The development and use of phospho-specific antibodies to study protein phosphorylation
The development and use of phospho-specific antibodies to study protein phosphorylation
The reversible phosphorylation of proteins is a key mechanism whereby signalling cascades involved in the response to extracellular stimuli bring about changes in cellular function. These proteins include the kinases/phosphatases that form such signaling pathways as well as the transcription factors involved in inducible changes in gene expression (1). Phosphorylation induces changes in the function of these proteins either by induction of allosteric conformational changes in the protein itself or in the regulation of its interaction with other cellular factors.
177-189
Blaydes, Jeremy P.
e957f999-fd91-4f77-ad62-5b4ef069b15b
Vojtesek, Borek
ac248301-6154-4047-90f0-7ddfc7c74cc1
Bloomberg, Graham B.
ed27bb6c-73d7-4246-b940-ad88d573277a
Hupp, Ted R.
5e2b65e8-052c-4f46-9814-49aff35fe3cc
2000
Blaydes, Jeremy P.
e957f999-fd91-4f77-ad62-5b4ef069b15b
Vojtesek, Borek
ac248301-6154-4047-90f0-7ddfc7c74cc1
Bloomberg, Graham B.
ed27bb6c-73d7-4246-b940-ad88d573277a
Hupp, Ted R.
5e2b65e8-052c-4f46-9814-49aff35fe3cc
Blaydes, Jeremy P., Vojtesek, Borek, Bloomberg, Graham B. and Hupp, Ted R.
(2000)
The development and use of phospho-specific antibodies to study protein phosphorylation.
Methods in Molecular Biology, 99 (II), .
(doi:10.1385/1592590543).
Abstract
The reversible phosphorylation of proteins is a key mechanism whereby signalling cascades involved in the response to extracellular stimuli bring about changes in cellular function. These proteins include the kinases/phosphatases that form such signaling pathways as well as the transcription factors involved in inducible changes in gene expression (1). Phosphorylation induces changes in the function of these proteins either by induction of allosteric conformational changes in the protein itself or in the regulation of its interaction with other cellular factors.
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Published date: 2000
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Local EPrints ID: 150559
URI: http://eprints.soton.ac.uk/id/eprint/150559
PURE UUID: 70674f59-26e9-4630-898d-b7971212ada9
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Date deposited: 20 Jul 2010 13:21
Last modified: 14 Mar 2024 02:45
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Author:
Borek Vojtesek
Author:
Graham B. Bloomberg
Author:
Ted R. Hupp
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