| Version |
2.5 |
| Creation Date |
2005-06-13 13:24:05 |
| Update Date |
2009-04-16 16:48:13 |
| Primary Accession Number |
DB01045 |
| Secondary Accession Number |
|
| Name |
Rifampin |
| Drug Type |
|
| Description |
A semisynthetic antibiotic produced from Streptomyces mediterranei. It has a broad antibacterial spectrum, including activity against several forms of Mycobacterium. In susceptible organisms it inhibits DNA-dependent RNA polymerase activity by forming a stable complex with the enzyme. It thus suppresses the initiation of RNA synthesis. Rifampin is bactericidal, and acts on both intracellular and extracellular organisms. (From Gilman et al., Goodman and Gilman's The Pharmacological Basis of Therapeutics, 9th ed, p1160) |
| Synonyms |
- RFP
|
| Brand Names |
- Archidyn
- L-5103 Lepetit
- R/AMP
- RAMP
- Rfamipicin
- Rifa
- Rifadin
- Rifadin IV
- Rifadine
- Rifagen
- Rifaldazin
- Rifaldazine
- Rifaldin
- Rifampicin
- Rifampicin SV
- Rifamycin
- Rifamycin Amp
- Rifaprodin
- Rifoldin
- Rifoldine
- Riforal
- Rimactan
- Rimactane
- Rimactin
- Rimazid
- Rofact
- Tubocin
|
| Brand Mixtures |
- Rifamate (Rifampin + Isoniazid)
- Rifater (Isoniazid + Pyrazinaamide + Rifampin)
|
| Chemical IUPAC Name |
(7S,9E,11S,12S,13R,14S,15R,16S,17R,18S,26E)-2,15,17,29-tetrahydroxy-11-methoxy-3,7,12,14,16,18,22-heptamethyl-26-{[(4-methylpiperazin-1-yl)amino]methylidene}-6,23,27-trioxo-8,30-dioxa-24-azatetracyclo[23.3.1.1^{4,7}.0^{5,28}]triaconta-1(28),2,4,9,19,21,25(29)-heptaen-13-yl acetate |
| Chemical Formula |
C43H58N4O12 |
| Chemical Structure |
 |
| CAS Registry Number |
13292-46-1 |
| InChI Identifier |
InChI=1/C43H58N4O12/c1-21-12-11-13-22(2)42(55)45-33-28(20-44-47-17-15-46(9)16-18-47)37(52)30-31(38(33)53)36(51)26(6)40-32(30)41(54)43(8,59-40)57-19-14-29(56-10)23(3)39(58-27(7)48)25(5)35(50)24(4)34(21)49/h11-14,19-21,23-25,29,34-35,39,44,49-51,53H,15-18H2,1-10H3,(H,45,55)/b12-11-,19-14+,22-13+,28-20+/t21-,23-,24-,25-,29-,34+,35+,39-,43-/m0/s1/f/h45H |
| InChI Key |
FZYOVNIOYYPUPY-DSWJFXGEDI |
| KEGG Drug |
D00211  |
| KEGG Compound |
C06688  |
| PubChem Compound |
5381226  |
| PubChem Substance |
168608  |
| ChEBI ID |
28077  |
| PharmGKB ID |
PA451250  |
| HET ID |
Not Available |
| GenBank ID |
Not Available |
| Drug ID Number [DIN] |
00393444  |
| RxList Link |
http://www.rxlist.com/cgi/generic2/rifampin.htm  |
| PDRhealth Link |
Not Available |
| Wikipedia Link |
http://en.wikipedia.org/wiki/Rifampin  |
| FDA Label |
|
| Material Safety Data Sheet (MSDS) |
|
| Synthesis Reference |
Not Available |
| Average Molecular Weight |
822.9402 |
| Monoisotopic Molecular Weight |
822.4051 |
| State |
Solid |
| Melting Point |
183 oC |
| Experimental Water Solubility |
1.4 mg/mL
Source: PhysProp
|
| Predicted Water Solubility |
6.71e-02 mg/mL
Calculated using ALOGPS
|
| Experimental LogP/Hydrophobicity |
2.7
Source: PhysProp
|
| Predicted LogP |
2.36
Calculated using ALOGPS
|
| Experimental LogS |
Not Available |
| Predicted LogS |
-4.09
Calculated using ALOGPS
|
| Experimental Caco2 Permeability |
Not Available |
| pKa/Isoelectric Point |
Not Available |
| Mass Spectrum |
Not Available
|
| MOL File |
Show | Download  |
| SDF File |
Show | Download  |
| PDB File |
Show | Download  |
| 2D Structure |
|
| 3D Structure |
|
| Experimental PDB ID |
1SKX  |
| Experimental PDB File |
Show |
| Experimental PDB Structure |
|
| Isomeric SMILES |
CO[C@H]1\C=C\O[C@@]2(C)OC3=C(C2=O)C2=C(C(O)=C3C)C(O)=C(NC(=O)\C(C)=C\C=C\[C@H](C)[C@@H](O)[C@H](C)[C@@H](O)[C@H](C)[C@@H](OC(C)=O)[C@H]1C)/C(=C\NN1CCN(C)CC1)C2=O |
| Canonical SMILES |
COC1C=COC2(C)OC3=C(C2=O)C2=C(C(O)=C3C)C(O)=C(NC(=O)C(C)=CC=CC(C)C(O)C(C)C(O)C(C)C(OC(C)=O)C1C)C(=CNN1CCN(C)CC1)C2=O |
| Drug Category |
- Antibiotics
- Antibiotics, Antitubercular
- Antituberculosis Agents
- Enzyme Inhibitors
- Leprostatic Agents
- Nucleic Acid Synthesis Inhibitors
|
| ATC Codes |
|
| AHFS Codes |
|
| Indication |
For the treatment of Tuberculosis and Tuberculosis-related mycobacterial infections. |
| Pharmacology |
Rifampin is an antibiotic that inhibits DNA-dependent RNA polymerase activity in susceptible cells. Specifically, it interacts with bacterial RNA polymerase but does not inhibit the mammalian enzyme. It is bactericidal and has a very broad spectrum of activity against most gram-positive and gram-negative organisms (including Pseudomonas aeruginosa) and specifically Mycobacterium tuberculosis. Because of rapid emergence of resistant bacteria, use is restricted to treatment of mycobacterial infections and a few other indications. Rifampin is well absorbed when taken orally and is distributed widely in body tissues and fluids, including the CSF. It is metabolized in the liver and eliminated in bile and, to a much lesser extent, in urine, but dose adjustments are unnecessary with renal insufficiency. |
| Mechanism of Action |
Rifampin acts via the inhibition of DNA-dependent RNA polymerase, leading to a suppression of RNA synthesis and cell death. |
| Absorption |
Well absorbed from gastrointestinal tract. |
| Toxicity |
LD50=1570 mg/kg (rat), chronic exposure may cause nausea and vomiting and unconsciousness |
| Protein Binding |
89% |
| Biotransformation |
Primarily hepatic, rapidly deacetylated. |
| Half Life |
3.35 (+/- 0.66) hours |
| Dosage Forms |
|
| Patient Information |
Show  |
| Contraindications |
Show  |
| Interactions |
Show  |
| Drug Interactions |
| Drug |
Interaction |
| Acenocoumarol |
The rifamycin decreases the anticoagulant effect |
| Acetohexamide |
Rifampin decreases the effect of sulfonylurea |
| Alfentanil |
Rifampin reduces levels and efficacy of alfentanil |
| Aminophylline |
Rifampin decreases the effect of theophylline |
| Amiodarone |
Rifampin decreases the effect of amiodarone |
| Amitriptyline |
The rifamycin decreases the effect of tricyclics |
| Amoxapine |
The rifamycin decreases the effect of tricyclics |
| Amprenavir |
In presence of rifampin, anticipate decrease of amprenavir |
| Anisindione |
The rifamycin decreases the anticoagulant effect |
| Aprepitant |
This CYP3A4 inducer decreases the effect of aprepitant |
| Atazanavir |
Rifampin reduces levels and efficacy of atazanavir |
| Atorvastatin |
The rifamycin decreases the effect of the statin drug |
| Atovaquone |
The agent decreases the effect of atovaquone |
| Betamethasone |
The enzyme inducer decreases the effect of the corticosteroid |
| Bisoprolol |
Rifampin decreases the effect of the metabolized beta-blocker |
| Bupropion |
Rifampin reduces bupropion levels |
| Buspirone |
Rifampin decreases the effect of buspirone |
| Caspofungin |
Decreased levels/effects of caspofungin |
| Celecoxib |
Decreased levels/effect of the NSAID |
| Cerivastatin |
The rifamycin decreases the effect of the statin drug |
| Chloramphenicol |
Rifampin decreases the effect of chloramphenicol |
| Chlorpropamide |
Rifampin decreases the effect of sulfonylurea |
| Clarithromycin |
