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of 6
pro vyhledávání: '"Katie L. I. M. Blundell"'
Autor:
Katie L. I. M. Blundell, Michael T. Wilson, Dimitri A. Svistunenko, Erik Vijgenboom, Jonathan A. R. Worrall
Publikováno v:
Open Biology, Vol 3, Iss 1 (2013)
Copper has an important role in the life cycle of many streptomycetes, stimulating the developmental switch between vegetative mycelium and aerial hyphae concomitant with the production of antibiotics. In streptomycetes, a gene encoding for a putativ
Externí odkaz:
https://doaj.org/article/b7fe75d3bd2e4b0b80bfd3dab2f95988
Publikováno v:
Biochemical Journal
Biochemical Journal, 459(3), 515-538
Biochemical Journal, 459(3), 515-538
In Streptomyces lividans an extracytoplasmic copper-binding Sco protein plays a role in two unlinked processes: (i) initiating a morphological development switch and (ii) facilitating the co-factoring of the CuA domain of CcO (cytochrome c oxidase).
Autor:
Jonathan A. R. Worrall, Gary Silkstone, Ann N. Edzuma, Katie L. I. M. Blundell, Badri S. Rajagopal, Valerian E. Kagan, Lewis A. Fraser, Dimitri A. Svistunenko, Michael A. Hough, Alexandr A. Kapralov, Michael T. Wilson, Julea N. Butt
Publikováno v:
Biochemical Journal. 456:441-452
We have investigated whether the pro-apoptotic properties of the G41S mutant of human cytochrome c can be explained by a higher than wild-type peroxidase activity triggered by phospholipid binding. A key complex in mitochondrial apoptosis involves cy
Autor:
Jonathan A. R. Worrall, Dimitri A. Svistunenko, Katie L. I. M. Blundell, Michael T. Wilson, Erik Vijgenboom
Publikováno v:
Open Biology, 3(1)
Open Biology
Open Biology, Vol 3, Iss 1 (2013)
Open Biology
Open Biology, Vol 3, Iss 1 (2013)
Copper has an important role in the life cycle of many streptomycetes, stimulating the developmental switch between vegetative mycelium and aerial hyphae concomitant with the production of antibiotics. In streptomycetes, a gene encoding for a putativ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f796179857707ab3d32f74504b46792
http://hdl.handle.net/1887/3209877
http://hdl.handle.net/1887/3209877
Publikováno v:
Dalton Transactions
The mechanisms and spectroscopic properties generated by intermediate states upon cupric ion binding to flexible peptide motifs in proteins are of considerable interest. One such motif is the Cys-X-X-X-Cys motif characteristic to members of the Sco f
Publikováno v:
PLoS ONE, Vol 12, Iss 3, p e0173543 (2017)
Tetratricopeptide (TPR) domains are known protein interaction domains. We show that the TPR domain of FKBP8 selectively binds Hsp90, and interactions upstream of the conserved MEEVD motif are critical for tight binding. In contrast FKBP8 failed to bi
Externí odkaz:
https://doaj.org/article/64c73e5028eb459e9baa62b68cbf1735