The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The identity is unambiguous: ABCB4 in this report is the human gene encoding ATP-binding cassette subfamily B member 4, also known as MDR3 or the phosphatidylcholine translocator, corresponding to UniProt P21439. The literature examined concerns human ABCB4/MDR3—not ABCB1/MDR1 and not rodent Abcb4/Mdr2. Human structural studies identify it as a full-size ABCB-family exporter with two transmembrane domains and two cytosolic nucleotide-binding/ATPase domains, matching the supplied AAA+-ATPase and ABC-transmembrane annotations. (weng2025clinicalgeneticand pages 1-2, nosol2021structuresofabcb4 pages 1-2, a2020structureofthe pages 1-5)
Its primary function is ATP-dependent translocation of phosphatidylcholine (PC) from the cytosolic leaflet to the canalicular/exoplasmic leaflet of the hepatocyte apical membrane. ABCB4 is therefore best annotated as a canalicular PC floppase, not as a physiologically important broad-spectrum multidrug pump. Bile salts subsequently extract exposed PC into the canalicular lumen, where PC enters mixed micelles that reduce bile-salt detergent toxicity and maintain cholesterol solubility. (nosol2021structuresofabcb4 pages 2-3, prescher2020stimulationofabcb4mdr3 pages 14-15, prescher2019abcb4mdr3inhealth pages 8-10)
| Category | Evidence-based annotation | Evidence type/strength |
|---|---|---|
| Identity and synonyms | ABCB4 encodes ATP-binding cassette subfamily B member 4, also called MDR3, P-glycoprotein 3, or phosphatidylcholine translocator; target accession UniProt P21439. It is distinct from human ABCB1/MDR1 and rodent Abcb4/Mdr2. (weng2025clinicalgeneticand pages 1-2, nosol2021structuresofabcb4 pages 1-1) | High confidence: supplied UniProt identity agrees with human molecular and structural literature. |
| Organism | Homo sapiens (human). The human protein is termed MDR3; the commonly studied mouse orthologue is Mdr2/Abcb4. (nosol2021structuresofabcb4 pages 1-1, wang2022geneticanalysisof pages 5-7) | High confidence: human structural studies supported by orthology-aware animal evidence. |
| Family and domain architecture | Full-size ABCB-family ABC exporter with two transmembrane domains and two cytosolic nucleotide-binding or ATPase domains. Conserved Walker A, Walker B, and ABC-signature motifs couple ATP turnover to transmembrane conformational change. (weng2025clinicalgeneticand pages 1-2, nosol2021structuresofabcb4 pages 1-2, a2020structureofthe pages 1-5) | High confidence: cryo-EM structures and conserved-domain annotation. |
| Primary substrate | The established physiological substrate is phosphatidylcholine (PC). Intact PC stimulates ATPase activity, whereas tested PE, PS, and sphingomyelin did not; PC acyl-chain composition quantitatively affects activity. (nosol2021structuresofabcb4 pages 2-3, prescher2020stimulationofabcb4mdr3 pages 14-15) | Strong direct evidence: purified-protein ATPase assays, proteoliposome transport, cellular extrusion, and mutagenesis. |
| Direction and energy source | ABCB4 uses ATP binding and hydrolysis to move PC from the cytosolic or inner leaflet toward the exoplasmic or outer leaflet of the hepatocyte canalicular membrane, making it a PC floppase. PC recruitment can precede ATP binding; ATP drives extrusion, and hydrolysis resets the transporter. (nosol2021structuresofabcb4 pages 2-3, prescher2020stimulationofabcb4mdr3 pages 14-15, wang2022geneticanalysisof pages 5-7) | Strong mechanistic evidence: transport assays, ATPase mutants, and structures of multiple catalytic states. |
| Precise localization | Functions at the apical canalicular plasma membrane of hepatocytes, facing the bile-canalicular lumen. Correct trafficking to this membrane is required for activity; some pathogenic variants are retained intracellularly. (weng2025clinicalgeneticand pages 1-2, lakli2024identificationofnew pages 12-13, a2020structureofthe pages 1-5) | High confidence: hepatocyte localization, polarized-cell models, and variant-trafficking experiments. |
