Niraparib 100mg tablets
Prescription only
Requires a prescription from a doctor or prescriber
Tablet
100mg
Oral
Niraparib is an orally active poly (ADP-ribose) polymerase (PARP) inhibitor.
Active ingredients:
Niraparib
No active safety alerts
Official documents, adverse reaction reporting, and safety monitoring
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Official medicine documents
Source: MHRA Products DatabaseOGL 3.0
Updated 3 months ago(16 Jan 2026)Safety monitoring data
Yellow Card reports
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Data from the MHRA Yellow Card scheme. A reported reaction does not necessarily mean the medicine caused it. Contains public sector information licensed under the Open Government Licence v3.0.
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Similarity based on WHO Anatomical Therapeutic Chemical (ATC) classification and NHS BNF section grouping. Source data: NHS dm+d via TRUD (OGL v3.0), WHO ATC/DDD Index.
NHS prescribing volume and spending trends
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Clinical guidelines and formulary information
British National Formulary
Niraparib
BNF
Drug monograph — bnf.nice.org.ukSource: British National Formulary, NICE. Joint Formulary Committee. Contains public sector information licensed under the Open Government Licence v3.0.
NICE clinical guidance(9)
Niraparib for maintenance treatment of relapsed, platinum-sensitive ovarian, fallopian tube and peritoneal cancer (TA784)
TA784
Technology appraisal
Updated Apr 2022Niraparib for maintenance treatment of advanced ovarian, fallopian tube and peritoneal cancer after response to first-line platinum-based chemotherapy (TA1129)
TA1129
Technology appraisal
Updated Feb 2026Niraparib with abiraterone acetate and prednisone for untreated hormone-relapsed metastatic prostate cancer (terminated appraisal) (TA1032)
TA1032
Technology appraisal
Updated Jan 2025Rucaparib for maintenance treatment of relapsed platinum-sensitive ovarian, fallopian tube or peritoneal cancer (TA1007)
TA1007
Technology appraisal
Updated Sept 2024Ovarian cancer: recognition and initial management (CG122)
CG122
Clinical guideline
Updated Oct 2023Olaparib for maintenance treatment of BRCA mutation-positive advanced ovarian, fallopian tube or peritoneal cancer after response to first-line platinum-based chemotherapy (TA962)
TA962
Technology appraisal
Updated Mar 2024Rucaparib for maintenance treatment of advanced ovarian, fallopian tube and peritoneal cancer after response to first-line platinum-based chemotherapy (TA1055)
TA1055
Technology appraisal
Updated Apr 2025Olaparib with bevacizumab for maintenance treatment of advanced high-grade epithelial ovarian, fallopian tube or primary peritoneal cancer (TA946)
TA946
Technology appraisal
Updated Jan 2024Olaparib for maintenance treatment of relapsed, platinum-sensitive ovarian, fallopian tube or peritoneal cancer after 2 or more courses of platinum-based chemotherapy (TA908)
TA908
Technology appraisal
Updated Jul 2023Source: National Institute for Health and Care Excellence (NICE). Contains public sector information licensed under the Open Government Licence v3.0.
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Supply & product information
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Codes for healthcare professionals and prescribing systems
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These codes are used by healthcare IT systems and prescribers to identify this medicine.
NHS UK identifiers
Browse tools
SNOMED CT and dm+d codes from NHS TRUD (Technology Reference data Update Distribution), licensed under the Open Government Licence v3.0. BNF codes from NHS Business Services Authority (NHSBSA). ATC codes from the WHO Collaborating Centre for Drug Statistics Methodology (whocc.no).
Active and completed clinical studies from ClinicalTrials.gov
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Searching UK clinical trials...
Source: ClinicalTrials.gov, a database of the U.S. National Library of Medicine (NLM), National Institutes of Health (NIH). Data accessed via ClinicalTrials.gov API v2. Trial information is provided for research purposes and does not constitute medical advice.
Pharmacology and chemical data from DrugBank
Key facts
Drug status
Approved
Major interactions
None known
Half-life
36 hours
Mechanism
Niraparib is a potent and selective inhibitor of poly(ADP-ribose) polymerase (PARP) enzymes, PARP-1 and PARP-2.
Food interactions
2 warnings
Human targets
2 targets
Data: DrugBank · CC BY-NC 4.0
Pharmacokinetics at a glance
Absorption
300 mg
Following a single-dose administration of 300 mg niraparib, the mean (±SD) peak plasma concentration (Cmax) was 804 (±403) ng/mL.…
Half-life
300 mg
Following multiple daily doses of 300 mg of niraparib, the mean half-life (t1/2) is 36 hours.
[L43277]
[L43277]
Protein binding
83%
Niraparib is 83% bound to human plasma proteins.
[L43277]
[L43277]
Volume of distribution
074 L
The average (±SD) apparent volume of distribution (Vd/F) was 1,220 (±1,114) L.…
Metabolism
Niraparib is primarily metabolized by carboxylesterases (CEs) to form M1, which is a major inactive metabolite.…
Elimination
300-mg
Niraparib is eliminated via multiple pathways, including liver metabolism, hepatobiliary excretion, and renal elimination.
[L43747]…
[L43747]…
Clearance
16.2 L/h
In a population pharmacokinetic analysis, the apparent total clearance (CL/F) of niraparib was 16.2 L/h in patients with cancer.
[L43277]
[L43277]
Pharmacokinetic data: DrugBank · CC BY-NC 4.0
Status:
Approved
Investigational
Small molecule
About this compound
Niraparib is an orally active poly (ADP-ribose) polymerase (PARP) inhibitor. By blocking the enzymes responsible for DNA repair, niraparib induces cytotoxicity in cancer cells.[L43277] Niraparib is selective towards PARP-1 and PARP-2.[A253248] First approved by the FDA on March 27, 2017,[A253912] niraparib is used to treat epithelial ovarian, fallopian tube, or primary peritoneal cancer.[L43277] Niraparib was approved by the European Commission on November 16, 2017 [L43742] and by Health Canada on June 27, 2019.[L43747]
On December 12, 2025, the FDA expanded niraparib and abiraterone acetate (AKEEGA) with prednisone for the treatment of patients with BRCA2-mutated metastatic castration-sensitive prostate cancer (mCSPC). [L54773][L54768]
On December 12, 2025, the FDA expanded niraparib and abiraterone acetate (AKEEGA) with prednisone for the treatment of patients with BRCA2-mutated metastatic castration-sensitive prostate cancer (mCSPC). [L54773][L54768]
Properties:
solid
Avg. mass: 320.40 Da
DrugBank indication
Niraparib is indicated for the maintenance treatment of adult patients with advanced or recurrent epithelial ovarian, fallopian tube, or primary peritoneal cancer who are in complete or partial response to first-line platinum-based chemotherapy.
