Evidence map›Paper›PMID 23104145›Full record

ReviewMolecular bioSystems2013

Understanding protein aggregation from the view of monomer dynamics.

Lisa J Lapidus

Abstract readReview
In one paragraph

Review in Molecular bioSystems, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Article
  2. Characterization of Amyloidogenic Peptide Aggregability in Helical Subspace.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  3. Rational Development of Stable PYYPharmaceutical research · 2021
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Prion protein dynamics before aggregation.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  9. Monomer Dynamics of Alzheimer Peptides and Kinetic Control of Early Aggregation in Alzheimer's Disease.Chemphyschem : a European journal of chemical physics and physical chemistry · 2016
    Article
  10. Article
  11. Review
  12. Effects of Mutations on the Reconfiguration Rate of α-Synuclein.The journal of physical chemistry. B · 2015
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. 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

1 author.

Lisa J LapidusDepartment of Physics and Astronomy and Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824, USA. lapidus@msu.edu

Funding

Preventing Protein Aggregation by Controlling Unfolded State DynamicsR01GM100908 · NIGMS · MICHIGAN STATE UNIVERSITY · PI LAPIDUS, LISA J · 2012 to 2016
$1.3M
NIGMS NIH HHS R01 GM100908
6 · The paper itself

Abstract

Much work in recent years has been devoted to understanding the complex process of protein aggregation. This review looks at the earliest stages of aggregation, long before the formation of fibrils that are the hallmark of many aggregation-based diseases, and proposes that the first steps are controlled by the reconfiguration dynamics of the monomer. When reconfiguration is much faster or much slower than bimolecular diffusion, then aggregation is slow, but when they are similar, aggregation is fast. The experimental evidence for this model is reviewed and the prospects for small molecule aggregation inhibitors to prevent disease are discussed.

Indexed as

AmyloidAmyloidosisHumansKineticsProteinsProtein SubunitsAmyloidProteinsProtein Subunits

Identifiers

PMID23104145
PMCPMC4834696

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.