The rifamycin decreases the effect of the macrolide |
| Clomipramine |
The rifamycin decreases the effect of tricyclics |
| Clozapine |
Rifampin decreases the effect of clozapine |
| Cortisone acetate |
The enzyme inducer decreases the effect of the corticosteroid |
| Cyclosporine |
The rifamycin decreases the effect of cyclosporine |
| Dapsone |
Decreased levels of dapsone |
| Dasatinib |
Decreased levels/efficacy of dasatinib |
| Delavirdine |
Rifampin decreases the effect of delavirdine |
| Desipramine |
The rifamycin decreases the effect of tricyclics |
| Dexamethasone |
The enzyme inducer decreases the effect of the corticosteroid |
| Diazepam |
Rifampin decreases the effect of benzodiazepine |
| Diclofenac |
Decreased levels/effect of the NSAID |
| Dicumarol |
The rifamycin decreases the anticoagulant effect |
| Diltiazem |
Rifampin decreases levels of diltiazem |
| Disopyramide |
Rifampin decreases the effect of disopyramide |
| Doxepin |
The rifamycin decreases the effect of tricyclics |
| Doxycycline |
The rifamycin decreases the effect of doxycycline |
| Dyphylline |
Rifampin decreases the effect of theophylline |
| Enalapril |
Rifampin decreases the effect of enalapril |
| Erlotinib |
Decreased levels/effect of erlotinib |
| Erythromycin |
The rifamycin decreases the effect of the macrolide |
| Ethinyl Estradiol |
This product may cause a slight decrease of contraceptive effect |
| Ethotoin |
Rifampin decreases the effect of the hydantoin |
| Etoricoxib |
Rifampin reduces levels and efficacy of etoricoxib |
| Fentanyl |
Rifampin reduces levels and efficacy of alfentanil |
| Fluconazole |
Fluconazole decreases the effect of imidazole |
| Fludrocortisone |
The enzyme inducer decreases the effect of the corticosteroid |
| Fluvastatin |
The rifamycin decreases the effect of the statin drug |
| Fosamprenavir |
In presence of rifampin, anticipate decrease of amprenavir |
| Fosphenytoin |
Rifampin decreases the effect of the hydantoin |
| Gefitinib |
Rifampin reduces levels and efficacy of gefitinib |
| Glibenclamide |
Rifampin decreases the effect of sulfonylurea |
| Gliclazide |
Rifampin decreases the effect of sulfonylurea |
| Glimepiride |
Rifampin decreases the effect of sulfonylurea |
| Glipizide |
Rifampin decreases the effect of sulfonylurea |
| Glisoxepide |
Rifampin decreases the effect of sulfonylurea |
| Glycodiazine |
Rifampin decreases the effect of sulfonylurea |
| Haloperidol |
The rifamycin decreases the effect of haloperidol |
| Hydrocortisone |
The enzyme inducer decreases the effect of the corticosteroid |
| Imatinib |
Rifampin decreases levels of imatinib |
| Imipramine |
The rifamycin decreases the effect of tricyclics |
| Indinavir |
Rifampin decreases the effect of indinavir |
| Itraconazole |
Rifampin decreases the effect of the imidazole |
| Josamycin |
The rifamycin decreases the effect of the macrolide |
| Ketoconazole |
Rifampin decreases the effect of the imidazole |
| Lamotrigine |
Rifampin decreases levels of lamotrigine |
| Leflunomide |
Rifampin increases the effect of leflunomide |
| Losartan |
Rifampin decreases the effect of losartan |
| Lovastatin |
The rifamycin decreases the effect of the statin drug |
| Mefloquine |
Rifampin lowers mefloquine levels |
| Mephenytoin |
Rifampin decreases the effect of the hydantoin |
| Mestranol |
This product may cause a slight decrease of contraceptive effect |
| Methadone |
The rifamycin decreases the effect of methadone |
| Methylprednisolone |
The enzyme inducer decreases the effect of the corticosteroid |
| Metoprolol |
Rifampin decreases the effect of the metabolized beta-blocker |
| Mexiletine |
Rifampin decreases the effect of mexiletine |
| Midazolam |
Rifampin decreases the effect of benzodiazepine |
| Morphine |
Rifampin decreases the effect of morphine/codeine |
| Mycophenolate mofetil |
Significant decrease in immunosuppressant levels |
| Nelfinavir |
Rifampin decreases the effect of nelfinavir |
| Nifedipine |
Rifampin decreases the effect of the calcium channel blocker |
| Norethindrone |
This product may cause a slight decrease of contraceptive effect |
| Nortriptyline |
The rifamycin decreases the effect of tricyclics |
| Oxtriphylline |
Rifampin decreases the effect of theophylline |
| Paramethasone |
The enzyme inducer decreases the effect of the corticosteroid |
| Phenytoin |
Rifampin decreases the effect of the hydantoin |
| Praziquantel |
Significant decrease in praziquantel level |
| Prednisolone |
The enzyme inducer decreases the effect of the corticosteroid |
| Prednisone |
The enzyme inducer decreases the effect of the corticosteroid |
| Propafenone |
Rifampin decreases the effect of propafenone |
| Propranolol |
Rifampin decreases the effect of the metabolized beta-blocker |
| Protriptyline |
The rifamycin decreases the effect of tricyclics |
| Quinidine |
Rifampin decreases the effect of quinidine |
| Quinidine barbiturate |
Rifampin decreases the effect of quinidine |
| Ramelteon |
Rifampin reduces the levels/effect of ramelteon |
| Repaglinide |
Rifampin decreases the effect of repaglinide |
| Ritonavir |
Rifampin decreases the effect of ritonavir |
| Rofecoxib |
Decreased levels/effect of the NSAID |
| Rosiglitazone |
Rifampin reduces levels and efficacy of rosiglitazone |
| Saquinavir |
Rifampin decreases the effect of saquinavir |
| Simvastatin |
The rifamycin decreases the effect of the statin drug |
| Sirolimus |
The rifamycin decreases the effect of sirolimus |
| Sunitinib |
Possible decrease in sunitinib levels |
| Tacrolimus |
The rifamycin decreases the effect of tacrolimus |
| Tadalafil |
Rifampin reduces levels and efficacy of tadalafil |
| Tamoxifen |
The rifamycin decreases the effect of anti-estrogen |
| Telithromycin |
Rifampin decreases the effect of telithromycin |
| Terbinafine |
Rifampin decreases the effect of terbinafine |
| Theophylline |
Rifampin decreases the effect of theophylline |
| Tocainide |
Rifampin lowers tocainide levels/effects |
| Tolazamide |
Rifampin decreases the effect of sulfonylurea |
| Tolbutamide |
Rifampin decreases the effect of sulfonylurea |
| Toremifene |
The rifamycin decreases the effect of anti-estrogen |
| Triamcinolone |
The enzyme inducer decreases the effect of the corticosteroid |
| Triazolam |
Rifampin decreases the effect of benzodiazepine |
| Trimethoprim |
Rifampin decreases the effect of trimethoprim |
| Trimipramine |
The rifamycin decreases the effect of tricyclics |
| Verapamil |
Rifampin decreases the effect of the calcium channel blocker |
| Voriconazole |
Rifampin decreases the effect of voriconazole |
| Warfarin |
The rifamycin decreases the anticoagulant effect |
| Zaleplon |
Rifampin decreases the effect of zaleplon |
| Zidovudine |
The rifamycin decreases levels of zidovudine |
|
| Food Interactions |
- Avoid alcohol.
- Take on empty stomach: 1 hour before or 2 hours after meals.
- Take with a full glass of water.
