article Open AccessTop 1% cited
Allosteric Akt (PKB) inhibitors: discovery and SAR of isozyme selective inhibitors
Bioorganic & Medicinal Chemistry Letters · 2004 · Vol. 15(3) · pp. 761–764
Craig W. Lindsley✉(United States Military Academy)Zhijian Zhao(United States Military Academy)William Leister(United States Military Academy)R. Robinson(United States Military Academy)Stanley F. Barnett(United States Military Academy)Deborah Defeo-Jones(United States Military Academy)Raymond E. Jones(United States Military Academy)George D. Hartman(United States Military Academy)Joel R. Huff(United States Military Academy)Hans E. Huber(United States Military Academy)Mark E. Duggan(United States Military Academy)
Quinazolinone synthesis and applicationsPI3K/AKT/mTOR signaling in cancerSynthesis and Biological EvaluationAKT1AKT2Protein kinase BChemistryAllosteric regulationPhosphorylationIn vivoKinaseEnzyme inhibitorBiochemistry
MeSH terms
Allosteric RegulationEnzyme InhibitorsHumansIsoenzymesPhosphorylationProto-Oncogene ProteinsQuinoxalinesStructure-Activity RelationshipApoptosisProtein Serine-Threonine KinasesInhibitory Concentration 50Proto-Oncogene Proteins c-akt
Citations
499
FWCI
14.59
field-weighted impact
References
19
Percentile
100%
vs. same field & year
Citations per year
Cited by
Exploiting the PI3K/AKT Pathway for Cancer Drug Discovery
Nature Reviews Drug Discovery · 2005 · 2,158 citations
Active-Site Inhibitors of mTOR Target Rapamycin-Resistant Outputs of mTORC1 and mTORC2
PLoS Biology · 2009 · 1,072 citations
Targeting cancer with small molecule kinase inhibitors
Nature reviews. Cancer · 2008 · 2,539 citations
References
The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification <sup>1</sup>
The FASEB Journal · 1995 · 2,294 citations
Related articles
Allosteric Akt (PKB) inhibitors: discovery and SAR of isozyme selective inhibitors
Bioorganic & Medicinal Chemistry Letters · 2004 · 499 citations
Citation Network
How this paper connects to the literature. Drag to explore, click any node to open that paper.