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Information on EC 7.6.2.2 - ABC-type xenobiotic transporter and Organism(s) Mus musculus and UniProt Accession P21447
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7.6.2.2 ABC-type xenobiotic transporterIUBMB Comments
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. The enzymes from Gram-positive bacteria and eukaryotic cells export a number of drugs with unusual specificity, covering various groups of unrelated substances while ignoring some that are closely related structurally. Several distinct enzymes may be present in a single eukaryotic cell. Many of them also transport glutathione---drug conjugates (see EC 7.6.2.3, ABC-type glutathione-S-conjugate transporter) while others also show some 'flippase' activity (cf. EC 7.6.2.1, P-type phospholipid transporter).
Specify your search results
Word Map
- 7.6.2.2
- verapamil
- doxorubicin
-
multidrug-resistant
-
blood-brain
- leukemia
-
cyclosporine
-
drug-resistant
- cholesterol
- xenobiotics
- rhodamine
-
disposition
- endothelial
- vincristine
-
caco-2
- paclitaxel
- cyp3a4
- vinblastine
-
chemosensitivity
- monolayers
-
chemoresistance
-
drug-drug
- cisplatin
- daunorubicin
- biliary
- etoposide
- adriamycin
-
pharmacodynamics
-
reversing
-
cross-resistance
-
basolateral
-
multi-drug
- anthracyclines
- digoxin
-
concentration-time
-
extrude
-
sublines
-
topoisomerase
- colchicine
-
pharmacogenetic
- docetaxel
- tacrolimus
- glucuronide
- hepatobiliary
- cyp2d6
-
pregnane
- cyp2c19
-
taxanes
- irinotecan
- ugt1a1
- ritonavir
- drug development
- diagnostics
- analysis
- pharmacology
- biofuel production
- medicine
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
+
+
xenobiotic[side 1]
=
+
+
xenobiotic[side 2]
Synonyms
p-glycoprotein, abcb1, abcg2, atp-binding cassette transporter, abcc2, breast cancer resistance protein, abcc1, multidrug resistance-associated protein, mdr1a, multidrug transporter, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ATP phosphohydrolase (xenobiotic-exporting)
-
-
-
-
MRP
-
-
-
-
multidrug-resistance protein
-
-
-
-
P-glycoprotein
Pgp
-
-
-
-
transporter protein MRP
-
-
-
-
xenobiotic-transporting ATPase
-
-
-
-
additional information
-
MRP4 is a member of the MRP/ABCC C subfamily of ATP-binding cassette transporters
P-glycoprotein
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (ABC-type, xenobiotic-exporting)
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. The enzymes from Gram-positive bacteria and eukaryotic cells export a number of drugs with unusual specificity, covering various groups of unrelated substances while ignoring some that are closely related structurally. Several distinct enzymes may be present in a single eukaryotic cell. Many of them also transport glutathione---drug conjugates (see EC 7.6.2.3, ABC-type glutathione-S-conjugate transporter) while others also show some 'flippase' activity (cf. EC 7.6.2.1, P-type phospholipid transporter).
CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + cyclosporine A[side 1]
ADP + phosphate + cyclosporine A[side 2]
-
-
-
?
ATP + H2O + quinidine[side 1]
ADP + phosphate + quinidine[side 2]
-
-
-
?
ATP + H2O + rhodamine 123[side 1]
ADP + phosphate + rhodamine 123[side 2]
-
-
-
?
ATP + H2O + verapamil[side 1]
ADP + phosphate + verapamil[side 2]
-
-
-
?
ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
-
-
-
?
3,6-bis(dimethylamino)-9-phenyl-selenoxanthylium bromide/in + ATP + H2O
3,6-bis(dimethylamino)-9-phenyl-selenoxanthylium bromide/out + ADP + phosphate
-
-
-
-
?
ATP + H2O + 9-hydroxyrisperidone/in
ADP + phosphate + 9-hydroxyrisperidone/out
-
-
-
-
?
ATP + H2O + dodecyloctaglycol/in
ADP + phosphate + dodecyloctaglycol/out
-
-
-
-
?
ATP + H2O + resveratrol disulfate/in
ADP + phosphate + resveratrol disulfate/out
-
substrate of BCRP in vitro
-
-
?