[L43277][L43742][L43747]
In Canada and the US, niraparib is also available in a combination product with [abiraterone], which is indicated with [prednisone] for the treatment of adults with deleterious or suspected deleterious BRCA-mutated (BRCAm) metastatic castration-resistant prostate cancer (mCRPC).
[L46896][L47755]
In Canada, this combination product is also used with [prednisolone] and is reserved for patients who are asymptomatic or mildly symptomatic, and in whom chemotherapy is not clinically indicated.
[L46896]
In the US, niraparib and abiraterone acetate with [prednisone] is also indicated for adults with deleterious or suspected deleterious BRCA2-mutated metastatic castration-sensitive prostate cancer (mCSPC).
[L54773][L54768]
[L43277][L43742][L43747]
In Canada and the US, niraparib is also available in a combination product with [abiraterone], which is indicated with [prednisone] for the treatment of adults with deleterious or suspected deleterious BRCA-mutated (BRCAm) metastatic castration-resistant prostate cancer (mCRPC).
[L46896][L47755]
In Canada, this combination product is also used with [prednisolone] and is reserved for patients who are asymptomatic or mildly symptomatic, and in whom chemotherapy is not clinically indicated.
[L46896]
In the US, niraparib and abiraterone acetate with [prednisone] is also indicated for adults with deleterious or suspected deleterious BRCA2-mutated metastatic castration-sensitive prostate cancer (mCSPC).
[L54773][L54768]
Also known as(60)
Niraparib
2.4.2.30
ADP-ribosyltransferase diphtheria toxin-like 1
ADPRT
ADPRT 1
ARTD1
DNA ADP-ribosyltransferase PARP1
NAD(+) ADP-ribosyltransferase 1
Dosage forms(10)
Tablet (Oral)
Tablet, film coated (Oral)
(Oral) — 100 mg
Capsule (Oral) — 100 mg
Capsule (Oral) — 100 mg/1
Tablet (Oral) — 100 mg
Tablet, film coated (Oral) — 100 mg
Tablet, film coated (Oral) — 100 mg/1
Molecular properties(19)
Drug interactions(38)
Known interactions with other medications. Always consult a healthcare professional.
Darbepoetin alfa
Unknown severity
The risk or severity of Thrombosis can be increased when Darbepoetin alfa is combined with Niraparib.
Erythropoietin
Unknown severity
The risk or severity of Thrombosis can be increased when Erythropoietin is combined with Niraparib.
Peginesatide
Unknown severity
The risk or severity of Thrombosis can be increased when Peginesatide is combined with Niraparib.
Methoxy polyethylene glycol-epoetin beta
Unknown severity
The risk or severity of Thrombosis can be increased when Methoxy polyethylene glycol-epoetin beta is combined with Niraparib.
The risk or severity of methemoglobinemia can be increased when Niraparib is combined with Lidocaine.
Ropivacaine
Unknown severity
The risk or severity of methemoglobinemia can be increased when Niraparib is combined with Ropivacaine.
Bupivacaine
Unknown severity
The risk or severity of methemoglobinemia can be increased when Niraparib is combined with Bupivacaine.
Cinchocaine
Unknown severity
The risk or severity of methemoglobinemia can be increased when Niraparib is combined with Cinchocaine.
The risk or severity of methemoglobinemia can be increased when Niraparib is combined with Dyclonine.
The risk or severity of methemoglobinemia can be increased when Niraparib is combined with Procaine.
Prilocaine
Unknown severity
The risk or severity of methemoglobinemia can be increased when Niraparib is combined with Prilocaine.
Proparacaine
Unknown severity
The risk or severity of methemoglobinemia can be increased when Niraparib is combined with Proparacaine.
The risk or severity of methemoglobinemia can be increased when Niraparib is combined with Meloxicam.
Oxybuprocaine
Unknown severity
The risk or severity of methemoglobinemia can be increased when Niraparib is combined with Oxybuprocaine.
The risk or severity of methemoglobinemia can be increased when Niraparib is combined with Cocaine.
Mepivacaine
Unknown severity
The risk or severity of methemoglobinemia can be increased when Niraparib is combined with Mepivacaine.
Levobupivacaine
Unknown severity
The risk or severity of methemoglobinemia can be increased when Niraparib is combined with Levobupivacaine.
Diphenhydramine
Unknown severity
The risk or severity of methemoglobinemia can be increased when Niraparib is combined with Diphenhydramine.
Benzocaine
Unknown severity
The risk or severity of methemoglobinemia can be increased when Niraparib is combined with Benzocaine.
Chloroprocaine
Unknown severity
The risk or severity of methemoglobinemia can be increased when Niraparib is combined with Chloroprocaine.
The risk or severity of methemoglobinemia can be increased when Niraparib is combined with Phenol.
Tetrodotoxin
Unknown severity
The risk or severity of methemoglobinemia can be increased when Niraparib is combined with Tetrodotoxin.
Benzyl alcohol
Unknown severity
The risk or severity of methemoglobinemia can be increased when Niraparib is combined with Benzyl alcohol.
The risk or severity of methemoglobinemia can be increased when Niraparib is combined with Capsaicin.
Etidocaine
Unknown severity
The risk or severity of methemoglobinemia can be increased when Niraparib is combined with Etidocaine.
The risk or severity of methemoglobinemia can be increased when Niraparib is combined with Articaine.
Tetracaine
Unknown severity
The risk or severity of methemoglobinemia can be increased when Niraparib is combined with Tetracaine.
Propoxycaine
Unknown severity
The risk or severity of methemoglobinemia can be increased when Niraparib is combined with Propoxycaine.
Pramocaine
Unknown severity
The risk or severity of methemoglobinemia can be increased when Niraparib is combined with Pramocaine.
