Literature DB >> 31449908

Protein domain microarrays as a platform to decipher signaling pathways and the histone code.

Jianji Chen1, Cari Sagum2, Mark T Bedford3.   

Abstract

Signal transduction is driven by protein interactions that are controlled by posttranslational modifications (PTM). Usually, protein domains are responsible for "reading" the PTM signal deposited on the interacting partners. Protein domain microarrays have been developed as a high throughput platform to facilitate the rapid identification of protein-protein interactions, and this approach has become broadly used in biomedical research. In this review, we will summarize the history, development and applications of this technique, including the use of protein domain microarrays in identifying both novel protein-protein interactions and small molecules that block these interactions. We will focus on the approaches we use in the Protein Array and Analysis Core - the PAAC - at MD Anderson Cancer Center. We will also address the technical limitations and discuss future directions.
Copyright © 2019 Elsevier Inc. All rights reserved.

Year:  2019        PMID: 31449908     DOI: 10.1016/j.ymeth.2019.08.007

Source DB:  PubMed          Journal:  Methods        ISSN: 1046-2023            Impact factor:   3.608


  3 in total

1.  Exploring the Ligand Preferences of the PHD1 Domain of Histone Demethylase KDM5A Reveals Tolerance for Modifications of the Q5 Residue of Histone 3.

Authors:  Sarah E Anderson; James E Longbotham; Patrick T O'Kane; Fatima S Ugur; Danica Galonić Fujimori; Milan Mrksich
Journal:  ACS Chem Biol       Date:  2020-12-14       Impact factor: 5.100

2.  Characterization of the plant homeodomain (PHD) reader family for their histone tail interactions.

Authors:  Kanishk Jain; Caroline S Fraser; Matthew R Marunde; Madison M Parker; Cari Sagum; Jonathan M Burg; Nathan Hall; Irina K Popova; Keli L Rodriguez; Anup Vaidya; Krzysztof Krajewski; Michael-Christopher Keogh; Mark T Bedford; Brian D Strahl
Journal:  Epigenetics Chromatin       Date:  2020-01-24       Impact factor: 4.954

3.  The histone and non-histone methyllysine reader activities of the UHRF1 tandem Tudor domain are dispensable for the propagation of aberrant DNA methylation patterning in cancer cells.

Authors:  Robert M Vaughan; Ariana Kupai; Caroline A Foley; Cari A Sagum; Bailey M Tibben; Hope E Eden; Rochelle L Tiedemann; Christine A Berryhill; Varun Patel; Kevin M Shaw; Krzysztof Krajewski; Brian D Strahl; Mark T Bedford; Stephen V Frye; Bradley M Dickson; Scott B Rothbart
Journal:  Epigenetics Chromatin       Date:  2020-10-23       Impact factor: 4.954

  3 in total

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