Affinage

ABCD3

ATP-binding cassette sub-family D member 3 · UniProt P28288

Round 2 corrected
Length
659 aa
Mass
75.5 kDa
Annotated
2026-04-28
65 papers in source corpus 23 papers cited in narrative 22 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

ABCD3 (PMP70) is a peroxisomal membrane ABC half-transporter that homodimerizes to import branched-chain fatty acids, long-chain dicarboxylic acids, and C27 bile acid intermediates as CoA esters into the peroxisome for β-oxidation and bile acid biosynthesis (PMID:24333844, PMID:25168382). ATP binding induces nucleotide-binding domain dimerization and conformational changes that drive an ATPase cycle with substrate-stimulated hydrolysis; Mg²⁺ is required for catalytic turnover, and substrate binding brings the two NBDs closer together to activate ATPase activity (PMID:12176987, PMID:11883951). Correct peroxisomal targeting depends on an N-terminal ER-suppressor motif (notably Ser5) cooperating with the first two transmembrane domains, and on co-translational chaperoning by Pex19p, while protein quality is maintained by VCP–FAF2-mediated regulation of ABCD3 ubiquitination that prevents excessive pexophagy (PMID:26711236, PMID:16344115, PMID:39929145). Loss-of-function mutations in ABCD3 cause accumulation of C27-bile acid intermediates and impaired pristanic acid oxidation in humans and mice, and CCG repeat expansions in ABCD3 cause oculopharyngodistal myopathy (PMID:25168382, PMID:39068203).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 1993 Medium

    Identifying ABCD3 as a peroxisomal ABC transporter established the gene family context and predicted ATP-dependent transport across the peroxisomal membrane.

    Evidence cDNA cloning and hydropathy analysis from rat and human liver libraries

    PMID:8411712

    Open questions at the time
    • No transport substrate identified
    • No functional assay performed
    • Domain architecture inferred from homology only
  2. 2002 High

    Biochemical dissection of ATP binding and hydrolysis revealed that ABCD3 requires Mg²⁺ for ATPase turnover and undergoes nucleotide-dependent conformational changes consistent with a dimeric catalytic mechanism, distinguishing it from vanadate-trappable ABC transporters.

    Evidence Photoaffinity labeling with azido-ATP analogs, limited trypsinolysis with multiple nucleotides, and gel filtration of rat liver peroxisomes

    PMID:11883951 PMID:12176987

    Open questions at the time
    • No transport substrate identified at this stage
    • ATPase assay performed on endogenous membranes rather than reconstituted protein
    • Dimerization stoichiometry inferred from fragment size on gel filtration
  3. 2004 High

    Purification of native PMP70 complexes from mouse liver demonstrated that ABCD3 predominantly forms homodimers in vivo, resolving the question of whether it required ABCD1 as a heterodimerization partner.

    Evidence Two-step purification to homogeneity and reciprocal immunoprecipitation of ALDP complexes from mouse liver

    PMID:15276650

    Open questions at the time
    • Heterodimerization with ABCD1 not excluded under all conditions
    • Functional significance of homodimer versus heterodimer not tested
  4. 2005 High

    Establishing that Pex19p chaperones nascent ABCD3 co-translationally to prevent aggregation answered how a polytopic membrane protein reaches the peroxisome post-translationally.

    Evidence In vitro translation with purified Pex19p, co-immunoprecipitation, and GFP-fusion localization in CHO cells

    PMID:16344115

    Open questions at the time
    • Identity of the membrane insertion machinery at the peroxisome not resolved
    • Whether Pex19p is strictly required or facilitatory was debated across studies
  5. 2007 High

    Live-cell FRET confirmed ABCD3 forms both homodimers and heterodimers with ABCD1 in intact peroxisomal membranes, refining the earlier homodimer-only model and raising questions about heterodimer-specific substrate channeling.

