Evidence map›Paper›PMID 37446630›Full record

ArticleMolecules (Basel, Switzerland)2023

Cysteine Redox Chemistry in Peptide Self-Assembly to Modulate Hydrogelation.

Maria Cristina Cringoli, Silvia Marchesan

Abstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. 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.

Maria Cristina CringoliDepartment of Chemical and Pharmaceutical Sciences, University of Trieste, 34127 Trieste, Italy.ORCID 0000-0003-0196-4525
Silvia MarchesanDepartment of Chemical and Pharmaceutical Sciences, University of Trieste, 34127 Trieste, Italy.ORCID 0000-0001-6089-3873

Funding

University of Trieste FRA2022
6 · The paper itself

Abstract

Cysteine redox chemistry is widely used in nature to direct protein assembly, and in recent years it has inspired chemists to design self-assembling peptides too. In this concise review, we describe the progress in the field focusing on the recent advancements that make use of Cys thiol-disulfide redox chemistry to modulate hydrogelation of various peptide classes.

Indexed as

CysteinePeptidesHydrogelsOxidation-ReductionSulfhydryl CompoundsCysteineHydrogelsPeptidesSulfhydryl Compoundsamyloidcysteinedisulfidefibrilshydrogelspeptideredoxself-assemblysupramolecularthiol

Identifiers

PMID37446630
PMCPMC10343219

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.