Affinage

ABCB10

ATP-binding cassette sub-family B member 10, mitochondrial · UniProt Q9NRK6

Length
738 aa
Mass
79.1 kDa
Annotated
2026-04-28
52 papers in source corpus 22 papers cited in narrative 22 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

ABCB10 is a homodimeric ATP-binding cassette transporter of the mitochondrial inner membrane that exports biliverdin to the cytosol and coordinates heme biosynthesis with mitochondrial iron import in erythroid and other cell types. Reconstitution in liposomes directly demonstrated biliverdin transport, and ABCB10 deletion causes mitochondrial biliverdin accumulation; in the cytosol, biliverdin is reduced to bilirubin, which acts as an antioxidant and modulates signaling through PTP1B inactivation and H₂O₂ scavenging (PMID:34011630, PMID:34823065). ABCB10 physically associates with mitoferrin-1 and ferrochelatase in an oligomeric complex that couples mitochondrial iron uptake to heme synthesis, and its ATPase activity—stimulated by zinc-mesoporphyrin and biliverdin via conserved transmembrane arginines R232/R295, and regulated by cardiolipin binding and glutathione redox status—is essential for erythroid hemoglobinization (PMID:19805291, PMID:30765471, PMID:41229075, PMID:37807693, PMID:28808058). Germline ABCB10 knockout causes embryonic lethality at E12.5 from failed primitive erythropoiesis driven by mitochondrial oxidative stress, and tissue-specific deletions reveal protective roles against ferroptosis in cardiomyocytes, metabolic dysfunction in hepatocytes and pancreatic β-cells, and impaired CD4⁺ T cell activation (PMID:22240895, PMID:38655715, PMID:34893527).

Mechanistic history

Synthesis pass · year-by-year structured walk · 15 steps
  1. 2004 High

    Establishing that ABCB10 is a mitochondrial inner-membrane homodimer resolved its subcellular location and oligomeric state, key prerequisites for understanding its transport function.

    Evidence Mutagenesis of the 105-aa mitochondrial targeting presequence, subcellular fractionation, and chemical cross-linking/mass spectrometry in mammalian cells

    PMID:15215243

    Open questions at the time
    • Substrate identity unknown at this point
    • No functional transport assay performed
    • Mechanism of homodimerization interface unresolved
  2. 2009 High

    Identifying ABCB10 as a physical partner of mitoferrin-1 that stabilizes the iron importer linked ABCB10 to mitochondrial iron homeostasis and heme biosynthesis for the first time.

    Evidence Reciprocal co-immunoprecipitation and mass spectrometry in erythroid and COS7 cells, protein half-life measurements

    PMID:19805291

    Open questions at the time
    • Whether ABCB10 ATPase activity is required for mitoferrin-1 stabilization was untested
    • No structural details of the interaction interface
  3. 2010 High

    Demonstrating that ferrochelatase joins the ABCB10–mitoferrin-1 complex expanded the model to a multiprotein assembly that physically couples iron import to protoporphyrin metallation.

    Evidence Affinity purification/MS and co-IP with endogenous proteins in MEL and HEK293 cells

    PMID:20427704

    Open questions at the time
    • Stoichiometry and architecture of the complex unknown
    • Whether complex formation is regulated during differentiation untested
  4. 2012 High

    ABCB10 knockout mice dying at E12.5 with severe oxidative stress in erythroid precursors—rescued by a SOD2 mimetic—established ABCB10 as essential for erythropoiesis and placed it upstream of mitochondrial ROS.

    Evidence Germline Abcb10 KO mouse, ex vivo erythroid differentiation, mitochondrial superoxide measurement, MnTBAP rescue

    PMID:22240895

    Open questions at the time
    • Transported substrate still unidentified
    • Whether the ROS phenotype reflects loss of heme synthesis vs. loss of a separate antioxidant mechanism was unresolved
  5. 2013 High

    Crystal structures in apo and nucleotide-bound states revealed an exporter fold with an unusual open-inward conformation even with ATP analogs, informing how substrate enters through a lateral portal.