    Evidence FRET microscopy with statistical probability-distribution analysis in living cells; C-terminal deletion mapping of dimerization domains

    PMID:17609205

    Open questions at the time
    • Functional consequences of heterodimerization not determined
    • Relative abundance of heterodimers versus homodimers in different tissues unknown
  6. 2009 Medium

    Systematic domain-swap experiments revealed that the N-terminal 80-residue segment suppresses an intrinsic ER-targeting signal in TM1, explaining how ABCD3 escapes the secretory pathway to reach peroxisomes.

    Evidence EGFP fusion constructs with deletions and domain swaps expressed in COS cells; fluorescence microscopy

    PMID:20007743

    Open questions at the time
    • Cytosolic factors recognizing the suppressor motif not identified at this stage
    • Mechanism by which TM1 alone targets ER not resolved
  7. 2013 High

    Functional complementation of yeast pxa1/pxa2Δ mutants with human ABCD3 defined its substrate preference for branched-chain, long-chain unsaturated, and dicarboxylic fatty acyl-CoAs, distinguishing ABCD3 from ABCD1 and ABCD2.

    Evidence β-oxidation assays with multiple fatty acid substrates in yeast expressing individual human ABCD transporters

    PMID:24333844

    Open questions at the time
    • Direct transport assay with purified protein not performed
    • In vivo substrate hierarchy in mammals not established
  8. 2014 High

    Human patient and mouse knockout studies proved ABCD3 is essential for peroxisomal import of C27 bile acid intermediates and pristanic acid, linking ABCD3 loss to a defined metabolic disease with bile acid accumulation.

    Evidence Fibroblast analysis from patient with truncating ABCD3 mutation; Abcd3−/− mice with bile acid profiling and phytol loading

    PMID:25168382

    Open questions at the time
    • Full clinical spectrum of ABCD3 deficiency not delineated
    • Whether residual transport occurs via ABCD1/ABCD2 compensation not quantified
  9. 2015 Medium

    Pinpointing Ser5 as the critical residue in the ER-suppressor motif showed that a single amino acid substitution reroutes ABCD3 to the ER, narrowing the targeting code to a defined molecular determinant.

    Evidence Ser5Ala point mutagenesis with fluorescence microscopy in COS cells; crosslinking to identify ~50 kDa and ~20 kDa binding partners

    PMID:26711236

    Open questions at the time
    • Identity of the ~50 kDa and ~20 kDa crosslinked proteins not determined
    • Whether Ser5 phosphorylation regulates targeting not tested
  10. 2018 High

    Demonstrating that peroxisomes accept acylcarnitines via ABCD3/HSD17B4 and compensate for mitochondrial FAO deficiency expanded the physiological scope of ABCD3 from bile acid/branched-chain metabolism to medium/long-chain fatty acid oxidation.

    Evidence CRISPR-Cas9 single and double KO in HEK-293 cells; CPT2 inhibition; acylcarnitine profiling; Hsd17b4 KO mouse with CPT2 inhibition

    PMID:30540494

    Open questions at the time
    • Whether ABCD3 directly transports acylcarnitines or CoA-converted intermediates not resolved
    • Tissue specificity of this compensatory pathway not fully mapped
  11. 2024 Medium

    Discovery of CCG repeat expansions in ABCD3 as a cause of oculopharyngodistal myopathy established a second distinct disease mechanism (repeat expansion/RNA toxicity) separate from loss-of-function metabolic disease.

    Evidence Repeat expansion genotyping, long-read sequencing, RT-qPCR of ABCD3 transcript in patient fibroblasts and muscle

    PMID:39068203

    Open questions at the time
    • RNA toxicity mechanism not directly demonstrated
    • Whether ABCD3 protein function is altered by repeat expansion not tested
    • Replication in larger cohorts needed
  12. 2025 Medium

    VCP–FAF2-mediated regulation of ABCD3 ubiquitination was shown to control peroxisome abundance by preventing excessive pexophagy, establishing ABCD3 as a key ubiquitination target in peroxisome quality control.

