Evidence map›Paper›PMID 31659041›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

SERF engages in a fuzzy complex that accelerates primary nucleation of amyloid proteins.

Ben A Meinen, Varun V Gadkari, Frederick Stull, Brandon T Ruotolo, James C A Bardwell

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

23 citing papers in PubMed, 36 citations in OpenAlex.

  1. International journal of molecular sciences · 2026
    Review
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  5. Molecular insights into the interaction between a disordered protein and a folded RNA.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  12. An ankyrin repeat chaperone targets toxic oligomers during amyloidogenesis.Protein science : a publication of the Protein Society · 2023
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  20. A novel knockout mouse for the small EDRK-rich factor 2 (Serf2) showing developmental and other deficits.Mammalian genome : official journal of the International Mammalian Genome Society · 2021
    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

5 authors at 2 institutions in 1 country.

Ben A MeinenDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109.
Varun V GadkariDepartment of Chemistry, University of Michigan, Ann Arbor, MI 48109.
Frederick StullDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109.
Brandon T RuotoloDepartment of Chemistry, University of Michigan, Ann Arbor, MI 48109.ORCID 0000-0002-6084-2328
James C A BardwellDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109; jbardwel@umich.edu.ORCID 0000-0003-1683-1944
Howard Hughes Medical Institute · USUniversity of Michigan · US

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

The assembly of small disordered proteins into highly ordered amyloid fibrils in Alzheimer's and Parkinson's patients is closely associated with dementia and neurodegeneration. Understanding the process of amyloid formation is thus crucial in the development of effective treatments for these devastating neurodegenerative diseases. Recently, a tiny, highly conserved and disordered protein called SERF was discovered to modify amyloid formation in

Indexed as

alpha-SynucleinAmyloid beta-PeptidesHumansKineticsParkinson DiseasePeptide FragmentsProtein AggregatesProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae Proteinsalpha-SynucleinAmyloid beta-Peptidesamyloid beta-protein (1-40)Peptide FragmentsProtein AggregatesSaccharomyces cerevisiae ProteinsYDL085C-A protein, S cerevisiaeAlzheimer’schaperoneprotein folding

Identifiers

PMID31659041
PMCPMC6859325
OpenAlexW2982553439

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.