    Evidence X-ray crystallography of multiple ABCB10–nucleotide-analog complexes

    PMID:23716676

    Open questions at the time
    • No substrate-bound structure obtained
    • Portal-mediated entry remained a proposal without mutagenesis validation at this stage
  6. 2015 High

    Identifying Walker A/B and C-loop residues required for ATPase activity, and showing redox regulation via glutathionylation at Cys547, connected ABCB10's catalytic cycle to mitochondrial redox state while excluding δ-ALA as a substrate.

    Evidence Site-directed mutagenesis, 8-azido-ATP photolabeling, ATPase assays, MS identification of glutathionylation

    PMID:26053025

    Open questions at the time
    • True transported substrate still unidentified
    • Physiological significance of GSSG stimulation not tested in cells
  7. 2017 High

    Showing that ABCB10 ATPase activity is required for hemoglobinization and that neither ALA nor protoporphyrin IX accumulates upon ABCB10 loss narrowed the substrate search and revealed downstream Bach1-mediated transcriptional consequences.

    Evidence shRNA knockdown in MEL cells, ATPase assays, metabolite quantification, transcriptional profiling with epistasis rescue

    PMID:28808058

    Open questions at the time
    • Substrate identity still unknown
    • Whether Bach1 derepression is a direct or indirect effect of ABCB10 loss undetermined
  8. 2019 High

    Mapping the ferrochelatase-bridged ABCB10–ABCB7 complex architecture showed that ferrochelatase contacts the nucleotide-binding domains of both transporters, suggesting coordinated regulation of two ABC transporters at the heme synthesis step.

    Evidence Chemical cross-linking/tandem MS and mutational analysis in inducible knockdown cell lines

    PMID:30765471

    Open questions at the time
    • Functional consequence of disrupting the ABCB10–ABCB7 bridge not fully characterized
    • Whether the complex exists in non-erythroid tissues unknown
  9. 2020 High

    Zinc-mesoporphyrin specifically stimulating ABCB10 ATPase in nanodiscs, while ALA and glutathione did not, provided the first biochemical evidence that a porphyrin-related molecule interacts with the substrate-binding site.

    Evidence Purified ABCB10 in lipid nanodiscs, ATPase assays with heme analogs and precursors

    PMID:33253225

    Open questions at the time
    • Direct transport of the stimulating compound not shown
    • Identity of the physiological substrate not conclusively established
  10. 2021 High

    Reconstitution of ABCB10 in liposomes directly demonstrated biliverdin transport, and hepatocyte-specific KO showed mitochondrial biliverdin accumulation, definitively identifying the transported substrate after over a decade of investigation.

    Evidence Liposome reconstitution transport assay, hepatocyte-specific Abcb10 KO mice, metabolite measurements, bilirubin rescue

    PMID:34011630

    Open questions at the time
    • Whether biliverdin is the sole substrate or one of several remains open
    • Structural basis of biliverdin recognition unknown
  11. 2021 Medium

    β-cell-specific ABCB10 deletion revealed that exported biliverdin/bilirubin modulates glucose-stimulated insulin secretion via H₂O₂ scavenging, extending ABCB10 function beyond erythropoiesis to metabolic signaling.

    Evidence Ins1Cre-Abcb10 KO mouse, GSIS assays, H₂O₂ measurement, bilirubin rescue in isolated islets

    PMID:34823065

    Open questions at the time
    • Single lab finding not independently replicated
    • Relative contribution of biliverdin export vs. other ABCB10 functions in β-cells not dissected
  12. 2023 High

    Demonstrating cooperative, high-affinity cardiolipin binding that regulates ATPase activity identified a lipid-based regulatory mechanism consistent with ABCB10's mitochondrial inner-membrane localization.

    Evidence Native mass spectrometry quantification of lipid binding, in vitro ATPase assays with various phospholipids

    PMID:37807693

    Open questions at the time
    • Cardiolipin binding sites not structurally mapped
    • Whether cardiolipin modulates biliverdin transport rates untested
  13. 2023 Medium

    ABCB10 deletion in erythroid cells causes arginine depletion and ATF4 nutrient-stress activation, revealing an unexpected metabolic consequence that contributes to the hemoglobinization defect.