| Structural recognition and mechanism | Cryo-EM supports alternating access through a central cavity. The PC choline group is coordinated by cation–π interactions involving W234 and F345, while H989 contacts the phosphate region. W234 or F345 mutation reduces extrusion to about 20%, and H989A lowers activity to about 40%. Posaconazole blocks the access pathway. (nosol2021structuresofabcb4 pages 1-1, nosol2021structuresofabcb4 pages 2-3, nosol2021structuresofabcb4 pages 1-2) | Strong direct evidence: substrate- and inhibitor-bound cryo-EM, mutagenesis, cell assays, and reconstituted transport; final lipid release remains partly model-dependent. |
| Role in bile formation | ABCB4 exposes PC for extraction by canalicular bile salts into mixed micelles. With ABCB11-mediated bile-salt secretion and ABCG5/G8-mediated cholesterol export, this reduces bile-salt detergent toxicity and maintains cholesterol solubility. PC constitutes about 30–44% of canalicular membrane phospholipid but approximately 90–95% of biliary phospholipid. (prescher2020stimulationofabcb4mdr3 pages 14-15, prescher2020stimulationofabcb4mdr3 pages 3-5, prescher2019abcb4mdr3inhealth pages 8-10) | High confidence: lipid-composition data, biochemistry, physiology, and genetic loss-of-function evidence. |
| Loss-of-function consequences | Reduced PC secretion produces phospholipid-poor, detergent-rich, lithogenic bile, causing canalicular or cholangiocyte injury, cholestasis, fibrosis, cirrhosis, and gallstones. Severe biallelic variants classically cause PFIC3; monoallelic or hypomorphic variants contribute to LPAC, pregnancy-associated cholestasis, adult cholangiopathy, and susceptibility to drug-induced liver injury. Mouse Abcb4 deletion nearly abolishes biliary phospholipid secretion. (OpenTargets Search: -ABCB4, prescher2019abcb4mdr3inhealth pages 10-13, wang2022geneticanalysisof pages 5-7, wang2022geneticanalysisof pages 2-4) | High confidence for PFIC3 and biliary-PC deficiency: strong human genetic and knockout support; penetrance of individual monoallelic variants varies. |
| Current clinical use | ABCB4 sequencing is used to diagnose unexplained high-GGT cholestasis, PFIC3, LPAC, and related phenotypes; MDR3 immunostaining and variant-specific trafficking or PC-secretion assays can support interpretation. Ursodeoxycholic acid is widely used, while advanced disease may require liver transplantation. Response depends partly on genotype and residual function. (weng2025clinicalgeneticand pages 1-2, weng2025clinicalgeneticand pages 14-15, heinrich2026functionalinactivationof pages 6-6) | Established diagnostic and clinical practice: treatment effects vary, and UDCA does not molecularly correct every variant. |
| 2023–2024 developments | A 2023 study evaluated genotype and UDCA response in 38 patients with PFIC3. In 2024, high-content screening identified six hits for traffic-defective ABCB4; three improved maturation or canalicular localization of two retained variants, and one significantly restored function. These correctors are preclinical research compounds, not approved therapies. (heinrich2026functionalinactivationof pages 6-6, weng2025clinicalgeneticand pages 15-16, lakli2024identificationofnew pages 12-13) | Emerging evidence: peer-reviewed clinical cohort and cell-based screening; candidate correctors require optimization, safety testing, and clinical trials. |
Table: Compact evidence map for human ABCB4/MDR3 (UniProt P21439), covering molecular identity, PC transport, canalicular physiology, disease consequences, clinical use, and recent research. It distinguishes established functions from preclinical variant-corrector studies.