ATP + H2O + resveratrol-3-glucuronide/in
ADP + phosphate + resveratrol-3-glucuronide/out
-
substrate of Mrp3 and BCRP in vitro as sulfate
-
-
?
ATP + H2O + resveratrol-3-sulfate [side 1]
ADP + phosphate + resveratrol-3-sulfate [side 2]
-
-
-
-
?
ATP + H2O + resveratrol/in
ADP + phosphate + resveratrol/out
-
substrate of BCRP in vitro as sulfate
-
-
?
ATP + H2O + verapamil/in
ADP + phosphate + verapamil/out
-
-
-
-
?
N-methyl-N-(9-phenyl-2,3,6,7-tetrahydro-1H,5H,12H-pyrido[3,2,1-ij]selenochromeno[2,3-f]quinolin-12-ylidene)methanaminium hexafluorophosphate/in + ATP + H2O
N-methyl-N-(9-phenyl-2,3,6,7-tetrahydro-1H,5H,12H-pyrido[3,2,1-ij]thiochromeno[2,3-f]quinolin-12-ylidene)methanaminium hexafluorophosphate/out + ADP + phosphate
-
-
-
-
?
vinblastine/in + ATP + H2O
vinblastine/out + ADP + phosphate
-
weak activity
-
?
ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
-
-
-
?
ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
in the brain, MRP4 limits the entry of drugs and is involved in nociception, probably as a result of reduced plasma prostaglandins. In the kidney, MRP4 mediates the active tubular secretion of diuretics, antiviral nucleosides and cephalosporins. In the liver, MRP4 mediates the efflux of bile acid to the blood, and knockout mice are more sensitive to cholestatic-induced liver injury. MRP4 protects bone marrow cells and the gastrointestinal tract against cytotoxic drugs and appears to be involved in secretory diarrhoea via coupling with CFTR
-
-
?
leukotriene C4/in + ATP + H2O
leukotriene C4/out + ADP + phosphate
-
-
-
?
leukotriene C4/in + ATP + H2O
leukotriene C4/out + ADP + phosphate
-
-
-
?
additional information
?
-
-
the enzyme functions as cotransporter of glutathione and natural product toxins
-
-
?
additional information
?
-
-
baseline enzyme expression protects cells from the toxic effects of xenobiotics by effluxing the xenobiotics and GSH from the intracellular compartment into the extracellular medium by a cotransport mechanism
-
-
?
additional information
?
-
-
the enzyme in the canalicular membrane plays an important role in the excretion of phospholipid into bile
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + xenobiotic[side 1]
ADP + phosphate + xenobiotic[side 2]
-
-
-
?
ATP + H2O + xenobiotic/in
ADP + phosphate + xenobiotic/out
-
in the brain, MRP4 limits the entry of drugs and is involved in nociception, probably as a result of reduced plasma prostaglandins. In the kidney, MRP4 mediates the active tubular secretion of diuretics, antiviral nucleosides and cephalosporins. In the liver, MRP4 mediates the efflux of bile acid to the blood, and knockout mice are more sensitive to cholestatic-induced liver injury. MRP4 protects bone marrow cells and the gastrointestinal tract against cytotoxic drugs and appears to be involved in secretory diarrhoea via coupling with CFTR
-
-
?
additional information
?
-
-
baseline enzyme expression protects cells from the toxic effects of xenobiotics by effluxing the xenobiotics and GSH from the intracellular compartment into the extracellular medium by a cotransport mechanism
-
-
?
additional information
?