    Evidence VCP inhibition and FAF2 KO with quantitative proteomics, ubiquitination assays, and USP30 rescue

    PMID:39929145

    Open questions at the time
    • Specific ubiquitination sites on ABCD3 not mapped
    • Whether ubiquitinated ABCD3 is directly recognized by autophagy receptors not resolved
  13. 2025 High

    Cryo-EM structures of apo and phytanoyl-CoA-bound ABCD3 revealed that substrate binding brings the two NBDs closer together, providing the structural basis for substrate-stimulated ATPase activity and completing the transport cycle model.

    Evidence Cryo-EM at 3.1–3.3 Å resolution of full-length human ABCD3; ATPase assay (preprint)

    PMID:bio_10.1101_2025.05.21.655323

    Open questions at the time
    • Structures of nucleotide-bound and post-hydrolysis states not yet captured
    • Mechanism of substrate release into the peroxisomal lumen not resolved
    • Preprint — awaits peer review

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key unresolved questions include the structural basis of the complete transport cycle (nucleotide-bound and outward-open states), the identity of cytosolic factors that interact with the Ser5 ER-suppressor motif, the functional significance of ABCD1–ABCD3 heterodimers versus homodimers in different tissues, and the molecular mechanism of RNA toxicity in ABCD3 repeat expansion disease.
  • Full transport cycle intermediates not structurally resolved
  • Tissue-specific roles of heterodimer versus homodimer unknown
  • RNA toxicity mechanism in OPDM not directly demonstrated

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0005215 transporter activity 3 GO:0016787 hydrolase activity 3 GO:0140657 ATP-dependent activity 3
Localization
GO:0005777 peroxisome 7
Pathway
R-HSA-382551 Transport of small molecules 5 R-HSA-1430728 Metabolism 3 R-HSA-1852241 Organelle biogenesis and maintenance 2 R-HSA-9612973 Autophagy 1
Partners
ABCD1FAF2HSD17B4INTS7PEX19PEX2USP30VCP
Complex memberships
ABCD1-ABCD3 heterodimerABCD3 homodimer