    Evidence CRISPR KO in MEL and K562 cells, metabolomics, transcriptomics, arginine supplementation rescue

    PMID:37269954

    Open questions at the time
    • Whether arginine depletion is a direct consequence of biliverdin accumulation or an independent effect is unknown
    • Mechanism linking ABCB10 loss to amino acid transporter changes unresolved
  14. 2024 Medium

    Cardiomyocyte-specific ABCB10 deletion causing lysosomal iron accumulation and ferroptosis extended the gene's protective role to cardiac tissue and linked it mechanistically to lysosomal integrity.

    Evidence Cardiomyocyte-specific Abcb10 KO mouse, iron chelator rescue, lipid peroxide and lysosomal morphology analysis

    PMID:38655715

    Open questions at the time
    • How mitochondrial biliverdin export prevents lysosomal iron accumulation is mechanistically unclear
    • Not independently replicated
  15. 2025 High

    Identifying transmembrane arginines R232 and R295 as required for biliverdin-stimulated ATPase activity and conformational change provided the first residue-level understanding of substrate recognition in the transport cycle.

    Evidence Site-directed mutagenesis, ATPase assays with biliverdin analogs, LRET conformational monitoring

    PMID:41229075

    Open questions at the time
    • No substrate-bound structure to confirm direct contact with R232/R295
    • Full transport cycle conformational dynamics not yet captured

Open questions

Synthesis pass · forward-looking unresolved questions
  • A substrate-bound structure of ABCB10, the complete transport cycle mechanism for biliverdin, and whether ABCB10 transports additional substrates remain unresolved.
  • No cryo-EM or crystal structure with biliverdin bound
  • Whether cardiolipin regulation and glutathione redox sensing converge on a single conformational switch is unknown
  • Mechanism linking biliverdin accumulation to arginine depletion and ATF4 activation uncharacterized

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140657 ATP-dependent activity 5 GO:0005215 transporter activity 2
Localization
GO:0005739 mitochondrion 5
Pathway
R-HSA-1430728 Metabolism 4 R-HSA-8953897 Cellular responses to stimuli 3 R-HSA-382551 Transport of small molecules 2
Partners
ABCB7FECHSLC25A37
Complex memberships
Mitoferrin-1–ABCB10–ferrochelatase–ABCB7 complex