|
| Pathways |
Not Available
|
| General References |
- Drugs.com

- Wikipedia

- RxList

|
| Organisms Affected |
- Mycobacteria
- Various gram-negative and gram-positive eubacteria
|
| Phase 1 Metabolizing Enzymes |
- Cytochrome P450 3A4 (CYP3A4)
- Cytochrome P450 1A2 (CYP1A2)
- Cytochrome P450 2C8 (CYP2C8)
- Glucuronosyltransferase
|
| Targets |
- DNA-directed RNA polymerase beta' chain
- DNA-directed RNA polymerase beta chain
- Orphan nuclear receptor PXR
- Multidrug resistance protein 1
|
|
Drug Target 1
[top]
|
| Target 1 ID |
208 |
| Target 1 Name |
DNA-directed RNA polymerase beta' chain |
| Target 1 Synonyms |
- EC 2.7.7.6
- RNA polymerase beta' subunit
- RNAP beta' subunit
- Transcriptase beta' chain
|
| Target 1 Gene Name |
rpoC |
| Target 1 Protein Sequence |
>DNA-directed RNA polymerase beta' chain
MLDVNFFDELRIGLATAEDIRQWSYGEVKKPETINYRTLKPEKDGLFCEKIFGPTRDWEC
YCGKYKRVRFKGIICERCGVEVTRAKVRRERMGHIELAAPVTHIWYFKGVPSRLGYLLDL
APKDLEKIIYFAAYVITSVDEEMRHNELSTLEAEMAVERKAVEDQRDGELEARAQKLEAD
LAELEAEGAKADARRKVRDGGEREMRQIRDRAQRELDRLEDIWSTFTKLAPKQLIVDENL
YRELVDRYGEYFTGAMGAESIQKLIENFDIDAEAESLRDVIRNGKGQKKLRALKRLKVVA
AFQQSGNSPMGMVLDAVPVIPPELRPMVQLDGGRFATSDLNDLYRRVINRNNRLKRLIDL
GAPEIIVNNEKRMLQESVDALFDNGRRGRPVTGPGNRPLKSLSDLLKGKQGRFRQNLLGK
RVDYSGRSVIVVGPQLKLHQCGLPKLMALELFKPFVMKRLVDLNHAQNIKSAKRMVERQR
PQVWDVLEEVIAEHPVLLNRAPTLHRLGIQAFEPMLVEGKAIQLHPLVCEAFNADFDGDQ
MAVHLPLSAEAQAEARILMLSSNNILSPASGRPLAMPRLDMVTGLYYLTTEVPGDTGEYQ
PASGDHPETGVYSSPAEAIMAADRGVLSVRAKIKVRLTQLRPPVEIEAELFGHSGWQPGD
AWMAETTLGRVMFNELLPLGYPFVNKQMHKKVQAAIINDLAERYPMIVVAQTVDKLKDAG
FYWATRSGVTVSMADVLVPPRKKEILDHYEERADKVEKQFQRGALNHDERNEALVEIWKE
ATDEVGQALREHYPDDNPIITIVDSGATGNFTQTRTLAGMKGLVTNPKGEFIPRPVKSSF
REGLTVLEYFINTHGARKGLADTALRTADSGYLTRRLVDVSQDVIVREHDCQTERGIVVE
LAERAPDGTLIRDPYIETSAYARTLGTDAVDEAGNVIVERGQDLGDPEIDALLAAGITQV
KVRSVLTCATSTGVCATCYGRSMATGKLVDIGEAVGIVAAQSIGEPGTQLTMRTFHQGGV
GEDITGGLPRVQELFEARVPRGKAPIADVTGRVRLEDGERFYKITIVPDDGGEEVVYDKI
SKRQRLRVFKHEDGSERVLSDGDHVEVGQQLMEGSADPHEVLRVQGPREVQIHLVREVQE
VYRAQGVSIHDKHIEVIVRQMLRRVTIIDSGSTEFLPGSLIDRAEFEAENRRVVAEGGEP
AAGRPVLMGITKASLATDSWLSAASFQETTRVLTDAAINCRSDKLNGLKENVIIGKLIPA
GTGINRYRNIAVQPTEEARAAAYTIPSYEDQYYSPDFGAATGAAVPLDDYGYSDYR
|
| Target 1 Number of Residues |
1337 |
| Target 1 Molecular Weight |
146771 |
| Target 1 Theoretical pI |
6.08 |
| Target 1 GO Classification |
|
Function
|
catalytic activity
transferase activity
transferase activity, transferring phosphorus-containing groups
nucleotidyltransferase activity
DNA-directed RNA polymerase activity
binding
nucleic acid binding
DNA binding |
|
Process
|
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
transcription |
|
Component
|
organelle
membrane-bound organelle
intracellular membrane-bound organelle
nucleus |
|
| Target 1 General Function |
Transcription |
| Target 1 Specific Function |
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates |
| Target 1 Pathways |
|
| Target 1 Reactions |
- nucleoside triphosphate + RNAn = diphosphate + RNAn+1
|
| Target 1 Pfam Domain Function |
|
| Target 1 Signals |
|
| Target 1 Transmembrane Regions |
|
| Target 1 Essentiality |
Essential |
| Target 1 GenBank ID Protein |
2143292  |
| Target 1 UniProtKB/Swiss-Prot ID |
P0A674  |
| Target 1 UniProtKB/Swiss-Prot Entry Name |
RPOC_MYCTU  |
| Target 1 PDB ID |
Not Available |
| Target 1 Cellular Location |
|
| Target 1 Gene Sequence |
>3951 bp
GTGCTCGACGTCAACTTCTTCGATGAACTCCGCATCGGTCTTGCTACCGCGGAGGACATC
AGGCAATGGTCCTATGGCGAGGTCAAAAAGCCGGAGACGATCAACTACCGCACGCTTAAG
CCGGAGAAGGACGGCCTGTTCTGCGAGAAGATCTTCGGGCCGACTCGCGACTGGGAATGC
TACTGCGGCAAGTACAAGCGGGTGCGCTTCAAGGGCATCATCTGCGAGCGCTGCGGCGTC
GAGGTGACCCGCGCCAAGGTGCGTCGTGAGCGGATGGGCCACATCGAGCTTGCCGCGCCC
GTCACCCACATCTGGTACTTCAAGGGTGTGCCCTCGCGGCTGGGGTATCTGCTGGACCTG
GCCCCGAAGGACCTGGAGAAGATCATCTACTTCGCTGCCTACGTGATCACCTCGGTCGAC
GAGGAGATGCGCCACAATGAGCTCTCCACGCTCGAGGCCGAAATGGCGGTGGAGCGCAAG
GCCGTCGAAGACCAGCGCGACGGCGAACTAGAGGCCCGGGCGCAAAAGCTGGAGGCCGAC
CTGGCCGAGCTGGAGGCCGAGGGCGCCAAGGCCGATGCGCGGCGCAAGGTTCGCGACGGC
GGCGAGCGCGAGATGCGCCAGATCCGTGACCGCGCGCAGCGTGAGCTGGACCGGTTGGAG
GACATCTGGAGCACTTTCACCAAGCTGGCGCCCAAGCAGCTGATCGTCGACGAAAACCTC
TACCGCGAACTCGTCGACCGCTACGGCGAGTACTTCACCGGTGCCATGGGCGCGGAGTCG
ATCCAGAAGCTGATCGAGAACTTCGACATCGACGCCGAAGCCGAGTCGCTGCGGGATGTC
ATCCGAAACGGCAAGGGGCAGAAGAAGCTTCGCGCCCTCAAGCGGCTGAAGGTGGTTGCG
GCGTTCCAACAGTCGGGCAACTCGCCGATGGGCATGGTGCTCGACGCCGTCCCGGTGATC
CCGCCGGAGCTGCGCCCGATGGTGCAGCTCGACGGCGGCCGGTTCGCCACGTCCGACTTG
AACGACCTGTACCGCAGGGTGATCAACCGCAACAACCGGCTGAAAAGGCTGATCGATCTG
GGTGCGCCGGAAATCATCGTCAACAACGAGAAGCGGATGCTGCAGGAATCCGTGGACGCG
CTGTTCGACAATGGCCGCCGCGGCCGGCCCGTCACCGGGCCGGGCAACCGTCCGCTCAAG
TCGCTTTCCGATCTGCTCAAGGGCAAGCAGGGCCGGTTCCGGCAGAACCTGCTCGGCAAG
CGTGTCGACTACTCGGGCCGGTCGGTCATCGTGGTCGGCCCGCAGCTCAAGCTGCACCAG
TGCGGTCTGCCCAAGCTGATGGCGCTGGAGCTGTTCAAGCCGTTCGTGATGAAGCGGCTG
GTGGACCTCAACCATGCGCAGAACATCAAGAGCGCCAAGCGCATGGTGGAGCGCCAGCGC
CCCCAAGTGTGGGATGTGCTCGAAGAGGTCATCGCCGAGCACCCGGTGTTGCTGAACCGC
GCACCCACCCTGCACCGGTTGGGTATCCAGGCCTTCGAGCCAATGCTGGTGGAAGGCAAG
GCCATTCAGCTGCACCCGTTGGTGTGTGAGGCGTTCAATGCCGACTTCGACGGTGACCAG
ATGGCCGTGCACCTGCCTTTGAGCGCCGAAGCGCAGGCCGAGGCTCGCATTTTGATGTTG
TCCTCCAACAACATCCTGTCGCCGGCATCTGGGCGTCCGTTGGCCATGCCGCGGCTGGAC
ATGGTGACCGGGCTGTACTACCTGACCACCGAGGTCCCCGGGGACACCGGCGAATACCAG
CCGGCCAGCGGGGATCACCCGGAGACTGGTGTCTACTCTTCGCCGGCCGAAGCGATCATG
GCGGCCGACCGCGGTGTCTTGAGCGTGCGGGCCAAGATCAAGGTGCGGCTGACCCAGCTG
CGGCCGCCGGTCGAGATCGAGGCCGAGCTATTCGGCCACAGCGGCTGGCAGCCGGGCGAT
GCGTGGATGGCCGAGACCACGCTGGGCCGGGTGATGTTCAACGAGCTGCTGCCGCTGGGT
TATCCGTTCGTCAACAAGCAGATGCACAAGAAGGTGCAGGCCGCCATCATCAACGACCTG
GCCGAGCGTTACCCGATGATCGTGGTCGCCCAGACCGTCGACAAGCTCAAGGACGCCGGC
TTCTACTGGGCCACCCGCAGCGGCGTGACGGTGTCGATGGCCGACGTGCTGGTGCCGCCG
CGCAAGAAGGAGATCCTCGACCACTACGAGGAGCGCGCGGACAAGGTCGAAAAGCAGTTC
CAGCGTGGCGCTTTGAACCACGACGAGCGCAACGAGGCGCTGGTGGAGATTTGGAAGGAA
GCCACCGACGAGGTCGGTCAGGCGTTGCGGGAGCACTACCCCGACGACAACCCGATCATC
