Evidence map›Paper›PMID 27589732›Full record

ReviewInternational journal of molecular sciences2016

PMEL Amyloid Fibril Formation: The Bright Steps of Pigmentation.

Christin Bissig, Leila Rochin, Guillaume van Niel

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

57 citing papers in PubMed, 122 citations in OpenAlex.

  1. Article
  2. Article
  3. Catalytic Amyloids: Turning Fibrils Into Biocatalysts.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026
    Review
  4. Pmel17 Deficiency Affects Melanogenesis and Promotes Tumor Vascularization.International journal of molecular sciences · 2026
    Article
  5. Review
  6. Article
  7. Zoological research · 2025
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Tape-Strip Proteomic Analysis of Female Melasma Skin Lesions in a Chinese Population.Clinical, cosmetic and investigational dermatology · 2025
    Article
  18. Article
  19. Article
  20. Amyloid, Crohn's disease, and Alzheimer's disease - are they linked?Frontiers in cellular and infection microbiology · 2024
    Review
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

3 authors at 2 institutions in 2 countries.

Christin BissigInstitut Curie, Paris Sciences et Lettres Research University, UMR144, Centre de Recherche, 26 rue d'ULM, Paris F-75231, France. christin.bissig@curie.fr.
Leila RochinDepartment of Cellular and Molecular Physiology, Institute of Translational Medicine, University of Liverpool, Liverpool L69 3BX, UK. Leila.Rochin@liverpool.ac.uk.
Guillaume van NielInstitut Curie, Paris Sciences et Lettres Research University, UMR144, Centre de Recherche, 26 rue d'ULM, Paris F-75231, France. guillaume.van-niel@curie.fr.
Centre National de la Recherche Scientifique · FRUniversity of Liverpool · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In pigment cells, melanin synthesis takes place in specialized organelles, called melanosomes. The biogenesis and maturation of melanosomes is initiated by an unpigmented step that takes place prior to the initiation of melanin synthesis and leads to the formation of luminal fibrils deriving from the pigment cell-specific pre-melanosomal protein (PMEL). In the lumen of melanosomes, PMEL fibrils optimize sequestration and condensation of the pigment melanin. Interestingly, PMEL fibrils have been described to adopt a typical amyloid-like structure. In contrast to pathological amyloids often associated with neurodegenerative diseases, PMEL fibrils represent an emergent category of physiological amyloids due to their beneficial cellular functions. The formation of PMEL fibrils within melanosomes is tightly regulated by diverse mechanisms, such as PMEL traffic, cleavage and sorting. These mechanisms revealed increasing analogies between the formation of physiological PMEL fibrils and pathological amyloid fibrils. In this review we summarize the known mechanisms of PMEL fibrillation and discuss how the recent understanding of physiological PMEL amyloid formation may help to shed light on processes involved in pathological amyloid formation.

Indexed as

Skin PigmentationAmyloidAnimalsgp100 Melanoma AntigenHumansMelanosomesProtein Processing, Post-TranslationalProtein TransportAmyloidgp100 Melanoma AntigenPMEL protein, humanamyloidapolipoprotein Efibril formationmelanocytemelanosomepigmentationPMELsecretases

Identifiers

PMID27589732
PMCPMC5037717
OpenAlexW2515264152

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.