Evidence map›Paper›PMID 40499748›Full record

ReviewJournal of molecular biology2025

Modeling Protein Aggregation Kinetics from NMR Data.

Vitali Tugarinov, Francesco Torricella, Shreya Ghosh, G Marius Clore

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Journal of molecular biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. 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

4 authors.

Vitali TugarinovLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520, USA. Electronic address: vitali.tugarinov@nih.gov.
Francesco TorricellaLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520, USA.
Shreya GhoshLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520, USA.
G Marius CloreLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520, USA. Electronic address: mariusc@mail.nih.gov.

Funding

NMR STUDIES OF THREE-DIMENSIONAL STRUCTURE OF MACROMOLECULES IN SOLUTIONZ01DK029023 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI CLORE, G. MARIUS · 1988 to 2008
$949k
Intramural NIH HHS Z01 DK029023
6 · The paper itself

Abstract

We provide an overview of the practical aspects of using NMR spectroscopy to follow the time course of protein fibril formation (aggregation) and quantitatively model the kinetics of aggregation processes. Following a brief survey of the theoretical foundations of the kinetics of protein aggregation and its inhibition, the modeling of aggregation kinetics, from data acquired by a series of fast two-dimensional

Indexed as

Nuclear Magnetic Resonance, BiomolecularProtein AggregatesAmyloid beta-PeptidesHumansHuntingtin ProteinHuntington DiseaseKineticsMagnetic Resonance SpectroscopyModels, MolecularPeptide FragmentsProtein Aggregation, PathologicalAmyloid beta-Peptidesamyloid beta-protein (1-42)Huntingtin ProteinPeptide FragmentsProtein AggregatesHuntington’s diseaseNMR fast acquisition methodsNMR spin relaxationprotein aggregation kineticsβ-amyloid fibril formation

Identifiers

PMID40499748
PMCPMC12235721

What Socratic holds

Textmetadata
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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 Socratic graph.