| 1. |
- Dimov, Stefan S., et al.
(author)
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4M Network of Excellence : Progress Report 2004-2006
- 2007
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In: 4M 2007. - Dunbeath : Whittles Publishing. - 9781904445531 - 9781420070040 ; , s. xvii-xxxi
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Conference paper (peer-reviewed)abstract
- The 4M Network of Excellence started on 1st October 2004. It is a consortium of 30 academic and research organisations that came together to form the network under the European Commission's 6th Framework Research Programme. The Network has developed a knowledge community in Micro- and Nano- Technology (MNT) for the batch-manufacture of microcomponents and devices in a variety of materials for future microsystems products, particularly in non-silicon materials. This paper gives an overview of the structure, operation and activity of the network since its inception, illustrating the network's progress towards its goals.
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| 2. |
- Dimov, Stefan S., et al.
(author)
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4M Network of Excellence, Progress Report 2006-2008
- 2008
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In: 4M 2008. - Dunbeath : Whittles Publishing. - 9781904445760 ; , s. xv-xxxi
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Conference paper (peer-reviewed)abstract
- This report follows on from last year's "Progress Report 2004-2006" and gives an update on the continuing activities, such as the 4M Network cross-divisional projects and annual conference, as well as a description of the new activities in its third and forth year, such as the first 4M Summer School and Book Series. Finally, as the end of the funded lifetime of the network approaches the steps being taken to set up a 4M Association, which aims to create the organizational infrastructure to support the 4M Knowledge Community established in the last five years, are described.
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| 3. |
- Dimov, Stefan S., et al.
(author)
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4M Network of Excellence, Progress report 2009
- 2009
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In: 4M/ICOMM 2009. ; , s. s.1-9
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Conference paper (peer-reviewed)abstract
- This paper gives a brief overview of the activities of the 4M Network of Excellence during the last nine months of its funded period. The 4M Divisions summarise their activity and outline their plans to continue to working together in future. Finally a summary of achievements during the whole lifetime of the Network is given
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| 4. |
- Lundbäck, Anna-Karin, et al.
(author)
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Assembly of Kch, a putative potassium channel from Escherichia coli
- 2009
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In: Journal of Structural Biology. - : Elsevier BV. - 1047-8477 .- 1095-8657. ; 168:2, s. 288-293
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Journal article (peer-reviewed)abstract
- Attempts to explore the structure and function of Kch, a putative potassium channel of Escherichia coli have yielded varying results; potassium-associated functions have been found in vivo but not in vitro. Here the kch gene is shown to produce two proteins, full-length Kch and the large C-terminal cytosolic domain (the RCK domain). Further, these two proteins are associated at the initial stages of purification. Previous structural studies of full-length Kch claim that the isolated protein forms large aggregates that are not suitable for analysis. The results presented here show that the purified protein sample, although heterogeneous, has one major population with a mass of about 400 kDa, implying the presence of two Kch tetramers in a complex form. A three dimensional reconstruction at 25 angstrom based on electron microscopy data from negatively stained particles, revealed a 210 angstrom long and 95 angstrom wide complex in which the two tetrameric Kch units are linked by their RCK domains, giving rise to a large central ring of density. The formation of this dimer of tetramers on expression or during purification, may explain why attempts to reconstitute Kch into liposomes for activity measurements have failed.
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| 5. |
- Scolari, Silvia, et al.
(author)
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Lateral distribution of the transmembrane domain of influenza virus hemagglutinin revealed by time-resolved fluorescence imaging.
- 2009
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In: Journal of Biological Chemistry. - 0021-9258 .- 1083-351X. ; 284:23, s. 15708-16
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Journal article (peer-reviewed)abstract
- Influenza virus hemagglutinin (HA) has been suggested to be enriched in liquid-ordered lipid domains named rafts, which represent an important step in virus assembly. We employed Förster resonance energy transfer (FRET) via fluorescence lifetime imaging microscopy to study the interaction of the cytoplasmic and transmembrane domain (TMD) of HA with agly co sylphos pha tidyl ino si tol (GPI)-anchored peptide, an established marker for rafts in the exoplasmic leaflet of living mammalian plasma membranes. Cyan fluorescent protein (CFP) was fused to GPI, whereas the HA sequence was tagged with yellow fluorescent protein (YFP) on its exoplasmic site (TMD-HA-YFP), avoiding any interference of fluorescent proteins with the proposed role of the cytoplasmic domain in lateral organization of HA. Constructs were expressed in Chinese hamster ovary cells (CHO-K1) for which cholesterol-sensitive lipid nanodomains and their dimension in the plasma membrane have been described (Sharma, P., Varma, R., Sarasij, R. C., Ira, Gousset, K., Krishnamoorthy, G., Rao, M., and Mayor, S. (2004) Cell 116, 577-589). Upon transfection in CHO-K1 cells, TMD-HA-YFP is partially expressed as a dimer. Only dimers are targeted to the plasma membrane. Clustering of TMD-HA-YFP with GPI-CFP was observed and shown to be reduced upon cholesterol depletion, a treatment known to disrupt rafts. No indication for association of TMD-HA-YFP with GPI-CFP was found when palmitoylation, an important determinant of raft targeting, was suppressed. Clustering of TMD-HA-YFP and GPI-CFP was also observed in purified plasma membrane suspensions by homoFRET. We concluded that the pal mit oy lated TMD-HA alone is sufficient to recruit HA to cholesterol-sensitive nanodomains. The corresponding construct of the spike protein E2 of Semliki Forest virus did not partition preferentially in such domains.
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