Evidence

Reading pass · 22 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2013 Crystal structures of ABCB10 in apo- and nucleotide-bound states reveal a classic exporter-fold ABC transporter in an open-inwards conformation; unexpectedly, ABCB10 adopts an open-inwards conformation even when complexed with non-hydrolysable ATP analogs (unlike other transporters that adopt open-outwards conformations with ATP), and a portal between two transmembrane helices is proposed to assist substrate entry into the binding cavity. X-ray crystallography with functional structural analysis; multiple ABCB10/ATP-analog complexes Proceedings of the National Academy of Sciences of the United States of America High 23716676
2004 ABCB10 contains an unusually long 105-amino acid mitochondrial targeting presequence (mTP); the central subdomain (aa 36-70) is sufficient for mitochondrial import, while the N-terminal subdomain participates in proper inner membrane import. Hydrophobic character of the mTP is required (L46Q/I47Q mutation greatly diminishes targeting). ABCB10 homodimerizes and homo-oligomerizes in the mitochondrial inner membrane as shown by mass spectrometry of chemically cross-linked immunoprecipitated protein. Mutagenesis of targeting sequence, subcellular fractionation/live imaging, mass spectrometry of cross-linked immunoprecipitated protein The Journal of biological chemistry High 15215243
2009 ABCB10 physically interacts with mitoferrin-1 (Mfrn1/Slc25a37) in the mitochondrial inner membrane of erythroid cells, and this interaction stabilizes Mfrn1 protein, thereby enhancing Mfrn1-dependent mitochondrial iron importation. The binding domain maps to the N-terminus of Mfrn1. In vivo epitope-tagging affinity purification and mass spectrometry, co-immunoprecipitation/Western blot, transfection in heterologous COS7 cells, protein half-life assays Proceedings of the National Academy of Sciences of the United States of America High 19805291
2010 Ferrochelatase (Fech), the terminal heme synthesis enzyme, forms an oligomeric complex with both mitoferrin-1 (Mfrn1) and ABCB10 in erythroid cells, physically integrating mitochondrial iron importation and heme biosynthesis. Affinity purification and mass spectrometry from stable MEL cell clones, immunoprecipitation/Western blot with endogenous and heterologous proteins in MEL and HEK293 cells Blood High 20427704
2019 Dimeric ferrochelatase bridges ABCB7 and ABCB10 homodimers in an architecturally defined multiprotein complex required for heme biosynthesis; the interaction interfaces were mapped by chemical cross-linking, tandem mass spectrometry, and mutational analyses, with ferrochelatase binding near the nucleotide-binding domains of each ABC transporter. Chemical cross-linking, tandem mass spectrometry, mutational analysis, inducible knockdown cell lines Haematologica High 30765471
2012 ABC-me/ABCB10 is essential for erythropoiesis in vivo: ABCB10-knockout mice die at embryonic day 12.5 with near-complete loss of primitive erythropoiesis; knockout erythroid precursors show increased mitochondrial superoxide production and protein carbonylation, and treatment with the SOD2 mimetic MnTBAP rescues survival and differentiation, placing ABCB10 upstream of oxidative stress-mediated apoptosis in erythroid development. Germline knockout mouse, in vivo and ex vivo erythroid differentiation assays, mitochondrial ROS measurement, antioxidant rescue experiments Cell death and differentiation High 22240895
2015 Gly497 and Lys498 (Walker A), Glu624 (Walker B), and Gly602 (C-loop) in ABCB10 are required for proper ATP binding and hydrolysis. Oxidized glutathione (GSSG) stimulates ABCB10 ATPase activity without affecting ATP binding, while reduced glutathione (GSH) inhibits both ATP binding and hydrolysis; ABCB10 is glutathionylated at Cys547. Delta-aminolevulinic acid (dALA) does not alter ATP binding, excluding it as a direct substrate. 8-azido-ATP photolabeling, site-directed mutagenesis, in vitro ATPase assays, mass spectrometry identification of glutathionylation site PloS one High 26053025
