The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
From Conventional to Unusual Enzyme Inhibitor Scaffolds: The Quest for Target Specificity
Abstract
The tremendous challenge presented by the specific molecular recognition of single biomacromolecular targets within complex biological systems demands novel and creative design strategies. This Minireview discusses some conventional and unusual approaches for the design of target‐selective enzyme inhibitors with a focus on the underlying chemical scaffolds. These include complicated natural‐product‐like organic molecules, stable octahedral metal complexes, fullerenes, carboranes, polymetallic clusters, and even polymers. Thus the whole repertoire of organic, inorganic, and macromolecular chemistry can be applied to tackle the problem of target‐specific enzyme inhibition.
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
A quantitative analysis of kinase inhibitor selectivity
Karaman, M. W., Herrgard, S., Treiber, D. K., Gallant, P., Atteridge, C. E., Campbell, B. T., Chan, K. W., Ciceri, P., Davis, M. I., Edeen, P. T., et al. (2008) · Nature Biotechnology · doi:10.1038/nbt1358 · Cited by 2,466
Small molecules: the missing link in the central dogma
Schreiber, S. L. (2005) · Nature Chemical Biology · doi:10.1038/nchembio0705-64 · Cited by 306
Cited by
You, Y., & Nam, W. (2012) · Chemical Society Reviews · doi:10.1039/c2cs35171d · Cited by 668
Toward Multi-Targeted Platinum and Ruthenium Drugs—A New Paradigm in Cancer Drug Treatment Regimens?
Kenny, R. G., & Marmion, C. J. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00271 · Cited by 636
Metal-based drugs that break the rules
Allardyce, C. S., & Dyson, P. J. (2016) · Dalton Transactions · doi:10.1039/c5dt03919c · Cited by 308
Metadata
- Authors
- Meggers, E.
- Venue
- Angewandte Chemie International Edition
- Publisher
- Wiley
- Published
- 2011-02-15
- Volume
- 50
- Issue
- 11
- Pages
- 2442-2448
- ISSN
- 1433-7851 (ISSN-L)
- 1521-3773
- OpenAlex
- W2098499111
- Cited by
- 158
- References
- 2
- FWCI
- 7.41
- 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: From Conventional to Unusual Enzyme Inhibitor Scaffolds: The Quest for Target Specificity. https://app.cochat.ai/papers/10.1002/anie.201005673
- The paper
- Meggers, E. (2011). From Conventional to Unusual Enzyme Inhibitor Scaffolds: The Quest for Target Specificity. Angewandte Chemie International Edition. https://doi.org/10.1002/anie.201005673
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.