Evidence map›Paper›PMID 35887107›Full record

ArticleInternational journal of molecular sciences2022

The Anfinsen Dogma: Intriguing Details Sixty-Five Years Later.

Giorgia Gambardella, Sara Notari, Dario Cavaterra, Federica Iavarone, Massimo Castagnola, Alessio Bocedi, Giorgio Ricci

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2022. 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
0.3field-weighted citation impact, top 48% 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, 4 citations in OpenAlex.

  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

7 authors at 3 institutions in 1 country.

Giorgia GambardellaDepartment of Chemical Sciences and Technologies, University of Rome 'Tor Vergata', Via della Ricerca Scientifica 1, 00133 Rome, Italy.
Sara NotariDepartment of Chemical Sciences and Technologies, University of Rome 'Tor Vergata', Via della Ricerca Scientifica 1, 00133 Rome, Italy.
Dario CavaterraDepartment of Chemical Sciences and Technologies, University of Rome 'Tor Vergata', Via della Ricerca Scientifica 1, 00133 Rome, Italy.
Federica IavaroneDipartimento di Scienze Biotecnologiche di Base, Cliniche Intensivologiche e Perioperatorie, Università Cattolica del Sacro Cuore, 00168 Rome, Italy.
Massimo CastagnolaLaboratorio di Proteomica, Centro Europeo di Ricerca sul Cervello, IRCCS Santa Lucia, 00179 Rome, Italy.ORCID 0000-0002-0959-7259
Alessio BocediDepartment of Chemical Sciences and Technologies, University of Rome 'Tor Vergata', Via della Ricerca Scientifica 1, 00133 Rome, Italy.
Giorgio RicciDepartment of Chemical Sciences and Technologies, University of Rome 'Tor Vergata', Via della Ricerca Scientifica 1, 00133 Rome, Italy.
University of Rome Tor Vergata · ITIstituti di Ricovero e Cura a Carattere Scientifico · ITUniversità Cattolica del Sacro Cuore · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The pioneering experiments of Anfinsen on the oxidative folding of RNase have been revisited discovering some details, which update the statement of his dogma and shed new light on the leading role of the correct disulfide in the attainment of the native structure. CD analysis, mass spectrometry, fluorescence spectroscopy and enzyme activity indicate that native disulfides drive the formation of the secondary and tertiary structures that cannot be entirely formed in their absence. This opposes a common opinion that these structures are first formed and then stabilized by the native disulfides. Our results also indicate that a spontaneous re-oxidation of a reduced RNase cannot produce a complete recovery of activity, as described by many textbooks; this can be obtained only in the presence of a reshuffling solution such as GSH/GSSG.

Indexed as

DisulfidesProtein FoldingOxidation-ReductionRibonuclease, PancreaticRibonucleasesDisulfidesRibonuclease, PancreaticRibonucleasesdisulfideoxidative foldingprotein foldingprotein structureribonuclease

Identifiers

PMID35887107
PMCPMC9318638
OpenAlexW4286239899

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.