Evidence map›Paper›PMID 38194274›Full record

ArticleACS applied materials & interfaces2024

Fluorogenic Hyaluronan Nanogels Track Individual Early Protein Aggregates Originated under Oxidative Stress.

Matteo Cingolani, Francesca Lugli, Mirko Zaffagnini, Damiano Genovese

Open access · hybridAbstract read
In one paragraph

Article in ACS applied materials & interfaces, 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
1.1field-weighted citation impact, top 22% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. 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

4 authors at 1 institution in 1 country.

Matteo CingolaniDipartimento di Chimica "Giacomo Ciamician", Università di Bologna, 40126 Bologna, Italy.
Francesca LugliDipartimento di Chimica "Giacomo Ciamician", Università di Bologna, 40126 Bologna, Italy.ORCID 0000-0001-6908-5469
Mirko ZaffagniniDipartimento di Farmacia e Biotecnologie, Università di Bologna, 40126 Bologna, Italy.ORCID 0000-0001-5115-0859
Damiano GenoveseDipartimento di Chimica "Giacomo Ciamician", Università di Bologna, 40126 Bologna, Italy.ORCID 0000-0002-4389-7247
University of Bologna · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins are broadly versatile biochemical materials, whose functionality is tightly related to their folding state. Native folding can be lost to yield misfolded conformations, often leading to formation of protein oligomers, aggregates, and biomolecular phase condensates. The fluorogenic hyaluronan HA-RB, a nonsulfonated glycosaminoglycan with a combination of polyanionic character and of hydrophobic spots due to rhodamine B dyes, binds to early aggregates of the model protein cytoplasmic glyceraldehyde-3-phosphate dehydrogenase 1 from

Indexed as

ArabidopsisHyaluronic AcidGlyceraldehyde-3-Phosphate DehydrogenasesNanogelsOxidative StressProtein AggregatesProtein FoldingProteinsGlyceraldehyde-3-Phosphate DehydrogenasesHyaluronic AcidNanogelsProtein AggregatesProteinsearly diagnosisfluorescence correlation spectroscopy (FCS)fluorescence microscopyfluorogenic probeglyceraldehyde-3-phosphate dehydrogenase (GAPDH)glycosaminoglycan (GAG)hyaluronic acidnanotrackingprotein aggregation

Identifiers

PMID38194274
PMCPMC10811615
OpenAlexW4390750612

What OpenQuestion holds

Textmetadata
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.