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Cited by 1,198

The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

Protein Kinase Inhibitors: Insights into Drug Design from Structure

Open access
Noble, Martin E. M., Endicott, Jane A., Johnson, Louise N.·2004·Science
DOI 10.1126/science.1095920
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Abstract

Protein kinases are targets for treatment of a number of diseases. This review focuses on kinase inhibitors that are in the clinic or in clinical trials and for which structural information is available. Structures have informed drug design and have illuminated the mechanism of inhibition. We review progress with the receptor tyrosine kinases (growth factor receptors EGFR, VEGFR, and FGFR) and nonreceptor tyrosine kinases (Bcr-Abl), where advances have been made with cancer therapeutic agents such as Herceptin and Gleevec. Among the serine-threonine kinases, p38, Rho-kinase, cyclin-dependent kinases, and Chk1 have been targeted with productive results for inflammation and cancer. Structures have provided insights into targeting the inactive or active form of the kinase, for targeting the global constellation of residues at the ATP site or less conserved additional pockets or single residues, and into targeting noncatalytic domains.

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Metadata

Authors
Noble, M. E. M., Endicott, J. A., & Johnson, L. N.
Venue
Science
Publisher
American Association for the Advancement of Science (AAAS)
Published
2004-03-19
Volume
303
Issue
5665
Pages
1800-1805
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
DOI
10.1126/science.1095920
OpenAlex
W2138072853
Cited by
1,198
References
3
FWCI
30.40
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Protein Kinase Inhibitors: Insights into Drug Design from Structure. https://app.cochat.ai/papers/10.1126/science.1095920
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Noble, M. E. M., Endicott, J. A., & Johnson, L. N. (2004). Protein Kinase Inhibitors: Insights into Drug Design from Structure. Science. https://doi.org/10.1126/science.1095920

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

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