The risk or severity of methemoglobinemia can be increased when Niraparib is combined with Butamben.
The risk or severity of methemoglobinemia can be increased when Niraparib is combined with Butacaine.
Oxethazaine
Unknown severity
The risk or severity of methemoglobinemia can be increased when Niraparib is combined with Oxetacaine.
Ethyl chloride
Unknown severity
The risk or severity of methemoglobinemia can be increased when Niraparib is combined with Ethyl chloride.
Butanilicaine
Unknown severity
The risk or severity of methemoglobinemia can be increased when Niraparib is combined with Butanilicaine.
Metabutethamine
Unknown severity
The risk or severity of methemoglobinemia can be increased when Niraparib is combined with Metabutethamine.
Quinisocaine
Unknown severity
The risk or severity of methemoglobinemia can be increased when Niraparib is combined with Quinisocaine.
The risk or severity of methemoglobinemia can be increased when Niraparib is combined with Ambroxol.
The risk or severity of immunosuppression can be increased when Niraparib is combined with Etrasimod.
Showing 38 of 38 interactions
Food & lifestyle interactions
Advice
Take at the same time every day.
Advice
Take with or without food. Food does not affect the absorption of niraparib.
Toxicity & overdose
There is limited information available regarding the acute toxicity profile and overdosage of niraparib.
How it works
Mechanism of action
Niraparib is a potent and selective inhibitor of poly(ADP-ribose) polymerase (PARP) enzymes, PARP-1 and PARP-2.[L43742][L43747] PARPs play an important role in DNA repair. They recognize and repair cellular DNA damage, such as single-strand breaks (SSBs) and double-strand breaks (DSBs). Different DNA repair pathways exist to repair these DNA damages, including the base excision repair (BER) pathway for SSBs and BRCA-dependent homologous recombination for DSBs.[A245985] If BER is impaired, SSBs accumulate and become DSBs, forcing cells to rely on other repair pathways, mainly the homologous recombination (HR) and the nonhomologous end joining, to repair DNA damages.[A18877] However, some cells can have defective or deficient HR resulting from specific mutations in DNA repair genes, such as BRCA1 and 2.[A253248] Inhibiting PARPs in the presence of HR deficiency leads to a phenomenon called 'synthetic lethality,' whereby the PARP inhibitor impedes BER, leading to genetic instability and cell death.[A18877][A253248]
Selectivity towards PARP-1 and PARP-2 is 100-fold higher than for other PARP family members.[A253248] Niraparib-induced cytotoxicity may involve inhibition of PARP enzymatic activity and increased formation of PARP-DNA complexes resulting in DNA damage, apoptosis, and cell death.[L43277][L43742][L43747]
Selectivity towards PARP-1 and PARP-2 is 100-fold higher than for other PARP family members.[A253248] Niraparib-induced cytotoxicity may involve inhibition of PARP enzymatic activity and increased formation of PARP-DNA complexes resulting in DNA damage, apoptosis, and cell death.[L43277][L43742][L43747]
Pharmacodynamics
Niraparib mediated cytotoxic effects in tumour cell lines with or without deficiencies in BRCA1/2. Decreased tumour growth was observed in both mouse xenograft models of human cancer cell lines with deficiencies in BRCA1/2 and human patient-derived xenograft tumour models with homologous recombination deficiency (HRD) that had either mutated or wild-type BRCA1/2.[L43277]
In vitro studies suggest that niraparib inhibits dopamine, norepinephrine, and serotonin transporters, which may explain its off-target cardiovascular effects such as increased pulse rate and blood pressure.[A253248]
In vitro studies suggest that niraparib inhibits dopamine, norepinephrine, and serotonin transporters, which may explain its off-target cardiovascular effects such as increased pulse rate and blood pressure.[A253248]
Pharmacokinetics
How the body processes this drug — absorption, distribution, metabolism, and elimination
Absorption
Following a single-dose administration of 300 mg niraparib, the mean (±SD) peak plasma concentration (Cmax) was 804 (±403) ng/mL. The exposure (Cmax and AUC) of niraparib increased in a dose-proportional manner with daily doses ranging from 30 mg (0.1 times the approved recommended dose) to 400 mg (1.3 times the approved recommended dose). The accumulation ratio of niraparib exposure following 21 days of repeated daily doses was approximately 2-fold for doses ranging from 30 to 400 mg.
The Tmax is about three hours.
[L43277]
The absolute bioavailability of niraparib is approximately 73%. Food does not appear to affect drug exposure.
[L43277]
The Tmax is about three hours.
[L43277]
The absolute bioavailability of niraparib is approximately 73%. Food does not appear to affect drug exposure.
[L43277]
Half-life
Following multiple daily doses of 300 mg of niraparib, the mean half-life (t1/2) is 36 hours.
[L43277]
[L43277]
Protein binding
Niraparib is 83% bound to human plasma proteins.
[L43277]
[L43277]
Volume of distribution
The average (±SD) apparent volume of distribution (Vd/F) was 1,220 (±1,114) L. In a population pharmacokinetic analysis, the Vd/F of niraparib was 1,074 L in patients with cancer.
[L43277]
[L43277]
Metabolism
Niraparib is primarily metabolized by carboxylesterases (CEs) to form M1, which is a major inactive metabolite. The M1 metabolite can subsequently undergo glucuronidation mediated by UDP-glucuronosyltransferases (UGTs) to form the M10 metabolite.
[L43277]
In a mass balance study, M1 and M10 were the major circulating metabolites.
[L43742]
The M1 metabolite can also undergo methylation, monooxygenation, and hydrogenation to form other minor metabolites.
[A253937]
[L43277]
In a mass balance study, M1 and M10 were the major circulating metabolites.
[L43742]
The M1 metabolite can also undergo methylation, monooxygenation, and hydrogenation to form other minor metabolites.
[A253937]
Route of elimination
Niraparib is eliminated via multiple pathways, including liver metabolism, hepatobiliary excretion, and renal elimination.
[L43747]
Following administration of a single oral 300-mg dose of radio-labeled niraparib, the average percent recovery of the administered dose over 21 days was 47.5% (range: 33.4% to 60.2%) in urine and 38.8% (range: 28.3% to 47.0%) in feces. In pooled samples collected over 6 days, unchanged niraparib accounted for 11% and 19% of the administered dose recovered in urine and feces, respectively.
