Evidence map›Paper›PMID 20404325›Full record

ArticleThe Journal of biological chemistry2010

Interaction of extracellular domain 2 of the human retina-specific ATP-binding cassette transporter (ABCA4) with all-trans-retinal.

Esther E Biswas-Fiss, Deepa S Kurpad, Kinjalben Joshi, Subhasis B Biswas

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.2field-weighted citation impact, top 23% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Assessment of ABCA4 Genetic Variants: Current Landscape and Future Prospects.Advances in experimental medicine and biology · 2025
    Review
  5. Review
  6. Article
  7. Structural and Pathogenic Impacts ofInternational journal of molecular sciences · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 3 institutions in 1 country.

Esther E Biswas-FissDepartment of Bioscience Technologies, Jefferson School of Health Professions, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA. esther.biswas@jefferson.edu
Deepa S Kurpad
Kinjalben Joshi
Subhasis B Biswas
Rowan University · USRutgers, The State University of New Jersey · USThomas Jefferson University · US

Funding

DNA HELICASE AND PRIMASE INHIBITORS FOR BIODEFENSER42AI064974 · NIAID · MICROBIOTIX, INC · PI MOIR, DONALD T · 2009 to 2010
$1.8M
DNA helicase and primase inhibitors for biodefenseR41AI064974 · NIAID · MICROBIOTIX, INC · PI MOIR, DONALD T · 2005 to 2006
$1.1M
MOLECULAR ANALYSIS GENETIC MUTATIONS IN VISUAL DISEASESR15EY013113 · NEI · UNIVERSITY OF DELAWARE · PI BISWAS-FISS, ESTHER ELISSA · 2000 to 2014
$1.1M
NEI NIH HHS EY 013113NEI NIH HHS R15 EY013113NIAID NIH HHS AI064974NIAID NIH HHS R41 AI064974NIAID NIH HHS R42 AI064974
6 · The paper itself

Abstract

The retina-specific ATP-binding cassette (ABC) transporter, ABCA4, is essential for transport of all-trans-retinal from the rod outer segment discs in the retina and is associated with a broad range of inherited retinal diseases, including Stargardt disease, autosomal recessive cone rod dystrophy, and fundus flavimaculatus. A unique feature of the ABCA subfamily of ABC transporters is the presence of highly conserved, long extracellular loops or domains (ECDs) with unknown function. The high degree of sequence conservation and mapped disease-associated mutations in these domains suggests an important physiological significance. Conformational analysis using CD spectroscopy of purified, recombinant ECD2 protein demonstrated that it has an ordered and stable structure composed of 27 +/- 3% alpha-helix, 20 +/- 3% beta-pleated sheet, and 53 +/- 3% coil. Significant conformational changes were observed in disease-associated mutant proteins. Using intrinsic tryptophan fluorescence emission spectrum of ECD2 polypeptide and fluorescence anisotropy, we have demonstrated that this domain specifically interacts with all-trans-retinal. Furthermore, the retinal interaction appeared preferential for the all-trans-isomer and was directly measurable through fluorescence anisotropy analysis. Our results demonstrate that the three macular degeneration-associated mutations lead to significant changes in the secondary structure of the ECD2 domain of ABCA4, as well as in its interaction with all-trans-retinal.

Indexed as

Adenosine TriphosphateAmino Acid SequenceAnimalsAnisotropyATP-Binding Cassette TransportersCircular DichroismHumansMicroscopy, FluorescenceMolecular Sequence DataProtein Structure, SecondaryProtein Structure, TertiaryRetinaRetinaldehydeSequence Homology, Amino AcidVision, OcularABCA4 protein, humanAdenosine TriphosphateATP-Binding Cassette TransportersRetinaldehyde

Identifiers

PMID20404325
PMCPMC2885217
OpenAlexW2010806114

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.