The supplied UniProt identity is fully consistent with the literature: gene ABCB4; protein MDR3; Homo sapiens. “MDR3” is historical nomenclature based on sequence similarity to P-glycoprotein, but ABCB4 does not principally confer classical multidrug resistance. Rodent literature commonly calls the orthologue Mdr2/Abcb4; those animal results are informative mechanistically but should not be mistaken for evidence about a different human protein. (nosol2021structuresofabcb4 pages 1-1, wang2022geneticanalysisof pages 5-7, prescher2019abcb4mdr3inhealth pages 8-10)
ABCB4 is a canonical full transporter containing two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The NBDs contain conserved Walker A, Walker B, ABC-signature/LSGGQ, Q-loop, H-loop, and D-loop elements. ATP binding promotes NBD closure and rearrangement of the transmembrane pathway; hydrolysis returns the transporter toward an inward-facing state. Cryo-EM structures captured inward-facing, PC-occluded, inhibitor-bound, and nucleotide-bound closed conformations, providing direct correspondence between the annotated ABC/AAA+-like ATPase machinery and lipid transport. (weng2025clinicalgeneticand pages 1-2, nosol2021structuresofabcb4 pages 1-1, nosol2021structuresofabcb4 pages 1-2, a2020structureofthe pages 1-5)
The 2020 human structure was determined at 3.2 Å and deposited as PDB 6S7P/EMD-10111. It showed two bound ATP molecules in a closed transporter and a central transmembrane cavity compatible with phospholipid passage. The work was published in Nature Structural & Molecular Biology in 2020; DOI/URL: https://doi.org/10.1038/s41594-019-0354-3. (a2020structureofthe pages 32-35, a2020structureofthe pages 1-5, a2020structureofthe pages 10-13)
The established physiological substrate class is intact phosphatidylcholine. Purified-protein assays found stimulation by 16:0–18:1 PC, whereas tested phosphatidylethanolamine, phosphatidylserine, and sphingomyelin did not stimulate ABCB4 above background. Both acyl chains and the glycerophospholipid backbone contribute to productive interaction; chain length and saturation quantitatively alter activity. Thus, “PC-selective floppase” is more precise than a generic phospholipid transporter, although ABCB4 can accommodate multiple PC molecular species rather than only one acyl-chain composition. (prescher2020stimulationofabcb4mdr3 pages 14-15, prescher2020stimulationofabcb4mdr3 pages 3-5)
The substrate preference is physiologically conspicuous. PC constitutes roughly 30–44% of canalicular membrane phospholipid, yet approximately 90–95% of biliary phospholipid. Reported enriched biliary species include 16:0–18:2 and 16:0–20:4 PC; bile-salt extraction adds a second layer of selectivity, so biliary composition should not be attributed to ABCB4 recognition alone. (prescher2020stimulationofabcb4mdr3 pages 14-15, prescher2020stimulationofabcb4mdr3 pages 3-5, prescher2019abcb4mdr3inhealth pages 8-10)
ABCB4 is classified under ATP-dependent transmembrane transport rather than as a chemical enzyme acting on PC. Its net reaction can be summarized as:
PC(inner/cytosolic leaflet) + ATP + H₂O → PC(outer/canalicular leaflet) + ADP + phosphate.
