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Protein Domain Microarrays as a Platform to Decipher Signaling Pathways and the Histone Code.

08:00 EDT 23rd August 2019 | BioPortfolio

Summary of "Protein Domain Microarrays as a Platform to Decipher Signaling Pathways and the Histone Code."

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. (125 words).

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Name: Methods (San Diego, Calif.)
ISSN: 1095-9130
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Medical and Biotech [MESH] Definitions

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A NOD-signaling adaptor protein that contains a C-terminal leucine-rich domain which recognizes bacterial PEPTIDOGLYCAN. It signals via an N-terminal caspase recruitment domain that interacts with other CARD SIGNALING ADAPTOR PROTEINS such as RIP SERINE-THEONINE KINASES. It plays a role in the host defense response by signaling the activation of CASPASES and the MAP KINASE SIGNALING SYSTEM.

An SHC-signaling adaptor protein that links GROWTH FACTOR RECEPTORS to SIGNAL TRANSDUCTION PATHWAYS in neurons.

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