ACCATCGTCGACTCCGGCGCCACCGGCAACTTCACCCAGACTCGAACGCTGGCCGGTATG
AAGGGCCTGGTGACCAACCCGAAGGGTGAGTTCATCCCGCGTCCGGTCAAGTCCTCCTTC
CGTGAGGGCCTGACCGTGCTGGAGTACTTCATCAACACCCACGGCGCTCGAAAGGGCTTG
GCGGACACCGCGTTGCGCACCGCCGACTCCGGCTACCTGACCCGACGTCTGGTGGACGTG
TCCCAGGACGTGATCGTGCGCGAGCACGACTGCCAGACCGAGCGCGGCATCGTCGTCGAG
CTGGCCGAGCGTGCACCCGACGGCACGCTGATCCGCGACCCGTACATCGAAACCTCGGCC
TACGCGCGGACCCTGGGCACCGACGCGGTCGACGAGGCCGGCAACGTCATCGTCGAGCGT
GGTCAAGACCTGGGCGATCCGGAGATTGACGCTCTGTTGGCTGCTGGTATTACCCAGGTC
AAGGTGCGTTCGGTGCTGACGTGTGCCACCAGCACCGGCGTGTGCGCGACCTGCTACGGG
CGTTCCATGGCCACCGGCAAGCTGGTCGACATCGGTGAAGCCGTCGGCATCGTGGCCGCC
CAGTCCATCGGCGAACCCGGCACCCAGCTGACCATGCGCACCTTCCACCAGGGTGGCGTC
GGTGAGGACATCACCGGTGGTCTGCCCCGGGTGCAGGAGCTGTTCGAGGCCCGGGTACCG
CGTGGCAAGGCGCCGATCGCCGACGTCACCGGCCGGGTTCGGCTCGAGGACGGCGAGCGG
TTCTACAAGATCACCATCGTTCCTGACGACGGCGGTGAGGAAGTGGTCTACGACAAGATC
TCCAAGCGGCAGCGGCTGCGGGTGTTCAAGCACGAAGACGGTTCCGAACGGGTGCTCTCC
GATGGCGACCACGTCGAGGTGGGCCAGCAGCTGATGGAAGGCTCGGCCGACCCGCATGAG
GTGCTGCGGGTGCAGGGCCCCCGCGAGGTGCAGATACACCTGGTTCGCGAGGTCCAGGAG
GTCTACCGCGCCCAAGGTGTGTCGATCCACGACAAGCACATCGAGGTGATCGTTCGCCAG
ATGCTGCGCCGGGTGACCATCATCGACTCGGGCTCGACGGAGTTTTTGCCTGGCTCGCTG
ATCGACCGCGCGGAGTTCGAGGCAGAGAACCGCCGAGTGGTGGCCGAGGGCGGTGAGCCC
GCGGCCGGCCGTCCGGTGCTGATGGGCATCACGAAGGCGTCGCTGGCCACCGACTCGTGG
CTGTCGGCGGCGTCGTTCCAGGAGACCACTCGCGTGCTGACCGATGCGGCGATCAACTGC
CGCAGCGATAAGCTCAACGGTCTGAAGGAAAACGTGATCATCGGCAAGCTGATCCCGGCC
GGTACCGGTATCAACCGCTACCGCAACATCGCGGTGCAGCCCACCGAGGAGGCCCGCGCT
GCGGCGTACACCATCCCGTCGTATGAGGATCAGTACTACAGCCCGGACTTCGGTGCGGCC
ACCGGTGCTGCCGTCCCGCTGGACGACTACGGCTACAGCGACTACCGCTAG
|
| 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  |
| Target 1 General References |
- 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
]
- Miller LP, Crawford JT, Shinnick TM: The rpoB gene of Mycobacterium tuberculosis. Antimicrob Agents Chemother. 1994 Apr;38(4):805-11. [PubMed
]
- 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
]
|
| Target 1 Drug References |
- 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
]
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed
]
- Buchstein SR, Hinkle DC: Genetic analysis of two bacterial RNA polymerase mutants that inhibit the growth of bacteriophage T7. Mol Gen Genet. 1982;188(2):211-8. [PubMed
]
- Miller LP, Crawford JT, Shinnick TM: The rpoB gene of Mycobacterium tuberculosis. Antimicrob Agents Chemother. 1994 Apr;38(4):805-11. [PubMed
]
- Babcock MJ, Buttner MJ, Keler CH, Clarke BR, Morris RA, Lewis CG, Brawner ME: Characterization of the rpoC gene of Streptomyces coelicolor A3(2) and its use to develop a simple and rapid method for the purification of RNA polymerase. Gene. 1997 Sep 1;196(1-2):31-42. [PubMed
]
|
|
Drug Target 2
[top]
|
| Target 2 ID |
284 |
| Target 2 Name |
DNA-directed RNA polymerase beta chain |
| Target 2 Synonyms |
- EC 2.7.7.6
- RNA polymerase beta subunit
- RNAP beta subunit
- Transcriptase beta chain
|
| Target 2 Gene Name |
rpoB |
| Target 2 Protein Sequence |
>DNA-directed RNA polymerase beta chain
MVYSYTEKKRIRKDFGKRPQVLDVPYLLSIQLDSFQKFIEQDPEGQYGLEAAFRSVFPIQ
SYSGNSELQYVSYRLGEPVFDVQECQIRGVTYSAPLRVKLRLVIYEREAPEGTVKDIKEQ
EVYMGEIPLMTDNGTFVINGTERVIVSQLHRSPGVFFDSDKGKTHSSGKVLYNARIIPYR
GSWLDFEFDPKDNLFVRIDRRRKLPATIILRALNYTTEQILDLFFEKVIFEIRDNKLQME
LVPERLRGETASFDIEANGKVYVEKGRRITARHIRQLEKDDVKLIEVPVEYIAGKVVAKD
YIDESTGELICAANMELSLDLLAKLSQSGHKRIETLFTNDLDHGPYISETLRVDPTNDRL
SALVEIYRMMRPGEPPTREAAESLFENLFFSEDRYDLSAVGRMKFNRSLLREEIEGSGIL
SKDDIIDVMKKLIDIRNGKGEVDDIDHLGNRRIRSVGEMAENQFRVGLVRVERAVKERLS
LGDLDTLMPQDMINAKPISAAVKEFFGSSQLSQFMDQNNPLSEITHKRRISALGPGGLTR
ERAGFEVRDVHPTHYGRVCPIETPEGPNIGLINSLSVYAQTNEYGFLETPYRKVTDGVVT
DEIHYLSAIEEGNYVIAQANSNLDEEGHFVEDLVTCRSKGESSLFSRDQVDYMDVSTQQV
VSVGASLIPFLEHDDANRALMGANMQRQAVPTLRADKPLVGTGMERAVAVDSGVTAVAKR
GGVVQYVDASRIVIKVNEDEMYPGEAGIDIYNLTKYTRSNQNTCINQMPCVSLGEPVERG
DVLADGPSTDLGELALGQNMRVAFMPWNGYNFEDSILVSERVVQEDRFTTIHIQELACVS
RDTKLGPEEITADIPNVGEAALSKLDESGIVYIGAEVTGGDILVGKVTPKGETQLTPEEK
LLRAIFGEKASDVKDSSLRVPNGVSGTVIDVQVFTRDGVEKDKRALEIEEMQLKQAKKDL
SEELQILEAGLFSRIRAVLVAGGVEAEKLDKLPRDRWLELGLTDEEKQNQLEQLAEQYDE
LKHEFEKKLEAKRRKITQGDDLAPGVLKIVKVYLAVKRRIQPGDKMAGRHGNKGVISKIN
PIEDMPYDENGTPVDIVLNPLGVPSRMNIGQILETHLGMAAKGIGDKINAMLKQQQEVAK
LREFIQRAYDLGADVRQKVDLSTFSDEEVMRLAENLRKGMPIATPVFDGAKEAEIKELLK
LGDLPTSGQIRLYDGRTGEQFERPVTVGYMYMLKLNHLVDDKMHARSTGSYSLVTQQPLG
GKAQFGGQRFGEMEVWALEAYGAAYTLQEMLTVKSDDVNGRTKMYKNIVDGNHQMEPGMP
ESFNVLLKEIRSLGINIELEDE
|
| Target 2 Number of Residues |
1364 |
| Target 2 Molecular Weight |
150635 |
| Target 2 Theoretical pI |
4.89 |
| Target 2 GO Classification |
|
Function
|
catalytic activity
transferase activity
transferase activity, transferring phosphorus-containing groups
nucleotidyltransferase activity
DNA-directed RNA polymerase activity
binding
nucleic acid binding
DNA binding |
|
Process
|
physiological process
metabolism
cellular metabolism
nucleobase, nucleoside, nucleotide and nucleic acid metabolism
transcription |
|
Component
|
| Not Available |
|
| Target 2 General Function |
Transcription |
| Target 2 Specific Function |
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates |
| Target 2 Pathways |
|
| Target 2 Reactions |
- nucleoside triphosphate + RNAn = diphosphate + RNAn+1
|
| Target 2 Pfam Domain Function |
|
| Target 2 Signals |
|
| Target 2 Transmembrane Regions |
|
| Target 2 Essentiality |
Essential |
| Target 2 GenBank ID Protein |
42818  |
| Target 2 UniProtKB/Swiss-Prot ID |
P0A8V2  |
| Target 2 UniProtKB/Swiss-Prot Entry Name |
RPOB_ECOLI  |
| Target 2 PDB ID |
Not Available |
| Target 2 Cellular Location |
|
| Target 2 Gene Sequence |
>4029 bp
ATGGTTTACTCCTATACCGAGAAAAAACGTATTCGTAAGGATTTTGGTAAACGTCCACAA
GTTCTGGATGTACCTTATCTCCTTTCTATCCAGCTTGACTCGTTTCAGAAATTTATCGAG
CAAGATCCTGAAGGGCAGTATGGTCTGGAAGCTGCTTTCCGTTCCGTATTCCCGATTCAG
AGCTACAGCGGTAATTCCGAGCTGCAATACGTCAGCTACCGCCTTGGCGAACCGGTGTTT
GACGTCCAGGAATGTCAAATCCGTGGCGTGACCTATTCCGCACCGCTGCGCGTTAAACTG