2017 ATPase activity of ABCB10 is necessary for hemoglobinization in erythroid MEL cells. Reduced ABCB10 does not cause protoporphyrin IX accumulation and does not affect ALA export from mitochondria, ruling out ALA as a transported substrate. ABCB10 silencing alters the heme biosynthesis transcriptional profile via Bach1-mediated repression, which can be partially rescued by overexpression of Alas2 or Gata1. shRNA knockdown in MEL cells, ATPase activity assays, succinylacetone inhibition of ALAD, metabolite measurements, transcriptional profiling, rescue experiments The Journal of biological chemistry High 28808058
2021 ABCB10 is a mitochondrial biliverdin exporter: ABCB10 reconstituted into liposomes transports biliverdin, and ABCB10 deletion causes accumulation of biliverdin inside mitochondria. In obese mice, ABCB10-driven biliverdin export amplifies cytosolic bilirubin content, which inactivates PTP1B and elevates SREBP-1c, exacerbating insulin resistance and steatosis; restoration of cellular bilirubin in ABCB10 KO hepatocytes reverses improvements in mitochondrial function and PTP1B inactivation. Reconstitution of ABCB10 in liposomes with transport assay, ABCB10 hepatocyte-specific KO mice, metabolite measurements, rescue with bilirubin treatment Science translational medicine High 34011630
2020 Zinc-mesoporphyrin stimulates ABCB10 ATPase activity (~70% increase) in purified ABCB10 reconstituted in lipid nanodiscs; this stimulation is specific to ABCB10 (not a bacterial ABC transporter control) and does not require typical heme regulatory motifs (cysteine-less ABCB10 also responds). Delta-aminolevulinic acid and glutathione do not activate ABCB10, further excluding them as direct substrates. Purified ABCB10 reconstituted in nanodiscs, in vitro ATPase assays with heme analogs and precursors PloS one High 33253225
2023 ABCB10 binds cardiolipin with significantly higher affinity than other phospholipids, with the first three cardiolipin binding events showing positive cooperativity suggestive of specific binding sites; cardiolipin regulates ABCB10 ATPase activity in a dose-dependent fashion. Native mass spectrometry for lipid binding, in vitro ATPase assays with various phospholipids Biochemistry High 37807693
2017 ABCB10 expression is regulated by the transcription factor Nrf2 in blood-brain barrier endothelial cells: Nrf2 silencing suppresses ABCB10 protein, while Nrf2 activation by sulforaphane upregulates ABCB10. Conversely, ABCB10 knockdown induces Nrf2-driven antioxidant responses and elevates endothelial-monocyte adhesion. siRNA knockdown of Nrf2 and ABCB10 in human BBB endothelial cells, Western blot, sulforaphane treatment Neuroscience letters Medium 28572033
2014 ABCB10 transcription is regulated by E2F transcription factors: E2F2, E2F3, and E2F4 activate transcription from the ABCB10 promoter; E2F4 directly binds to ABCB10 promoter sites (confirmed by EMSA and ChIP), and silencing E2F factors reduces basal ABCB10 expression. Promoter cloning, luciferase reporter assay, EMSA, ChIP, siRNA knockdown of E2F factors Genomics Medium 25220178
2019 Mutant huntingtin (mtHtt) inhibits the mitochondrial unfolded protein response (UPRmt) by impairing ABCB10 mRNA stability; ABCB10 depletion reduces UPRmt markers HSP60, Clpp, and CHOP, and increases mitochondrial ROS and cell death, while ABCB10 overexpression rescues these phenotypes. HD mouse striatal cells and patient fibroblasts, siRNA knockdown, overexpression, mRNA stability assays, ROS measurement, Western blot Biochimica et biophysica acta. Molecular basis of disease Medium 30802639
2017 ABCB10 depletion in HepG2 cells upregulates ROS and ROS-detoxifying enzymes (SOD2, GSTA1, GSTA2, SESN3) and significantly decreases expression of UPRmt-related mitochondrial chaperones (HSPD1, DNAJA3) and protease LONP1, supporting a role for ABCB10 in UPRmt signaling similar to C. elegans HAF-1. siRNA knockdown in HepG2 cells, Western blot, ROS measurement, qPCR Biochemical and biophysical research communications Low 28315685