This is “flop”—movement from the cytosolic to the exoplasmic leaflet. It does not chemically modify PC. Early membrane recruitment and binding can occur without ATP, whereas ATP binding drives outward transition and extrusion; ATP hydrolysis resets the transporter. Functional disruption of one ATPase site can abolish transport, indicating that the two NBDs operate as a coupled catalytic unit. (nosol2021structuresofabcb4 pages 2-3, a2020structureofthe pages 7-10, prescher2020stimulationofabcb4mdr3 pages 14-15)
Cryo-EM and functional studies favor alternating access through a central cavity. In the inward-facing state, a lateral opening admits PC from the inner membrane leaflet. In the occluded state, a single PC occupies a roughly 6,500 ų Y-shaped cavity formed prominently by TM4 and TM10. The choline head group is stabilized by cation–π interactions involving W234 and F345, while H989 interacts near the phosphate. Mutation of W234 and/or F345 reduced extrusion to approximately 20%, and H989A reduced activity to approximately 40%, strongly linking the observed site to function. (nosol2021structuresofabcb4 pages 1-1, nosol2021structuresofabcb4 pages 2-3, nosol2021structuresofabcb4 pages 1-2)
These data also refine the older “credit-card-swipe” concept. The strongest current structural interpretation is that the entire phospholipid enters a central pathway, although membrane-facing recruitment and final reorientation into the outer leaflet remain partly model-dependent. Extracellular loops and cavity residues V985, H989, and A990 contribute to transport and likely assist release or lipid reorientation. (a2020structureofthe pages 10-13, a2020structureofthe pages 7-10)
The antifungal posaconazole occupies the substrate-access pathway and prevents PC from reaching the central cavity. This provides a molecular mechanism by which drug-mediated ABCB4 inhibition may contribute to cholestatic drug injury; it does not make posaconazole a normal transported substrate. The relevant structural study was published in PNAS in August 2021; DOI/URL: https://doi.org/10.1073/pnas.2106702118. (nosol2021structuresofabcb4 pages 1-1, nosol2021structuresofabcb4 pages 2-3)
ABCB4 functions predominantly at the apical canalicular plasma membrane of hepatocytes, facing the bile-canalicular lumen. This polarized location is essential: the protein must first mature through the secretory pathway and be delivered to the canalicular membrane. Some pathogenic missense variants retain catalytic potential but misfold or remain in intracellular compartments, producing loss of biliary PC secretion despite protein synthesis. (weng2025clinicalgeneticand pages 1-2, lakli2024identificationofnew pages 12-13, a2020structureofthe pages 1-5)
The operational site is therefore the hepatocyte–bile interface, not the sinusoidal membrane, cholangiocyte plasma membrane, or extracellular bile after secretion. ABCB4 supplies PC to the canalicular outer leaflet; bile salts then extract it into the lumen. This distinction matters because measuring PC released into culture medium combines two processes—ABCB4-mediated transbilayer movement and acceptor-mediated extraction—and does not by itself prove direct translocation. (prescher2019abcb4mdr3inhealth pages 16-18)
ABCB4 participates in a coordinated canalicular lipid-secretion system:
This arrangement converts detergent bile salts into less membrane-damaging mixed micelles, protects hepatocyte canalicular and bile-duct membranes, and limits cholesterol crystallization. (wang2022geneticanalysisof pages 5-7, prescher2019abcb4mdr3inhealth pages 8-10, wang2022geneticanalysisof pages 2-4)
The physiological assignment is supported by several independent evidence classes. Human biochemical and genetic studies associate ABCB4 dysfunction with low biliary PC. Mouse Abcb4/Mdr2 deletion nearly abolishes biliary phospholipid secretion. Structural studies directly visualize bound PC, while proteoliposome assays reproduce ATP-dependent PC transport and discrimination over PE. Together, these are substantially stronger than annotation inferred only from sequence homology. (nosol2021structuresofabcb4 pages 1-1, nosol2021structuresofabcb4 pages 2-3, wang2022geneticanalysisof pages 5-7)
Loss of ABCB4 shifts bile toward a phospholipid-poor, detergent-rich, lithogenic composition. Unshielded bile salts damage canalicular and cholangiocyte membranes, promoting inflammation, duct injury, cholestasis, fibrosis, portal hypertension, and ultimately cirrhosis. Reduced PC also impairs cholesterol solubilization and favors sludge, microlithiasis, and gallstones. PFIC3 bile-salt:phospholipid and cholesterol:phospholipid ratios have been reported at approximately fivefold above normal. (prescher2019abcb4mdr3inhealth pages 10-13, wang2022geneticanalysisof pages 5-7, wang2022geneticanalysisof pages 2-4)
