ArticleNature communications2022
Structural basis of substrate recognition and translocation by human very long-chain fatty acid transporter ABCD1.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
20 citing papers in PubMed, 31 citations in OpenAlex.
- Article
- Genomic divergence, adaptation, and the genetic basis of quality traits in ancient walnut landraces and wild relatives.Horticulture research · 2026Article
- Structural basis for LMBD1-dependent trafficking and cobalamin export of ABCD4.Nature communications · 2026Article
- Structural insights into Arabidopsis thaliana CTS-mediated fatty acid and hormone metabolism.Nature communications · 2026Article
- Predictive modelling of the COMATOSE transporter reveals a conserved ligand binding pocket for acyl-CoAs.Scientific reports · 2026Article
- Adenosine triphosphate-binding cassette transporters: key players in maintaining fetal health during pregnancy.Frontiers in endocrinology · 2026Review
- Molecular mechanism of substrate transport by human peroxisomal ABCD3.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Review
- Novel ABCD1 and MTHFSD Variants in Taiwanese Bipolar Disorder: A Genetic Association Study.Medicina (Kaunas, Lithuania) · 2025Article
- Mechanism and therapeutic potential of liver injury induced by cholesterol-associated proteins.Frontiers in pharmacology · 2025Review
- Review
- Structural insights into human ABCD3-mediated peroxisomal acyl-CoA translocation.Cell discovery · 2024Article
- Transport mechanism of human bilirubin transporter ABCC2 tuned by the inter-module regulatory domain.Nature communications · 2024Article
- The peroxisome: an update on mysteries 3.0.Histochemistry and cell biology · 2024Review
- Innovative tree-based method for sampling molecular conformations: exploring the ATP-binding cassette subfamily D member 1 (ABCD1) transporter as a case study.Frontiers in molecular biosciences · 2024Article
- The Physiological and Pathological Role of Acyl-CoA Oxidation.International journal of molecular sciences · 2023Review
- Structural insights into human ABCC4-mediated transport of platelet agonist and antagonist.Nature cardiovascular research · 2023Article
- Structural basis for substrate and inhibitor recognition of human multidrug transporter MRP4.Communications biology · 2023Article
- Structural insights into substrate recognition and translocation of human peroxisomal ABC transporter ALDP.Signal transduction and targeted therapy · 2023Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human ABC transporter ABCD1 transports very long-chain fatty acids from cytosol to peroxisome for β-oxidation, dysfunction of which usually causes the X-linked adrenoleukodystrophy (X-ALD). Here, we report three cryogenic electron microscopy structures of ABCD1: the apo-form, substrate- and ATP-bound forms. Distinct from what was seen in the previously reported ABC transporters, the two symmetric molecules of behenoyl coenzyme A (C22:0-CoA) cooperatively bind to the transmembrane domains (TMDs). For each C22:0-CoA, the hydrophilic 3'-phospho-ADP moiety of CoA portion inserts into one TMD, with the succeeding pantothenate and cysteamine moiety crossing the inter-domain cavity, whereas the hydrophobic fatty acyl chain extends to the opposite TMD. Structural analysis combined with biochemical assays illustrates snapshots of ABCD1-mediated substrate transport cycle. It advances our understanding on the selective oxidation of fatty acids and molecular pathology of X-ALD.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.