Evidence map›Paper›PMID 31399000›Full record

ReviewAnnual review of cell and developmental biology2019

Coatopathies: Genetic Disorders of Protein Coats.

Esteban C Dell'Angelica, Juan S Bonifacino

Abstract readReview
In one paragraph

Review in Annual review of cell and developmental biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
–field-weighted citation impact
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

74 citing papers in PubMed.

  1. Article
  2. Interstitial lung disease and the STING pathway.The Journal of clinical investigation · 2026
    Review
  3. Review
  4. Article
  5. Article
  6. GARP Complex in Golgi Physiology.Sub-cellular biochemistry · 2026
    Review
  7. A novel homozygousFrontiers in pediatrics · 2026
    Article
  8. Article
  9. Review
  10. Uncovering cargo clients and accessory factors of AP-1 and AP-4 through vesicle proteomics.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Structural elucidation of how ARF small GTPases induce membrane tubulation for vesicle fission.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  20. Review

14 more citing papers are in PubMed but not listed here.

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

2 authors.

Esteban C Dell'AngelicaDepartment of Human Genetics, David Geffen School of Medicine, University of California, Los Angeles, California 90095, USA.
Juan S BonifacinoCell Biology and Neurobiology Branch, Eunice Kennedy Shriver National Institute of Child Health and Human Development (NICHD), National Institutes of Health, Bethesda, Maryland 20892, USA; email: juan.bonifacino@nih.gov.

Funding

Protein Trafficking In The Endosomal-Lysosomal SystemZIAHD001607 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI BONIFACINO, JUAN · 2009 to 2025
$48.3M
REGULATION OF THE FATE OF NEWLY SYNTHESIZED PROTEINSZ01HD001607 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI BONIFACINO, JUAN · 1991 to 2008
$4.4M
Biogenesis of melanosomes and other lysosome-related organellesR01GM112942 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI DELL'ANGELICA, ESTEBAN C · 2015 to 2018
$1.3M
Intramural NIH HHS Z01 HD001607Intramural NIH HHS ZIA HD001607NICHD NIH HHS ZIA HD001607NIGMS NIH HHS R01 GM112942
6 · The paper itself

Abstract

Protein coats are supramolecular complexes that assemble on the cytosolic face of membranes to promote cargo sorting and transport carrier formation in the endomembrane system of eukaryotic cells. Several types of protein coats have been described, including COPI, COPII, AP-1, AP-2, AP-3, AP-4, AP-5, and retromer, which operate at different stages of the endomembrane system. Defects in these coats impair specific transport pathways, compromising the function and viability of the cells. In humans, mutations in subunits of these coats cause various congenital diseases that are collectively referred to as coatopathies. In this article, we review the fundamental properties of protein coats and the diseases that result from mutation of their constituent subunits.

Indexed as

AnimalsCoat Protein Complex IEndosomesGenetic Diseases, InbornHumansProtein TransportVesicular Transport ProteinsCoat Protein Complex IVesicular Transport Proteinsclathrincoatomerneurological disordersprotein traffickingrare diseasessorting signals

Identifiers

PMID31399000
PMCPMC7310445

What OpenQuestion holds

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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.