-
-
the enzyme in the canalicular membrane plays an important role in the excretion of phospholipid into bile
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3,6-bis(dimethylamino)-9-(4-dimethylaminophenyl)-thioxanthylium hexafluorophosphate
-
competitive inhibition of verapamil-dependent ATPase-activity
3,6-bis(dimethylamino)-9-phenyl-selenoxanthylium bromide
-
i.e. selenium-derivative of tetramethylrosamine, competitive inhibition of verapamil-dependent ATPase-activity
dodecyloctaglycol
-
uncompetitive inhibition of verapamil-induced Pgp ATPase activity
N-(4-[2-(1,2,3,4-tetrahydro-6,7-dimethoxy-2-isoquinolinyl)ethyl]-phenyl)-9,10-dihydro-5-methoxy-9-oxo-4-acridine carboxamide
-
-
N-methyl-N-(9-phenyl-2,3,6,7-tetrahydro-1H,5H,12H-pyrido[3,2,1-ij]selenochromeno[2,3-f]quinolin-12-ylidene)methanaminium hexafluorophosphate
-
competitive inhibition of verapamil-dependent ATPase-activity
N-methyl-N-(9-phenyl-2,3,6,7-tetrahydro-1H,5H,12H-pyrido[3,2,1-ij]thiochromeno[2,3-f]quinolin-12-ylidene)methanaminium hexafluorophosphate
-
competitive inhibition of verapamil-dependent ATPase-activity
PSC 833
-
PgP inhibitors increase uptake of doxorubicin in tumor cells close to blood vessels, have little effect on drug uptake into tumor cells at intermediate distances, and might have a paradoxical effect to decrease doxorubicin uptake into distal tumor cells. This effect probably contributes to the limited success of PgP inhibitors in clinical trials
resveratrol disulfate
-
acts as a competitive inhibitor of BCRP-mediated methotrexate transport
ritonavir
-
inhibition of intestinal P-glycoprotein by ritonavir causes increased darunavir absorption
tert-butyl (4R)-4-(benzyloxy)-1-(tert-butoxycarbonyl)-L-prolyl-N6-[(benzyloxy)carbonyl]-L-lysinate
-
noncompetitive inhibitor towards daunorubicin and Hoechst 33342
Triton X-100
-
uncompetitive inhibition of verapamil-induced Pgp ATPase activity
verapamil
-
inhibition of P-gp enhances the suppressive effect of kaempferol on aryl hydrocarbon receptor (AhR) transformation through an increase in the intracellular kaempferol concentration
verapamil
-
PgP inhibitors increase uptake of doxorubicin in tumor cells close to blood vessels, have little effect on drug uptake into tumor cells at intermediate distances, and might have a paradoxical effect to decrease doxorubicin uptake into distal tumor cells. This effect probably contributes to the limited success of PgP inhibitors in clinical trials
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3,6-bis(dimethylamino)-9-(3-phenoxypropyl)-thioxanthylium hexafluorophosphate
-
-
3,6-bis(dimethylamino)-9-(N,N-diethyl-5-thiophene-2-carboxamide)selenoxanthylium hexafluorophosphate
-
-
3,6-bis(dimethylamino)-9-(N,N-diethyl-5-thiophene-2-carboxamide)thioxanthylium hexafluorophosphate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.078
N-methyl-N-(9-phenyl-2,3,6,7-tetrahydro-1H,5H,12H-pyrido[3,2,1-ij]thiochromeno[2,3-f]quinolin-12-ylidene)methanaminium hexafluorophosphate
-
pH 7.4, 37°C
0.004
ATP
-
pH 7.4, 37°C, presence of 3,6-bis(dimethylamino)-9-(N,N-diethyl-5-thiophene-2-carboxamide)thioxanthylium hexafluorophosphate
0.006
ATP
-
pH 7.4, 37°C, presence of 3,6-bis(dimethylamino)-9-(N,N-diethyl-5-thiophene-2-carboxamide)selenoxanthylium hexafluorophosphate
0.007
ATP
-
pH 7.4, 37°C, presence of 3,6-bis(dimethylamino)-9-(3-methoxyphenyl)-xanthylium hexafluorophosphate
0.009
ATP
-
pH 7.4, 37°C, presence of 3,6-bis(dimethylamino)-9-(3-phenoxypropyl)-thioxanthylium hexafluorophosphate
0.018
ATP
-
pH 7.4, 37°C, presence of 3,6-bis(dimethylamino)-9-(3-aminophenyl)-thioxanthylium hexafluorophosphate
0.07
ATP
-
pH 7.4, 37°C, presence of 3,6-bis(dimethylamino)-9-phenyl-thioxanthylium bromide
0.074
ATP
-
pH 7.4, 37°C, presence of 3,6-bis(dimethylamino)-9-phenyl-selenoxanthylium bromide
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.008
3,6-bis(dimethylamino)-9-(4-dimethylaminophenyl)-thioxanthylium hexafluorophosphate
-
pH 7.4, 37°C
0.007
N-methyl-N-(9-phenyl-2,3,6,7-tetrahydro-1H,5H,12H-pyrido[3,2,1-ij]selenochromeno[2,3-f]quinolin-12-ylidene)methanaminium hexafluorophosphate
-
pH 7.4, 37°C
0.002
N-methyl-N-(9-phenyl-2,3,6,7-tetrahydro-1H,5H,12H-pyrido[3,2,1-ij]thiochromeno[2,3-f]quinolin-12-ylidene)methanaminium hexafluorophosphate
-
pH 7.4, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
