A mechanistic design principle for protein tyrosine kinase sensors: Application to a validated cancer target

Aya Wakata; Sean M. Cahill; Michael Blumenstein; Rosalind H. Gunby; Steffen Jockusch; Angel A. Marti; Barbara Cimbro; Carlo Gambacorti-Passerini; Arianna Donella-Deana; Lorenzo A. Pinna; Nicholas J. Turro; David S. Lawrence

doi:10.1021/ol702675b

A mechanistic design principle for protein tyrosine kinase sensors: Application to a validated cancer target

Aya Wakata
, Sean M. Cahill
, Michael Blumenstein
, Rosalind H. Gunby
, Steffen Jockusch
, Angel A. Marti
, Barbara Cimbro
, Carlo Gambacorti-Passerini
, Arianna Donella-Deana
, Lorenzo A. Pinna
, Nicholas J. Turro
, David S. Lawrence

Biochemistry

Research output: Contribution to journal › Article › peer-review

15 Scopus citations

Abstract

(Graph Presented) A new mechanistic principle for reporting the phosphorylation of tyrosine is described, which should prove applicable to even the most fastidious of protein tyrosine kinases, as demonstrated by the acquisition of a fluorescent sensor for the extraordinarily demanding anaplastic lymphoma kinase.

Original language	English (US)
Pages (from-to)	301-304
Number of pages	4
Journal	Organic Letters
Volume	10
Issue number	2
DOIs	https://doi.org/10.1021/ol702675b
State	Published - Jan 17 2008

ASJC Scopus subject areas

Biochemistry
Physical and Theoretical Chemistry
Organic Chemistry

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1021/ol702675b

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Wakata, A., Cahill, S. M., Blumenstein, M., Gunby, R. H., Jockusch, S., Marti, A. A., Cimbro, B., Gambacorti-Passerini, C., Donella-Deana, A., Pinna, L. A., Turro, N. J., & Lawrence, D. S. (2008). A mechanistic design principle for protein tyrosine kinase sensors: Application to a validated cancer target. Organic Letters, 10(2), 301-304. https://doi.org/10.1021/ol702675b

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abstract = "(Graph Presented) A new mechanistic principle for reporting the phosphorylation of tyrosine is described, which should prove applicable to even the most fastidious of protein tyrosine kinases, as demonstrated by the acquisition of a fluorescent sensor for the extraordinarily demanding anaplastic lymphoma kinase.",

author = "Aya Wakata and Cahill, \{Sean M.\} and Michael Blumenstein and Gunby, \{Rosalind H.\} and Steffen Jockusch and Marti, \{Angel A.\} and Barbara Cimbro and Carlo Gambacorti-Passerini and Arianna Donella-Deana and Pinna, \{Lorenzo A.\} and Turro, \{Nicholas J.\} and Lawrence, \{David S.\}",

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AU - Blumenstein, Michael

AU - Gunby, Rosalind H.

AU - Jockusch, Steffen

AU - Marti, Angel A.

AU - Cimbro, Barbara

AU - Gambacorti-Passerini, Carlo

AU - Donella-Deana, Arianna

AU - Pinna, Lorenzo A.

AU - Turro, Nicholas J.

AU - Lawrence, David S.

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AB - (Graph Presented) A new mechanistic principle for reporting the phosphorylation of tyrosine is described, which should prove applicable to even the most fastidious of protein tyrosine kinases, as demonstrated by the acquisition of a fluorescent sensor for the extraordinarily demanding anaplastic lymphoma kinase.

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JO - Organic Letters

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ER -

A mechanistic design principle for protein tyrosine kinase sensors: Application to a validated cancer target

Abstract

ASJC Scopus subject areas

UN SDGs

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