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Studying of Telomeric Protein–Protein Interactions by Bi-Molecular Fluorescence Complementation (BiFC) and Peptide Array-Based Assays

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Telomeres and Telomerase

Part of the book series: Methods in Molecular Biology ((MIMB,volume 735))

Abstract

Studying protein–protein interactions is critical to our understanding of the signaling pathways. The Telomere Interactome is assembled around the telomeres and consists of proteins and factors from diverse pathways. Dissecting how this protein network contributes to telomere protection and length regulation requires the elucidation of the complex and dynamic interactions between the proteins within the interactome. Here, we focus on the Bi-molecular fluorescence complementation (BiFC) and peptide array methods that have proven vital in our studies of telomere protein interaction networks.

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References

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Acknowledgment

We would like to thank Dr. Dan Liu for comments. This work is supported by NCI CA133249, NIGMS GM081627, National Basic Research Program 2010CB945400, and the Welch Foundation Q-1673. Z.S. is a Leukemia and Lymphoma Society Scholar. We would also like to acknowledge the support of the GRSA Shared Resource (P30CA125123), and the Administrative and Genome-wide RNAi Screens Cores (IDDRC P30HD024064).

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Correspondence to Zhou Songyang .

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Ma, W., Kim, H., Songyang, Z. (2011). Studying of Telomeric Protein–Protein Interactions by Bi-Molecular Fluorescence Complementation (BiFC) and Peptide Array-Based Assays. In: Songyang, Z. (eds) Telomeres and Telomerase. Methods in Molecular Biology, vol 735. Humana Press. https://doi.org/10.1007/978-1-61779-092-8_16

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  • DOI: https://doi.org/10.1007/978-1-61779-092-8_16

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  • Publisher Name: Humana Press

  • Print ISBN: 978-1-61779-091-1

  • Online ISBN: 978-1-61779-092-8

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