAGAAACCACCACCGGAGCCGCTAGCAACGGCTGT
CCCGTCGTGGGTCATATGAAATACCCCGTCGAGGGCGGCGGAAACCAGGACTGGTGGCCC
AACCGGCTCAATCTGAAGGTACTGCACCAAAACCCGGCCGTCGCTGACCCGATGGGTGCG
GCGTTCGACTATGCCGCGGAGGTCGCGACCATCGACGTTGACGCCCTGACGCGGGACATC
GAGGAAGTGATGACCACCTCGCAGCCGTGGTGGCCCGCCGACTACGGCCACTACGGGCCG
CTGTTTATCCGGATGGCGTGGCACGCTGCCGGCACCTACCGCATCCACGACGGCCGCGGC
GGCGCCGGGGGCGGCATGCAGCGGTTCGCGCCGCTTAACAGCTGGCCCGACAACGCCAGC
TTGGACAAGGCGCGCCGGCTGCTGTGGCCGGTCAAGAAGAAGTACGGCAAGAAGCTCTCA
TGGGCGGACCTGATTGTTTTCGCCGGCAACTGCGCGCTGGAATCGATGGGCTTCAAGACG
TTCGGGTTCGGCTTCGGCCGGGTCGACCAGTGGGAGCCCGATGAGGTCTATTGGGGCAAG
GAAGCCACCTGGCTCGGCGATGAGCGTTACAGCGGTAAGCGGGATCTGGAGAACCCGCTG
GCCGCGGTGCAGATGGGGCTGATCTACGTGAACCCGGAGGCGCCGAACGGCAACCCGGAC
CCCATGGCCGCGGCGGTCGACATTCGCGAGACGTTTCGGCGCATGGCCATGAACGACGTC
GAAACAGCGGCGCTGATCGTCGGCGGTCACACTTTCGGTAAGACCCATGGCGCCGGCCCG
GCCGATCTGGTCGGCCCCGAACCCGAGGCTGCTCCGCTGGAGCAGATGGGCTTGGGCTGG
AAGAGCTCGTATGGCACCGGAACCGGTAAGGACGCGATCACCAGCGGCATCGAGGTCGTA
TGGACGAACACCCCGACGAAATGGGACAACAGTTTCCTCGAGATCCTGTACGGCTACGAG
TGGGAGCTGACGAAGAGCCCTGCTGGCGCTTGGCAATACACCGCCAAGGACGGCGCCGGT
GCCGGCACCATCCCGGACCCGTTCGGCGGGCCAGGGCGCTCCCCGACGATGCTGGCCACT
GACCTCTCGCTGCGGGTGGATCCGATCTATGAGCGGATCACGCGTCGCTGGCTGGAACAC
CCCGAGGAATTGGCCGACGAGTTCGCCAAGGCCTGGTACAAGCTGATCCACCGAGACATG
GGTCCCGTTGCGAGATACCTTGGGCCGCTGGTCCCCAAGCAGACCCTGCTGTGGCAGGAT
CCGGTCCCTGCGGTCAGCCACGACCTCGTCGGCGAAGCCGAGATTGCCAGCCTTAAGAGC
CAGATCCGGGCATCGGGATTGACTGTCTCACAGCTAGTTTCGACCGCATGGGCGGCGGCG
TCGTCGTTCCGTGGTAGCGACAAGCGCGGCGGCGCCAACGGTGGTCGCATCCGCCTGCAG
CCACAAGTCGGGTGGGAGGTCAACGACCCCGACGGGGATCTGCGCAAGGTCATTCGCACC
CTGGAAGAGATCCAGGAGTCATTCAACTCCGCGGCGCCGGGGAACATCAAAGTGTCCTTC
GCCGACCTCGTCGTGCTCGGTGGCTGTGCCGCCATAGAGAAAGCAGCAAAGGCGGCTGGC
CACAACATCACGGTGCCCTTCACCCCGGGCCGCACGGATGCGTCGCAGGAACAAACCGAC
GTGGAATCCTTTGCCGTGCTGGAGCCCAAGGCAGATGGCTTCCGAAACTACCTCGGAAAG
GGCAACCCGTTGCCGGCCGAGTACATGCTGCTCGACAAGGCGAACCTGCTTACGCTCAGT
GCCCCTGAGATGACGGTGCTGGTAGGTGGCCTGCGCGTCCTCGGCGCAAACTACAAGCGC
TTACCGCTGGGCGTGTTCACCGAGGCCTCCGAGTCACTGACCAACGACTTCTTCGTGAAC
CTGCTCGACATGGGTATCACCTGGGAGCCCTCGCCAGCAGATGACGGGACCTACCAGGGC
AAGGATGGCAGTGGCAAGGTGAAGTGGACCGGCAGCCGCGTGGACCTGGTCTTCGGGTCC
AACTCGGAGTTGCGGGCGCTTGTCGAGGTCTATGGCGCCGATGACGCGCAGCCGAAGTTC
GTGCAGGACTTCGTCGCTGCCTGGGACAAGGTGATGAACCTCGACAGGTTCGACGTGCGC
TGA
Target 2 GenBank Gene ID
Target 2 GeneCard ID Not Available