inside-out plasma membrane vesicles of MDR1-transfected mouse embryo fibroblasts (NIH-MDR1-G185)
-
Mrp3 is located in the basolateral, Bcrp1 in the apical membranes of enterocytes
additional information
-
isozymes Mdr1a and Mdr1b show a developmental pattern of low expression at birth, followed by a gradual increase to mature levels at approximately 30 days of age in all tissues. In contrast, Mdr2 mRNA in liver is markedly up-regulated at birth, which returns to low levels by 5 days of age and then gradually increases to mature levels. The three Mdr transporters in mice are expressed in a tissue-specific and age-dependent pattern, there are gender differences in expression, and Mdr transporters are inducible by only a few microsomal enzyme inducers
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
absence of Mrp3 in knockout mice results in altered disposition of resveratrol-3-glucuronide and its parent compound resveratrol, leading to a reduced percentage of resveratrol being excreted via the urine in Mrp3-/- mice. Knockout of BCRP in mice results in high plasma levels of resveratrol-di-sulfate, a resveratrol metabolite hardly detectable in the plasma of wild-type mice and in an increased disposal of resveratrol via the urine
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MDR1A_MOUSE
1276
11
140647
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
-
glycosylation is not essential for ATPase or transport function, the N-linked oligosaccharides appear to influence the conformation of the protein in a subtle way
glycoprotein
-
one glycosylation site is in the second half of the P-glycoprotein, the second glycosylation site links transmembrane domains 8 and 9 in the traditional model of the P-glycoprotein topology
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 100 mM HEPES, pH 7.5, 200 mM NaCl, 25% (w/v) PEG400
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
cysteine-free mouse MDR3 P-glycoprotein (Pgp) is constructed by mutagenesis of the nine natural Cys to Ala. Yield, purity, ATPase activity, KM (MgATP), and stimulation of ATPase by verapamil are similar to wild-type mouse Ppg. After long-term storage at -70 °C (6 months), or incubation at 37 °C for up to 2h, it shows the same stability as wild type (as measured by retention of ATPase activity)
additional information
-
absence of Mrp3 in knockout mice results in altered disposition of resveratrol-3-glucuronide and its parent compound resveratrol, leading to a reduced percentage of resveratrol being excreted via the urine in Mrp3-/- mice. Knockout of BCRP in mice results in high plasma levels of resveratrol-di-sulfate, a resveratrol metabolite hardly detectable in the plasma of wild-type mice and in an increased disposal of resveratrol via the urine
additional information
-
construction of a Mrp4-knockout mouse model with cell-type specific expression and subcellular localisation, overview
additional information
-
introduction of cysteine residues into Cys-less P-glycoprotein and cysteine-mediated cross-linking. For mutant A627C/S1276C, disulfide formation is with high efficiency and cross-linked P-glycoprotein retains 30-68% drug-stimulated ATPase activity compared with reduced or cysteine-less P-glycoprotein. Cysteine pairs K615C/S1276C and A627C/K1260C also form a disulfide, but to a lesser extent, and the cross-linked form of these two mutants have lower drug-stimulated ATPase activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, 6 months, cysteine-free mutant shows the same stability as the wild-type enzyme
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cysteine-free mouse MDR3 P-glycoprotein (Pgp) is constructed by mutagenesis of the nine natural Cys to Ala, expressed in Pichia pastoris and purified
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
determination tissue and developmental expression patterns of genes Mdr1a, Mdr1b, and Mdr2, overview
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
use of in vitro transporter assays for analysis of the role of P-glycoprotein mediated efflux activity. The transwell assay is a valuable tool to evaluate P-glycoprotein interaction with compounds for assessing brain penetration of new chemical entities
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sharom, F.J.; Liu, R.; Romsicki, Y.; Lu, P.
