Protein folding creates structure-based, noncontiguous consensus phosphorylation motifs recognized by kinases-Reference-Cited by-同舟云学术

Protein folding creates structure-based, noncontiguous consensus phosphorylation motifs recognized by kinases

Published:2014-11-04 Issue:350 Volume:7 Page:
ISSN:1945-0877
Container-title:Science Signaling
language:en
Short-container-title:Sci. Signal.

Author:

Duarte Mariana Lemos¹,Pena Darlene Aparecida¹,Nunes Ferraz Felipe Augusto²,Berti Denise Aparecida¹,Paschoal Sobreira Tiago José²,Costa-Junior Helio Miranda¹,Abdel Baqui Munira Muhammad³,Disatnik Marie-Hélène⁴,Xavier-Neto José²,Lopes de Oliveira Paulo Sérgio²,Schechtman Deborah¹

Affiliation:

1. Departamento de Bioquímica, Instituto de Química, Universidade de São Paulo, São Paulo 05508000, Brazil.

2. Laboratório Nacional de Biociências, Centro Nacional de Pesquisa em Energia e Materiais, Campinas 13083-970, Brazil.

3. Departamento de Biologia Celular e Molecular, Faculdade de Medicina de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, São Paulo 14049-900, Brazil.

4. Department of Chemical and Systems Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.

Abstract

Kinases can recognize consensus motifs that are noncontiguous in folded proteins.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference33 articles.

1. Substrate specificity of the cyclic AMP-dependent protein kinase.

2. Substrate specificity of protein kinases and computational prediction of substrates

3. A rapid method for determining protein kinase phosphorylation specificity

4. Use of an oriented peptide library to determine the optimal substrates of protein kinases

5. Profiling the Substrate Specificity of Protein Kinases by On-Bead Screening of Peptide Libraries

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