CGTCTGGTGATCTATGAGCGCGAAGCGCCGGAAGGCACCGTAAAAGACATTAAAGAACAA
GAAGTCTACATGGGCGAAATTCCGCTCATGACAGACAACGGTACCTTTGTTATCAACGGT
ACTGAGCGTGTTATCGTTTCCCAGCTGCACCGTAGTCCGGGCGTCTTCTTTGACTCCGAC
AAAGGTAAAACCCACTCTTCGGGTAAAGTGCTGTATAACGCGCGTATCATCCCTTACCGT
GGTTCCTGGCTGGACTTCGAATTCGATCCGAAGGACAACCTGTTCGTACGTATCGACCGT
CGCCGTAAACTGCCTGCGACCATCATTCTGCGCGCCCTGAACTACACCACAGAGCAGATC
CTCGACCTGTTCTTTGAAAAAGTTATCTTTGAAATCCGTGATAACAAGCTGCAGATGGAA
CTGGTGCCGGAACGCCTGCGTGGTGAAACCGCATCTTTTGACATCGAAGCTAACGGTAAA
GTGTACGTAGAAAAAGGCCGCCGTATCACTGCGCGCCACATTCGCCAGCTGGAAAAAGAC
GACGTCAAACTGATCGAAGTCCCGGTTGAGTACATCGCAGGTAAAGTGGTTGCTAAAGAC
TATATTGATGAGTCTACCGGCGAGCTGATCTGCGCAGCGAACATGGAGCTGAGCCTGGAT
CTGCTGGCTAAGCTGAGCCAGTCTGGTCACAAGCGTATCGAAACGCTGTTCACCAACGAT
CTGGATCACGGCCCATATATCTCTGAAACCTTACGTGTCGACCCAACTAACGACCGTCTG
AGCGCACTGGTAGAAATCTACCGCATGATGCGCCCTGGCGAGCCGCCGACTCGTGAAGCA
GCTGAAAGCCTGTTCGAGAACCTGTTCTTCTCCGAAGACCGTTATGACTTGTCTGCGGTT
GGTCGTATGAAGTTCAACCGTTCTCTGCTGCGCGAAGAAATCGAAGGTTCCGGTATCCTG
AGCAAAGACGACATCATTGATGTTATGAAAAAGCTCATCGATATCCGTAACGGTAAAGGC
GAAGTCGATGATATCGACCACCTCGGCAACCGTCGTATCCGTTCCGTTGGCGAAATGGCG
GAAAACCAGTTCCGCGTTGGCCTGGTACGTGTAGAGCGTGCGGTGAAAGAGCGTCTGTCT
CTGGGCGATCTGGATACCCTGATGCCACAGGATATGATCAACGCCAAGCCGATTTCCGCA
GCAGTGAAAGAGTTCTTCGGTTCCAGCCAGCTGTCTCAGTTTATGGTCCAGAACAACCCG
CTGTCTGAGATTACGCACAAACGTCGTATCTCCGCACTCGGCCCAGGCGGTCTGACCCGT
GAACGTGCAGGCTTCGAAGTTCGAGACGTACACCCGACTCACTACGGTCGCGTATGTCCA
ATCGAAACCCCTGAAGGTCCGAACATCGGTCTGATCAACTCTCTGTCCGTGTACGCACAG
ACTAACGAATACGGCTTCCTTGAGACTCCGTATCGTAAAGTGACCGACGGTGTTGTAACT
GACGAAATTCACTACCTGTCTGCTATCGAAGAAGGCAACTACGTTATCGCCCAGGCGAAC
TCCAACTTGGATGAAGAAGGCCACTTCGTAGAAGACCTGGTAACTTGCCGTAGCAAAGGC
GAATCCAGCTTGTTCAGCCGCGACCAGGTTGACTACATGGACGTATCCACCCAGCAGGTG
GTATCCGTCGGTGCGTCCCTGATCCCGTTCCTGGAACACGATGACGCCAACCGTGCATTG
ATGGGTGCGAACATGCAACGTCAGGCCGTTCCGACTCTGCGCGCTGATAAGCCGCTGGTT
GGTACTGGTATGGAACGTGCTGTTGCCGTTGACTCCGGTGTAACTGCGGTAGCTAAACGT
GGTGGTGTCGTTCAGTACGTGGATGCTTCCCGTATCGTTATCAAAGTTAACGAAGACGAG
ATGTATCCGGGTGAAGCAGGTATCGACATCTACAACCTGACCAAATACACCCGTTCTAAC
CAGAACACCTGTATCAACCAGATGCCGTGTGTGTCTCTGGGTGAACCGGTTGAACGTGGC
GACGTGCTGGCAGACGGTCCGTCCACCGACCTCGGTGAACTGGCGCTTGGTCAGAACATG
CGCGTAGCGTTCATGCCGTGGAATGGTTACAACTTCGAAGACTCCATCCTCGTATCCGAG
CGTGTTGTTCAGGAAGACCGTTTCACCACCATCCACATTCAGGAACTGGCGTGTGTGTCC
CGTGACACCAAGCTGGGTCCGGAAGAGATCACCGCTGACATCCCGAACGTGGGTGAAGCT
GCGCTCTCCAAACTGGATGAATCCGGTATCGTTTACATTGGTGCGGAAGTGACCGGTGGC
GACATTCTGGTTGGTAAGGTAACGCCGAAAGGTGAAACTCAGCTGACCCCAGAAGAAAAA
CTGCTGCGTGCGATCTTCGGTGAGAAAGCCTCTGACGTTAAAGACTCTTCTCTGCGCGTA
CCAAACGGTGTATCCGGTACGGTTATCGACGTTCAGGTCTTTACTCGCGATGGCGTAGAA
AAAGACAAACGTGCGCTGGAAATCGAAGAAATGCAGCTCAAACAGGCGAAGAAAGACCTG
TCTGAAGAACTGCAGATCCTCGAAGCGGGTCTGTTCAGCCGTATCCGTGCTGTGCTGGTA
GCCGGTGGCGTTGAAGCTGAGAAGCTCGACAAACTGCCGCGCGATCGCTGGCTGGAGCTG
GGCCTGACAGACGAAGAGAAACAAAATCAGCTGGAACAGCTGGCTGAGCAGTATGACGAA
CTGAAACACGAGTTCGAGAAGAAACTCGAAGCGAAACGCCGCAAAATCACCCAGGGCGAC
GATCTGGCACCGGGCGTGCTGAAGATTGTTAAGGTATATCTGGCGGTTAAACGCCGTATC
CAGCCTGGTGACAAGATGGCAGGTCGTCACGGTAACAAGGGTGTAATTTCTAAGATCAAC
CCGATCGAAGATATGCCTTACGATGAAAACGGTACGCCGGTAGACATCGTACTGAACCCG
CTGGGCGTACCGTCTCGTATGAACATCGGTCAGATCCTCGAAACCCACCTGGGTATGGCT
GCGAAAGGTATCGGCGACAAGATCAACGCCATGCTGAAACAGCAGCAAGAAGTCGCGAAA
CTGCGCGAATTCATCCAGCGTGCGTACGATCTGGGCGCTGACGTTCGTCAGAAAGTTGAC
CTGAGTACCTTCAGCGATGAAGAAGTTATGCGTCTGGCTGAAAACCTGCGCAAAGGTATG
CCAATCGCAACGCCGGTGTTCGACGGTGCGAAAGAAGCAGAAATTAAAGAGCTGCTGAAA
CTTGGCGACCTGCCGACTTCCGGTCAGATCCGCCTGTACGATGGTCGCACTGGTGAACAG
TTCGAGCGTCCGGTAACCGTTGGTTACATGTACATGCTGAAACTGAACCACCTGGTCGAC
GACAAGATGCACGCGCGTTCCACCGGTTCTTACAGCCTGGTTACTCAGCAGCCGCTGGGT
GGTAAGGCACAGTTCGGTGGTCAGCGTTTCGGGGAGATGGAAGTGTGGGCGCTGGAAGCA
TACGGCGCAGCATACACCCTGCAGGAAATGCTCACCGTTAAGTCTGATGACGTGAACGGT
CGTACCAAGATGTATAAAAACATCGTGGACGGCAACCATCAGATGGAGCCGGGCATGCCA
GAATCCTTCAACGTATTGTTGAAAGAGATTCGTTCGCTGGGTATCAACATCGAACTGGAA
GACGAGTAA
|
| 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  |
| Target 2 General References |
- Lee J, Kashlev M, Borukhov S, Goldfarb A: A beta subunit mutation disrupting the catalytic function of Escherichia coli RNA polymerase. Proc Natl Acad Sci U S A. 1991 Jul 15;88(14):6018-22. [PubMed
]
- Post LE, Strycharz GD, Nomura M, Lewis H, Dennis PP: Nucleotide sequence of the ribosomal protein gene cluster adjacent to the gene for RNA polymerase subunit beta in Escherichia coli. Proc Natl Acad Sci U S A. 1979 Apr;76(4):1697-701. [PubMed
]
- Ovchinnikov YA, Monastyrskaya GS, Gubanov VV, Guryev SO, Chertov OYu, Modyanov NN, Grinkevich VA, Makarova IA, Marchenko TV, Polovnikova IN, Lipkin VM, Sverdlov ED: The primary structure of Escherichia coli RNA polymerase. Nucleotide sequence of the rpoB gene and amino-acid sequence of the beta-subunit. Eur J Biochem. 1981 Jun 1;116(3):621-9. [PubMed
]
- Delcuve G, Downing W, Lewis H, Dennis PP: Nucleotide sequence of the proximal portion of the RNA polymerase beta subunit gene of Escherichia coli. Gene. 1980 Nov;11(3-4):367-73. [PubMed
]
- Blattner FR, Burland V, Plunkett G 3rd, Sofia HJ, Daniels DL: Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes. Nucleic Acids Res. 1993 Nov 25;21(23):5408-17. [PubMed
]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-74. [PubMed
]
|
| Target 2 Drug References |
- Nicholson WL, Maughan H: The spectrum of spontaneous rifampin resistance mutations in the rpoB gene of Bacillus subtilis 168 spores differs from that of vegetative cells and resembles that of Mycobacterium tuberculosis. J Bacteriol. 2002 Sep;184(17):4936-40. [PubMed
]
- Maughan H, Galeano B, Nicholson WL: Novel rpoB mutations conferring rifampin resistance on Bacillus subtilis: global effects on growth, competence, sporulation, and germination. J Bacteriol. 2004 Apr;186(8):2481-6. [PubMed
]
- 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
]
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed
]