Evidence

Reading pass · 22 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1993 PMP70 (ABCD3) was identified as an ATP-binding cassette (ABC) transporter localized to the peroxisomal membrane, with a domain structure comprising six transmembrane segments and a hydrophilic ATP-binding domain homologous to other ABC transporters, suggesting involvement in ATP-dependent transport across the peroxisomal membrane. cDNA cloning and hydropathy analysis of rat and human liver cDNA libraries Nihon rinsho. Japanese journal of clinical medicine Medium 8411712
1998 The human PMP70 gene (PXMP1/ABCD3) was mapped to chromosome 1p21-p22, spans ~65 kb with 23 exons, and its promoter contains housekeeping gene features (high GC content, Sp1 sites) but no peroxisome proliferator responsive element, distinguishing it structurally from the related ALD gene. Genomic cloning, exon-intron mapping, 5' flanking region analysis, chromosomal localization Genomics Medium 9521874
1998 Overexpression of PMP70 (ABCD3) restores peroxisome biogenesis in PEX2-deficient CHO cell clones, as confirmed by subcellular latency of catalase, immunolocalization of catalase, and beta-oxidation of very long chain fatty acids; a Zellweger syndrome-associated mutant allele of PMP70 failed to rescue, indicating a functional interaction between PEX2 and PMP70 in peroxisome membrane assembly. Transfection rescue experiments in PEX2-mutant CHO cells; catalase latency assay; immunohistochemistry; VLCFA beta-oxidation assay European journal of cell biology High 9765053
2000 PMP70 (ABCD3) is synthesized on free polysomes and posttranslationally inserted into peroxisomal membranes, where it assembles as dimeric or oligomeric forms, consistent with a role in long-chain acyl-CoA transport across the peroxisomal membrane. Cell fractionation, immunoblot, and biochemical characterization of peroxisomal membranes Cell biochemistry and biophysics Medium 11330039
2001 Efficient peroxisomal targeting of human PMP70 (ABCD3) requires three targeting elements in the amino-terminal region: amino acids 61–80 in the cytosol, and the first and second transmembrane domains; PEX19 interaction is not required for targeting. Expression of deletion constructs in CHO cells; immunofluorescence localization Biochemical and biophysical research communications Medium 11453642
2002 PMP70 (ABCD3) binds ATP tightly in the absence of Mg2+; in the presence of Mg2+, bound ATP is hydrolyzed to ADP which then dissociates, enabling ATPase turnover. PMP70 is also phosphorylated at a tyrosine residue(s). Vanadate-induced nucleotide trapping was not observed, distinguishing its mechanism from some other ABC transporters. Photoaffinity labeling of rat liver peroxisomes with 8-azido-[α-32P]ATP and 8-azido-[γ-32P]ATP; co-immunoprecipitation; Mg2+-dependent hydrolysis assay; vanadate trapping assay; phosphorylation detection The Journal of biological chemistry High 12176987
2002 ATP binding to PMP70 (ABCD3) induces nucleotide-dependent conformational changes detectable by limited trypsin digestion: MgATP or MgADP stabilize a ~30 kDa C-terminal fragment spanning the helical domain between Walker A and B motifs, while MgATP-γS protects the entire protein. The C-terminal fragment forms an ~60 kDa complex consistent with PMP70 dimerization on peroxisomal membranes. Limited trypsin digestion of rat liver peroxisomes pre-incubated with various nucleotides; immunoblot with anti-C-terminal antibody; gel filtration Biochemical and biophysical research communications High 11883951
2004 Mouse liver PMP70 (ABCD3) forms predominantly homomeric complexes in vivo; no evidence of heteromeric interactions with ALDP (ABCD1) or accessory proteins was found under normal physiological expression conditions. Two-step purification of PMP70 protein complex to homogeneity; preparative immunoprecipitation of ALDP complex; protein identification Biochimica et biophysica acta High 15276650