[L43277]
[L43747]
Following administration of a single oral 300-mg dose of radio-labeled niraparib, the average percent recovery of the administered dose over 21 days was 47.5% (range: 33.4% to 60.2%) in urine and 38.8% (range: 28.3% to 47.0%) in feces. In pooled samples collected over 6 days, unchanged niraparib accounted for 11% and 19% of the administered dose recovered in urine and feces, respectively.
[L43277]
Clearance
In a population pharmacokinetic analysis, the apparent total clearance (CL/F) of niraparib was 16.2 L/h in patients with cancer.
[L43277]
[L43277]
Drug targets(2)
Proteins and enzymes this drug interacts with in the body
Poly [ADP-ribose] polymerase 1
PARP1
inhibitor
Specific functionchromatin binding
Cellular location
Chromosome
General function & pharmacology
Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair .
PMID:17177976 PMID:18055453 PMID:18172500 PMID:19344625 PMID:19661379 PMID:20388712 PMID:21680843 PMID:22582261 PMID:23230272 PMID:25043379 PMID:26344098 PMID:26626479 PMID:26626480 PMID:30104678 PMID:31796734 PMID:32028527 PMID:32241924 PMID:32358582 PMID:33186521 PMID:34465625 PMID:34737271
Mediates glutamate, aspartate, serine, histidine or tyrosine ADP-ribosylation of proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of target residues and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units .
PMID:19764761 PMID:25043379 PMID:28190768 PMID:29954836 PMID:35393539 PMID:7852410 PMID:9315851
Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage .
PMID:33186521 PMID:34874266
Specificity for the different amino acids is conferred by interacting factors, such as HPF1 and NMNAT1 .
PMID:28190768 PMID:29954836 PMID:32028527 PMID:33186521 PMID:33589610 PMID:34625544 PMID:34874266
Following interaction with HPF1, catalyzes serine ADP-ribosylation of target proteins; HPF1 confers serine specificity by completing the PARP1 active site .
PMID:28190768 PMID:29954836 PMID:32028527 PMID:33186521 PMID:33589610 PMID:34625544 PMID:34874266
Also catalyzes tyrosine ADP-ribosylation of target proteins following interaction with HPF1 .
PMID:29954836 PMID:30257210
Following interaction with NMNAT1, catalyzes glutamate and aspartate ADP-ribosylation of target proteins; NMNAT1 confers glutamate and aspartate specificity (By similarity). PARP1 initiates the repair of DNA breaks: recognizes and binds DNA breaks within chromatin and recruits HPF1, licensing serine ADP-ribosylation of target proteins, such as histones (H2BS6ADPr and H3S10ADPr), thereby promoting decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks .
PMID:17177976 PMID:18172500 PMID:19344625 PMID:19661379 PMID:23230272 PMID:27067600 PMID:34465625 PMID:34874266
HPF1 initiates serine ADP-ribosylation but restricts the polymerase activity of PARP1 in order to limit the length of poly-ADP-ribose chains .
PMID:33683197 PMID:34732825 PMID:34795260
In addition to base excision repair (BER) pathway, also involved in double-strand breaks (DSBs) repair: together with TIMELESS, accumulates at DNA damage sites and promotes homologous recombination repair by mediating poly-ADP-ribosylation .
PMID:26344098 PMID:30356214
Mediates the poly-ADP-ribosylation of a number of proteins, including itself, APLF, CHFR, RPA1 and NFAT5 .
PMID:17396150 PMID:19764761 PMID:24906880 PMID:34049076
In addition to proteins, also able to ADP-ribosylate DNA: catalyzes ADP-ribosylation of DNA strand break termini containing terminal phosphates and a 2'-OH group in single- and double-stranded DNA, respectively .
PMID:27471034
Required for PARP9 and DTX3L recruitment to DNA damage sites .
PMID:23230272
PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites .
PMID:23230272
PARP1-mediated DNA repair in neurons plays a role in sleep: senses DNA damage in neurons and promotes sleep, facilitating efficient DNA repair (By similarity). In addition to DNA repair, also involved in other processes, such as transcription regulation, programmed cell death, membrane repair, adipogenesis and innate immunity .
PMID:15607977 PMID:17177976 PMID:19344625 PMID:27256882 PMID:32315358 PMID:32844745 PMID:35124853 PMID:35393539 PMID:35460603
Acts as a repressor of transcription: binds to nucleosomes and modulates chromatin structure in a manner similar to histone H1, thereby altering RNA polymerase II .
PMID:15607977 PMID:22464733
Acts both as a positive and negative regulator of transcription elongation, depending on the context .
PMID:27256882 PMID:35393539
Acts as a positive regulator of transcription elongation by mediating poly-ADP-ribosylation of NELFE, preventing RNA-binding activity of NELFE and relieving transcription pausing .
PMID:27256882
Acts as a negative regulator of transcription elongation in response to DNA damage by catalyzing poly-ADP-ribosylation of CCNT1, disrupting the phase separation activity of CCNT1 and subsequent activation of CDK9 .
PMID:35393539
Involved in replication fork progression following interaction with CARM1: mediates poly-ADP-ribosylation at replication forks, slowing fork progression .
PMID:33412112
Poly-ADP-ribose chains generated by PARP1 also play a role in poly-ADP-ribose-dependent cell death, a process named parthanatos (By similarity).
Also acts as a negative regulator of the cGAS-STING pathway .
PMID:32315358 PMID:32844745 PMID:35460603
Acts by mediating poly-ADP-ribosylation of CGAS: PARP1 translocates into the cytosol following phosphorylation by PRKDC and catalyzes poly-ADP-ribosylation and inactivation of CGAS .
PMID:35460603
Acts as a negative regulator of adipogenesis: catalyzes poly-ADP-ribosylation of histone H2B on 'Glu-35' (H2BE35ADPr) following interaction with NMNAT1, inhibiting phosphorylation of H2B at 'Ser-36' (H2BS36ph), thereby blocking expression of pro-adipogenetic genes (By similarity). Involved in the synthesis of ATP in the nucleus, together with NMNAT1, PARG and NUDT5 .