- He X, Zhuang Y, Li G: [Application of PCR-SSCP technique in detection of rpoB gene mutation in rifampin-resistant Mycobacterium tuberculosis] Zhonghua Jie He He Hu Xi Za Zhi. 1996 Dec;19(6):338-41. [PubMed
]
|
|
Drug Target 3
[top]
|
| Target 3 ID |
1284 |
| Target 3 Name |
Orphan nuclear receptor PXR |
| Target 3 Synonyms |
- Orphan nuclear receptor PAR1
- Pregnane X receptor
- SXR
- Steroid and xenobiotic receptor
|
| Target 3 Gene Name |
NR1I2 |
| Target 3 Protein Sequence |
>Orphan nuclear receptor PXR
MEVRPKESWNHADFVHCEDTESVPGKPSVNADEEVGGPQICRVCGDKATGYHFNVMTCEG
CKGFFRRAMKRNARLRCPFRKGACEITRKTRRQCQACRLRKCLESGMKKEMIMSDEAVEE
RRALIKRKKSERTGTQPLGVQGLTEEQRMMIRELMDAQMKTFDTTFSHFKNFRLPGVLSS
GCELPESLQAPSREEAAKWSQVRKDLCSLKVSLQLRGEDGSVWNYKPPADSGGKEIFSLL
PHMADMSTYMFKGIISFAKVISYFRDLPIEDQISLLKGAAFELCQLRFNTVFNAETGTWE
CGRLSYCLEDTAGGFQQLLLEPMLKFHYMLKKLQLHEEEYVLMQAISLFSPDRPGVLQHR
VVDQLQEQFAITLKSYIECNRPQPAHRFLFLKIMAMLTELRSINAQHTQRLLRIQDIHPF
ATPLMQELFGITGS
|
| Target 3 Number of Residues |
441 |
| Target 3 Molecular Weight |
49762 |
| Target 3 Theoretical pI |
8.44 |
| Target 3 GO Classification |
|
Function
|
signal transducer activity
receptor activity
ligand-dependent nuclear receptor activity
steroid hormone receptor activity
binding
nucleic acid binding
DNA binding
transcription factor activity |
|
Process
|
regulation of biological process
regulation of physiological process
regulation of metabolism
regulation of cellular metabolism
regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
regulation of transcription
regulation of transcription, DNA-dependent |
|
Component
|
organelle
membrane-bound organelle
intracellular membrane-bound organelle
nucleus |
|
| Target 3 General Function |
Involved in transcription factor activity |
| Target 3 Specific Function |
Orphan receptor; its natural ligand is probably pregnane. Binds to a response element in the CYP3A4 and ABCB1/MDR1 genes promoter. Activates its expression in response to a wide variety of endobiotics and xenobiotics |
| Target 3 Pathways |
Not Available
|
| Target 3 Reactions |
Not Available |
| Target 3 Pfam Domain Function |
|
| Target 3 Signals |
|
| Target 3 Transmembrane Regions |
|
| Target 3 Essentiality |
Non-Essential |
| Target 3 GenBank ID Protein |
3511138  |
| Target 3 UniProtKB/Swiss-Prot ID |
O75469  |
| Target 3 UniProtKB/Swiss-Prot Entry Name |
PXR_HUMAN  |
| Target 3 PDB ID |
1NRL  |
| Target 3 PDB File |
Show |
| Target 3 3D Structure |
|
| Target 3 Cellular Location |
|
| Target 3 Gene Sequence |
>1305 bp
CTGGAGGTGAGACCCAAAGAAAGCTGGAACCATGCTGACTTTGTACACTGTGAGGACACA
GAGTCTGTTCCTGGAAAGCCCAGTGTCAACGCAGATGAGGAAGTCGGAGGTCCCCAAATC
TGCCGTGTATGTGGGGACAAGGCCACTGGCTATCACTTCAATGTCATGACATGTGAAGGA
TGCAAGGGCTTTTTCAGGAGGGCCATGAAACGCAACGCCCGGCTGAGGTGCCCCTTCCGG
AAGGGCGCCTGCGAGATCACCCGGAAGACCCGGCGACAGTGCCAGGCCTGCCGCCTGCGC
AAGTGCCTGGAGAGCGGCATGAAGAAGGAGATGATCATGTCCGACGAGGCCGTGGAGGAG
AGGCGGGCCTTGATCAAGCGGAAGAAAAGTGAACGGACAGGGACTCAGCCACTGGGAGTG
CAGGGGCTGACAGAGGAGCAGCGGATGATGATCAGGGAGCTGATGGACGCTCAGATGAAA
ACCTTTGACACTACCTTCTCCCATTTCAAGAATTTCCGGCTGCCAGGGGTGCTTAGCAGT
GGCTGCGAGTTGCCAGAGTCTCTGCAGGCCCCATCGAGGGAAGAAGCTGCCAAGTGGAGC
CAGGTCCGGAAAGATCTGTGCTCTTTGAAGGTCTCTCTGCAGCTGCGGGGGGAGGATGGC
AGTGTCTGGAACTACAAACCCCCAGCCGACAGTGGCGGGAAAGAGATCTTCTCCCTGCTG
CCCCACATGGCTGACATGTCAACCTACATGTTCAAAGGCATCATCAGCTTTGCCAAAGTC
ATCTCCTACTTCAGGGACTTGCCCATCGAGGACCAGATCTCCCTGCTGAAGGGGGCCGCT
TTCGAGCTGTGTCAACTGAGATTCAACACAGTGTTCAACGCGGAGACTGGAACCTGGGAG
TGTGGCCGGCTGTCCTACTGCTTGGAAGACACTGCAGGTGGCTTCCAGCAACTTCTACTG
GAGCCCATGCTGAAATTCCACTACATGCTGAAGAAGCTGCAGCTGCATGAGGAGGAGTAT
GTGCTGATGCAGGCCATCTCCCTCTTCTCCCCAGACCGCCCAGGTGTGCTGCAGCACCGC
GTGGTGGACCAGCTGCAGGAGCAATTCGCCATTACTCTGAAGTCCTACATTGAATGCAAT
CGGCCCCAGCCTGCTCATAGGTTCTTGTTCCTGAAGATCATGGCTATGCTCACCGAGCTC
CGCAGCATCAATGCTCAGCACACCCAGCGGCTGCTGCGCATCCAGGACATACACCCCTTT
GCTACGCCCCTCATGCAGGAGTTGTTCGGCATCACAGGTAGCTGA
|
| Target 3 GenBank Gene ID |
|
| Target 3 GeneCard ID |
NR1I2  |
| Target 3 GenAtlas ID |
NR1I2  |
| Target 3 HGNC ID |
HGNC:7968  |
| Target 3 Chromosome Location |
3 |
| Target 3 Locus |
3q12-q13.3 |
| Target 3 SNPs |
SNPJam Report  |
| Target 3 General References |
- Watkins RE, Wisely GB, Moore LB, Collins JL, Lambert MH, Williams SP, Willson TM, Kliewer SA, Redinbo MR: The human nuclear xenobiotic receptor PXR: structural determinants of directed promiscuity. Science. 2001 Jun 22;292(5525):2329-33. Epub 2001 Jun 14. [PubMed
]
- Zhang J, Kuehl P, Green ED, Touchman JW, Watkins PB, Daly A, Hall SD, Maurel P, Relling M, Brimer C, Yasuda K, Wrighton SA, Hancock M, Kim RB, Strom S, Thummel K, Russell CG, Hudson JR Jr, Schuetz EG, Boguski MS: The human pregnane X receptor: genomic structure and identification and functional characterization of natural allelic variants. Pharmacogenetics. 2001 Oct;11(7):555-72. [PubMed
]
- Kawana K, Ikuta T, Kobayashi Y, Gotoh O, Takeda K, Kawajiri K: Molecular mechanism of nuclear translocation of an orphan nuclear receptor, SXR. Mol Pharmacol. 2003 Mar;63(3):524-31. [PubMed
]
- Lehmann JM, McKee DD, Watson MA, Willson TM, Moore JT, Kliewer SA: The human orphan nuclear receptor PXR is activated by compounds that regulate CYP3A4 gene expression and cause drug interactions. J Clin Invest. 1998 Sep 1;102(5):1016-23. [PubMed
]
- Bertilsson G, Heidrich J, Svensson K, Asman M, Jendeberg L, Sydow-Backman M, Ohlsson R, Postlind H, Blomquist P, Berkenstam A: Identification of a human nuclear receptor defines a new signaling pathway for CYP3A induction. Proc Natl Acad Sci U S A. 1998 Oct 13;95(21):12208-13. [PubMed
]
- Blumberg B, Sabbagh W Jr, Juguilon H, Bolado J Jr, van Meter CM, Ong ES, Evans RM: SXR, a novel steroid and xenobiotic-sensing nuclear receptor. Genes Dev. 1998 Oct 15;12(20):3195-205. [PubMed
]
|
| Target 3 Drug References |
Not Available |
|
Drug Target 4
[top]
|
| Target 4 ID |
1588 |
| Target 4 Name |
Multidrug resistance protein 1 |