2005 Pex19p acts as a chaperone for PMP70 (ABCD3) during synthesis, binding co-translationally to prevent aggregation; the interaction requires both the N-terminal 61 amino acids and the region around TMD6 of PMP70, and deletion of either region abolishes peroxisomal localization. In vitro translation with purified Pex19p; co-immunoprecipitation; GFP fusion constructs expressed in CHO cells; immunofluorescence localization Biochimica et biophysica acta High 16344115
2007 In living cells, ALDP (ABCD1) and PMP70 (ABCD3) form both homodimers and heterodimers (ALDP/PMP70) in the peroxisomal membrane, with ALDP homodimers predominating. The last 87 C-terminal amino acids of ALDP constitute the primary dimerization domain, with the N-terminal transmembrane region providing additional stabilization of ALDP homodimers. FRET microscopy in intact living cells; probability distribution shift analysis; Kolmogorov-Smirnov statistics; C-terminal deletion constructs of ALDP The Journal of biological chemistry High 17609205
2008 Knockdown of PMP70 (ABCD3) in rat C6 glial cells impairs peroxisomal beta-oxidation and causes oxidative stress (elevated nitric oxide via iNOS upregulation, increased superoxide and lipid peroxidation, altered antioxidant enzyme activities). The resulting oxidative phenotype is dependent on IL-12 release rather than being a direct consequence of PMP70 loss. Stable RNAi knockdown of ABCD3 in C6 cells; nitrite measurement; superoxide and TBARS assays; antioxidant enzyme activity; cytokine quantification; neutralizing antibodies against IL-12 Neurochemistry international Medium 18992293
2009 The N-terminal 80-amino-acid segment (N80) of PMP70 (ABCD3) is critical for suppressing the intrinsic ER-targeting function of the TM1 segment: TM1 alone directs protein to the ER, the N80 segment alone targets mitochondrial outer membrane, but together N80 + TM1-TM2 directs exclusively to peroxisomes. Cooperation of multiple organelle-targeting signals enables correct peroxisomal localization. EGFP fusion constructs expressed in COS cells; fluorescence microscopy; deletion and domain-swap analysis Journal of biochemistry Medium 20007743
2013 ABCD3 (PMP70) transports long-chain unsaturated, long branched-chain, and long-chain dicarboxylic fatty acids (as CoA esters) into peroxisomes for beta-oxidation, with a substrate preference distinct from ABCD1 (favoring C24:0/C26:0) and ABCD2 (favoring C22:0/C22:6). Each peroxisomal half-transporter can function as a homodimer, demonstrated by partial rescue of the pxa1/pxa2Δ yeast mutant by human ABCD3. Functional complementation of pxa1/pxa2Δ yeast mutant; fatty acid oxidation measurements with multiple substrates in yeast expressing human ABCD transporters Biochimica et biophysica acta High 24333844
2014 ABCD3 is essential for peroxisomal transport of branched-chain fatty acids (e.g., pristanic acid) and C27 bile acid intermediates, making it a crucial step in bile acid biosynthesis. Loss of ABCD3 (patient with truncating mutation p.Y635NfsX1; Abcd3−/− mice) causes accumulation of C27-bile acid intermediates, reduced C24 bile acids, and reduced pristanic acid beta-oxidation, with peroxisomes remaining import-competent but reduced in number and enlarged. Patient fibroblast analysis; genetic analysis; Abcd3−/− mouse model; bile acid profiling in liver, bile and intestine; phytol loading assay; peroxisomal beta-oxidation assays Human molecular genetics High 25168382
2015 A short N-terminal sequence of nine residues in PMP70 (ABCD3), specifically Ser5, acts as an ER-targeting suppressor by blocking the intrinsic ER-targeting signal of the TM1 segment. The Ser5Ala point mutation causes PMP70 to localize predominantly to the ER. Two proteins of ~50 kDa and ~20 kDa crosslink with this suppressor motif. Point mutagenesis (Ser5Ala); fluorescence microscopy in COS cells; crosslinking to identify binding proteins; recombinant motif-GST competition assay Journal of biochemistry Medium 26711236
