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PI Research

Ajioka Research

 
Brierley Research

 
Coleman Research

 
Cooke Research

 
Crump Research 1

 
Crump Research 2

 
DAvino Research

 
Doorbar Research

Our past work has identified important changes in viral gene expression that underlie the development of HPV-associated cervical intraepithelial neoplasias (top left). A series of molecular studies that we have published in the Journal of Virology over the last few years has revealed how one of the viral proteins (E4) is post-transcriptionally modified to facilitate its deposition as amyloid-like fibrils (bottom left). An image of E4 staining in a patient biopsy of a cervical neoplasia prepared using a cross-reactive E4 antibody prepared in the lab is shown in the MRC Strategic Plan www.mrc.ac.uk/strategicplan to illustrate to potential of such research in the development of diagnostic strategies for disease stratification.

Du Research

 
Dunne Research

 
Edwards Research

 
Ferguson Research

 
Firth Research 2

 
Firth Research 1

 
Fraser Research

Flagella on the surface of the bacterial cell (inset top right, Salmonella cell membrane stained green and flagella stained red, visualized by epifluorescence microscopy) comprise three contiguous substructures - the basal body, hook and filament - that are assembled sequentially. A central channel runs through these substructures to the flagellum tip. The basal body houses the flagellar export machinery (A) and the rod (FliE, FlgB, FlgC, FlgF and FlgG), which extends from the inner membrane (IM) and crosses the periplasm, peptidoglycan (PG) cell wall and outer membrane (OM). The cell surface hook (FlgE) is a flexible universal joint that connects the external flagellum filament (flagellin, FliC) to the basal body. (A) Subunits of the rod, hook and filament link head-to-tail at the cytoplasmic membrane export machinery. Subunits are first unfolded by the export ATPase complex (red) and then dock at the FlhB export gate (orange). The N-terminal helix of the docked subunit is then captured by the free C-terminal helix of an exiting subunit in the flagellum channel. (B) Sequential subunits are linked head-to-tail in a chain by juxtaposed terminal helices forming parallel coiled-coils. The resulting chain of unfolded subunits is connected through the flagellum central channel to the distal tip of the flagellum. (C) The subunits in the chain transit from the gate to the tip. Subunits fold and incorporate into the flagellum tip beneath cap foldases (FlgJ for rod, FlgD for hook and FliD for filament subunit assembly). Subunit folding and/or crystallization not only provides a strong anchor at the flagellum tip, it also shortens the chain in the channel thus exerting a pulling force on the next subunit at the export gate, pulling it from the gate. The pulling force then drops rapidly as the new unfolded subunit enters the channel. This process repeats for each subunit captured into the chain.

Graham Research

 
Holmes Research

 
Hughes Research 2

 
Hughes Research 1

 
Humphreys Research

 
Kaufman Research

 
Kelly Research

 
Koronakis Research 4

 
Koronakis Research 1

 
Koronakis Research 5

 
Kouzarides Research

 
Laman Research

 
Moffett Research

 
Rawlins Research

 
Rudd Research

 
Smith Research

 
Sweeney

 
Trowsdale Research

Receptors in the Leukocyte Receptor Complex and some proposed ligands

Turner Research

 
Watson Research

 
Xuereb Research

 
Wilson Research

 
Fraser Research 2

 
Graham Research 2

 
Graham Research 2

 
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affara-epigentic-dna

 
affara-foetus

 
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