| Target 4 Synonyms |
- ATP-binding cassette sub-family B member 1
- CD243 antigen
- EC 3.6.3.44
- P-glycoprotein 1
|
| Target 4 Gene Name |
ABCB1 |
| Target 4 Protein Sequence |
>Multidrug resistance protein 1
MDLEGDRNGGAKKKNFFKLNNKSEKDKKEKKPTVSVFSMFRYSNWLDKLYMVVGTLAAII
HGAGLPLMMLVFGEMTDIFANAGNLEDLMSNITNRSDINDTGFFMNLEEDMTRYAYYYSG
IGAGVLVAAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVS
KINEGIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFT
DKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIG
AAFLLIYASYALAFWYGTTLVLSGEYSIGQVLTVFFSVLIGAFSVGQASPSIEAFANARG
AAYEIFKIIDNKPSIDSYSKSGHKPDNIKGNLEFRNVHFSYPSRKEVKILKGLNLKVQSG
QTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLF
ATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIA
IARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAG
FDDGVIVEKGNHDELMKEKGIYFKLVTMQTAGNEVELENAADESKSEIDALEMSSNDSRS
SLIRKRSTRRSVRGSQAQDRKLSTKEALDESIPPVSFWRIMKLNLTEWPYFVVGVFCAII
NGGLQPAFAIIFSKIIGVFTRIDDPETKRQNSNLFSLLFLALGIISFITFFLQGFTFGKA
GEILTKRLRYMVFRSMLRQDVSWFDDPKNTTGALTTRLANDAAQVKGAIGSRLAVITQNI
ANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGAGKIATEA
IENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQAMMYFSYAGCFRFG
AYLVAHKLMSFEDVLLVFSAVVFGAMAVGQVSSFAPDYAKAKISAAHIIMIIEKTPLIDS
YSTEGLMPNTLEGNVTFGEVVFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVV
QLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSRVV
SQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLD
EATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQL
LAQKGIYFSMVSVQAGTKRQ
|
| Target 4 Number of Residues |
1301 |
| Target 4 Molecular Weight |
141464 |
| Target 4 Theoretical pI |
9.44 |
| Target 4 GO Classification |
|
Function
|
ATPase activity
hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
ATPase activity, coupled to transmembrane movement of substances
purine nucleotide binding
adenyl nucleotide binding
ATP binding
catalytic activity
hydrolase activity
hydrolase activity, acting on acid anhydrides
hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
pyrophosphatase activity
nucleoside-triphosphatase activity
binding
nucleotide binding |
|
Process
|
physiological process
cellular physiological process
transport |
|
Component
|
cell
membrane
intrinsic to membrane
integral to membrane |
|
| Target 4 General Function |
Defense mechanisms and drug export |
| Target 4 Specific Function |
Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells |
| Target 4 Pathways |
Not Available
|
| Target 4 Reactions |
- ATP + H2O + xenobioticin = ADP + phosphate + xenobioticout
|
| Target 4 Pfam Domain Function |
|
| Target 4 Signals |
|
| Target 4 Transmembrane Regions |
- 52-72
- 120-140
- 189-209
- 216-236
- 297-317
- 326-346
- 711-731
- 757-777
- 833-853
- 854-874
- 937-957
- 974-994
|
| Target 4 Essentiality |
Non-Essential |
| Target 4 GenBank ID Protein |
307180  |
| Target 4 UniProtKB/Swiss-Prot ID |
P08183  |
| Target 4 UniProtKB/Swiss-Prot Entry Name |
MDR1_HUMAN  |
| Target 4 PDB ID |
Not Available |
| Target 4 Cellular Location |
- Membrane
- multi-pass membrane protein
|
| Target 4 Gene Sequence |
>3843 bp
ATGGATCTTGAAGGGGACCGCAATGGAGGAGCAAAGAAGAAGAACTTTTTTAAACTGAAC
AATAAAAGTGAAAAAGATAAGAAGGAAAAGAAACCAACTGTCAGTGTATTTTCAATGTTT
CGCTATTCAAATTGGCTTGACAAGTTGTATATGGTGGTGGGAACTTTGGCTGCCATCATC
CATGGGGCTGGACTTCCTCTCATGATGCTGGTGTTTGGAGAAATGACAGATATCTTTGCA
AATGCAGGAAATTTAGAAGATCTGATGTCAAACATCACTAATAGAAGTGATATCAATGAT
ACAGGGTTCTTCATGAATCTGGAGGAAGACATGACCAGGTATGCCTATTATTACAGTGGA
ATTGGTGCTGGGGTGCTGGTTGCTGCTTACATTCAGGTTTCATTTTGGTGCCTGGCAGCT
GGAAGACAAATACACAAAATTAGAAAACAGTTTTTTCATGCTATAATGCGACAGGAGATA
GGCTGGTTTGATGTGCACGATGTTGGGGAGCTTAACACCCGACTTACAGATGATGTCTCT
AAGATTAATGAAGTTATTGGTGACAAAATTGGAATGTTCTTTCAGTCAATGGCAACATTT
TTCACTGGGTTTATAGTAGGATTTACACGTGGTTGGAAGCTAACCCTTGTGATTTTGGCC
ATCAGTCCTGTTCTTGGACTGTCAGCTGCTGTCTGGGCAAAGATACTATCTTCATTTACT
GATAAAGAACTCTTAGCGTATGCAAAAGCTGGAGCAGTAGCTGAAGAGGTCTTGGCAGCA
ATTAGAACTGTGATTGCATTTGGAGGACAAAAGAAAGAACTTGAAAGGTACAACAAAAAT
TTAGAAGAAGCTAAAAGAATTGGGATAAAGAAAGCTATTACAGCCAATATTTCTATAGGT
GCTGCTTTCCTGCTGATCTATGCATCTTATGCTCTGGCCTTCTGGTATGGGACCACCTTG
GTCCTCTCAGGGGAATATTCTATTGGACAAGTACTCACTGTATTCTTTTCTGTATTAATT
GGGGCTTTTAGTGTTGGACAGGCATCTCCAAGCATTGAAGCATTTGCAAATGCAAGAGGA
GCAGCTTATGAAATCTTCAAGATAATTGATAATAAGCCAAGTATTGACAGCTATTCGAAG
AGTGGGCACAAACCAGATAATATTAAGGGAAATTTGGAATTCAGAAATGTTCACTTCAGT
TACCCATCTCGAAAAGAAGTTAAGATCTTGAAGGGCCTGAACCTGAAGGTGCAGAGTGGG
CAGACGGTGGCCCTGGTTGGAAACAGTGGCTGTGGGAAGAGCACAACAGTCCAGCTGATG
CAGAGGCTCTATGACCCCACAGAGGGGATGGTCAGTGTTGATGGACAGGATATTAGGACC
ATAAATGTAAGGTTTCTACGGGAAATCATTGGTGTGGTGAGTCAGGAACCTGTATTGTTT
GCCACCACGATAGCTGAAAACATTCGCTATGGCCGTGAAAATGTCACCATGGATGAGATT
GAGAAAGCTGTCAAGGAAGCCAATGCCTATGACTTTATCATGAAACTGCCTCATAAATTT
GACACCCTGGTTGGAGAGAGAGGGGCCCAGTTGAGTGGTGGGCAGAAGCAGAGGATCGCC
ATTGCACGTGCCCTGGTTCGCAACCCCAAGATCCTCCTGCTGGATGAGGCCACGTCAGCC
TTGGACACAGAAAGCGAAGCAGTGGTTCAGGTGGCTCTGGATAAGGCCAGAAAAGGTCGG
ACCACCATTGTGATAGCTCATCGTTTGTCTACAGTTCGTAATGCTGACGTCATCGCTGGT
TTCGATGATGGAGTCATTGTGGAGAAAGGAAATCATGATGAACTCATGAAAGAGAAAGGC
ATTTACTTCAAACTTGTCACAATGCAGACAGCAGGAAATGAAGTTGAATTAGAAAATGCA
GCTGATGAATCCAAAAGTGAAATTGATGCCTTGGAAATGTCTTCAAATGATTCAAGATCC
AGTCTAATAAGAAAAAGATCAACTCGTAGGAGTGTCCGTGGATCACAAGCCCAAGACAGA
AAGCTTAGTACCAAAGAGGCTCTGGATGAAAGTATACCTCCAGTTTCCTTTTGGAGGATT
ATGAAGCTAAATTTAACTGAATGGCCTTATTTTGTTGTTGGTGTATTTTGTGCCATTATA
AATGGAGGCCTGCAACCAGCATTTGCAATAATATTTTCAAAGATTATAGGGGTTTTTACA
AGAATTGATGATCCTGAAACAAAACGACAGAATAGTAACTTGTTTTCACTATTGTTTCTA
GCCCTTGGAATTATTTCTTTTATTACATTTTTCCTTCAGGGTTTCACATTTGGCAAAGCT
GGAGAGATCCTCACCAAGCGGCTCCGATACATGGTTTTCCGATCCATGCTCAGACAGGAT
GTGAGTTGGTTTGATGACCCTAAAAACACCACTGGAGCATTGACTACCAGGCTCGCCAAT
GATGCTGCTCAAGTTAAAGGGGCTATAGGTTCCAGGCTTGCTGTAATTACCCAGAATATA
GCAAATCTTGGGACAGGAATAATTATATCCTTCATCTATGGTTGGCAACTAACACTGTTA
CTCTTAGCAATTGTACCCATCATTGCAATAGCAGGAGTTGTTGAAATGAAAATGTTGTCT
GGACAAGCACTGAAAGATAAGAAAGAACTAGAAGGTGCTGGGAAGATCGCTACTGAAGCA