The main human phenotypic spectrum includes:
Open Targets independently records ABCB4 associations with PFIC3, pregnancy-associated intrahepatic cholestasis, cholelithiasis, and gallbladder disorders. Penetrance and severity of individual heterozygous variants remain variable, so variant detection alone is not equivalent to causality. (OpenTargets Search: -ABCB4, weng2025clinicalgeneticand pages 1-2)
Variant effects fall into mechanistically useful classes: absent synthesis, defective maturation/trafficking, reduced membrane stability, impaired ATP coupling, or defective PC binding/translocation. For example, the structurally studied A286V variant retained approximately normal membrane expression but nearly no function, whereas A953D showed both reduced function (29%) and reduced expression (16.3%). Such examples demonstrate why localization and functional assays complement sequence interpretation. (a2020structureofthe pages 32-35)
ABCB4 sequencing is used in unexplained high-GGT cholestasis, suspected PFIC3, LPAC, pregnancy-related cholestasis, and cryptogenic adult cholangiopathy. Interpretation may be strengthened by liver MDR3 immunostaining, polarized-cell localization, maturation analysis, PC-secretion assays, and structural or variant-specific prediction. In a recent five-adult series, whole-exome sequencing found seven variants; three patients had cholestasis, two cirrhosis, all five had elevated GGT, and three of four biopsied patients had bile-duct dilatation. All tested missense variants reduced PC secretion, although they did not all mislocalize, illustrating functional heterogeneity. The study was published 14 April 2025; DOI/URL: https://doi.org/10.3748/wjg.v31.i14.104975. (weng2025clinicalgeneticand pages 1-2)
Ursodeoxycholic acid (UDCA) is widely used because it makes the bile-acid pool more hydrophilic and can reduce detergent injury; benefit is greatest when some ABCB4 function remains. It does not directly repair every molecular defect. Advanced PFIC3 with progressive liver failure may require liver transplantation. Symptom-directed cholestasis treatments and, in selected PFIC settings, interruption of enterohepatic bile-acid circulation can reduce bile-acid burden, but these approaches do not replace ABCB4-mediated PC transport. (weng2025clinicalgeneticand pages 14-15, heinrich2026functionalinactivationof pages 6-6, heinrich2026functionalinactivationof pages 1-2)
Clinical response should therefore be interpreted mechanistically. A trafficking-defective variant might be amenable to a corrector, whereas an absent protein or catalytic-site null allele is less likely to respond to trafficking rescue. Genotype, residual canalicular MDR3, PC secretion, and biochemical response to UDCA are more informative together than any single measurement. (weng2025clinicalgeneticand pages 14-15, lakli2024identificationofnew pages 12-13)
A 2023 JHEP Reports study examined outcomes, genotype, and UDCA response in 38 patients with PFIC3, reflecting the field’s movement from a binary diagnosis toward residual-function and treatment-response stratification. Publication: October 2023; DOI/URL: https://doi.org/10.1016/j.jhepr.2023.100844. The retrieved material verifies the cohort size and study focus but did not expose all outcome denominators; unsupported response percentages are therefore not reported here. (heinrich2026functionalinactivationof pages 6-6)
The most notable 2024 mechanism-directed development was Lakli et al.’s high-content screen for pharmacological correction of trafficking-defective ABCB4. Across screening that included a 3,200-compound library, six hits were identified; three improved maturation and canalicular localization of two retained variants, and one significantly restored function. Work on I541F and L556R showed that partial trafficking correction could potentially restore enough PC secretion to increase clinical responsiveness. These molecules remain preclinical leads, not approved treatments. Publication: July 2024, Communications Biology; DOI/URL: https://doi.org/10.1038/s42003-024-06590-y. (weng2025clinicalgeneticand pages 15-16, lakli2024identificationofnew pages 12-13)
Recent genomic studies also emphasize that ABCB4 disease spans pediatric PFIC3 and milder adult phenotypes rather than forming isolated categories. However, large prospective studies are still needed to quantify penetrance of monoallelic variants and determine which functional assays best predict outcomes. No clearly ABCB4-specific interventional trial was identified in the clinical-trial search, consistent with variant correction remaining experimental.
