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Your search keyword '"Cockman, Matthew E."' showing total 2 results
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2 results on '"Cockman, Matthew E."'

1. The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis.

Author

Maxwell, Patrick H., Wiesener, Michael S., Chang, Gin-Wen, Clifford, Steven C., Vaux, Emma C., Cockman, Matthew E., Wykoff, Charles C., Pugh, Christopher W., Maher, Eamonn R., and Ratcliffe, Peter J.

Subjects
TUMOR suppressor genes, HYPOXEMIA, CELLULAR control mechanisms, PROTEINS, PHYSIOLOGY, GENETICS
Abstract

Presents research which demonstrated the role of the von Hippel-Lindau (VHL) tumor suppressor gene product pVHL in hypoxia-inducible factor-1 (HIF-1) regulation. Role of HIF-1 in cellular responses to hypoxia; Degradation of the alpha subunits of HIF; Traits of VHL-defective cells; Effects of re-expression of pVHL; Iron dependency of HIF-1 and pVHL interactions; HIF-1 activation underlying the angiogenic phenotype of VHL-associated tumors; Application to cellular oxygen sensing studies.

Published
1999
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2. Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans.

Author

Ge, Wei, Wolf, Alexander, Feng, Tianshu, Ho, Chia-hua, Sekirnik, Rok, Zayer, Adam, Granatino, Nicolas, Cockman, Matthew E, Loenarz, Christoph, Loik, Nikita D, Hardy, Adam P, Claridge, Timothy D W, Hamed, Refaat B, Chowdhury, Rasheduzzaman, Gong, Lingzhi, Robinson, Carol V, Trudgian, David C, Jiang, Miao, Mackeen, Mukram M, and Mccullagh, James S

Subjects
RIBOSOMAL proteins, OXYGENASE regulation, HYDROXYLATION kinetics, GENETIC transcription, MYC oncogenes, GENE targeting
Abstract

The finding that oxygenase-catalyzed protein hydroxylation regulates animal transcription raises questions as to whether the translation machinery and prokaryotic proteins are analogously modified. Escherichia coli ycfD is a growth-regulating 2-oxoglutarate oxygenase catalyzing arginyl hydroxylation of the ribosomal protein Rpl16. Human ycfD homologs, Myc-induced nuclear antigen (MINA53) and NO66, are also linked to growth and catalyze histidyl hydroxylation of Rpl27a and Rpl8, respectively. This work reveals new therapeutic possibilities via oxygenase inhibition and by targeting modified over unmodified ribosomes. [ABSTRACT FROM AUTHOR]

Published
2012
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