Evidence map›Paper›PMID 30017921›Full record

ReviewJournal of molecular biology2018

Amyloid by Design: Intrinsic Regulation of Microbial Amyloid Assembly.

Maya Deshmukh, Margery L Evans, Matthew R Chapman

Open access · greenAbstract readReview
In one paragraph

Review in Journal of molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

28 citing papers in PubMed, 53 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Staphylococcus epidermidis biofilm assembly and self-dispersion: bacteria and matrix dynamics.International microbiology : the official journal of the Spanish Society for Microbiology · 2024
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Evaluation of Amyloid Inhibitor Efficiency to Block Bacterial Survival.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  12. Review
  13. The protein disorder cycle.Biophysical reviews · 2021
    Review
  14. Catalytic amyloids: Is misfolding folding?Current opinion in chemical biology · 2021
    Review
  15. Review
  16. Review
  17. Review
  18. Article
  19. Review
  20. 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

3 authors at 1 institution in 1 country.

Maya DeshmukhDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, 1105 N University Ave, Ann Arbor, MI 48109-1085, USA.
Margery L EvansDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, 1105 N University Ave, Ann Arbor, MI 48109-1085, USA.
Matthew R ChapmanDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, 1105 N University Ave, Ann Arbor, MI 48109-1085, USA. Electronic address: chapmanm@umich.edu.
University of Michigan–Ann Arbor · US

Funding

Protein and Chemical Modulation of Curli Amyloid BiogenesisR01GM118651 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Matthew Richard Chapman · 2016 to 2026
$3.0M
Transthyretin as a generic inhibitor of amyloid and amyloid-associated biofilm infectionsR21AI137535 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI CHAPMAN, MATTHEW RICHARD · 2018 to 2019
$489k
NIAID NIH HHS R21 AI137535NIGMS NIH HHS R01 GM118651
6 · The paper itself

Abstract

The term amyloid has historically been used to describe fibrillar aggregates formed as the result of protein misfolding and that are associated with a range of diseases broadly termed amyloidoses. The discovery of "functional amyloids" expanded the amyloid umbrella to encompass aggregates structurally similar to disease-associated amyloids but that engage in a variety of biologically useful tasks without incurring toxicity. The mechanisms by which functional amyloid systems ensure nontoxic assembly has provided insights into potential therapeutic strategies for treating amyloidoses. Some of the most-studied functional amyloids are ones produced by bacteria. Curli amyloids are extracellular fibers made by enteric bacteria that function to encase and protect bacterial communities during biofilm formation. Here we review recent studies highlighting microbial functional amyloid assembly systems that are tailored to enable the assembly of non-toxic amyloid aggregates.

Indexed as

AmyloidAmyloidosisAnimalsBacterial ProteinsCell SurvivalHumansProtein AggregatesProtein Aggregation, PathologicalProtein FoldingProtein Interaction Domains and MotifsProtein MultimerizationProtein StabilityStructure-Activity RelationshipAmyloidBacterial ProteinsCrl protein, BacteriaProtein Aggregatesfunctional amyloidmicrobial amyloidsnature-inspired therapeuticsprotein misfoldingtoxic oligomer

Identifiers

PMID30017921
PMCPMC6168361
OpenAlexW2883650869

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.