2018 Peroxisomes can oxidize medium- and long-chain fatty acids (lauric and palmitic acid) through a pathway requiring both ABCD3 and HSD17B4 (D-bifunctional protein). Peroxisomes accept acylcarnitines (not only acyl-CoAs) as substrates. This peroxisomal pathway becomes physiologically relevant when mitochondrial FAO is defective, as demonstrated in vivo by altered plasma acylcarnitine profiles in Hsd17b4 KO mice after acute CPT2 inhibition. CRISPR-Cas9 single and double KO of ABCD3, HSD17B4, and CPT2 in HEK-293 cells; pharmacological CPT2 inhibition; acylcarnitine profiling; Hsd17b4 KO mouse model with CPT2 inhibition FASEB journal High 30540494
2021 ABCD3 interacts with INTS7 in bone marrow mesenchymal stem cells; this INTS7-ABCD3 interaction promotes BM-MSC proliferation and osteoblastic differentiation while suppressing adipogenic differentiation, through suppression of oxidative stress (reduced ROS and γ-H2AX, maintained antioxidant levels). HDLBP, also identified as an ABCD3 interactor, did not share these functions. Co-immunoprecipitation (INTS7-ABCD3 interaction); siRNA knockdown of INTS7, ABCD3, and HDLBP; ROS quantification; γ-H2AX measurement; Alizarin Red S and Oil Red O staining for differentiation; apoptosis assays Frontiers in physiology Medium 34880777
2024 CCG repeat expansions in ABCD3 (118–694 repeats) cause oculopharyngodistal myopathy (OPDM) in individuals of European ancestry; ABCD3 transcript appears upregulated in fibroblasts and skeletal muscle from affected individuals, suggesting gain-of-function RNA toxicity as a disease mechanism. Repeat expansion genotyping; long-read sequencing; RT-qPCR of ABCD3 transcript levels in patient fibroblasts and skeletal muscle Nature communications Medium 39068203
2025 The VCP-FAF2 complex prevents excessive pexophagy by regulating the accumulation of ubiquitinated ABCD3; loss of FAF2 or inhibition of VCP increases ubiquitination of ABCD3 and drives peroxisome degradation via selective autophagy (pexophagy), which can be rescued by USP30 overexpression or depletion of autophagy receptors. VCP inhibition and FAF2 knockout; quantitative proteomics; ubiquitination assays for ABCD3; autophagy flux assays; USP30 overexpression rescue Autophagy Medium 39929145
2025 ABCD3 depletion in colorectal cancer cells reduces cell viability, proliferation, invasion, and migration; mechanistically, ABCD3 suppresses Wnt/β-catenin signaling, and its loss activates this pathway to promote malignant behavior. ABCD3 protein also protects against excessive lipid peroxidation and maintains neutral lipid and lipid droplet homeostasis in cancer cells. siRNA knockdown; CCK-8 proliferation assay; Transwell invasion/migration assay; Western blot; TCGA/WGCNA bioinformatics; lipid peroxidation assays; neutral lipid staining Molecular biology reports / Cell death & disease Low 40229252 40668324
2025 Cryo-EM structures of full-length human ABCD3 in apo (3.33 Å) and phytanoyl-CoA-bound (3.13 Å) states reveal that substrate binding brings the two nucleotide-binding domains (NBDs) closer together, mechanistically explaining how substrate binding stimulates ATPase activity. Biochemical assays confirm substrate-dependent ATPase activation. Cryo-EM structure determination; ATPase activity biochemical assay; structural comparison of apo vs. substrate-bound conformations bioRxiv (preprint)preprint High bio_10.1101_2025.05.21.655323
2025 Edited miR-579-3p (A-to-I editing) acquires ABCD3 as a novel target, suppressing ABCD3-mediated VLCFA beta-oxidation in astrocytes and thereby exacerbating hypoxic-ischemic brain damage; wild-type miR-579-3p does not target ABCD3. Dual-luciferase reporter assay confirming miRNA-ABCD3 3'UTR interaction; VLCFA measurement by ELISA; Western blot and RT-qPCR; in vivo HIBD mouse model Neurological research Medium 40937863

