Spatial Conformation and Topography of the Tyrosine Aromatic Ring in Substrate Recognition by Protein Tyrosine Kinases-Reference-Cited by-同舟云学术

Spatial Conformation and Topography of the Tyrosine Aromatic Ring in Substrate Recognition by Protein Tyrosine Kinases

Published:2006-02-16 Issue:6 Volume:49 Page:1916-1924
ISSN:0022-2623
Container-title:Journal of Medicinal Chemistry
language:en
Short-container-title:J. Med. Chem.

Author:

Ruzza Paolo¹,Cesaro Luca¹,Tourwé Dirk¹,Calderan Andrea¹,Biondi Barbara¹,Maes Veronique¹,Menegazzo Ileana¹,Osler Alessio¹,Rubini Chiara¹,Guiotto Andrea¹,Pinna Lorenzo A.¹,Borin Gianfranco¹,Donella-Deana Arianna¹

Affiliation:

1. Institute of Biomolecular Chemistry of CNR, Padova Unit, via F. Marzolo 1, 35131 Padova, Italy, Department of Biological Chemistry, University of Padova, via G. Colombo 3, 35131 Padova, Italy, Vrije Universiteit Brussel, Organic Chemistry Department, Pleinlann 2, B-1050 Brussel, Belgium, and Department of Chemical Sciences, University of Padova, via F. Marzolo 1, 35131 Padova, Italy

Publisher

American Chemical Society (ACS)

Subject

Drug Discovery,Molecular Medicine

Link

https://pubs.acs.org/doi/pdf/10.1021/jm051080q

Reference50 articles.

1. Protein Phosphorylation

2. Conformational constraints of tyrosine in protein tyrosine kinase substrates: Information about preferred bioactive side-chain orientation

3. Specific monitoring of Syk protein kinase activity by peptide substrates including constrained analogs of tyrosine

4. Site specificity of p72sykprotein tyrosine kinase: efficient phosphorylation of motifs recognized by Src homology 2 domains of the Src family

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