Evidence map›Paper›PMID 38998901›Full record

ArticleMolecules (Basel, Switzerland)2024

The Temperature Dependence of Hydrogen Bonds Is More Uniform in Stable Proteins: An Analysis of NMR

Andrei T Alexandrescu, Aurelio J Dregni

Abstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2024. 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. Article
  2. High-pH NMR to Identify Macromolecular Hydrogen-Bonds and Foldons.bioRxiv : the preprint server for biology · 2026
    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

2 authors.

Andrei T AlexandrescuDepartment of Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269, USA.ORCID 0000-0002-8425-9276
Aurelio J DregniDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.ORCID 0000-0003-3422-4734

Funding

TR&D 4 -- Advanced Magic Angle Spinning NMR methodsP41GM132079 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2019 to 2021
$3.6M
Molecular structures of tau aggregates studied by solid-state NMRRF1AG059661 · NIA · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI HONG, MEI · 2018 to 2021
$2.1M
Tau structure and dynamics in Alzheimer's diseaseR01AG059661 · NIA · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI Mei Hong · 2023 to 2026
$1.8M
Investigation of Seeded Alzheimer's Disease Tau Fibrils with Solid-State NMRF31AG069418 · NIA · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI DREGNI, AURELIO JAMES · 2020 to 2021
$85k
NIA NIH HHS F31 AG069418NIA NIH HHS R01 AG059661NIA NIH HHS RF1 AG059661NIGMS NIH HHS P41 GM132079
6 · The paper itself

Abstract

Long-range HNCO NMR spectra for proteins show crosspeaks due to

Indexed as

Hydrogen BondingTemperatureHemolysin ProteinsMagnetic Resonance SpectroscopyModels, MolecularNuclear Magnetic Resonance, BiomolecularProtein ConformationProteinsProtein StabilityHemolysin ProteinsProteinschi-1 angle temperature dependencem-valueNMR structureprotein foldingstructure conservation

Identifiers

PMID38998901
PMCPMC11243222

What OpenQuestion holds

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LicenceCC BY
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.