Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Oleg Iourin"'
Publikováno v:
Cell Reports, Vol 3, Iss 1, Pp 30-35 (2013)
Enveloped viruses have developed various adroit mechanisms to invade their host cells. This process requires one or more viral envelope glycoprotein to achieve cell attachment and membrane fusion. Members of the Flaviviridae such as flaviviruses poss
Externí odkaz:
https://doaj.org/article/653c8ce7bc0c4c0fa7600eaad588a642
Publikováno v:
Cell Reports, Vol 3, Iss 1, Pp 30-35 (2013)
Cell Reports
Cell Reports
Summary Enveloped viruses have developed various adroit mechanisms to invade their host cells. This process requires one or more viral envelope glycoprotein to achieve cell attachment and membrane fusion. Members of the Flaviviridae such as flaviviru
Autor:
David I. Stuart, Karl Harlos, Andrew Palmer, Jan Kadlec, Jonathan M. Grimes, Ian M. Jones, Carole J. Thomas, Kamel El Omari, W. Lu, Christoph Meier, Joe Brownlie, Munir Iqbal, Oleg Iourin
Bovine viral diarrhoea virus (BVDV) is an economically important animal pathogen which is closely related to Hepatitis C virus. Of the structural proteins, the envelope glycoprotein E2 of BVDV is the major antigen which induces neutralizing antibodie
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::26dfb490d9e9e449fc06a76ab6890388
https://ora.ox.ac.uk/objects/uuid:aebf3e14-c613-4bd9-9abd-5dca5b4e5d8a
https://ora.ox.ac.uk/objects/uuid:aebf3e14-c613-4bd9-9abd-5dca5b4e5d8a
The Gag polyprotein is key to the budding of retroviruses from host cells and is cleaved upon virion maturation, the N-terminal membrane-binding domain forming the matrix protein (MA). The 2.8-Å resolution crystal structure of MA of equine infectio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0de042ca40d143524a461931a6e91127
https://ora.ox.ac.uk/objects/uuid:8d6ee370-d030-4dc9-b9a3-c9105549af75
https://ora.ox.ac.uk/objects/uuid:8d6ee370-d030-4dc9-b9a3-c9105549af75
Autor:
David I. Stuart, Zihe Rao, Oleg Iourin, Elizabeth E. Fry, Alan J. Kingsman, Karl Harlos, Nico Riffel
Publikováno v:
Structure. 10(12):1627-1636
Matrix proteins associated with the viral membrane are important in the formation of the viral particle and in virus maturation. The 1.0 Å crystal structure of the ecotropic Gammaretrovirus Moloney murine leukemia virus (M-MuLV) matrix protein revea
Autor:
Alan J. Kingsman, Susan M. Kingsman, Carmen Sieiro-Vazquez, Catherine S. Adamson, Elaine D. Byles, Ekaterini Kotsopoulou, Stuart A. Wilson, Oleg Iourin, Nick J. Edwards, Enca Martin-Rendon
Publikováno v:
Biochemical Journal. 342:97-103
The cDNA for a human homologue (hIF2) of bacterial (bIF2) and yeast (yIF2) translation initiation factor two (IF2) has been identified during a screen for proteins which interact with HIV-1 matrix. The hIF2 cDNA encodes a 1220-amino-acid protein with
Autor:
Raymond A. Dwek, Oleg Iourin, Pauline M. Rudd, Nasi Mian, Geoffrey Keir, Bryan Winchester, Taj S. Mattu
Publikováno v:
Glycoconjugate Journal. 13:1031-1042
One of the biochemical characteristics of carbohydrate deficient glycoprotein syndromes is the presence of abnormal glycoforms in serum transferrin. Both glycoform heterogeneity and variable site occupancy may, in principle, lead to the generation of
Autor:
Kamel El Omari, Karl Harlos, Geoff Sutton, Jonathan M. Grimes, Dave Stuart, David Hall, R. Fearn, Oleg Iourin, Jan Kadlec
Publikováno v:
Acta Crystallographica Section A Foundations and Advances. 70:C1803-C1803
Single-wavelength anomalous dispersion of sulfur atoms (S-SAD) is an elegant phasing method to determine crystal structures that does not require heavy atom incorporation or selenomethionine derivatization. Nevertheless this technique has been limite
Autor:
Stephen Matthews, Paula M. Cannon, Elaine D. Byles, A J Kingsman, David J. Hockley, Nigel Clark, Oleg Iourin, Susan M. Kingsman
Publikováno v:
Scopus-Elsevier
The human immunodeficiency virus type 1 (HIV-1) matrix protein, p17, plays important roles in both the early and late stages of the viral life cycle. Using our previously determined solution structure of p17, we have undertaken a rational mutagenesis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::429136e1425f84082b744126d418ea0d
http://www.scopus.com/inward/record.url?eid=2-s2.0-0030901738&partnerID=MN8TOARS
http://www.scopus.com/inward/record.url?eid=2-s2.0-0030901738&partnerID=MN8TOARS