Evidence map›Paper›PMID 40174314›Full record

ReviewCurrent opinion in structural biology2025

Raman spectroscopy and imaging of protein droplet formation and aggregation.

Matthew D Watson, Jennifer C Lee

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Review
  2. Review
  3. 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.

Matthew D WatsonLaboratory of Protein Conformation and Dynamics, Biochemistry and Biophysics Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, USA.
Jennifer C LeeLaboratory of Protein Conformation and Dynamics, Biochemistry and Biophysics Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, USA. Electronic address: leej4@nhlbi.nih.gov.

Funding

Raman Spectroscopic Studies of AmyloidsZIAHL006236 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI LEE, JENNIFER · 2018 to 2025
$5.5M
Intramural NIH HHS ZIA HL006236
6 · The paper itself

Abstract

Raman microscopy offers a unique combination of chemical and spatial resolution with structural sensitivity. This makes it an ideal tool for studies of protein structural changes in heterogenous samples such as protein liquid-liquid phase separation (LLPS) and amyloid formation. These processes are characterized by the spontaneous assembly of proteins to form either microscopic liquid droplets or insoluble filaments stabilized by β-sheets. LLPS and amyloid formation are closely related, with many proteins that undergo LLPS also forming amyloids. This has led to the proposal that development of β-sheets in droplets is an initiating event in toxic amyloid formation. This review surveys recent applications of Raman microscopic methods to studies of LLPS and amyloid formation both in vitro and in cellulo.

Indexed as

Protein AggregatesProteinsSpectrum Analysis, RamanAmyloidAnimalsHumansAmyloidProtein AggregatesProteins

Identifiers

PMID40174314
PMCPMC12146085

What OpenQuestion holds

Textmetadata
LicenceTDM
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.