Evidence map›Paper›PMID 40667093›Full record

ArticlebioRxiv : the preprint server for biology2025

Phosphoglycerate Kinase Can Adopt a Topologically Misfolded Form that is More Stable than its Native State.

Yingzi Xia, Barbara Amann, Richard E Gillilan, Piyoosh Sharma, Sreemantee Sen, Karen G Fleming, Stephen D Fried

Abstract readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Yingzi XiaDepartment of Chemistry, Johns Hopkins University, Baltimore, MD 21218, USA.ORCID 0009-0005-0885-6959
Barbara AmannT. C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, MD 21218, USA.ORCID 0000-0002-7839-9029
Richard E GillilanCenter for High Energy X-ray Sciences (CHEXS), Ithaca, New York 14853, USA.ORCID 0000-0002-7636-3188
Piyoosh SharmaDepartment of Chemistry, Johns Hopkins University, Baltimore, MD 21218, USA.ORCID 0000-0002-1102-8602
Sreemantee SenDepartment of Chemistry, Johns Hopkins University, Baltimore, MD 21218, USA.ORCID 0000-0001-6713-815X
Karen G FlemingT. C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, MD 21218, USA.ORCID 0000-0001-5417-8830
Stephen D FriedDepartment of Chemistry, Johns Hopkins University, Baltimore, MD 21218, USA.ORCID 0000-0003-2494-2193

Funding

Training and OutreachP30GM124166 · NIGMS · CORNELL UNIVERSITY · PI RICHARD A. CERIONE · 2019 to 2026
$28.3M
Watching Proteins Fold (or Misfold) in vivo with Mass SpectrometryDP2GM140926 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI FRIED, STEPHEN DAVID · 2020 to 2020
$2.3M
Forces Driving Membrane Protein FoldsR35GM148199 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI Karen G. Fleming · 2023 to 2026
$1.9M
NIGMS NIH HHS DP2 GM140926NIGMS NIH HHS P30 GM124166NIGMS NIH HHS R35 GM148199
6 · The paper itself

Abstract

The native states of globular proteins are typically viewed as being the most stable conformations on their respective proteins' soluble free energy landscapes. This view, known as the Thermodynamic Hypothesis, explains why many proteins can reversibly refold after being denatured. Here we report an intriguing counterexample to this paradigm. When

Identifiers

PMID40667093
PMCPMC12262362

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.