ATAGAAAACTTCCGAACCGTTGTTTCTTTGACTCAGGAGCAGAAGTTTGAACATATGTAT
GCTCAGAGTTTGCAGGTACCATACAGAAACTCTTTGAGGAAAGCACACATCTTTGGAATT
ACATTTTCCTTCACCCAGGCAATGATGTATTTTTCCTATGCTGGATGTTTCCGGTTTGGA
GCCTACTTGGTGGCACATAAACTCATGAGCTTTGAGGATGTTCTGTTAGTATTTTCAGCT
GTTGTCTTTGGTGCCATGGCCGTGGGGCAAGTCAGTTCATTTGCTCCTGACTATGCCAAA
GCCAAAATATCAGCAGCCCACATCATCATGATCATTGAAAAAACCCCTTTGATTGACAGC
TACAGCACGGAAGGCCTAATGCCGAACACATTGGAAGGAAATGTCACATTTGGTGAAGTT
GTATTCAACTATCCCACCCGACCGGACATCCCAGTGCTTCAGGGACTGAGCCTGGAGGTG
AAGAAGGGCCAGACGCTGGCTCTGGTGGGCAGCAGTGGCTGTGGGAAGAGCACAGTGGTC
CAGCTCCTGGAGCGGTTCTACGACCCCTTGGCAGGGAAAGTGCTGCTTGATGGCAAAGAA
ATAAAGCGACTGAATGTTCAGTGGCTCCGAGCACACCTGGGCATCGTGTCCCAGGAGCCC
ATCCTGTTTGACTGCAGCATTGCTGAGAACATTGCCTATGGAGACAACAGCCGGGTGGTG
TCACAGGAAGAGATCGTGAGGGCAGCAAAGGAGGCCAACATACATGCCTTCATCGAGTCA
CTGCCTAATAAATATAGCACTAAAGTAGGAGACAAAGGAACTCAGCTCTCTGGTGGCCAG
AAACAACGCATTGCCATAGCTCGTGCCCTTGTTAGACAGCCTCATATTTTGCTTTTGGAT
GAAGCCACGTCAGCTCTGGATACAGAAAGTGAAAAGGTTGTCCAAGAAGCCCTGGACAAA
GCCAGAGAAGGCCGCACCTGCATTGTGATTGCTCACCGCCTGTCCACCATCCAGAATGCA
GACTTAATAGTGGTGTTTCAGAATGGCAGAGTCAAGGAGCATGGCACGCATCAGCAGCTG
CTGGCACAGAAAGGCATCTATTTTTCAATGGTCAGTGTCCAGGCTGGAACAAAGCGCCAG
TGA
|
| Target 4 GenBank Gene ID |
|
| Target 4 GeneCard ID |
ABCB1  |
| Target 4 GenAtlas ID |
ABCB1  |
| Target 4 HGNC ID |
HGNC:40  |
| Target 4 Chromosome Location |
7 |
| Target 4 Locus |
7q21.1 |
| Target 4 SNPs |
SNPJam Report  |
| Target 4 General References |
- Hoffmeyer S, Burk O, von Richter O, Arnold HP, Brockmoller J, Johne A, Cascorbi I, Gerloff T, Roots I, Eichelbaum M, Brinkmann U: Functional polymorphisms of the human multidrug-resistance gene: multiple sequence variations and correlation of one allele with P-glycoprotein expression and activity in vivo. Proc Natl Acad Sci U S A. 2000 Mar 28;97(7):3473-8. [PubMed
]
- Decleves X, Chevillard S, Charpentier C, Vielh P, Laplanche JL: A new polymorphism (N21D) in the exon 2 of the human MDR1 gene encoding the P-glycoprotein. Hum Mutat. 2000 May;15(5):486. [PubMed
]
- Cascorbi I, Gerloff T, Johne A, Meisel C, Hoffmeyer S, Schwab M, Schaeffeler E, Eichelbaum M, Brinkmann U, Roots I: Frequency of single nucleotide polymorphisms in the P-glycoprotein drug transporter MDR1 gene in white subjects. Clin Pharmacol Ther. 2001 Mar;69(3):169-74. [PubMed
]
- Kerb R, Hoffmeyer S, Brinkmann U: ABC drug transporters: hereditary polymorphisms and pharmacological impact in MDR1, MRP1 and MRP2. Pharmacogenomics. 2001 Feb;2(1):51-64. [PubMed
]
- Saito S, Iida A, Sekine A, Miura Y, Ogawa C, Kawauchi S, Higuchi S, Nakamura Y: Three hundred twenty-six genetic variations in genes encoding nine members of ATP-binding cassette, subfamily B (ABCB/MDR/TAP), in the Japanese population. J Hum Genet. 2002;47(1):38-50. [PubMed
]
- Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed
]
- Chen CJ, Clark D, Ueda K, Pastan I, Gottesman MM, Roninson IB: Genomic organization of the human multidrug resistance (MDR1) gene and origin of P-glycoproteins. J Biol Chem. 1990 Jan 5;265(1):506-14. [PubMed
]
- Gekeler V, Weger S, Probst H: mdr1/P-glycoprotein gene segments analyzed from various human leukemic cell lines exhibiting different multidrug resistance profiles. Biochem Biophys Res Commun. 1990 Jun 15;169(2):796-802. [PubMed
]
- Kioka N, Tsubota J, Kakehi Y, Komano T, Gottesman MM, Pastan I, Ueda K: P-glycoprotein gene (MDR1) cDNA from human adrenal: normal P-glycoprotein carries Gly185 with an altered pattern of multidrug resistance. Biochem Biophys Res Commun. 1989 Jul 14;162(1):224-31. [PubMed
]
- Chen CJ, Chin JE, Ueda K, Clark DP, Pastan I, Gottesman MM, Roninson IB: Internal duplication and homology with bacterial transport proteins in the mdr1 (P-glycoprotein) gene from multidrug-resistant human cells. Cell. 1986 Nov 7;47(3):381-9. [PubMed
]
- 2897240 Choi KH, Chen CJ, Kriegler M, Roninson IB: An altered pattern of cross-resistance in multidrug-resistant human cells results from spontaneous mutations in the mdr1 (P-glycoprotein) gene. Cell. 1988 May 20;53(4):519-29.
- 9038218 Chen G, Duran GE, Steger KA, Lacayo NJ, Jaffrezou JP, Dumontet C, Sikic BI: Multidrug-resistant human sarcoma cells with a mutant P-glycoprotein, altered phenotype, and resistance to cyclosporins. J Biol Chem. 1997 Feb 28;272(9):5974-82.
- 9473242 Mickley LA, Lee JS, Weng Z, Zhan Z, Alvarez M, Wilson W, Bates SE, Fojo T: Genetic polymorphism in MDR-1: a tool for examining allelic expression in normal cells, unselected and drug-selected cell lines, and human tumors. Blood. 1998 Mar 1;91(5):1749-56.
|
| Target 4 Drug References |
- Kuypers DR, Verleden G, Naesens M, Vanrenterghem Y: Drug interaction between mycophenolate mofetil and rifampin: possible induction of uridine diphosphate-glucuronosyltransferase. Clin Pharmacol Ther. 2005 Jul;78(1):81-8. [PubMed
]
- Gurley BJ, Barone GW, Williams DK, Carrier J, Breen P, Yates CR, Song PF, Hubbard MA, Tong Y, Cheboyina S: Effect of milk thistle (Silybum marianum) and black cohosh (Cimicifuga racemosa) supplementation on digoxin pharmacokinetics in humans. Drug Metab Dispos. 2006 Jan;34(1):69-74. Epub 2005 Oct 12. [PubMed
]
- Chen J, Raymond K: Roles of rifampicin in drug-drug interactions: underlying molecular mechanisms involving the nuclear pregnane X receptor. Ann Clin Microbiol Antimicrob. 2006 Feb 15;5:3. [PubMed
]
- Lamba J, Strom S, Venkataramanan R, Thummel KE, Lin YS, Liu W, Cheng C, Lamba V, Watkins PB, Schuetz E: MDR1 genotype is associated with hepatic cytochrome P450 3A4 basal and induction phenotype. Clin Pharmacol Ther. 2006 Apr;79(4):325-38. Epub 2006 Feb 20. [PubMed
]
- Huang R, Murry DJ, Kolwankar D, Hall SD, Foster DR: Vincristine transcriptional regulation of efflux drug transporters in carcinoma cell lines. Biochem Pharmacol. 2006 Jun 14;71(12):1695-704. Epub 2006 Apr 18. [PubMed
]
|