The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Embracing proteins: structural themes in aptamer–protein complexes
Open accessAbstract
Understanding the structural rules that govern specific, high-affinity binding characteristic of aptamer-protein interactions is important in view of the increasing use of aptamers across many applications. From the modest number of 16 aptamer-protein structures currently available, trends are emerging. The flexible phosphodiester backbone allows folding into precise three-dimensional structures using known nucleic acid motifs as scaffolds that orient specific functional groups for target recognition. Still, completely novel motifs essential for structure and function are found in modified aptamers with diversity-enhancing side chains. Aptamers and antibodies, two classes of macromolecules used as affinity reagents with entirely different backbones and composition, recognize protein epitopes of similar size and with comparably high shape complementarity.
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
Aptamer-Based Multiplexed Proteomic Technology for Biomarker Discovery
Gold, L., Ayers, D., Bertino, J., Bock, C., Bock, A., Brody, E. N., Carter, J., Dalby, A. B., Eaton, B. E., Fitzwater, T., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015004 · Cited by 1,754
Cited by
Analysis of aptamer discovery and technology
Dunn, M. R., Jimenez, R. M., & Chaput, J. C. (2017) · Nature Reviews Chemistry · doi:10.1038/s41570-017-0076 · Cited by 938
Nucleic Acid Aptamers for Molecular Diagnostics and Therapeutics: Advances and Perspectives
Li, L., Xu, S., Yan, H., Li, X., Yazd, H. S., Li, X., Huang, T., Cui, C., Jiang, J., & Tan, W. (2021) · Angewandte Chemie International Edition · doi:10.1002/anie.202003563 · Cited by 432
SELEX: Critical factors and optimization strategies for successful aptamer selection
Kohlberger, M., & Gadermaier, G. (2022) · Biotechnology and Applied Biochemistry · doi:10.1002/bab.2244 · Cited by 341
Aptamers: A Review of Their Chemical Properties and Modifications for Therapeutic Application
Adachi, T., & Nakamura, Y. (2019) · Molecules · doi:10.3390/molecules24234229 · Cited by 300
Metadata
- Authors
- Gelinas, A. D., Davies, D. R., & Janjic, N.
- Venue
- Current Opinion in Structural Biology
- Publisher
- Elsevier BV
- Published
- 2016-02
- Volume
- 36
- Pages
- 122-132
- ISSN
- 0959-440X (ISSN-L)
- OpenAlex
- W2283601867
- Cited by
- 206
- References
- 1
- FWCI
- 1.19
- Type
- journal article
- Language
- en
- Open access
- hybrid
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: Embracing proteins: structural themes in aptamer–protein complexes. https://app.cochat.ai/papers/10.1016/j.sbi.2016.01.009
- The paper
- Gelinas, A. D., Davies, D. R., & Janjic, N. (2016). Embracing proteins: structural themes in aptamer–protein complexes. Current Opinion in Structural Biology. https://doi.org/10.1016/j.sbi.2016.01.009
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.
