The DOI matches its Crossref record; 80 of the 80 references it cites were found in a registry or an index.
Peptidic foldamers: ramping up diversity
Abstract
Non-natural folded polymers (foldamers) display considerable versatility, and the design of such molecules is of great current interest. In this respect, peptidic foldamers are perhaps the best-characterized systems, as they populate a number of residue-controlled secondary structures, which have found various biological applications and have also led to the creation of nanostructured materials. This critical review covers recent developments related to diverse building blocks and modern foldamer design principles, such as the stereochemical patterning methods. The recent achievements concerning tertiary/quaternary structures and the self-assembling foldameric nanostructures are also addressed (176 references).
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.
Integrity signals
Registry
Cites
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.
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
Gellman, S. H. (1998) · Accounts of Chemical Research · doi:10.1021/ar960298r · Cited by 2,506
Hill, D. J., Mio, M. J., Prince, R. B., Hughes, T. S., & Moore, J. S. (2001) · Chemical Reviews · doi:10.1021/cr990120t · Cited by 2,239
The Diels-Alder Reaction in Total Synthesis
Nicolaou, K. C., Snyder, S. A., Montagnon, T., & Vassilikogiannakis, G. E. (2002) · Angewandte Chemie International Edition · doi:10.1002/1521-3773(20020517)41:10<1718::aid-anie1718>3.0.co;2-2 · Cited by 1,883
A Switch Between Two-, Three-, and Four-stranded Coiled Coils in GCN4 Leucine Zipper Mutants
Harbury, P. B., Zhang, T., Kim, P. S., & Alber, T. (1993) · Science · doi:10.1126/science.8248779 · Cited by 1,490
X-Ray Structure of the GCN4 Leucine Zipper, a Two-Stranded, Parallel Coiled Coil
O'Shea, E. K., Klemm, J. D., Kim, P. S., & Alber, T. (1991) · Science · doi:10.1126/science.1948029 · Cited by 1,440
Seebach, D., Beck, A. K., & Bierbaum, D. J. (2004) · Chemistry & Biodiversity · doi:10.1002/cbdv.200490087 · Cited by 932
Foldamers as versatile frameworks for the design and evolution of function
Goodman, C. M., Choi, S., Shandler, S., & DeGrado, W. F. (2007) · Nature Chemical Biology · doi:10.1038/nchembio876 · Cited by 899
Huc, I. (2004) · European Journal of Organic Chemistry · doi:10.1002/ejoc.200300495 · Cited by 714
Seebach, D., & Gardiner, J. (2008) · Accounts of Chemical Research · doi:10.1021/ar700263g · Cited by 709
Foldamers with Heterogeneous Backbones
Horne, W. S., & Gellman, S. H. (2008) · Accounts of Chemical Research · doi:10.1021/ar800009n · Cited by 689
Cited by
Biomimetic peptide self-assembly for functional materials
Levin, A., Hakala, T. A., Schnaider, L., Bernardes, G. J. L., Gazit, E., & Knowles, T. P. J. (2020) · Nature Reviews Chemistry · doi:10.1038/s41570-020-0215-y · Cited by 853
The Road from Host-Defense Peptides to a New Generation of Antimicrobial Drugs
Boto, A., Pérez de la Lastra, J., & González, C. (2018) · Molecules · doi:10.3390/molecules23020311 · Cited by 136
Continuous‐Flow Solid‐Phase Peptide Synthesis: A Revolutionary Reduction of the Amino Acid Excess
Mándity, I. M., Olasz, B., Ötvös, S. B., & Fülöp, F. (2014) · ChemSusChem · doi:10.1002/cssc.201402436 · Cited by 65
Self-citationEfficient molecular encoding in multifunctional self-immolative urethanes
Dahlhauser, S. D., Moor, S. R., Vera, M. S., York, J. T., Ngo, P., Boley, A. J., Coronado, J. N., Simpson, Z. B., & Anslyn, E. V. (2021) · Cell Reports Physical Science · doi:10.1016/j.xcrp.2021.100393 · Cited by 38
Metadata
- Authors
- Martinek, T. A., & Fülöp, F.
- Venue
- Chem. Soc. Rev.
- Publisher
- Royal Society of Chemistry (RSC)
- Published
- 2012
- Volume
- 41
- Issue
- 2
- Pages
- 687-702
- ISSN
- 0306-0012 (ISSN-L)
- 1460-4744
- OpenAlex
- W2032891742
- Cited by
- 485
- References
- 80
- FWCI
- 2.96
- 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: Peptidic foldamers: ramping up diversity. https://app.cochat.ai/papers/10.1039/c1cs15097a
- The paper
- Martinek, T. A., & Fülöp, F. (2012). Peptidic foldamers: ramping up diversity. Chem. Soc. Rev. https://doi.org/10.1039/c1cs15097a
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.
