Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Edward R. Jack"'
Autor:
David A. Middleton, Photini Sinnis, Bridie A. Kelly, Curtis B. Dobson, Stuart J. D. Neil, Edward R. Jack, Joana M. Santos, Áine McKnight
Publikováno v:
FEBS Journal. 274:4511-4525
Host-derived anti-infective proteins represent an important source of sequences for designing antimicrobial peptides (AMPs). However such sequences are often long and comprise diverse amino acids with uncertain contribution to biological effects. Pre
Autor:
Peter G. Stockley, Louise C. Serpell, David A. Middleton, Sheena E. Radford, Jillian Madine, Edward R. Jack
Publikováno v:
Journal of the American Chemical Society. 130(45)
Many unrelated proteins and peptides can assemble into amyloid or amyloid-like nanostructures, all of which share the cross-beta motif of repeat arrays of beta-strands hydrogen-bonded along the fibril axis. Yet, paradoxically, structurally polymorphi
Publikováno v:
Molecular membrane biology. 25(1)
Rho GTPases are a multifunctional family of proteins that are localized at cellular membranes via an isoprenyl group covalently linked to a C-terminal cysteine. Close to this primary site of membrane anchoring there is often found an additional polyb
Autor:
Bridie A, Kelly, Stuart J, Neil, Aine, McKnight, Joana M, Santos, Photini, Sinnis, Edward R, Jack, David A, Middleton, Curtis B, Dobson
Publikováno v:
The FEBS journal. 274(17)
Host-derived anti-infective proteins represent an important source of sequences for designing antimicrobial peptides (AMPs). However such sequences are often long and comprise diverse amino acids with uncertain contribution to biological effects. Pre
Publikováno v:
Journal of the American Chemical Society. 128(25)
Some 25 diseases are associated with proteins and peptides that assemble into amyloid fibrils composed of beta-strands connected by hydrogen bonds oriented parallel to the fiber long axis. There is mounting evidence that amyloid formation involves sp