PMID:27257257
Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming PMID:27257257
PMID:17177976 PMID:18055453 PMID:18172500 PMID:19344625 PMID:19661379 PMID:20388712 PMID:21680843 PMID:22582261 PMID:23230272 PMID:25043379 PMID:26344098 PMID:26626479 PMID:26626480 PMID:30104678 PMID:31796734 PMID:32028527 PMID:32241924 PMID:32358582 PMID:33186521 PMID:34465625 PMID:34737271
Mediates glutamate, aspartate, serine, histidine or tyrosine ADP-ribosylation of proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of target residues and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units .
PMID:19764761 PMID:25043379 PMID:28190768 PMID:29954836 PMID:35393539 PMID:7852410 PMID:9315851
Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage .
PMID:33186521 PMID:34874266
Specificity for the different amino acids is conferred by interacting factors, such as HPF1 and NMNAT1 .
PMID:28190768 PMID:29954836 PMID:32028527 PMID:33186521 PMID:33589610 PMID:34625544 PMID:34874266
Following interaction with HPF1, catalyzes serine ADP-ribosylation of target proteins; HPF1 confers serine specificity by completing the PARP1 active site .
PMID:28190768 PMID:29954836 PMID:32028527 PMID:33186521 PMID:33589610 PMID:34625544 PMID:34874266
Also catalyzes tyrosine ADP-ribosylation of target proteins following interaction with HPF1 .
PMID:29954836 PMID:30257210
Following interaction with NMNAT1, catalyzes glutamate and aspartate ADP-ribosylation of target proteins; NMNAT1 confers glutamate and aspartate specificity (By similarity). PARP1 initiates the repair of DNA breaks: recognizes and binds DNA breaks within chromatin and recruits HPF1, licensing serine ADP-ribosylation of target proteins, such as histones (H2BS6ADPr and H3S10ADPr), thereby promoting decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks .
PMID:17177976 PMID:18172500 PMID:19344625 PMID:19661379 PMID:23230272 PMID:27067600 PMID:34465625 PMID:34874266
HPF1 initiates serine ADP-ribosylation but restricts the polymerase activity of PARP1 in order to limit the length of poly-ADP-ribose chains .
PMID:33683197 PMID:34732825 PMID:34795260
In addition to base excision repair (BER) pathway, also involved in double-strand breaks (DSBs) repair: together with TIMELESS, accumulates at DNA damage sites and promotes homologous recombination repair by mediating poly-ADP-ribosylation .
PMID:26344098 PMID:30356214
Mediates the poly-ADP-ribosylation of a number of proteins, including itself, APLF, CHFR, RPA1 and NFAT5 .
PMID:17396150 PMID:19764761 PMID:24906880 PMID:34049076
In addition to proteins, also able to ADP-ribosylate DNA: catalyzes ADP-ribosylation of DNA strand break termini containing terminal phosphates and a 2'-OH group in single- and double-stranded DNA, respectively .
PMID:27471034
Required for PARP9 and DTX3L recruitment to DNA damage sites .
PMID:23230272
PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites .
PMID:23230272
PARP1-mediated DNA repair in neurons plays a role in sleep: senses DNA damage in neurons and promotes sleep, facilitating efficient DNA repair (By similarity). In addition to DNA repair, also involved in other processes, such as transcription regulation, programmed cell death, membrane repair, adipogenesis and innate immunity .
PMID:15607977 PMID:17177976 PMID:19344625 PMID:27256882 PMID:32315358 PMID:32844745 PMID:35124853 PMID:35393539 PMID:35460603
Acts as a repressor of transcription: binds to nucleosomes and modulates chromatin structure in a manner similar to histone H1, thereby altering RNA polymerase II .
PMID:15607977 PMID:22464733
Acts both as a positive and negative regulator of transcription elongation, depending on the context .
PMID:27256882 PMID:35393539
Acts as a positive regulator of transcription elongation by mediating poly-ADP-ribosylation of NELFE, preventing RNA-binding activity of NELFE and relieving transcription pausing .
PMID:27256882
Acts as a negative regulator of transcription elongation in response to DNA damage by catalyzing poly-ADP-ribosylation of CCNT1, disrupting the phase separation activity of CCNT1 and subsequent activation of CDK9 .
PMID:35393539
Involved in replication fork progression following interaction with CARM1: mediates poly-ADP-ribosylation at replication forks, slowing fork progression .
PMID:33412112
Poly-ADP-ribose chains generated by PARP1 also play a role in poly-ADP-ribose-dependent cell death, a process named parthanatos (By similarity).
Also acts as a negative regulator of the cGAS-STING pathway .
PMID:32315358 PMID:32844745 PMID:35460603
Acts by mediating poly-ADP-ribosylation of CGAS: PARP1 translocates into the cytosol following phosphorylation by PRKDC and catalyzes poly-ADP-ribosylation and inactivation of CGAS .
PMID:35460603
Acts as a negative regulator of adipogenesis: catalyzes poly-ADP-ribosylation of histone H2B on 'Glu-35' (H2BE35ADPr) following interaction with NMNAT1, inhibiting phosphorylation of H2B at 'Ser-36' (H2BS36ph), thereby blocking expression of pro-adipogenetic genes (By similarity). Involved in the synthesis of ATP in the nucleus, together with NMNAT1, PARG and NUDT5 .
PMID:27257257
Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming PMID:27257257
Poly [ADP-ribose] polymerase 2
PARP2
inhibitor
Specific functionchromatin binding
Cellular location
Nucleus
General function & pharmacology
Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair .
PMID:10364231 PMID:25043379 PMID:27471034 PMID:30104678 PMID:32028527 PMID:32939087 PMID:34108479 PMID:34486521 PMID:34874266
Mediates glutamate, aspartate or serine ADP-ribosylation of proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of target residues and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units .
PMID:25043379 PMID:30104678 PMID:30321391
Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage .
PMID:32939087
Mediates glutamate and aspartate ADP-ribosylation of target proteins in absence of HPF1 .
PMID:25043379
Following interaction with HPF1, catalyzes serine ADP-ribosylation of target proteins; HPF1 conferring serine specificity by completing the PARP2 active site .
PMID:28190768 PMID:32028527 PMID:34108479 PMID:34486521 PMID:34874266
PARP2 initiates the repair of double-strand DNA breaks: recognizes and binds DNA breaks within chromatin and recruits HPF1, licensing serine ADP-ribosylation of target proteins, such as histones, thereby promoting decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks .
PMID:10364231 PMID:32939087 PMID:34108479
HPF1 initiates serine ADP-ribosylation but restricts the polymerase activity of PARP2 in order to limit the length of poly-ADP-ribose chains .
PMID:34732825 PMID:34795260
Specifically mediates formation of branched poly-ADP-ribosylation .
PMID:30104678
Branched poly-ADP-ribose chains are specifically recognized by some factors, such as APLF .
PMID:30104678
In addition to proteins, also able to ADP-ribosylate DNA: preferentially acts on 5'-terminal phosphates at DNA strand breaks termini in nicked duplex PMID:27471034 PMID:29361132
PMID:10364231 PMID:25043379 PMID:27471034 PMID:30104678 PMID:32028527 PMID:32939087 PMID:34108479 PMID:34486521 PMID:34874266
Mediates glutamate, aspartate or serine ADP-ribosylation of proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of target residues and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units .
PMID:25043379 PMID:30104678 PMID:30321391
Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage .
PMID:32939087
Mediates glutamate and aspartate ADP-ribosylation of target proteins in absence of HPF1 .
PMID:25043379
Following interaction with HPF1, catalyzes serine ADP-ribosylation of target proteins; HPF1 conferring serine specificity by completing the PARP2 active site .
PMID:28190768 PMID:32028527 PMID:34108479 PMID:34486521 PMID:34874266
PARP2 initiates the repair of double-strand DNA breaks: recognizes and binds DNA breaks within chromatin and recruits HPF1, licensing serine ADP-ribosylation of target proteins, such as histones, thereby promoting decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks .
PMID:10364231 PMID:32939087 PMID:34108479
HPF1 initiates serine ADP-ribosylation but restricts the polymerase activity of PARP2 in order to limit the length of poly-ADP-ribose chains .
PMID:34732825 PMID:34795260
Specifically mediates formation of branched poly-ADP-ribosylation .
PMID:30104678
Branched poly-ADP-ribose chains are specifically recognized by some factors, such as APLF .
PMID:30104678
In addition to proteins, also able to ADP-ribosylate DNA: preferentially acts on 5'-terminal phosphates at DNA strand breaks termini in nicked duplex PMID:27471034 PMID:29361132
Metabolizing enzymes(2)
Enzymes involved in drug metabolism — important for understanding drug interactions
Enzyme activity key
substrate
inhibitor
inducer
CES1A1aCarboxylesterase
substrate
CYP1A2Cytochrome P450 1A2
inducer
Transporters(4)
Proteins that transport this drug across cell membranes
Broad substrate specificity ATP-binding cassette transporter ABCG2
ABCG2
substrate
inhibitor
Specific functionABC-type xenobiotic transporter activity
Cellular location
Cell membrane
General function & pharmacology
Broad substrate specificity ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes a wide variety of physiological compounds, dietary toxins and xenobiotics from cells .
PMID:11306452 PMID:12958161 PMID:19506252 PMID:20705604 PMID:28554189 PMID:30405239 PMID:31003562
Involved in porphyrin homeostasis, mediating the export of protoporphyrin IX (PPIX) from both mitochondria to cytosol and cytosol to extracellular space, it also functions in the cellular export of heme .
PMID:20705604 PMID:23189181
Also mediates the efflux of sphingosine-1-P from cells .
PMID:20110355
Acts as a urate exporter functioning in both renal and extrarenal urate excretion .
PMID:19506252 PMID:20368174 PMID:22132962 PMID:31003562 PMID:36749388
In kidney, it also functions as a physiological exporter of the uremic toxin indoxyl sulfate (By similarity). Also involved in the excretion of steroids like estrone 3-sulfate/E1S, 3beta-sulfooxy-androst-5-en-17-one/DHEAS, and other sulfate conjugates .
PMID:12682043 PMID:28554189 PMID:30405239
Mediates the secretion of the riboflavin and biotin vitamins into milk (By similarity). Extrudes pheophorbide a, a phototoxic porphyrin catabolite of chlorophyll, reducing its bioavailability (By similarity).
Plays an important role in the exclusion of xenobiotics from the brain (Probable). It confers to cells a resistance to multiple drugs and other xenobiotics including mitoxantrone, pheophorbide, camptothecin, methotrexate, azidothymidine, and the anthracyclines daunorubicin and doxorubicin, through the control of their efflux .
PMID:11306452 PMID:12477054 PMID:15670731 PMID:18056989 PMID:31254042
In placenta, it limits the penetration of drugs from the maternal plasma into the fetus (By similarity). May play a role in early stem cell self-renewal by blocking differentiation (By similarity).
In inflammatory macrophages, exports itaconate from the cytosol to the extracellular compartment and limits the activation of TFEB-dependent lysosome biogenesis involved in antibacterial innate immune response
PMID:11306452 PMID:12958161 PMID:19506252 PMID:20705604 PMID:28554189 PMID:30405239 PMID:31003562
Involved in porphyrin homeostasis, mediating the export of protoporphyrin IX (PPIX) from both mitochondria to cytosol and cytosol to extracellular space, it also functions in the cellular export of heme .
PMID:20705604 PMID:23189181
Also mediates the efflux of sphingosine-1-P from cells .
PMID:20110355
Acts as a urate exporter functioning in both renal and extrarenal urate excretion .
PMID:19506252 PMID:20368174 PMID:22132962 PMID:31003562 PMID:36749388
In kidney, it also functions as a physiological exporter of the uremic toxin indoxyl sulfate (By similarity). Also involved in the excretion of steroids like estrone 3-sulfate/E1S, 3beta-sulfooxy-androst-5-en-17-one/DHEAS, and other sulfate conjugates .
PMID:12682043 PMID:28554189 PMID:30405239
Mediates the secretion of the riboflavin and biotin vitamins into milk (By similarity). Extrudes pheophorbide a, a phototoxic porphyrin catabolite of chlorophyll, reducing its bioavailability (By similarity).
Plays an important role in the exclusion of xenobiotics from the brain (Probable). It confers to cells a resistance to multiple drugs and other xenobiotics including mitoxantrone, pheophorbide, camptothecin, methotrexate, azidothymidine, and the anthracyclines daunorubicin and doxorubicin, through the control of their efflux .
