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pro vyhledávání: '"Craig N. Lumb"'
Autor:
Craig N Lumb, Mark S P Sansom
Publikováno v:
PLoS Computational Biology, Vol 8, Iss 7, p e1002617 (2012)
Interactions between protein domains and lipid molecules play key roles in controlling cell membrane signalling and trafficking. The pleckstrin homology (PH) domain is one of the most widespread, binding specifically to phosphatidylinositol phosphate
Externí odkaz:
https://doaj.org/article/6594a0ba60cf4c2fa6b11c655614e9d2
Autor:
Judith P. Armitage, Claudio Silvestrin, Boguslaw Obara, Mostyn T. Brown, Bradley C. Steel, Nicolas J. Delalez, Richard M. Berry, David A. Wilkinson, Craig N. Lumb
Swimming Escherichia coli cells are propelled by the rotary motion of their flagellar filaments. In the normal swimming pattern, filaments positioned randomly over the cell form a bundle at the posterior pole. It has long been assumed that the hook f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::595d5ab51740f2fac0866a924c1056e8
https://doi.org/10.1128/jb.00209-12
https://doi.org/10.1128/jb.00209-12
Autor:
Louise E. Bird, Robert J.C. Gilbert, Luke A. Yates, David A. Calderwood, Nina N. Brahme, Ruta Zalyte, Craig N. Lumb, Raymond J. Owens, Luigi De Colibus, Mark S.P. Sansom
Publikováno v:
The Journal of Biological Chemistry
Background: Kindlins are essential co-activators with talin of integrins. Results: Kindlin-1 PH domain is necessary for integrin activation and has low affinity for PtdInsP species partly determined by a salt bridge across its binding pocket. Conclus
Finding a Needle in a Haystack: The Role of Electrostatics in Target Lipid Recognition by PH Domains
Autor:
Mark S.P. Sansom, Craig N. Lumb
Publikováno v:
PLoS Computational Biology
PLoS Computational Biology, Vol 8, Iss 7, p e1002617 (2012)
PLoS Computational Biology, Vol 8, Iss 7, p e1002617 (2012)
Interactions between protein domains and lipid molecules play key roles in controlling cell membrane signalling and trafficking. The pleckstrin homology (PH) domain is one of the most widespread, binding specifically to phosphatidylinositol phosphate
Biophysical and computational studies of membrane penetration by the GRP1 pleckstrin homology domain
Autor:
Craig N. Lumb, Robert V. Stahelin, Ju He, Mark S.P. Sansom, Yi Xue, Phillip J. Stansfeld, Tatiana G. Kutateladze
Publikováno v:
Structure(London, England:1993)
Summary The pleckstrin homology (PH) domain of the general receptor for phosphoinositides 1 (GRP1) exhibits specific, high-affinity, reversible binding to phosphatidylinositol (3,4,5)-trisphosphate (PI(3,4,5)P3) at the plasma membrane, but the nature
Autor:
Mark S.P. Sansom, Craig N. Lumb
Publikováno v:
Biophysical Journal. 102:19a
PTEN is a tumour-suppressor protein responsible for regulating the phosphatidylinositol 3-kinase (PI3K) signalling pathway. The action of PI3K generates PI(3,4,5)P3, which goes on to promote several downstream processes such as cell proliferation and
Publikováno v:
The Journal of Chemical Physics. 130:114507
We report the results of extensive molecular dynamics simulations of a simple, but experimentally achievable model of dipolar colloids. It is shown that a modest elongation of the particles and dipoles to make dipolar dumbbells favors branching of th
Publikováno v:
Biophysical Journal. (3):88a-89a
Successful recruitment of peripheral proteins to the cytoplasmic leaflet of the cell membrane is an essential step in several cell signaling pathways, and robust membrane attachment is often achieved via a modular membrane-binding domain. The general
Autor:
Phillip J. Stansfeld, Daniel L. Parton, Antreas C. Kalli, Gareth J. Morgan, Mark S.P. Sansom, Craig N. Lumb
Publikováno v:
Biophysical Journal. (3):7a
Signalling across, within, and at the cytoplasmic surface of cell membranes is central to the regulation of many processes in mammalian cells, ranging from development and maintenance of tissues to immune responses. Multiscale molecular simulations m