D
Dennis Joseph Mcnamara
Researcher at Parke-Davis
Publications - 49
Citations - 2404
Dennis Joseph Mcnamara is an academic researcher from Parke-Davis. The author has contributed to research in topics: Peptide & Autophosphorylation. The author has an hindex of 23, co-authored 49 publications receiving 2356 citations. Previous affiliations of Dennis Joseph Mcnamara include Pfizer & University of Michigan.
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Irreversible inhibitors of tyrosine kinases
Alexander James Bridges,William Alexander Denny,Ellen Myra Dobrusin,Annette Marian Doherty,David W. Fry,Dennis Joseph Mcnamara,Howard Daniel Hollis Showalter,Jeffrey Bruce Smaill,Zhou Hairong +8 more
TL;DR: In this article, a method for treating cancer, restenosis, atherosclerosis, endometriosis, and psoriasis and a pharmaceutical composition that comprises a compound that is an irreversible inhibitor of tyrosine kinases.
Journal ArticleDOI
Specific, irreversible inactivation of the epidermal growth factor receptor and erbB2, by a new class of tyrosine kinase inhibitor
David W. Fry,Alexander James Bridges,William A. Denny,Annette Marian Doherty,Kenneth D. Greis,James L. Hicks,Kenneth E. Hook,Paul R. Keller,Wilbur R. Leopold,Joseph A. Loo,Dennis Joseph Mcnamara,James M. Nelson,Veronika Sherwood,Jeff B. Smaill,Susanne Trumpp-Kallmeyer,Ellen Myra Dobrusin +15 more
TL;DR: A direct comparison between 6-acrylamido-4-anilinoquinazoline and an equally potent but reversible analog shows that the irreversible inhibitor has far superior in vivo antitumor activity in a human epidermoid carcinoma xenograft model with no overt toxicity at therapeutically active doses.
Journal ArticleDOI
Substrate specificity of the protein tyrosine phosphatases.
Zhong Yin Zhang,Andrea M. Thieme-Sefler,Derek Maclean,Dennis Joseph Mcnamara,Ellen Myra Dobrusin,Tomi K. Sawyer,Jack E. Dixon +6 more
TL;DR: The results demonstrate that chemical features in the primary structure surrounding the dephosphorylation site contribute to PTPase substrate specificity and suggest that phosphate dianion is favored for substrate binding.
Journal ArticleDOI
Protein tyrosine phosphatase substrate specificity: size and phosphotyrosine positioning requirements in peptide substrates
Zhong Yin Zhang,Derek Maclean,Derek Maclean,Dennis Joseph Mcnamara,Dennis Joseph Mcnamara,Tomi K. Sawyer,Tomi K. Sawyer,Jack E. Dixon,Jack E. Dixon +8 more
TL;DR: It is demonstrated that the thiophosphoryl analog in which one of the phosphate oxygens is replaced by sulfur can be hydrolyzed by PTPases, whereas the phosphonomethylphenylalanine analog is a competitive and nonhydrolyzable inhibitor.
Journal ArticleDOI
Pyrido[2,3-d]pyrimidin-7-ones as specific inhibitors of cyclin-dependent kinase 4.
Scott Norman Vanderwel,Patricia J. Harvey,Dennis Joseph Mcnamara,Joseph Thomas Repine,Paul R. Keller,John Quin,R. John Booth,William Elliott,Ellen Myra Dobrusin,David W. Fry,Peter L. Toogood +10 more
TL;DR: It is reported that the introduction of a methyl substituent at the C-5 position of the pyrido[2,3-d]pyrimidin-7-one template is sufficient to confer excellent selectivity for Cdk4 vs other Cdks and representative tyrosine kinases.