Insight into the structure and substrate interactions of the P-glycoprotein multidrug transporter from spectroscopic studies
Biochim. Biophys. Acta
1461
327-345
1999
Homo sapiens, Mus musculus, Rattus norvegicus
Cole, S.P.C.; Deeley, R.G.
Multidrug resistance mediated by the ATP-binding cassette transporter protein MRP
Bioessays
20
931-940
1998
Homo sapiens, Mus musculus
Frijters, C.M.G.; Ottenhoff, R.; van Wijland, M.J.A.; van Nieuwkerk, C.; Groen, A.K.; Oude Elferink, R.P.J.
Influence of bile salts on hepatic mdr2 P-glycoprotein expression
Adv. Enzyme Regul.
36
351-363
1996
Homo sapiens, Mus musculus
Bellamy, W.T.
P-glycoproteins and multidrug resistance
Annu. Rev. Pharmacol. Toxicol.
36
161-183
1996
Cricetinae, Homo sapiens, Mus musculus
Rappa, G.; Lorico, A.; Flavell, R.A.; Sartorelli, A.C.
Evidence that the multidrug resistance protein (MRP) functions as a Co-transporter of glutathione and natural product toxins
Cancer Res.
57
5232-5237
1997
Mus musculus
Paul, S.; Breuninger, L.M.; Tew, K.D.; Shen, H.; Kruh, G.D.
ATP-dependent uptake of natural product cytotoxic drugs by membrane vesicles estabilshes MRP as a broad specificity transporter
Proc. Natl. Acad. Sci. USA
93
6929-6934
1996
Mus musculus
Tombline, G.; Urbatsch, I.L.; Virk, N.; Muharemagic, A.; White, L.B.; Senior, A.E.
Expression, purification, and characterization of cysteine-free mouse P-glycoprotein
Arch. Biochem. Biophys.
445
124-128
2006
Mus musculus
Katoh, M.; Suzuyama, N.; Takeuchi, T.; Yoshitomi, S.; Asahi, S.; Yokoi, T.
Kinetic analyses for species differences in P-glycoprotein-mediated drug transport
J. Pharm. Sci.
95
2673-2683
2006
Canis lupus familiaris, Homo sapiens, Mus musculus, Rattus norvegicus
Tombline, G.; Donnelly, D.J.; Holt, J.J.; You, Y.; Ye, M.; Gannon, M.K.; Nygren, C.L.; Detty, M.R.
Stimulation of P-glycoprotein ATPase by analogues of tetramethylrosamine: coupling of drug binding at the "R" site to the ATP hydrolysis transition state
Biochemistry
45
8034-8047
2006
Mus musculus
Tombline, G.; Holt, J.J.; Gannon, M.K.; Donnelly, D.J.; Wetzel, B.; Sawada, G.A.; Raub, T.J.; Detty, M.R.
ATP occlusion by P-glycoprotein as a surrogate measure for drug coupling
Biochemistry
47
3294-3307
2008
Mus musculus
Feng, B.; Mills, J.B.; Davidson, R.E.; Mireles, R.J.; Janiszewski, J.S.; Troutman, M.D.; de Morais, S.M.
In vitro P-glycoprotein assays to predict the in vivo interactions of P-glycoprotein with drugs in the central nervous system
Drug Metab. Dispos.
36
268-275
2008
Homo sapiens, Mus musculus
Carrier, I.; Urbatsch, I.L.; Senior, A.E.; Gros, P.
Mutational analysis of conserved aromatic residues in the A-loop of the ABC transporter ABCB1A (mouse Mdr3)
FEBS Lett.
581
301-308
2007
Mus musculus
Cui, Y.J.; Cheng, X.; Weaver, Y.M.; Klaassen, C.D.
Tissue distribution, gender-divergent expression, ontogeny, and chemical induction of multidrug resistance transporter genes (Mdr1a, Mdr1b, Mdr2) in mice
Drug Metab. Dispos.
