F
Felicity Alcock
Researcher at University of Oxford
Publications - 25
Citations - 749
Felicity Alcock is an academic researcher from University of Oxford. The author has contributed to research in topics: Twin-arginine translocation pathway & Translocase. The author has an hindex of 15, co-authored 22 publications receiving 649 citations. Previous affiliations of Felicity Alcock include University of Manchester & Newcastle University.
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Journal ArticleDOI
Conserved Motifs Reveal Details of Ancestry and Structure in the Small TIM Chaperones of the Mitochondrial Intermembrane Space
Ian E Gentle,Andrew J. Perry,Felicity Alcock,Vladimir A Likic,Pavel Dolezal,Ee Ting Ng,Anthony W. Purcell,Malcolm McConnville,Thomas Naderer,Anne-Laure Chanez,Fabien Charrière,Caroline Aschinger,André Schneider,Kostas Tokatlidis,Kostas Tokatlidis,Trevor Lithgow +15 more
TL;DR: It is shown that no "Tim12" family of proteins exist, but rather that variant forms of the cognate small TIMs have been recently duplicated and modified to provide new functions: the yeast Tim12 is a modified form of Tim10, whereas in humans and some protists variant formsof Tim9, Tim8, and Tim13 are found instead.
Journal ArticleDOI
Live cell imaging shows reversible assembly of the TatA component of the twin-arginine protein transport system
Felicity Alcock,Matthew A. B. Baker,Nicholas P. Greene,Tracy Palmer,Mark I. Wallace,Ben C. Berks +5 more
TL;DR: Direct imaging of fluorescent protein-tagged Tat components in bacterial cells is used to show that the TatA element of the Tat system undergoes substrate- and proton motive force-dependent oligomerization, suggesting that TatA assembly reaches a critical point at which oligomersization can be reversed only by substrate transport.
Journal ArticleDOI
Minor modifications and major adaptations: The evolution of molecular machines driving mitochondrial protein import ☆
TL;DR: Comparative analysis of these systems is revealing both possible routes for the evolution of the mitochondrial membrane translocases and a greater understanding of the mechanisms behind mitochondrial protein import.
Journal ArticleDOI
The Structural Basis of the TIM10 Chaperone Assembly
Hui Lu,Alexander P. Golovanov,Felicity Alcock,J. Günter Grossmann,Scott P. Allen,Lu-Yun Lian,Kostas Tokatlidis,Kostas Tokatlidis +7 more
TL;DR: NMR data here demonstrates unequivocally that only the oxidized states of the Tim9 and Tim10 proteins are capable of forming a complex and provides an explanation for the escorting function of this non-ATP-powered chaperone particle.
Journal ArticleDOI
Assembling the Tat protein translocase
Felicity Alcock,Phillip J. Stansfeld,Hajra Basit,Johann Habersetzer,Matthew A. B. Baker,Tracy Palmer,Mark I. Wallace,Ben C. Berks +7 more
TL;DR: This work combines sequence co-evolution analysis, molecular simulations, and experimentation to define the interactions between the Tat proteins of Escherichia coli at molecular-level resolution and finds that TatA also associates with TatC at the polar cluster site.