The evidence for the central annotation—ATP-driven canalicular PC floppase—is exceptionally strong because human genetics, knockout physiology, purified-protein biochemistry, cell biology, and cryo-EM converge on the same function. The most defensible substrate statement is “intact PC-family phospholipids,” not a single PC molecular species. ABCB4 selects the choline-containing lipid class, while acyl-chain effects and subsequent bile-salt extraction shape the final biliary profile. (nosol2021structuresofabcb4 pages 2-3, prescher2020stimulationofabcb4mdr3 pages 14-15, prescher2019abcb4mdr3inhealth pages 8-10)
Important unresolved issues include the atomic sequence of lipid release into the outer leaflet, how membrane composition and curvature alter the catalytic cycle, and how much specific heterozygous variants increase disease risk under pregnancy, drug, hormonal, or metabolic stress. Variant predictors can prioritize experiments but should not replace segregation, localization, and transport measurements. Likewise, rescue in overexpression systems does not yet establish clinical efficacy.
ABCB4/P21439 is a human hepatocyte canalicular, ATP-dependent phosphatidylcholine floppase. It recruits intact PC from the cytosolic membrane leaflet, transports it through an alternating-access transmembrane cavity, and exposes it to canalicular bile salts for extraction into bile. This supplies mixed micelles that buffer bile-salt detergent activity and solubilize cholesterol. Loss of expression, trafficking, ATP coupling, or PC translocation causes phospholipid-poor toxic bile and the PFIC3–LPAC–pregnancy/adult cholestasis spectrum.
References
(weng2025clinicalgeneticand pages 1-2): Yu-Hang Weng, Yu-Feng Zheng, Dan-Dan Yin, Qing-Fang Xiong, Jin-Long Li, Shun-Xin Li, Wei Chen, and Yong-Feng Yang. Clinical, genetic and functional perspectives on atp-binding cassette subfamily b member 4 variants in five cholestasis adults. World Journal of Gastroenterology, Apr 2025. URL: https://doi.org/10.3748/wjg.v31.i14.104975, doi:10.3748/wjg.v31.i14.104975. This article has 1 citations.
(nosol2021structuresofabcb4 pages 1-2): Kamil Nosol, Rose Bang-Sørensen, Rossitza N. Irobalieva, Satchal K. Erramilli, Bruno Stieger, Anthony A. Kossiakoff, and Kaspar P. Locher. Structures of abcb4 provide insight into phosphatidylcholine translocation. Proceedings of the National Academy of Sciences, Aug 2021. URL: https://doi.org/10.1073/pnas.2106702118, doi:10.1073/pnas.2106702118. This article has 49 citations and is from a highest quality peer-reviewed journal.
(a2020structureofthe pages 1-5): Jeppe A Olsen, Amer Alam, Julia Kowal, Bruno Stieger, and Kaspar P Locher. Structure of the human lipid exporter abcb4 in a lipid environment. Nature Structural & Molecular Biology, 27:62-70, Dec 2020. URL: https://doi.org/10.1038/s41594-019-0354-3, doi:10.1038/s41594-019-0354-3. This article has 92 citations and is from a highest quality peer-reviewed journal.
(nosol2021structuresofabcb4 pages 2-3): Kamil Nosol, Rose Bang-Sørensen, Rossitza N. Irobalieva, Satchal K. Erramilli, Bruno Stieger, Anthony A. Kossiakoff, and Kaspar P. Locher. Structures of abcb4 provide insight into phosphatidylcholine translocation. Proceedings of the National Academy of Sciences, Aug 2021. URL: https://doi.org/10.1073/pnas.2106702118, doi:10.1073/pnas.2106702118. This article has 49 citations and is from a highest quality peer-reviewed journal.
(prescher2020stimulationofabcb4mdr3 pages 14-15): Martin Prescher, Sander H.J. Smits, and Lutz Schmitt. Stimulation of abcb4/mdr3 atpase activity requires an intact phosphatidylcholine lipid. Dec 2020. URL: https://doi.org/10.1194/jlr.ra120000889, doi:10.1194/jlr.ra120000889. This article has 10 citations and is from a peer-reviewed journal.