2023 Loss of Abcb10 in erythroid cells causes decreased cellular arginine levels, altered expression of amino acid transporters, and activation of the ATF4 nutrient stress pathway (increased eIF2α phosphorylation, upregulated ATF4 and targets CHOP, Chac1, Rars), with arginine supplementation improving proliferation and hemoglobinization in Abcb10-null cells. CRISPR/Cas9 deletion in MEL and K562 cells, metabolomic and transcriptional analyses, arginine supplementation rescue The Journal of biological chemistry Medium 37269954
2021 ABCB10 loss in CD4+ T cells impairs specific cytokine expression upon activation, reduces CD4+ cell numbers and Ag-specific memory formation in vivo, and disrupts the switch to aerobic glycolysis upon activation in Jurkat T cells; CD8+ T cells are less affected, indicating a cell-type-selective metabolic role. Conditional Abcb10 KO mice, in vivo viral infection model, CRISPR KO in Jurkat cells, cytokine assays, metabolic profiling Journal of immunology Medium 34893527
2024 Cardiomyocyte-specific deletion of Abcb10 causes progressive cardiac fibrosis and mitochondrial structural abnormalities, leading to lysosomal dysfunction (decreased NAD+ levels, Hif1α upregulation), accumulation of Fe2+ and lipid peroxides in lysosomes, and ferroptosis; iron chelator treatment suppresses lipid peroxidation, implicating lysosomal iron accumulation as the mechanistic driver. Cardiomyocyte-specific Abcb10 KO mouse, ABCB10 knockdown in HeLa cells, iron chelator treatment, ROS and lipid peroxide measurement, lysosomal morphology analysis Bioscience reports Medium 38655715
2024 Induced deletion of Abcb10 in adult mouse hematopoietic stem cells (HSCs) causes increased erythroid progenitor numbers and decreased HSC number; Abcb10-deficient HSCs show excess mitochondrial iron accumulation and oxidative stress, with a skew toward erythroid-lineage differentiation, but no alteration in mitochondrial bioenergetic function. Inducible Abcb10 KO in adult mice, flow cytometry of bone marrow progenitors, mitochondrial iron and ROS measurement, in vivo iron chelator and antioxidant treatment Experimental hematology Medium 38493949
2024 Hepatocyte-specific ABCB10 gain-of-function in mice with alcoholic hepatitis increases the mitochondrial GSH/GSSG ratio and decreases hepatic 4-HNE protein adducts, reducing MPO gene expression and histone H3 citrullination (NET formation marker), demonstrating that ABCB10-mediated ROS reduction in hepatocytes mitigates neutrophilic inflammation. Hepatocyte-specific ABCB10 overexpression in alcoholic hepatitis mouse model, redox assays, MPO/NET markers, GSH/GSSG ratio Redox biology Medium 38290384
2021 Beta-cell-specific deletion of Abcb10 protects mice from high-fat diet-induced hyperinsulinemia and insulin resistance by limiting beta-cell expansion; ABCB10 activity limits glucose-stimulated insulin secretion (GSIS) and H2O2-mediated signaling, and bilirubin treatment of ABCB10 KO islets reverses increased H2O2 and GSIS, placing bilirubin as the effector downstream of ABCB10. Beta-cell-specific Abcb10 KO mouse (Ins1Cre-Abcb10flox/flox), GSIS assays, H2O2 measurement, bilirubin rescue in isolated islets Molecular metabolism Medium 34823065
2025 Conserved transmembrane arginine residues R232 and R295 of ABCB10 are required for biliverdin-stimulated ATPase activity; mutation of these residues decreases stimulation by biliverdin and alters conformational equilibrium detected by LRET. Biliverdin dimethyl ester does not stimulate (and mesobiliverdin inhibits) ABCB10 ATPase, indicating specific complementarity between biliverdin functional groups and the substrate binding pocket. GDN detergent abolishes biliverdin-induced stimulation, suggesting it interferes with substrate binding. Site-directed mutagenesis of transmembrane arginines, in vitro ATPase assay with biliverdin analogs, Luminescence Resonance Energy Transfer (LRET) conformational assay Protein science High 41229075

