Conformational Flexibility in the Immunoglobulin-Like Domain of the Hepatitis C Virus Glycoprotein E2

Autor: Ieva Vasiliauskaite, Ania Owsianka, Patrick England, Abdul Ghafoor Khan, Sarah Cole, Dorothea Bankwitz, Steven K. H. Foung, Thomas Pietschmann, Joseph Marcotrigiano, Felix A. Rey, Arvind H. Patel, Thomas Krey

Publikováno v: mBio, Vol 8, Iss 3 (2017)

ABSTRACT The hepatitis C virus (HCV) glycoprotein E2 is the major target of neutralizing antibodies and is therefore highly relevant for vaccine design. Its structure features a central immunoglobulin (Ig)-like β-sandwich that contributes to the bin

Externí odkaz: https://doaj.org/article/a3bea6c8045c419198f363ad02f506f7

Structure of a human intramembrane ceramidase explains enzymatic dysfunction found in leukodystrophy

Autor: Christoph Arenz, Thierry Waltrich Augusto, François Hoh, Shibom Basu, Claire M. Grison, Essa M. Saied, Sébastien Granier, Mathieu Fortier, Pascal Rochaix, Remy Sounier, Robert D. Healey, Ieva Vasiliauskaite Brooks, Cedric Leyrat

Alkaline ceramidases (ACERs) are a class of poorly understood transmembrane enzymes controlling the homeostasis of ceramides. They are implicated in human pathophysiology, including progressive leukodystrophy, colon cancer as well as acute myeloid le

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::533e51d2f04bb9c6e74a1b24fec63f86

Conformational flexibility in the immunoglobulin-like domain of the Hepatitis C Virus Glycoprotein E2

Autor: Dorothea Bankwitz, Steven K. H. Foung, Ieva Vasiliauskaite, Arvind H. Patel, Thomas Krey, Joseph Marcotrigiano, Sarah Cole, Patrick England, Félix A. Rey, Ania M. Owsianka, Thomas Pietschmann, Abdul Ghafoor Khan

Publikováno v: mBio
mBio, Vol 8, Iss 3 (2017)
mBio, 2017, 8 (3), pp.e00382-17. ⟨10.1128/mBio.00382⟩
mBio, Vol 8, Iss 3, p e00382-17 (2017)

The hepatitis C virus (HCV) glycoprotein E2 is the major target of neutralizing antibodies and is therefore highly relevant for vaccine design. Its structure features a central immunoglobulin (Ig)-like β-sandwich that contributes to the binding site

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46115abb57c9817644e9aa1c663e240b
https://eprints.gla.ac.uk/140242/1/140242.pdf

Wound occlusion and decay in Picea abies stems

Autor: Rimvydas Vasaitis, Albertas Vasiliauskas, Ieva Vasiliauskaite, Vaidotas Lygis

Publikováno v: European Journal of Forest Research. 131:1211-1216

In forest stands, Picea abies is commonly subjected to logging and bark stripping injuries. Most mechanical wounds do not exceed 300 cm2, but their pathological consequences are unclear. The aim of the study was to estimate the rate of wound occlusio

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::6a6c0be8a43a5a368a936c6c3efb60e2
https://doi.org/10.1007/s10342-011-0592-3

Robust and low cost uniform (15)N-labeling of proteins expressed in Drosophila S2 cells and Spodoptera frugiperda Sf9 cells for NMR applications

Autor: Félix A. Rey, Thomas Krey, Julia Chamot-Rooke, Christian Malosse, Célia Deville, Christine Girard-Blanc, Pablo Guardado-Calvo, Eric Guittet, François Bontems, Ieva Vasiliauskaite, Scott A. Jeffers, Stéphane Petres, Christina Sizun, Annalisa Meola, Carine van Heijenoort

Publikováno v: Journal of Structural Biology
Journal of Structural Biology, Elsevier, 2014, 188 (1), pp.71-78. ⟨10.1016/j.jsb.2014.08.002⟩
Journal of Structural Biology, 2014, 188 (1), pp.71-78. ⟨10.1016/j.jsb.2014.08.002⟩

International audience; Nuclear magnetic resonance spectroscopy is a powerful tool to study structural and functional properties of proteins, provided that they can be enriched in stable isotopes such as (15)N, (13)C and (2)H. This is usually easy an

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::61c35b59588d92465841fd7af2ae02cf
https://hal.archives-ouvertes.fr/hal-01077147