Evidence map›Paper›PMID 35167075›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2022

Computer Simulations Aimed at Exploring Protein Aggregation and Dissociation.

Phuong H Nguyen, Philippe Derreumaux

Open access · greenAbstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.9field-weighted citation impact, top 30% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. Disassembly of Amyloid Fibril with Infrared Free Electron Laser.International journal of molecular sciences · 2023
    Review
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

2 authors at 1 institution in 1 country.

Phuong H NguyenLaboratoire de Biochimie Théorique, UPR 9080, CNRS, Université de Paris, Paris, France.ORCID https://orcid.org/0000-0003-1284-967X
Philippe DerreumauxLaboratoire de Biochimie Théorique, UPR 9080, CNRS, Université de Paris, Paris, France. philippe.derreumaux@ibpc.fr.ORCID https://orcid.org/0000-0001-9110-5585
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein aggregation can lead to well-defined structures that are functional, but is also the cause of the death of neuron cells in many neurodegenerative diseases. The complexity of the molecular events involved in the aggregation kinetics of amyloid proteins and the transient and heterogeneous characters of all oligomers prevent high-resolution structural experiments. As a result, computer simulations have been used to determine the atomic structures of amyloid proteins at different association stages as well as to understand fibril dissociation. In this chapter, we first review the current computer simulation methods used for aggregation with some atomistic and coarse-grained results aimed at better characterizing the early formed oligomers and amyloid fibril formation. Then we present the applications of non-equilibrium molecular dynamics simulations to comprehend the dissociation of protein assemblies.

Indexed as

Molecular Dynamics SimulationProtein AggregatesAmyloidAmyloid beta-PeptidesComputer SimulationKineticsAmyloidAmyloid beta-PeptidesProtein AggregatesAggregationAll-atomAmyloidAqueous solutionCoarse-grained force fieldComputer equilibrium and non-equilibrium simulationsDynamicsLipid membrane bilayerStructureThermodynamics

Identifiers

PMID35167075
OpenAlexW4212973770

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.