Source papers

Stage 0 corpus · 52 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2017 Circular RNA circ-ABCB10 promotes breast cancer proliferation and progression through sponging miR-1271. American journal of cancer research 305 28744405
2013 Structures of ABCB10, a human ATP-binding cassette transporter in apo- and nucleotide-bound states. Proceedings of the National Academy of Sciences of the United States of America 191 23716676
2009 Abcb10 physically interacts with mitoferrin-1 (Slc25a37) to enhance its stability and function in the erythroid mitochondria. Proceedings of the National Academy of Sciences of the United States of America 169 19805291
2010 Ferrochelatase forms an oligomeric complex with mitoferrin-1 and Abcb10 for erythroid heme biosynthesis. Blood 128 20427704
2020 Circ-ABCB10 Contributes to Paclitaxel Resistance in Breast Cancer Through Let-7a-5p/DUSP7 Axis. Cancer management and research 79 32273769
2012 Mitochondrial ABC transporters function: the role of ABCB10 (ABC-me) as a novel player in cellular handling of reactive oxygen species. Biochimica et biophysica acta 69 22884976
2004 Targeting, import, and dimerization of a mammalian mitochondrial ATP binding cassette (ABC) transporter, ABCB10 (ABC-me). The Journal of biological chemistry 57 15215243
2020 Knockdown of circ-ABCB10 promotes sensitivity of lung cancer cells to cisplatin via miR-556-3p/AK4 axis. BMC pulmonary medicine 46 31931771
2019 Dimeric ferrochelatase bridges ABCB7 and ABCB10 homodimers in an architecturally defined molecular complex required for heme biosynthesis. Haematologica 44 30765471
2021 ABCB10 exports mitochondrial biliverdin, driving metabolic maladaptation in obesity. Science translational medicine 43 34011630
2012 The mitochondrial transporter ABC-me (ABCB10), a downstream target of GATA-1, is essential for erythropoiesis in vivo. Cell death and differentiation 43 22240895
2019 Circular RNA ABCB10 correlates with advanced clinicopathological features and unfavorable survival, and promotes cell proliferation while reduces cell apoptosis in epithelial ovarian cancer. Cancer biomarkers : section A of Disease markers 42 31381507
2000 M-ABC2, a new human mitochondrial ATP-binding cassette membrane protein. FEBS letters 37 10922475
2017 Blood-brain barrier disruption in diabetic mice is linked to Nrf2 signaling deficits: Role of ABCB10? Neuroscience letters 36 28572033
2020 Circular RNA ABCB10 promotes non-small cell lung cancer progression by increasing E2F5 expression through sponging miR-584-5p. Cell cycle (Georgetown, Tex.) 31 32420810
2019 Mutant huntingtin inhibits the mitochondrial unfolded protein response by impairing ABCB10 mRNA stability. Biochimica et biophysica acta. Molecular basis of disease 31 30802639
2017 Reductions in the mitochondrial ABC transporter Abcb10 affect the transcriptional profile of heme biosynthesis genes. The Journal of biological chemistry 26 28808058
2019 Circular RNA ABCB10 promotes hepatocellular carcinoma progression by increasing HMG20A expression by sponging miR-670-3p. Cancer cell international 24 31889891
2016 Identification of a novel β-adrenergic octopamine receptor-like gene (βAOR-like) and increased ATP-binding cassette B10 (ABCB10) expression in a Rhipicephalus microplus cell line derived from acaricide-resistant ticks. Parasites & vectors 22 27484910
2021 Circular RNA ABCB10 promotes cell proliferation and invasion, but inhibits apoptosis via regulating the microRNA‑1271‑mediated Capn4/Wnt/β‑catenin signaling pathway in epithelial ovarian cancer. Molecular medicine reports 21 33760208
2020 Circular RNA-ABCB10 suppresses hepatocellular carcinoma progression through upregulating NRP1/ABL2 via sponging miR-340-5p/miR-452-5p. European review for medical and pharmacological sciences 19 32196586
2020 Circ-ABCB10 acts as an oncogene in glioma cells via regulation of the miR-620/FABP5 axis. European review for medical and pharmacological sciences 17 32633377
2021 Circular RNA circ_ABCB10 in cancer. Clinica chimica acta; international journal of clinical chemistry 15 33746018
2021 Circ-ABCB10 knockdown inhibits the malignant progression of cervical cancer through microRNA-128-3p/ZEB1 axis. Biological procedures online 15 34493213
2017 ABCB10 depletion reduces unfolded protein response in mitochondria. Biochemical and biophysical research communications 15 28315685