Source papers

Stage 0 corpus · 65 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
1997 A new class of membrane-bound chemokine with a CX3C motif. Nature 1651 9024663
2002 Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proceedings of the National Academy of Sciences of the United States of America 1479 12477932
1997 Identification and molecular characterization of fractalkine receptor CX3CR1, which mediates both leukocyte migration and adhesion. Cell 1173 9390561
2021 Dual proteome-scale networks reveal cell-specific remodeling of the human interactome. Cell 705 33961781
2011 Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Briefings in bioinformatics 656 21873635
2003 The disintegrin-like metalloproteinase ADAM10 is involved in constitutive cleavage of CX3CL1 (fractalkine) and regulates CX3CL1-mediated cell-cell adhesion. Blood 603 12714508
1998 Chemokines regulate hippocampal neuronal signaling and gp120 neurotoxicity. Proceedings of the National Academy of Sciences of the United States of America 569 9826729
1997 Neurotactin, a membrane-anchored chemokine upregulated in brain inflammation. Nature 535 9177350
2001 Tumor necrosis factor-alpha-converting enzyme (ADAM17) mediates the cleavage and shedding of fractalkine (CX3CL1). The Journal of biological chemistry 533 11495925
2010 Regulation of tau pathology by the microglial fractalkine receptor. Neuron 523 20920788
1994 Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. Gene 492 8125298
2003 Fractalkine preferentially mediates arrest and migration of CD16+ monocytes. The Journal of experimental medicine 449 12810688
2004 The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome research 438 15489334
2008 CX3CL1/fractalkine is released from apoptotic lymphocytes to stimulate macrophage chemotaxis. Blood 371 18799722
2000 Expression of CX3CR1 chemokine receptors on neurons and their role in neuronal survival. Proceedings of the National Academy of Sciences of the United States of America 321 10869418
2000 Fractalkine modulates TNF-alpha secretion and neurotoxicity induced by microglial activation. Glia 305 10652441
2009 Fractalkine and CX 3 CR1 regulate hippocampal neurogenesis in adult and aged rats. Neurobiology of aging 289 20018408
2013 Neuron-glia crosstalk in health and disease: fractalkine and CX3CR1 take centre stage. Open biology 278 24352739
2000 Fractalkine cleavage from neuronal membranes represents an acute event in the inflammatory response to excitotoxic brain damage. The Journal of neuroscience : the official journal of the Society for Neuroscience 262 10899174
2002 Dual functions of fractalkine/CX3C ligand 1 in trafficking of perforin+/granzyme B+ cytotoxic effector lymphocytes that are defined by CX3CR1 expression. Journal of immunology (Baltimore, Md. : 1950) 261 12055230
1999 Characterization of fractalkine in rat brain cells: migratory and activation signals for CX3CR-1-expressing microglia. Journal of immunology (Baltimore, Md. : 1950) 260 10415068
2003 Fractalkine in vascular biology: from basic research to clinical disease. Arteriosclerosis, thrombosis, and vascular biology 258 12969992
2000 Rapid progression to AIDS in HIV+ individuals with a structural variant of the chemokine receptor CX3CR1. Science (New York, N.Y.) 257 10731151
1998 Identification of CX3CR1. A chemotactic receptor for the human CX3C chemokine fractalkine and a fusion coreceptor for HIV-1. The Journal of biological chemistry 242 9726990
2015 Structural biology. Structural basis for chemokine recognition and activation of a viral G protein-coupled receptor. Science (New York, N.Y.) 235 25745166
2002 CX(3)C chemokine fractalkine in pulmonary arterial hypertension. American journal of respiratory and critical care medicine 205 12016106
2002 Fractalkine and fractalkine receptors in human neurons and glial cells. Journal of neuroscience research 191 12125082
1999 Molecular uncoupling of fractalkine-mediated cell adhesion and signal transduction. Rapid flow arrest of CX3CR1-expressing cells is independent of G-protein activation. The Journal of biological chemistry 185 10187784
2006 Fractalkine stimulates angiogenesis by activating the Raf-1/MEK/ERK- and PI3K/Akt/eNOS-dependent signal pathways. American journal of physiology. Heart and circulatory physiology 167 16877565
2009 Gene-centric association signals for lipids and apolipoproteins identified via the HumanCVD BeadChip. American journal of human genetics 164 19913121
2018 Peroxisomes can oxidize medium- and long-chain fatty acids through a pathway involving ABCD3 and HSD17B4. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 101 30540494
2002 Catalog of 605 single-nucleotide polymorphisms (SNPs) among 13 genes encoding human ATP-binding cassette transporters: ABCA4, ABCA7, ABCA8, ABCD1, ABCD3, ABCD4, ABCE1, ABCF1, ABCG1, ABCG2, ABCG4, ABCG5, and ABCG8. Journal of human genetics 95 12111378
2014 A novel bile acid biosynthesis defect due to a deficiency of peroxisomal ABCD3. Human molecular genetics 93 25168382
2013 A role for the human peroxisomal half-transporter ABCD3 in the oxidation of dicarboxylic acids. Biochimica et biophysica acta 83 24333844
