Evidence map›Paper›PMID 37237566›Full record

ReviewBiology2023

The Action of Chemical Denaturants: From Globular to Intrinsically Disordered Proteins.

Antonella Paladino, Luigi Vitagliano, Giuseppe Graziano

Open access · goldAbstract readReview
In one paragraph

Review in Biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

9 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Fluorescence-Based Protein Stability Monitoring-A Review.International journal of molecular sciences · 2024
    Review
  9. 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

3 authors at 2 institutions in 1 country.

Antonella PaladinoInstitute of Biostructures and Bioimaging, CNR, Via Pietro Castellino 111, 80131 Naples, Italy.ORCID 0000-0002-9397-1572
Luigi VitaglianoInstitute of Biostructures and Bioimaging, CNR, Via Pietro Castellino 111, 80131 Naples, Italy.ORCID 0000-0002-3032-3375
Giuseppe GrazianoDepartment of Science and Technology, University of Sannio, via Francesco de Sanctis snc, 82100 Benevento, Italy.ORCID 0000-0001-6935-8172
Institute of Biostructure and Bioimaging · ITUniversity of Sannio · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins perform their many functions by adopting either a minimal number of strictly similar conformations, the native state, or a vast ensemble of highly flexible conformations. In both cases, their structural features are highly influenced by the chemical environment. Even though a plethora of experimental studies have demonstrated the impact of chemical denaturants on protein structure, the molecular mechanism underlying their action is still debated. In the present review, after a brief recapitulation of the main experimental data on protein denaturants, we survey both classical and more recent interpretations of the molecular basis of their action. In particular, we highlight the differences and similarities of the impact that denaturants have on different structural classes of proteins, i.e., globular, intrinsically disordered (IDP), and amyloid-like assemblies. Particular attention has been given to the IDPs, as recent studies are unraveling their fundamental importance in many physiological processes. The role that computation techniques are expected to play in the near future is illustrated.

Indexed as

conformational ensembledenaturantsguanidiniumintrinsically disordered proteinssolventurea

Identifiers

PMID37237566
PMCPMC10215825
OpenAlexW4377291849

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.