PMID:11306452 PMID:12477054 PMID:15670731 PMID:18056989 PMID:31254042
In placenta, it limits the penetration of drugs from the maternal plasma into the fetus (By similarity). May play a role in early stem cell self-renewal by blocking differentiation (By similarity).
In inflammatory macrophages, exports itaconate from the cytosol to the extracellular compartment and limits the activation of TFEB-dependent lysosome biogenesis involved in antibacterial innate immune response
Multidrug and toxin extrusion protein 1
SLC47A1
substrate
inhibitor
Specific functionantiporter activity
Cellular location
Cell membrane
General function & pharmacology
Multidrug efflux pump that functions as a H(+)/organic cation antiporter .
PMID:16330770 PMID:17509534
Plays a physiological role in the excretion of cationic compounds including endogenous metabolites, drugs, toxins through the kidney and liver, into urine and bile respectively .
PMID:16330770 PMID:17495125 PMID:17509534 PMID:17582384 PMID:18305230 PMID:19158817 PMID:21128598 PMID:24961373
Mediates the efflux of endogenous compounds such as creatinine, vitamin B1/thiamine, agmatine and estrone-3-sulfate .
PMID:16330770 PMID:17495125 PMID:17509534 PMID:17582384 PMID:18305230 PMID:19158817 PMID:21128598 PMID:24961373
May also contribute to regulate the transport of cationic compounds in testis across the blood-testis-barrier (Probable)
PMID:16330770 PMID:17509534
Plays a physiological role in the excretion of cationic compounds including endogenous metabolites, drugs, toxins through the kidney and liver, into urine and bile respectively .
PMID:16330770 PMID:17495125 PMID:17509534 PMID:17582384 PMID:18305230 PMID:19158817 PMID:21128598 PMID:24961373
Mediates the efflux of endogenous compounds such as creatinine, vitamin B1/thiamine, agmatine and estrone-3-sulfate .
PMID:16330770 PMID:17495125 PMID:17509534 PMID:17582384 PMID:18305230 PMID:19158817 PMID:21128598 PMID:24961373
May also contribute to regulate the transport of cationic compounds in testis across the blood-testis-barrier (Probable)
Multidrug and toxin extrusion protein 2
SLC47A2
substrate
inhibitor
Specific functionantiporter activity
Cellular location
Cell membrane
General function & pharmacology
Multidrug efflux pump that functions as a H(+)/organic cation antiporter. Mediates the efflux of cationic compounds, such as the model cations, tetraethylammonium (TEA) and 1-methyl-4-phenylpyridinium (MPP+), the platinum-based drug oxaliplatin or weak bases that are positively charged at physiological pH, cimetidine, the platinum-based drugs cisplatin and oxaliplatin or the antidiabetic drug metformin. Mediates the efflux of endogenous compounds such as, creatinine, thiamine and estrone-3-sulfate.
Plays a physiological role in the excretion of drugs, toxins and endogenous metabolites through the kidney
Plays a physiological role in the excretion of drugs, toxins and endogenous metabolites through the kidney
ATP-dependent translocase ABCB1
ABCB1
substrate
Specific functionABC-type xenobiotic transporter activity
Cellular location
Cell membrane
General function & pharmacology
Translocates drugs and phospholipids across the membrane .
PMID:2897240 PMID:35970996 PMID:8898203 PMID:9038218 PMID:35507548
Catalyzes the flop of phospholipids from the cytoplasmic to the exoplasmic leaflet of the apical membrane. Participates mainly to the flop of phosphatidylcholine, phosphatidylethanolamine, beta-D-glucosylceramides and sphingomyelins .
PMID:8898203
Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells PMID:2897240 PMID:35970996 PMID:9038218
PMID:2897240 PMID:35970996 PMID:8898203 PMID:9038218 PMID:35507548
Catalyzes the flop of phospholipids from the cytoplasmic to the exoplasmic leaflet of the apical membrane. Participates mainly to the flop of phosphatidylcholine, phosphatidylethanolamine, beta-D-glucosylceramides and sphingomyelins .
PMID:8898203
Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells PMID:2897240 PMID:35970996 PMID:9038218
Carriers(1)
Proteins that carry this drug through the body
Albumin
ALB
binder
Specific functionantioxidant activity
Cellular location
Secreted
General function & pharmacology
Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs (Probable). Its main function is the regulation of the colloidal osmotic pressure of blood (Probable). Major zinc transporter in plasma, typically binds about 80% of all plasma zinc .
PMID:19021548
Major calcium and magnesium transporter in plasma, binds approximately 45% of circulating calcium and magnesium in plasma (By similarity).
Potentially has more than two calcium-binding sites and might additionally bind calcium in a non-specific manner (By similarity). The shared binding site between zinc and calcium at residue Asp-273 suggests a crosstalk between zinc and calcium transport in the blood (By similarity). The rank order of affinity is zinc > calcium > magnesium (By similarity).
Binds to the bacterial siderophore enterobactin and inhibits enterobactin-mediated iron uptake of E.coli from ferric transferrin, and may thereby limit the utilization of iron and growth of enteric bacteria such as E.coli .
PMID:6234017
Does not prevent iron uptake by the bacterial siderophore aerobactin PMID:6234017
PMID:19021548
Major calcium and magnesium transporter in plasma, binds approximately 45% of circulating calcium and magnesium in plasma (By similarity).
Potentially has more than two calcium-binding sites and might additionally bind calcium in a non-specific manner (By similarity). The shared binding site between zinc and calcium at residue Asp-273 suggests a crosstalk between zinc and calcium transport in the blood (By similarity). The rank order of affinity is zinc > calcium > magnesium (By similarity).
Binds to the bacterial siderophore enterobactin and inhibits enterobactin-mediated iron uptake of E.coli from ferric transferrin, and may thereby limit the utilization of iron and growth of enteric bacteria such as E.coli .
PMID:6234017
Does not prevent iron uptake by the bacterial siderophore aerobactin PMID:6234017
Scientific references(5)
Chen A.
PARP inhibitors: its role in treatment of cancer.
Chin Journal Cancer
2011 Jul30(7):463-71. doi: 10.5732/cjc.011.10111
Heo Y.A., Duggan S.T.
Niraparib: A Review in Ovarian Cancer.
