Evidence map›Paper›PMID 40919591›Full record

ReviewMagnetic resonance letters2024

Solid-state NMR studies of proteins in condensed phases.

Jiani Xiang, Xialian Wu, Angelo L Chu, Junxia Lu

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Magnetic resonance letters, 2024. 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
–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

1 citing paper in PubMed.

  1. 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

4 authors.

Jiani XiangKey Laboratory of Industrial Fermentation (Ministry of Education), School of Life and Health Sciences, Hubei University of Technology, Wuhan, 430068, China.
Xialian WuInterdisciplinary Institute of NMR and Molecular Sciences, School of Chemistry and Chemical Engineering, The State Key Laboratory of Refractories and Metallurgy, Wuhan University of Science and Technology, Wuhan, 430081, China.
Angelo L ChuThomas Jefferson High School for Science and Technology, 6560 Braddock Rd, Alexandria, VA, 22312, USA.
Junxia LuInterdisciplinary Institute of NMR and Molecular Sciences, School of Chemistry and Chemical Engineering, The State Key Laboratory of Refractories and Metallurgy, Wuhan University of Science and Technology, Wuhan, 430081, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Some proteins perform their biological functions by changing their material states through liquid-liquid phase separation. Upon phase separation, the protein condenses into a concentrated liquid phase and sometimes into a gel phase, changing its dynamic properties and intermolecular interactions, thereby regulating cellular functions. Although the biological significance of this phenomenon has been widely recognized by researchers, there is still a lack of a comprehensive understanding of the structural and dynamic properties of the protein in the condensed phase. In this phase, molecules usually contain domains with varied dynamic properties and undergo intermediate exchanges. Magic angle spinning (MAS) solid-state NMR (SSNMR) experiments are very powerful in studying rigid protein polymers such as amyloid. The incorporation of solution-like experiments into SSNMR and the development of

Indexed as

J-coupling based MAS SSNMRLiquid-liquid phase separationMagic angle spinning (MAS) solid-state NMR (SSNMR)Protein condenses

Identifiers

PMID40919591
PMCPMC12406584

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.