(prescher2019abcb4mdr3inhealth pages 8-10): Martin Prescher, Tim Kroll, and Lutz Schmitt. Abcb4/mdr3 in health and disease – at the crossroads of biochemistry and medicine. Biological Chemistry, 400:1245-1259, Mar 2019. URL: https://doi.org/10.1515/hsz-2018-0441, doi:10.1515/hsz-2018-0441. This article has 31 citations and is from a peer-reviewed journal.
(nosol2021structuresofabcb4 pages 1-1): Kamil Nosol, Rose Bang-Sørensen, Rossitza N. Irobalieva, Satchal K. Erramilli, Bruno Stieger, Anthony A. Kossiakoff, and Kaspar P. Locher. Structures of abcb4 provide insight into phosphatidylcholine translocation. Proceedings of the National Academy of Sciences, Aug 2021. URL: https://doi.org/10.1073/pnas.2106702118, doi:10.1073/pnas.2106702118. This article has 49 citations and is from a highest quality peer-reviewed journal.
(wang2022geneticanalysisof pages 5-7): Helen H. Wang, Piero Portincasa, Min Liu, and David Q.-H. Wang. Genetic analysis of abcb4 mutations and variants related to the pathogenesis and pathophysiology of low phospholipid-associated cholelithiasis. Genes, 13:1047, Jun 2022. URL: https://doi.org/10.3390/genes13061047, doi:10.3390/genes13061047. This article has 72 citations.
(lakli2024identificationofnew pages 12-13): Mounia Lakli, Julie Dumont, Virginie Vauthier, Julie Charton, Veronica Crespi, Manon Banet, Yosra Riahi, Amel Ben Saad, Elodie Mareux, Martine Lapalus, Emmanuel Gonzales, Emmanuel Jacquemin, Florent Di Meo, Benoit Deprez, Florence Leroux, and Thomas Falguières. Identification of new correctors for traffic-defective abcb4 variants by a high-content screening approach. Communications Biology, Jul 2024. URL: https://doi.org/10.1038/s42003-024-06590-y, doi:10.1038/s42003-024-06590-y. This article has 5 citations and is from a peer-reviewed journal.
(prescher2020stimulationofabcb4mdr3 pages 3-5): Martin Prescher, Sander H.J. Smits, and Lutz Schmitt. Stimulation of abcb4/mdr3 atpase activity requires an intact phosphatidylcholine lipid. Dec 2020. URL: https://doi.org/10.1194/jlr.ra120000889, doi:10.1194/jlr.ra120000889. This article has 10 citations and is from a peer-reviewed journal.
(OpenTargets Search: -ABCB4): Open Targets Query (-ABCB4, 5 results). Buniello, A. et al. (2025). Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery. Nucleic Acids Research.
(prescher2019abcb4mdr3inhealth pages 10-13): Martin Prescher, Tim Kroll, and Lutz Schmitt. Abcb4/mdr3 in health and disease – at the crossroads of biochemistry and medicine. Biological Chemistry, 400:1245-1259, Mar 2019. URL: https://doi.org/10.1515/hsz-2018-0441, doi:10.1515/hsz-2018-0441. This article has 31 citations and is from a peer-reviewed journal.
(wang2022geneticanalysisof pages 2-4): Helen H. Wang, Piero Portincasa, Min Liu, and David Q.-H. Wang. Genetic analysis of abcb4 mutations and variants related to the pathogenesis and pathophysiology of low phospholipid-associated cholelithiasis. Genes, 13:1047, Jun 2022. URL: https://doi.org/10.3390/genes13061047, doi:10.3390/genes13061047. This article has 72 citations.
