Evidence map›Paper›PMID 23350640›Full record

ReviewPigment cell & melanoma research2013

PMEL: a pigment cell-specific model for functional amyloid formation.

Brenda Watt, Guillaume van Niel, Graça Raposo, Michael S Marks

Abstract readReview
In one paragraph

Review in Pigment cell & melanoma research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 papers.

0numbers the graph read from it
0cells of the map it votes in
104citing papers in PubMed
4.6field-weighted citation impact, top 5% 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

104 citing papers in PubMed, 185 citations in OpenAlex.

  1. Article
  2. Article
  3. Lysosome-related organelles orchestrate guanine crystal formation in pigment cells.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Article
  5. Pmel17 Deficiency Affects Melanogenesis and Promotes Tumor Vascularization.International journal of molecular sciences · 2026
    Article
  6. Article
  7. Disrupting melanin transfer: innovative strategy for anti-pigmentation drug discovery.Journal of enzyme inhibition and medicinal chemistry · 2025
    Review
  8. Article
  9. Article
  10. Article
  11. The Evolution of Functional Amyloids and Their Impact on Host-Microbe Interactions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. AnInternational journal of molecular sciences · 2025
    Article
  17. Article
  18. Article
  19. Article
  20. Article

44 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

4 authors at 2 institutions in 2 countries.

Brenda WattDepartment of Pathology and Laboratory Medicine, Department of Physiology, and Cell and Molecular Biology Graduate Group, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA.
Guillaume van Niel
Graça Raposo
Michael S Marks
Centre National de la Recherche Scientifique · FRUniversity of Pennsylvania · US

Funding

TRAINING PROGRAM IN CELL AND MOLECULAR BIOLOGYT32GM007229 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI BARTOLOMEI, MARISA S. · 1985 to 2023
$14.0M
Hermansky Pudlak Syndrome &melanosome formationR01EY015625 · NEI · UNIVERSITY OF PENNSYLVANIA · PI Michael S Marks · 2004 to 2026
$9.2M
Melanosome BiogenesisR01AR048155 · NIAMS · UNIVERSITY OF PENNSYLVANIA · PI MARKS, MICHAEL S · 2002 to 2017
$4.2M
Role of PMEL 17 in melanosome biogenesisF31GM081917 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI WATT, BRENDA · 2007 to 2008
$82k
NEI NIH HHS R01 EY015625NIAMS NIH HHS R01 AR048155NIGMS NIH HHS F31 GM081917NIGMS NIH HHS F31GM081917NIGMS NIH HHS T32 GM007229
6 · The paper itself

Abstract

PMEL is a pigment cell-specific protein responsible for the formation of fibrillar sheets within the pigment organelle, the melanosome. The fibrillar sheets serve as a template upon which melanins polymerize as they are synthesized. The PMEL fibrils are required for optimal pigment cell function, as animals that either lack PMEL expression or express mutant PMEL variants show varying degrees of hypopigmentation and pigment cell inviability. The PMEL fibrils have biophysical properties of amyloid, a protein fold that is frequently associated with neurodegenerative and other diseases. However, PMEL is one of a growing number of non-pathogenic amyloid proteins that contribute to the function of the cell and/or organism that produces them. Understanding how PMEL generates amyloid in a non-pathogenic manner might provide insights into how to avoid toxicity due to pathological amyloid formation. In this review, we summarize and reconcile data concerning the fate of PMEL from its site of synthesis in the endoplasmic reticulum to newly formed melanosomes and the role of distinct PMEL subdomains in trafficking and amyloid fibril formation. We then discuss how its progression through the secretory pathway into the endosomal system might allow for the regulated and non-toxic conversion of PMEL into an ordered amyloid polymer.

Indexed as

Models, BiologicalAmyloidAnimalsgp100 Melanoma AntigenHumansMelanocytesOrgan SpecificityAmyloidgp100 Melanoma Antigen

Identifiers

PMID23350640
PMCPMC3633693
OpenAlexW2066615572

What OpenQuestion holds

Textmetadata
LicenceTDM
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.