Evidence map›Paper›PMID 34723279›Full record

ArticleJACS Au2021

ATP Can Efficiently Stabilize Protein through a Unique Mechanism.

Xinwen Ou, Yichong Lao, Jingjie Xu, Yanee Wutthinitikornkit, Rui Shi, Xiangjun Chen, Jingyuan Li

Open access · goldAbstract read
In one paragraph

Article in JACS Au, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.5field-weighted citation impact, top 6% 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

22 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
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  7. ATP Can Act as a Stabilizer on Neutral Macromolecules.The journal of physical chemistry letters · 2025
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  15. CombinedACS omega · 2023
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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

7 authors at 1 institution in 1 country.

Xinwen OuZhejiang Province Key Laboratory of Quantum Technology and Device, Department of Physics, Zhejiang University, Zheda Road 38, Hangzhou 310027, China.
Yichong LaoZhejiang Province Key Laboratory of Quantum Technology and Device, Department of Physics, Zhejiang University, Zheda Road 38, Hangzhou 310027, China.
Jingjie XuEye Center of the Second Affiliated Hospital, Institute of Translational Medicine, School of Medicine, Zhejiang University, Hangzhou 310009, China.
Yanee WutthinitikornkitZhejiang Province Key Laboratory of Quantum Technology and Device, Department of Physics, Zhejiang University, Zheda Road 38, Hangzhou 310027, China.
Rui ShiZhejiang Province Key Laboratory of Quantum Technology and Device, Department of Physics, Zhejiang University, Zheda Road 38, Hangzhou 310027, China.ORCID https://orcid.org/0000-0002-0411-3067
Xiangjun ChenEye Center of the Second Affiliated Hospital, Institute of Translational Medicine, School of Medicine, Zhejiang University, Hangzhou 310009, China.
Jingyuan LiZhejiang Province Key Laboratory of Quantum Technology and Device, Department of Physics, Zhejiang University, Zheda Road 38, Hangzhou 310027, China.ORCID https://orcid.org/0000-0003-2926-1864
Second Affiliated Hospital of Zhejiang University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Recent experiments suggested that ATP can effectively stabilize protein structure and inhibit protein aggregation when its concentration is less than 10 mM, which is significantly lower than cosolvent concentrations required in conventional mechanisms. The ultrahigh efficiency of ATP suggests a unique mechanism that is fundamentally different from previous models of cosolvents. In this work, we used molecular dynamics simulation and experiments to study the interactions of ATPs with three proteins: lysozyme, ubiquitin, and malate dehydrogenase. ATP tends to bind to the surface regions with high flexibility and high degree of hydration. These regions are also vulnerable to thermal perturbations. The bound ATPs further assemble into ATP clusters mediated by Mg

Identifiers

PMID34723279
PMCPMC8549052
OpenAlexW3208063362

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.