Evidence map›Paper›PMID 32345723›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

Amyloid assembly is dominated by misregistered kinetic traps on an unbiased energy landscape.

Zhiguang Jia, Jeremy D Schmit, Jianhan Chen

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.7field-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

26 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. A tunable affinity fusion tag for protein self-assembly.bioRxiv : the preprint server for biology · 2025
    Article
  5. Review
  6. Review
  7. Article
  8. Nucleation and Growth of Amyloid Fibrils.The journal of physical chemistry. B · 2023
    Article
  9. Direct Observation of Seeded Conformational Conversion of hIAPPJournal of chemical information and modeling · 2023
    Article
  10. Article
  11. Article
  12. Controllable membrane damage by tunable peptide aggregation with albumin.AIChE journal. American Institute of Chemical Engineers · 2022
    Article
  13. Article
  14. Article
  15. Multi-eGO: An in silico lens to look into protein aggregation kinetics at atomic resolution.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  16. Article
  17. Protein assembly and crowding simulations.Current opinion in structural biology · 2022
    Review
  18. Review
  19. Article
  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 2 institutions in 1 country.

Zhiguang JiaDepartment of Chemistry, University of Massachusetts, Amherst, MA 01003.
Jeremy D SchmitDepartment of Physics, Kansas State University, Manhattan, KS 66506; schmit@phys.ksu.edu jianhanc@umass.edu.ORCID 0000-0002-0104-5468
Jianhan ChenDepartment of Chemistry, University of Massachusetts, Amherst, MA 01003; schmit@phys.ksu.edu jianhanc@umass.edu.ORCID 0000-0002-5281-1150
University of Massachusetts Amherst · USKansas State University · US

Funding

Theoretical and computational modeling of amyloid aggregationR01GM107487 · NIGMS · KANSAS STATE UNIVERSITY · PI SCHMIT, JEREMY DAVID · 2014 to 2018
$1.4M
NIGMS NIH HHS R01 GM107487
6 · The paper itself

Abstract

Atomistic description of protein fibril formation has been elusive due to the complexity and long time scales of the conformational search. Here, we develop a multiscale approach combining numerous atomistic simulations in explicit solvent to construct Markov State Models (MSMs) of fibril growth. The search for the in-register fully bound fibril state is modeled as a random walk on a rugged two-dimensional energy landscape defined by β-sheet alignment and hydrogen-bonding states, whereas transitions involving states without hydrogen bonds are derived from kinetic clustering. The reversible association/dissociation of an incoming peptide and overall growth kinetics are then computed from MSM simulations. This approach is applied to derive a parameter-free, comprehensive description of fibril elongation of Aβ

Indexed as

MutationAmyloidAmyloid beta-PeptidesComputer SimulationHumansHydrogen BondingKineticsModels, MolecularPeptide FragmentsPhenylalanineProtein Structure, SecondaryThermodynamicsAmyloidAmyloid beta-Peptidesamyloid beta-protein (16-22)cyclohexylalaninePeptide FragmentsPhenylalanineaggregationamyloidMarkov State Modelmolecular dynamics

Identifiers

PMID32345723
PMCPMC7229673
OpenAlexW3017784424

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.