Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Wesley I. Booth"'
Publikováno v:
PLoS ONE, Vol 10, Iss 8, p e0136732 (2015)
During endocytosis in S. cerevisiae, actin polymerization is proposed to provide the driving force for invagination against the effects of turgor pressure. In previous studies, Ysc84 was demonstrated to bind actin through a conserved N-terminal domai
Externí odkaz:
https://doaj.org/article/d2b5406b6c34417ca1aa17b7c5cdcf00
Autor:
Robert K. Poole, Stephen A. Baldwin, Mark Shepherd, Wesley I. Booth, Yvonne Nyathi, Masao Yamashita, Vincent L. G. Postis, Svetomir B. Tzokov, Per A. Bullough, Hao Xie
Publikováno v:
The Journal of Biological Chemistry
Background: The ABC transporter CydDC, which pumps sulfur compounds, is required for assembly of the bacterial respiratory machinery. Results: ATP hydrolysis by CydCD in response to sulfur compounds is modulated by hemes. Conclusion: Hemes regulate C
Autor:
Wesley I. Booth, Ritu Mishra, Kathryn R. Ayscough, Iwona I. Smaczynska-de Rooij, Ellen G. Allwood, Soheil Aghamohammadzadeh, Martin W. Goldberg
Publikováno v:
Traffic. 13:317-328
Dynamins are a conserved family of proteins involved in many membrane fusion and fission events. Previously, the dynamin-related protein Vps1 was shown to localize to endocytic sites, and yeast carrying deletions for genes encoding both the BAR domai
Autor:
Stephen A. Baldwin, Wesley I. Booth, Kalypso Charalambous, Vincent L. G. Postis, Christopher A.P. Glover, Per A. Bullough, Sarah E. Deacon, Bonnie A. Wallace, Svetomir B. Tzokov
Publikováno v:
Journal of Structural Biology. 176:419-424
Contamination with the multidrug transporter AcrB represents a potential pitfall in the structural analysis of recombinant membrane proteins expressed in Escherichia coli , especially when high-throughput approaches are adopted. This can be a particu
Autor:
Iwona I, Smaczynska-de Rooij, Christopher J, Marklew, Ellen G, Allwood, Sarah E, Palmer, Wesley I, Booth, Ritu, Mishra, Martin W, Goldberg, Kathryn R, Ayscough
Publikováno v:
Molecular and Cellular Biology
The family of dynamin proteins is known to function in many eukaryotic membrane fusion and fission events. The yeast dynamin-related protein Vps1 functions at several stages of membrane trafficking, including Golgi apparatus to endosome and vacuole,
Publikováno v:
PLoS ONE
PLoS ONE, Vol 10, Iss 8, p e0136732 (2015)
PLoS ONE, Vol 10, Iss 8, p e0136732 (2015)
During endocytosis in S. cerevisiae, actin polymerization is proposed to provide the driving force for invagination against the effects of turgor pressure. In previous studies, Ysc84 was demonstrated to bind actin through a conserved N-terminal domai
Publikováno v:
Current biology : CB. 23(3)
Summary Background Actin nucleation is the key rate-limiting step in actin polymerization, and tight regulation of this process is critical to ensure that actin filaments form only at specific regions of the cell. Las17 is the primary activator of Ar
Autor:
Iwona I, Smaczynska-de Rooij, Ellen G, Allwood, Ritu, Mishra, Wesley I, Booth, Soheil, Aghamohammadzadeh, Martin W, Goldberg, Kathryn R, Ayscough
Publikováno v:
Traffic (Copenhagen, Denmark). 13(2)
Dynamins are a conserved family of proteins involved in many membrane fusion and fission events. Previously, the dynamin-related protein Vps1 was shown to localize to endocytic sites, and yeast carrying deletions for genes encoding both the BAR domai
Autor:
Urbanek, Agnieszka N.1, Allwood, Ellen G.1, Smith, Adam P.1, Booth, Wesley I.1, Ayscough, Kathryn R.1 k.ayscough@sheffield.ac.uk
Publikováno v:
PLoS ONE. 8/27/2015, Vol. 10 Issue 8, p1-19. 19p.