37
203-210
2009
Mus musculus
van de Wetering, K.; Burkon, A.; Feddema, W.; Bot, A.; de Jonge, H.; Somoza, V.; Borst, P.
Intestinal breast cancer resistance protein (BCRP)/Bcrp1 and multidrug resistance protein 3 (MRP3)/Mrp3 are involved in the pharmacokinetics of resveratrol
Mol. Pharmacol.
75
876-885
2009
Mus musculus
Russel, F.G.; Koenderink, J.B.; Masereeuw, R.
Multidrug resistance protein 4 (MRP4/ABCC4): a versatile efflux transporter for drugs and signalling molecules
Trends Pharmacol. Sci.
29
200-207
2008
Homo sapiens, Mus musculus
Li-Blatter, X.; Nervi, P.; Seelig, A.
Detergents as intrinsic P-glycoprotein substrates and inhibitors
Biochim. Biophys. Acta
1788
2335-2344
2009
Mus musculus
Mukai, R.; Satsu, H.; Shimizu, M.; Ashida, H.
Inhibition of P-glycoprotein enhances the suppressive effect of kaempferol on transformation of the aryl hydrocarbon receptor
Biosci. Biotechnol. Biochem.
73
1635-1639
2009
Mus musculus
Patel, K.J.; Tannock, I.F.
The influence of P-glycoprotein expression and its inhibitors on the distribution of doxorubicin in breast tumors
BMC Cancer
9
356
2009
Mus musculus
Holmstock, N.; Mols, R.; Annaert, P.; Augustijns, P.
In situ intestinal perfusion in knockout mice demonstrates inhibition of intestinal P-glycoprotein by ritonavir causing increased darunavir absorption
Drug Metab. Dispos.
38
1407-1410
2010
Mus musculus
Arnaud, O.; Koubeissi, A.; Ettouati, L.; Terreux, R.; Alame?, G.; Grenot, C.; Dumontet, C.; Di Pietro, A.; Paris, J.; Falson, P.
Potent and Fully Noncompetitive Peptidomimetic Inhibitor of Multidrug Resistance P-Glycoprotein
J. Med. Chem.
53
6720-6729
2010
Homo sapiens, Mus musculus
Verhalen, B.; Wilkens, S.
P-glycoprotein retains drug-stimulated ATPase activity upon covalent linkage of the two nucleotide binding domains at their C-terminal ends
J. Biol. Chem.
286
10476-10482
2011
Mus musculus
Esser, L.; Zhou, F.; Pluchino, K.M.; Shiloach, J.; Ma, J.; Tang, W.K.; Gutierrez, C.; Zhang, A.; Shukla, S.; Madigan, J.P.; Zhou, T.; Kwong, P.D.; Ambudkar, S.V.; Gottesman, M.M.; Xia, D.
Structures of the multidrug transporter P-glycoprotein reveal asymmetric ATP binding and the mechanism of polyspecificity
J. Biol. Chem.
292
446-461
2017
Mus musculus (P21447), Mus musculus
Shaheen, A.; Iqbal, M.; Mirza, O.; Rahman, M.
Structural biology meets drug resistance an overview on multidrug resistance transporters
J. Indian Inst. Sci.
97
165-175
2017
Bacillus subtilis, Salmonella enterica, Staphylococcus aureus, Mus musculus, Pseudomonas aeruginosa, Escherichia coli (P0AEY8)
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EXTERNAL LINKS (specific for EC-Number 7.6.2.2)
Transporter Classification Database (TCDB): 3.A.1.208.43, 3.A.1.204.2, 9.A.1.1.1, 3.A.1.208.21, 3.A.1.106.13, 3.A.1.208.5, 3.A.1.201.24, 3.A.1.208.8, 3.A.1.208.2, 3.A.1.201.31, 3.A.1.208.6, 3.A.1.201.4, 3.A.1.201.1, 3.A.1.208.17, 3.A.1.201.13, 3.A.1.209.4, 3.A.1.208.20, 3.A.1.117.1, 3.A.1.208.9, 3.A.1.208.7, 3.A.1.208.15, 3.A.1.208.31, 3.A.1.208.13, 3.A.1.211.5, 3.A.1.201.14, 3.A.1.208.47, 3.A.1.204.15
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