Evidence map›Paper›PMID 35737839›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

Multi-eGO: An in silico lens to look into protein aggregation kinetics at atomic resolution.

Emanuele Scalone, Luca Broggini, Cristina Visentin, Davide Erba, Fran Bačić Toplek, Kaliroi Peqini, Sara Pellegrino, Stefano Ricagno, Cristina Paissoni, Carlo Camilloni

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.6field-weighted citation impact, top 9% 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

11 citing papers in PubMed, 22 citations in OpenAlex.

  1. A machine learning protocol for predicting structural distributions of amyloid-forming proteins from 2D IR spectra.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. A PDZ tandem repeat folds and unfolds via different pathways.Protein science : a publication of the Protein Society · 2024
    Article
  6. Article
  7. Article
  8. Multi-Journal of chemical theory and computation · 2024
    Article
  9. Review
  10. 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
  11. 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

10 authors at 1 institution in 2 countries.

Emanuele ScaloneDipartimento di Bioscienze, Università degli Studi di Milano, 20133 Milano, Italy.
Luca BrogginiDipartimento di Bioscienze, Università degli Studi di Milano, 20133 Milano, Italy.
Cristina VisentinDipartimento di Bioscienze, Università degli Studi di Milano, 20133 Milano, Italy.
Davide ErbaDipartimento di Bioscienze, Università degli Studi di Milano, 20133 Milano, Italy.ORCID 0000-0002-0313-6419
Fran Bačić ToplekDipartimento di Bioscienze, Università degli Studi di Milano, 20133 Milano, Italy.ORCID 0000-0002-8331-0885
Kaliroi PeqiniDipartimento di Scienze Farmaceutiche, Sezione Chimica Generale e Organica, Università degli Studi di Milano, 20133 Milano, Italy.
Sara PellegrinoDipartimento di Scienze Farmaceutiche, Sezione Chimica Generale e Organica, Università degli Studi di Milano, 20133 Milano, Italy.
Stefano RicagnoDipartimento di Bioscienze, Università degli Studi di Milano, 20133 Milano, Italy.ORCID 0000-0001-6678-5873
Cristina PaissoniDipartimento di Bioscienze, Università degli Studi di Milano, 20133 Milano, Italy.ORCID 0000-0002-3101-6705
Carlo CamilloniDipartimento di Bioscienze, Università degli Studi di Milano, 20133 Milano, Italy.ORCID 0000-0002-9923-8590
University of Milan · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein aggregation into amyloid fibrils is the archetype of aberrant biomolecular self-assembly processes, with more than 50 associated diseases that are mostly uncurable. Understanding aggregation mechanisms is thus of fundamental importance and goes in parallel with the structural characterization of the transient oligomers formed during the process. Oligomers have been proven elusive to high-resolution structural techniques, while the large sizes and long time scales, typical of aggregation processes, have limited the use of computational methods to date. To surmount these limitations, we here present multi-

Indexed as

AmyloidProtein AggregatesComputer SimulationKineticsMolecular Dynamics SimulationAmyloidProtein Aggregatesaggregation kineticsamyloidsmolecular dynamicsprotein aggregationstructure-based models

Identifiers

PMID35737839
PMCPMC9245614
OpenAlexW4283328159

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.