Target 2 GenAtlas ID Not Available
Target 2 HGNC ID Not Available
Target 2 Chromosome Location Not Available
Target 2 Locus Not Available
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Fleischmann RD, Alland D, Eisen JA, Carpenter L, White O, Peterson J, DeBoy R, Dodson R, Gwinn M, Haft D, Hickey E, Kolonay JF, Nelson WC, Umayam LA, Ermolaeva M, Salzberg SL, Delcher A, Utterback T, Weidman J, Khouri H, Gill J, Mikula A, Bishai W, Jacobs Jr WR Jr, Venter JC, Fraser CM: Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains. J Bacteriol. 2002 Oct;184(19):5479-90. [PubMed Link Image]
  2. Zhang Y, Heym B, Allen B, Young D, Cole S: The catalase-peroxidase gene and isoniazid resistance of Mycobacterium tuberculosis. Nature. 1992 Aug 13;358(6387):591-3. [PubMed Link Image]
  3. Heym B, Zhang Y, Poulet S, Young D, Cole ST: Characterization of the katG gene encoding a catalase-peroxidase required for the isoniazid susceptibility of Mycobacterium tuberculosis. J Bacteriol. 1993 Jul;175(13):4255-9. [PubMed Link Image]
  4. Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE 3rd, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Krogh A, McLean J, Moule S, Murphy L, Oliver K, Osborne J, Quail MA, Rajandream MA, Rogers J, Rutter S, Seeger K, Skelton J, Squares R, Squares S, Sulston JE, Taylor K, Whitehead S, Barrell BG: Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 1998 Jun 11;393(6685):537-44. [PubMed Link Image]
Target 2 Drug References
  1. Morlock GP, Metchock B, Sikes D, Crawford JT, Cooksey RC: ethA, inhA, and katG loci of ethionamide-resistant clinical Mycobacterium tuberculosis isolates. Antimicrob Agents Chemother. 2003 Dec;47(12):3799-805. [PubMed Link Image]
  2. Lavender C, Globan M, Sievers A, Billman-Jacobe H, Fyfe J: Molecular characterization of isoniazid-resistant Mycobacterium tuberculosis isolates collected in Australia. Antimicrob Agents Chemother. 2005 Oct;49(10):4068-74. [PubMed Link Image]
  3. 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]
  4. Guo H, Seet Q, Denkin S, Parsons L, Zhang Y: Molecular characterization of isoniazid-resistant clinical isolates of Mycobacterium tuberculosis from the USA. J Med Microbiol. 2006 Nov;55(Pt 11):1527-31. [PubMed Link Image]
  5. 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.