Výsledky vyhledávání - "Nicholas T Redpath"

LRIG1 Extracellular Domain: Structure and Function Analysis

Autor: Thomas P. J. Garrett, Nicos A. Nicola, Priscilla Soo, Yibin Xu, Francesca Walker, Chin Wee Tan, Timothy E. Adams, Nicholas T. Redpath, Antony W. Burgess, Hui Hua Zhang, Jian-Guo Zhang

Publikováno v: Journal of Molecular Biology. 427:1934-1948

We have expressed and purified three soluble fragments of the human LRIG1-ECD (extracellular domain): the LRIG1-LRR (leucine-rich repeat) domain, the LRIG1-3Ig (immunoglobulin-like) domain, and the LRIG1-LRR-1Ig fragment using baculovirus vectors in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d6408a59a1629d1ec0f7db83262fa95d
https://doi.org/10.1016/j.jmb.2015.03.001

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Conservation of Functional Sites on Interleukin-6 and Implications for Evolution of Signaling Complex Assembly and Therapeutic Intervention

Autor: Bruce Carrington, Nicholas T. Redpath, Terry Baker, Richard J. K. Taylor, Alastair D. G. Lawson, Mark D. Carr, Frederick W. Muskett, Alistair James Henry, Vaclav Veverka

Publikováno v: Journal of Biological Chemistry. 287:40043-40050

A number of secreted cytokines, such as interleukin-6 (IL-6), are attractive targets for the treatment of inflammatory diseases. We have determined the solution structure of mouse IL-6 to assess the functional significance of apparent differences in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0fd46dbff9ca00295496206002be1c51
https://doi.org/10.1074/jbc.m112.405597

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The ageing heart: influence of cellular and tissue ageing on total content and distribution of the variants of elongation factor-2

Autor: Ingrid Heinroth-Hoffmann, Ursula Müller-Werdan, Nicholas T Redpath, Karl Werdan, Klaus Pönicke, Doris Jäger, Sylvana P. Müller, Jürgen Holtz

Publikováno v: Mechanisms of Ageing and Development. 123:1305-1319

The involvement of elongation factor-2 (EEF-2), a key-protein of peptide-chain elongation, in the slowing down of protein synthesis during cardiac ageing was addressed. EEF-2 was measured in rat heart extracts and isolated rat cardiomyocytes (CM) fro

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::851fbebccaf69e37e1e139d63ac52cc3
https://doi.org/10.1016/s0047-6374(02)00040-4

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Phosphorylation of elongation factor-2 kinase on serine 499 by cAMP-dependent protein kinase induces Ca2+/calmodulin-independent activity

Autor: Tricia A. DIGGLE, Tatiana SUBKHANKULOVA, Kathryn S. LILLEY, Nita SHIKOTRA, Anne E. WILLIS, Nicholas T. REDPATH

Publikováno v: Biochemical Journal. 353:621-626

Elongation factor-2 kinase (eEF-2K) negatively regulates mRNA translation via the phosphorylation and inactivation of elongation factor-2 (eEF-2). We have shown previously that purified eEF-2K can be phosphorylated in vitro by cAMP-dependent protein

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::20ce92ac7db61ccd968d0fa5f1c14a16
https://doi.org/10.1042/bj3530621

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Heterogeneity of cardiac rat and human elongation factor 2

Autor: Nicholas T. Redpath, Karl Werdan, Ivar Friedrich, Christian Seliger, Klaus Pönicke, Doris Jäger, Rolf-Edgar Silber, Ursula Müller-Werdan

Publikováno v: Electrophoresis. 21:2729-2736

Elongation factor 2 (EF-2) catalyses the last step of the elongation cycle, translocation, in the course of protein biosynthesis. A system for analyzing post-translational modifications of EF-2, which is a single polypeptide of 857 amino acids, is re

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::6ad5ae1bcc9a2b51bf960bfe8a79ea24
https://doi.org/10.1002/1522-2683(20000701)21:13<2729::aid-elps2729>3.0.co

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Production of a human neutralizing monoclonal antibody and its crystal structure in complex with ectodomain 3 of the interleukin-13 receptor α1

Publikováno v: The Biochemical journal. 451(2)

Gene deletion studies in mice have revealed critical roles for IL (interleukin)-4 and -13 in asthma development, with the latter controlling lung airways resistance and mucus secretion. We have now developed human neutralizing monoclonal antibodies a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::45eb3760f8aad5f03cd91c2019461d1c
https://pubmed.ncbi.nlm.nih.gov/23535171

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Cloning and Expression of cDNA Encoding Protein Synthesis Elongation Factor-2 Kinase

Autor: Christopher G. Proud, Nigel T. Price, Nicholas T. Redpath

Publikováno v: Journal of Biological Chemistry. 271:17547-17554

A cDNA from rat skeletal muscle encoding calcium/calmodulin-dependent eukaryotic elongation factor-2 kinase (eEF-2K) has been cloned and sequenced, and the amino acid sequence of the protein has been deduced. The kinase is composed of 724 amino acids

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b52f485b1f80235c07df889ef30a0621
https://doi.org/10.1074/jbc.271.29.17547

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Regulation of translation elongation factor-2 by insulin via a rapamycin-sensitive signalling pathway

Autor: Emily J. Foulstone, Christopher G. Proud, Nicholas T. Redpath

Publikováno v: The EMBO Journal. 15:2291-2297

It is well established that insulin and serum stimulate gene expression at the level of mRNA translation in animal cells, and previous studies have mainly focused on the initiation process. Here we show that, in Chinese hamster ovary cells expressing

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::0ed99ef9e6c3d06cd6acf4a1d20de9b8
https://doi.org/10.1002/j.1460-2075.1996.tb00582.x

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Purification and phosphorylation of elongation factor-2 kinase from rabbit reticulocytes

Autor: Christopher G. Proud, Nicholas T. Redpath

Publikováno v: European Journal of Biochemistry. 212:511-520

Eukaryotic elongation-factor-2 kinase has been purified to homogeneity from rabbit reticulocytes through a seven-step procedure and has been identified as a protein with a molecular mass of approximately 103 kDa as judged by SDS/PAGE. A degradation p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2f603432c57b2fa9bb79a50331384035
https://doi.org/10.1111/j.1432-1033.1993.tb17688.x

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Differing effects of the protein phosphatase inhibitors okadaic acid and microcystin on translation in reticulocyte lysates

Autor: Nicholas T. Redpath, Christopher G. Proud

Publikováno v: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1093:36-41

The effects of the cyanobacterial toxin and protein phosphatase inhibitor, microcystin, on translation in rabbit reticulocyte lysates have been studied. Microcystin inhibited translation with similar potency to the protein phosphatase inhibitor okada

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c6d35c9b581fcc5d57577d9117aec858
https://doi.org/10.1016/0167-4889(91)90135-k

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