Student or educator? Sign up with your school email and get 6 months of Pro free.
Cited by 170

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Folding of small disulfide-rich proteins: clarifying the puzzle

Open access
Arolas, Joan L., Aviles, Francesc X., Chang, Jui-Yoa, Ventura, Salvador·2006·Trends in Biochemical Sciences

Abstract

The process by which small proteins fold to their native conformations has been intensively studied over the past few decades. The particular chemistry of disulfide-bond formation has facilitated the characterization of the oxidative folding of numerous small, disulfide-rich proteins with results that illustrate a high level of diversity in folding mechanisms, differing in the heterogeneity and native disulfide-bond content of their intermediates. Information from folding studies of these proteins, together with the recent structural determinations of predominant intermediates, has provided new molecular insights into oxidative folding and clarifies the major rules that govern it.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1016/j.tibs.2006.03.005

Cites

2 of 2 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Show all 2 references

Cited by

See all 170

Metadata

Authors
Arolas, J. L., Aviles, F. X., Chang, J.-Y., & Ventura, S.
Venue
Trends in Biochemical Sciences
Publisher
Elsevier BV
Published
2006-05
Volume
31
Issue
5
Pages
292-301
ISSN
0968-0004 (ISSN-L)
OpenAlex
W2140768489
Cited by
170
References
2
FWCI
0.65
Type
journal article
Language
en
Open access
green

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: Folding of small disulfide-rich proteins: clarifying the puzzle. https://app.cochat.ai/papers/10.1016/j.tibs.2006.03.005
The paper
Arolas, J. L., Aviles, F. X., Chang, J.-Y., & Ventura, S. (2006). Folding of small disulfide-rich proteins: clarifying the puzzle. Trends in Biochemical Sciences. https://doi.org/10.1016/j.tibs.2006.03.005

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.