2002 ATP binding/hydrolysis by and phosphorylation of peroxisomal ATP-binding cassette proteins PMP70 (ABCD3) and adrenoleukodystrophy protein (ABCD1). The Journal of biological chemistry 51 12176987
2004 Mouse liver PMP70 and ALDP: homomeric interactions prevail in vivo. Biochimica et biophysica acta 42 15276650
2007 Live cell FRET microscopy: homo- and heterodimerization of two human peroxisomal ABC transporters, the adrenoleukodystrophy protein (ALDP, ABCD1) and PMP70 (ABCD3). The Journal of biological chemistry 41 17609205
2005 Role of Pex19p in the targeting of PMP70 to peroxisome. Biochimica et biophysica acta 41 16344115
2000 The 70-kDa peroxisomal membrane protein (PMP70), an ATP-binding cassette transporter. Cell biochemistry and biophysics 39 11330039
1995 Localization of mRNAs for adrenoleukodystrophy and the 70 kDa peroxisomal (PMP70) proteins in the rat brain during post-natal development. Journal of neuroscience research 31 8583512
2010 Identification of novel SNPs of ABCD1, ABCD2, ABCD3, and ABCD4 genes in patients with X-linked adrenoleukodystrophy (ALD) based on comprehensive resequencing and association studies with ALD phenotypes. Neurogenetics 27 20661612
2021 INTS7-ABCD3 Interaction Stimulates the Proliferation and Osteoblastic Differentiation of Mouse Bone Marrow Mesenchymal Stem Cells by Suppressing Oxidative Stress. Frontiers in physiology 26 34880777
2001 Targeting elements in the amino-terminal part direct the human 70-kDa peroxisomal integral membrane protein (PMP70) to peroxisomes. Biochemical and biophysical research communications 26 11453642
2024 A CCG expansion in ABCD3 causes oculopharyngodistal myopathy in individuals of European ancestry. Nature communications 21 39068203
2002 Nucleotide-induced conformational changes of PMP70, an ATP binding cassette transporter on rat liver peroxisomal membranes. Biochemical and biophysical research communications 19 11883951
2000 Immunodetection of hepatic peroxisomal PMP70 as an indicator of peroxisomal proliferation in the mummichog, Fundulus heteroclitus. Marine environmental research 17 11460719
1998 Genomic organization of the 70-kDa peroxisomal membrane protein gene (PXMP1). Genomics 14 9521874
2009 Multiple organelle-targeting signals in the N-terminal portion of peroxisomal membrane protein PMP70. Journal of biochemistry 13 20007743
2015 Immunohistological analysis of ABCD3 expression in Caucasian and African American prostate tumors. BioMed research international 12 25802834
1998 Restoration of PEX2 peroxisome assembly defects by overexpression of PMP70. European journal of cell biology 12 9765053
2008 PMP70 knock-down generates oxidative stress and pro-inflammatory cytokine production in C6 glial cells. Neurochemistry international 10 18992293
1992 Major ATPases on clofibrate-induced rat liver peroxisomes are not associated with 70 kDa peroxisomal membrane protein (PMP70). Journal of biochemistry 10 1295880
2017 Flow Cytometric Analysis of the Expression Pattern of Peroxisomal Proteins, Abcd1, Abcd2, and Abcd3 in BV-2 Murine Microglial Cells. Methods in molecular biology (Clifton, N.J.) 8 28409470
2005 Limkain b1, a novel human autoantigen localized to a subset of ABCD3 and PXF marked peroxisomes. Clinical and experimental immunology 8 15932519
2002 Effects of vehicle, diet and gender on the expression of PMP70- and CYP2K1/2M1-like proteins in the mummichog. Marine environmental research 6 12408580
1998 Genomic organization and chromosomal localization of the human peroxisomal membrane protein-1-like protein (PXMP1-L) gene encoding a peroxisomal ABC transporter. FEBS letters 6 9599016
2025 Peroxisomal membrane protein PMP70 confers drug resistance in colorectal cancer. Cell death & disease 5 40229252
1998 The mouse gene encoding the peroxisomal membrane protein 1-like protein (PXMP1-L): cDNA cloning, genomic organization and comparative expression studies. FEBS letters 5 9738957
2019 Initiation of the ABCD3-I algorithm for expediated evaluation of transient ischemic attack patients in an emergency department. The American journal of emergency medicine 4 31230922
2015 The N-terminal motif of PMP70 suppresses cotranslational targeting to the endoplasmic reticulum. Journal of biochemistry 4 26711236
1993 [PMP70, the 70-kDa peroxisomal membrane protein: a member of the ATP-binding cassette transporters]. Nihon rinsho. Japanese journal of clinical medicine 3 8411712
2025 Quality control of ABCD3 by the VCP-FAF2 complex suppresses excessive pexophagy. Autophagy 1 39929145
2025 Mechanism of ABCD3 inhibiting colorectal cancer progression by regulating Wnt/β-catenin. Molecular biology reports 0 40668324
2025 A-to-I editing of miR-579-3p exacerbates neonatal hypoxic-ischemic brain injury via regulation of ABCD3-dependent lipid metabolism in astrocytes. Neurological research 0 40937863
2018 TIA patients with higher ABCD3-I scores are prone to a higher incidence of intracranial stenosis, unstable carotid plaques and multiple-vessel involvement. Functional neurology 0 30663969