2021 Circular RNA ABCB10 contributes to laryngeal squamous cell carcinoma (LSCC) progression by modulating the miR-588/CXCR4 axis. Aging 13 34015764
2020 Circular RNA circ-ABCB10 promotes non-small cell lung cancer proliferation and inhibits cell apoptosis through repressing KISS1. European review for medical and pharmacological sciences 12 32196602
2020 Stimulation of the human mitochondrial transporter ABCB10 by zinc-mesoporphrin. PloS one 11 33253225
2024 Cardiomyocyte-specific deletion of the mitochondrial transporter Abcb10 causes cardiac dysfunction via lysosomal-mediated ferroptosis. Bioscience reports 10 38655715
2020 Circ-ABCB10 accelerates the malignant progression of oral squamous cell carcinoma by absorbing miRNA-145-5p. European review for medical and pharmacological sciences 10 32016969
2015 ATP Binding and Hydrolysis Properties of ABCB10 and Their Regulation by Glutathione. PloS one 10 26053025
2022 CircRNA-ABCB10 promotes gastric cancer progression by sponging miR-1915-3p to upregulate RaC1. Digestive and liver disease : official journal of the Italian Society of Gastroenterology and the Italian Association for the Study of the Liver 9 34987010
2020 Circ-ABCB10 promotes proliferation and invasion of esophageal squamous cell carcinoma cells by modulating microRNA-670-3p. European review for medical and pharmacological sciences 9 32572924
2020 Circ-ABCB10 promotes growth and metastasis of nasopharyngeal carcinoma by upregulating ROCK1. European review for medical and pharmacological sciences 9 33336739
2023 Cardiolipin Regulates the Activity of the Mitochondrial ABC Transporter ABCB10. Biochemistry 8 37807693
2020 Circular RNA circ-ABCB10 promotes the proliferation and invasion of thyroid cancer by targeting KLF6. European review for medical and pharmacological sciences 7 32096158
2020 Circular RNA circ-ABCB10 promotes the proliferation and invasion of thyroid cancer by targeting KLF6. European review for medical and pharmacological sciences 7 33090448
2023 Loss of the mitochondrial protein Abcb10 results in altered arginine metabolism in MEL and K562 cells and nutrient stress signaling through ATF4. The Journal of biological chemistry 6 37269954
2022 The Emerging Roles of Circ-ABCB10 in Cancer. Frontiers in cell and developmental biology 6 35646916
2020 Circular RNA-ABCB10 promotes angiogenesis induced by conditioned medium from human amnion-derived mesenchymal stem cells via the microRNA-29b-3p/vascular endothelial growth factor A axis. Experimental and therapeutic medicine 6 32782512
2014 Regulation of the human ABCB10 gene by E2F transcription factors. Genomics 5 25220178
2024 The mitochondrial biliverdin exporter ABCB10 in hepatocytes mitigates neutrophilic inflammation in alcoholic hepatitis. Redox biology 4 38290384
2021 [Effects of silencing circRNA ABCB10 expression on biological properties of colorectal cancer cells]. Zhonghua zhong liu za zhi [Chinese journal of oncology] 4 33902207
2020 Circular RNA circ-ABCB10 promotes non-small cell lung cancer proliferation and inhibits cell apoptosis through repressing KISS1. European review for medical and pharmacological sciences 4 32706038
2021 Deletion of ABCB10 in beta-cells protects from high-fat diet induced insulin resistance. Molecular metabolism 3 34823065
2022 Circular RNA circ-ABCB10 Promotes Proliferation and Inhibits Apoptosis of Laryngeal Carcinoma by Inhibiting KLF6. Computational and mathematical methods in medicine 2 35756421
2026 Mitochondrial Transporter ABCB10 Protects Against Doxorubicin-Induced Respiratory Muscle Dysfunction Independent of Changes to Diaphragm Accumulation. Journal of cachexia, sarcopenia and muscle 1 41545030
2024 Abcb10 regulates murine hematopoietic stem cell potential and erythroid differentiation. Experimental hematology 1 38493949
2021 ABCB10 Loss Reduces CD4+ T Cell Activation and Memory Formation. Journal of immunology (Baltimore, Md. : 1950) 1 34893527
2025 The ATPase activity of ABCB10 is modulated by conserved transmembrane arginine residues and by functional groups in the biliverdin molecule. Protein science : a publication of the Protein Society 0 41229075
2023 Retracted: Circular RNA circ-ABCB10 Promotes Proliferation and Inhibits Apoptosis of Laryngeal Carcinoma by Inhibiting KLF6. Computational and mathematical methods in medicine 0 37416291
2020 Retraction Note to: Circular RNA ABCB10 promotes hepatocellular carcinoma progression by increasing HMG20A expression by sponging miR-670-3p. Cancer cell international 0 33041666