Student or educator? Sign up with your school email and get 6 months of Pro free.
Cited by 418

The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.

Constraining Cyclic Peptides To Mimic Protein Structure Motifs

Hill, Timothy A., Shepherd, Nicholas E., Diness, Frederik, Fairlie, David P.·2014·Angewandte Chemie International Edition

Abstract

Many proteins exert their biological activities through small exposed surface regions called epitopes that are folded peptides of well‐defined three‐dimensional structures. Short synthetic peptide sequences corresponding to these bioactive protein surfaces do not form thermodynamically stable protein‐like structures in water. However, short peptides can be induced to fold into protein‐like bioactive conformations (strands, helices, turns) by cyclization, in conjunction with the use of other molecular constraints, that helps to fine‐tune three‐dimensional structure. Such constrained cyclic peptides can have protein‐like biological activities and potencies, enabling their uses as biological probes and leads to therapeutics, diagnostics and vaccines. This Review highlights examples of cyclic peptides that mimic three‐dimensional structures of strand, turn or helical segments of peptides and proteins, and identifies some additional restraints incorporated into natural product cyclic peptides and synthetic macrocyclic peptidomimetics that refine peptide structure and confer biological properties.

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 · 10.1002/anie.201401058

Cites

24 of 24 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 24 references

Cited by

See all 418

Metadata

Authors
Hill, T. A., Shepherd, N. E., Diness, F., & Fairlie, D. P.
Venue
Angewandte Chemie International Edition
Publisher
Wiley
Published
2014-10-06
Volume
53
Issue
48
Pages
13020-13041
ISSN
  • 1433-7851 (ISSN-L)
  • 1521-3773
OpenAlex
W1967671116
Cited by
418
References
24
FWCI
14.72
Type
journal article
Language
en
Open access
closed

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: Constraining Cyclic Peptides To Mimic Protein Structure Motifs. https://app.cochat.ai/papers/10.1002/anie.201401058
The paper
Hill, T. A., Shepherd, N. E., Diness, F., & Fairlie, D. P. (2014). Constraining Cyclic Peptides To Mimic Protein Structure Motifs. Angewandte Chemie International Edition. https://doi.org/10.1002/anie.201401058

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.