Target Oncology
2018 Aug13(4):533-539. doi: 10.1007/s11523-018-0582-1
Ison G., Howie L.J., Amiri-Kordestani L., Zhang L., Tang S., Sridhara R., Pierre V., Charlab R., Ramamoorthy A., Song P., Li F., Yu J., Manheng W., Palmby T.R., Ghosh S., Horne H.N., Lee E.Y., Philip R., Dave K., Chen X.H., Kelly S.L., Janoria K.G., Banerjee A., Eradiri O., Dinin J., Goldberg K.B., Pierce W.F., Ibrahim A., Kluetz P.G., Blumenthal G.M., Beaver J.A., Pazdur R.
FDA Approval Summary: Niraparib for the Maintenance Treatment of Patients with Recurrent Ovarian Cancer in Response to Platinum-Based Chemotherapy.
Clinical Cancer Research
2018 Sep 124(17):4066-4071. doi: 10.1158/1078-0432.CCR-18-0042. Epub 2018 Apr 12
Bochum S., Berger S., Martens U.M.
Olaparib.
Recent Results Cancer Research
2018211:217-233. doi: 10.1007/978-3-319-91442-8_15
van Andel L., Zhang Z., Lu S., Kansra V., Agarwal S., Hughes L., Tibben M.M., Gebretensae A., Lucas L., Hillebrand M.J.X., Rosing H., Schellens J.H.M., Beijnen J.H.
Human mass balance study and metabolite profiling of (14)C-niraparib, a novel poly(ADP-Ribose) polymerase (PARP)-1 and PARP-2 inhibitor, in patients with advanced cancer.
Invest New Drugs
2017 Dec35(6):751-765. doi: 10.1007/s10637-017-0451-2. Epub 2017 Mar 16
ATC classification(2 codes)
ATC L01XK02
ATC L01XK52
Affected organisms(1)
Humans and other mammals
Salt forms(3)
Niraparib hydrochloride(DBSALT002076)
Niraparib tosylate(DBSALT002589)
Niraparib tosylate monohydrate(DBSALT002590)
Experimental properties(1)
Commercial products(19)
Chemical identifiers
CAS, UNII, InChI Key and database cross-references
Show
Chemical identifiers
CAS, UNII, InChI Key and database cross-references
Linked compound data from DrugBank Open Data (CC BY-NC 4.0)
Niraparib
Additional database identifiers
Drugs Product Database (DPD)
23270
ChemSpider
24531930
BindingDB
50316226
PDB
3JD
ZINC
ZINC000043206370
HUGO Gene Nomenclature Committee (HGNC)
HGNC:270
GenAtlas
PARP1
GeneCards
PARP1
GenBank Gene Database
X16674
GenBank Protein Database
1017423
Guide to Pharmacology
2771
UniProt Accession
PARP1_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:272
GeneCards
PARP2
GenBank Gene Database
AJ236912
GenBank Protein Database
6688130
Guide to Pharmacology
2772
UniProt Accession
PARP2_HUMAN
UniProt Accession
Q6LAP9_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:2596
GenAtlas
CYP1A2
GeneCards
CYP1A2
GenBank Gene Database
Z00036
Guide to Pharmacology
1319
UniProt Accession
CP1A2_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:399
GenAtlas
ALB
GeneCards
ALB
GenBank Gene Database
V00494
GenBank Protein Database
28590
UniProt Accession
ALBU_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:74
GenAtlas
ABCG2
GeneCards
ABCG2
GenBank Gene Database
AF103796
GenBank Protein Database
4185796
Guide to Pharmacology
792
UniProt Accession
ABCG2_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:25588
GeneCards
SLC47A1
GenBank Gene Database
AK001709
GenBank Protein Database
7023138
Guide to Pharmacology
1216
UniProt Accession
S47A1_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:26439
GeneCards
SLC47A2
Guide to Pharmacology
1217
UniProt Accession
S47A2_HUMAN
HUGO Gene Nomenclature Committee (HGNC)
HGNC:40
GenAtlas
ABCB1
GeneCards
ABCB1
GenBank Gene Database
M14758
GenBank Protein Database
307180
Guide to Pharmacology
768
UniProt Accession
MDR1_HUMAN
Patent information
13 active patents
11730725
United States
Approved 22 Aug 2023 · Expires 4 Jan 2039
12y 9m
11091459
United States
Approved 17 Aug 2021 · Expires 27 Mar 2038
11y 12m
11673877
United States
Approved 13 Jun 2023 · Expires 27 Mar 2038
11y 12m
11207311
United States
Approved 28 Dec 2021 · Expires 28 Jul 2037
11y 3m
11992486
United States
Approved 28 May 2024 · Expires 28 Jul 2037
11y 3m
The earliest active patent expires August 2027. Generic versions may become available after this date.
Source: DrugBank · CC BY-NC 4.0. Patent data sourced from national patent offices. Expiry dates may not reflect extensions, regulatory exclusivity periods, or legal challenges.
DrugBank citations
If you use DrugBank data in your research, please cite the following publications:
Knox C., Wilson M., Klinger C.M., et al
DrugBank 6.
0: the DrugBank Knowledgebase for 2024
Nucleic Acids Res. 2024 Jan 552(D1):D1265-D1275
Wishart D.S., Feunang Y.D., Guo A.C., et al
DrugBank 5.
0: a major update to the DrugBank database for 2018
Nucleic Acids Res. 2017 Nov 846(D1):D1074-D1082
Show earlier publications
Law V., Knox C., Djoumbou Y., et al
DrugBank 4.
0: shedding new light on drug metabolism
Nucleic Acids Res. 2014 Jan 142(1):D1091-7
Knox C., Law V., Jewison T., et al
DrugBank 3.
0: a comprehensive resource for 'omics' research on drugs
Nucleic Acids Res. 2011 Jan39(Database issue):D1035-41
Wishart D.S., Knox C., Guo A.C., et al
DrugBank: a knowledgebase for drugs, drug actions and drug targets.
Nucleic Acids Research
2008 Jan36(Database issue):D901-6
Wishart D.S., Knox C., Guo A.C., et al
DrugBank: a comprehensive resource for in silico drug discovery and exploration.
Nucleic Acids Research
2006 Jan 134(Database issue):D668-72
Source: go.drugbank.comCC BY-NC 4.0
Updated 30 days ago(4 Mar 2026)