(weng2025clinicalgeneticand pages 14-15): Yu-Hang Weng, Yu-Feng Zheng, Dan-Dan Yin, Qing-Fang Xiong, Jin-Long Li, Shun-Xin Li, Wei Chen, and Yong-Feng Yang. Clinical, genetic and functional perspectives on atp-binding cassette subfamily b member 4 variants in five cholestasis adults. World Journal of Gastroenterology, Apr 2025. URL: https://doi.org/10.3748/wjg.v31.i14.104975, doi:10.3748/wjg.v31.i14.104975. This article has 1 citations.
(heinrich2026functionalinactivationof pages 6-6): Sophia Heinrich, Annika Behrendt, Malte Sgodda, Holger Gohlke, Bernd Auber, Amelie Stalke, Björn Hartleben, Heiner Wedemeyer, Tobias Cantz, and Richard Taubert. Functional inactivation of mdr3 caused by a homozygous abcb4 missense variant leading to liver failure. Frontiers in Genetics, Apr 2026. URL: https://doi.org/10.3389/fgene.2026.1802238, doi:10.3389/fgene.2026.1802238. This article has 0 citations and is from a peer-reviewed journal.
(weng2025clinicalgeneticand pages 15-16): Yu-Hang Weng, Yu-Feng Zheng, Dan-Dan Yin, Qing-Fang Xiong, Jin-Long Li, Shun-Xin Li, Wei Chen, and Yong-Feng Yang. Clinical, genetic and functional perspectives on atp-binding cassette subfamily b member 4 variants in five cholestasis adults. World Journal of Gastroenterology, Apr 2025. URL: https://doi.org/10.3748/wjg.v31.i14.104975, doi:10.3748/wjg.v31.i14.104975. This article has 1 citations.
(a2020structureofthe pages 32-35): Jeppe A Olsen, Amer Alam, Julia Kowal, Bruno Stieger, and Kaspar P Locher. Structure of the human lipid exporter abcb4 in a lipid environment. Nature Structural & Molecular Biology, 27:62-70, Dec 2020. URL: https://doi.org/10.1038/s41594-019-0354-3, doi:10.1038/s41594-019-0354-3. This article has 92 citations and is from a highest quality peer-reviewed journal.
(a2020structureofthe pages 10-13): Jeppe A Olsen, Amer Alam, Julia Kowal, Bruno Stieger, and Kaspar P Locher. Structure of the human lipid exporter abcb4 in a lipid environment. Nature Structural & Molecular Biology, 27:62-70, Dec 2020. URL: https://doi.org/10.1038/s41594-019-0354-3, doi:10.1038/s41594-019-0354-3. This article has 92 citations and is from a highest quality peer-reviewed journal.
(a2020structureofthe pages 7-10): Jeppe A Olsen, Amer Alam, Julia Kowal, Bruno Stieger, and Kaspar P Locher. Structure of the human lipid exporter abcb4 in a lipid environment. Nature Structural & Molecular Biology, 27:62-70, Dec 2020. URL: https://doi.org/10.1038/s41594-019-0354-3, doi:10.1038/s41594-019-0354-3. This article has 92 citations and is from a highest quality peer-reviewed journal.
(prescher2019abcb4mdr3inhealth pages 16-18): Martin Prescher, Tim Kroll, and Lutz Schmitt. Abcb4/mdr3 in health and disease – at the crossroads of biochemistry and medicine. Biological Chemistry, 400:1245-1259, Mar 2019. URL: https://doi.org/10.1515/hsz-2018-0441, doi:10.1515/hsz-2018-0441. This article has 31 citations and is from a peer-reviewed journal.
(heinrich2026functionalinactivationof pages 1-2): Sophia Heinrich, Annika Behrendt, Malte Sgodda, Holger Gohlke, Bernd Auber, Amelie Stalke, Björn Hartleben, Heiner Wedemeyer, Tobias Cantz, and Richard Taubert. Functional inactivation of mdr3 caused by a homozygous abcb4 missense variant leading to liver failure. Frontiers in Genetics, Apr 2026. URL: https://doi.org/10.3389/fgene.2026.1802238, doi:10.3389/fgene.2026.1802238. This article has 0 citations and is from a peer-reviewed journal.