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Nick Totty
Researcher at London Research Institute
Publications - 49
Citations - 8262
Nick Totty is an academic researcher from London Research Institute. The author has contributed to research in topics: Peptide sequence & Phosphorylation. The author has an hindex of 35, co-authored 49 publications receiving 8054 citations. Previous affiliations of Nick Totty include Ludwig Institute for Cancer Research.
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Journal ArticleDOI
Close similarity of epidermal growth factor receptor and v- erb-B oncogene protein sequences
Julian Downward,Yosef Yarden,E. Mayes,G. Scrace,Nick Totty,P. Stockwell,Axel Ullrich,Joseph Schlessinger,Mike Waterfield +8 more
TL;DR: Six peptides derived from the human epidermal growth factor receptor very closely matches a part of the deduced sequence of the v-erb-B transforming protein of avian erythroblastosis virus (AEV).
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The Complete Primary Structure of Protein Kinase C—the Major Phorbol Ester Receptor
Peter J. Parker,Lisa M. Coussens,Nick Totty,Lucy Rhee,Susan Young,Ellson Y. Chen,Silvia Stabel,Michael D. Waterfield,Axel Ullrich +8 more
TL;DR: The complete amino acid sequence of bovine protein kinase C was determined, revealing a domain structure that shows substantial homology, but not identity, to sequences of other protein kinases.
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Modulation of the glycogen synthase kinase-3 family by tyrosine phosphorylation.
TL;DR: It is demonstrated that GSK‐3 beta activity and function are shown to be dependent on tyrosine phosphorylation, equivalent to that required for activity by mitogen‐activated protein (MAP) kinases.
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Human lysozyme gene mutations cause hereditary systemic amyloidosis
Mark B. Pepys,Philip N. Hawkins,David R. Booth,D M Vigushin,Glenys A. Tennent,Anne K. Soutar,Nick Totty,O. Nguyen,Colin C.F. Blake,C. J. Terry,T. G. Feest,A. M. Zalin,J. Justin Hsuan +12 more
TL;DR: It is reported that in two unrelated English families under the authors' care, lysozyme is the amyloid fibril protein in these two families, the first report of naturally occurring variants of human ly sozyme and of lyso enzyme-associated disease.
Journal ArticleDOI
PI 3-kinase is a dual specificity enzyme: autoregulation by an intrinsic protein-serine kinase activity.
Ritu Dhand,Ian Hiles,George Panayotou,Serge Roche,Michael J. Fry,Ivan Gout,Nick Totty,Oanh Truong,P Vicendo,K. Yonezawa +9 more
TL;DR: Tryptic phosphopeptide mapping revealed that the same major peptide was phosphorylated in p85 alpha both in vivo in cultured cells and in the purified recombinant enzyme, having implications for the role of inter‐subunit serine phosphorylation in the regulation of the PI 3‐kinase in vivo.