Martin, HL, Bedford, R, Heseltine, SJ et al. (5 more authors) (2018) Non-immunoglobulin scaffold proteins: Precision tools for studying protein-protein interactions in cancer. New Biotechnology, 45. pp. 28-35. ISSN 1871-6784
Abstract
Cancer is frequently characterised by dysregulation of the cellular signalling processes that govern proliferation, survival and attachment. Understanding such dysregulation continues to present a challenge given the importance of protein-protein interactions in intracellular processes. Exploring this protein-protein interactome requires novel tools capable of discriminating between highly homologous proteins, individual domains and post-translational modifications. This review examines the potential of scaffold-based binding proteins to fulfil these requirements. It also explores protein-protein interactions in the context of intracellular signalling pathways and cancer, and demonstrates the uses of scaffold proteins as functional moderators, biosensors and imaging reagents. This review also highlights the timeliness and potential to develop international consortia to develop and validate highly specific “proteome” scaffold-based binding protein reagents with the ultimate aim of developing screening tools for studying the interactome.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2018, published by Elsevier B.V. This is an author produced version of a paper published in New Biotechnology. Uploaded in accordance with the publisher's self-archiving policy. |
Keywords: | Affimer; Monobody; DARPins; protein-protein interaction; intracellular signalling |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) > Synthetic Biology (Leed) |
Depositing User: | Symplectic Publications |
Date Deposited: | 20 Feb 2018 12:30 |
Last Modified: | 21 Feb 2019 01:38 |
Status: | Published |
Publisher: | Elsevier |
Identification Number: | 10.1016/j.nbt.2018.02.008 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:127712 |