Zobrazeno 1 - 10
of 96
pro vyhledávání: '"Gregor, Meyers"'
Autor:
Bjoern Petersen, Robert Kammerer, Antje Frenzel, Petra Hassel, Tung Huy Dau, Roswitha Becker, Angele Breithaupt, Reiner Georg Ulrich, Andrea Lucas-Hahn, Gregor Meyers
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-13 (2021)
Abstract The TRDC-locus encodes the T cell receptor delta constant region, one component of the γδ T cell receptor which is essential for development of γδ T cells. In contrast to peptide recognition by αβ T cells, antigens activating γδ T ce
Externí odkaz:
https://doaj.org/article/9fee6125b0b4471aa566d3bbc4915e51
Autor:
Jolene Carlson, Robert Kammerer, Jens Peter Teifke, Julia Sehl-Ewert, Christiane Pfarrer, Gregor Meyers
Publikováno v:
PLoS Pathogens, Vol 17, Iss 12 (2021)
In contrast to wild type bovine viral diarhea virus (BVDV) specific double deletion mutants are not able to establish persistent infection upon infection of a pregnant heifer. Our data shows that this finding results from a defect in transfer of the
Externí odkaz:
https://doaj.org/article/5c06ecf6839943109bd89f1d3b7e636b
Autor:
Manjula Mischler, Gregor Meyers
Publikováno v:
Viruses, Vol 13, Iss 11, p 2204 (2021)
The pestivirus classical swine fever virus (CSFV) represents one of the most important pathogens of swine. Its virulence is dependent on the RNase activity of the essential structural glycoprotein Erns that uses an amphipathic helix as a membrane anc
Externí odkaz:
https://doaj.org/article/1c8256f650444128b56cb0eebbd89c50
Publikováno v:
Viruses, Vol 13, Iss 7, p 1203 (2021)
Pestiviruses express the unique essential envelope protein Erns, which exhibits RNase activity, is attached to membranes by a long amphipathic helix, and is partially secreted from infected cells. The RNase activity of Erns is directly connected with
Externí odkaz:
https://doaj.org/article/b27858027f294e2097c30ce5cce661e0
Publikováno v:
Viruses, Vol 13, Iss 3, p 444 (2021)
The pestivirus envelope protein Erns is anchored in membranes via a long amphipathic helix. Despite the unusual membrane topology of the Erns membrane anchor, it is cleaved from the following glycoprotein E1 by cellular signal peptidase. This was pro
Externí odkaz:
https://doaj.org/article/c34258c9a318442caf3637c9337a7375
Publikováno v:
PLoS ONE, Vol 10, Iss 8, p e0135680 (2015)
Pestiviruses express a peculiar protein named Erns representing envelope glycoprotein and RNase, which is important for control of the innate immune response and persistent infection. The latter functions are connected with secretion of a certain amo
Externí odkaz:
https://doaj.org/article/9d8a377403ee48d9bfc4fdad9e9dfd34
Publikováno v:
Journal of Virology
Pestiviruses are members of the family Flaviviridae, a group of enveloped viruses that bud at intracellular membranes. Pestivirus particles contain three glycosylated envelope proteins, Erns, E1, and E2. Among them, E1 is the least characterized conc
Autor:
Roswitha Becker, Gregor Meyers, Angele Breithaupt, Reiner Ulrich, Petra Hassel, Bjoern Petersen, Antje Frenzel, Robert Kammerer, Andrea Lucas-Hahn, Tung Huy Dau
Publikováno v:
Scientific Reports
Scientific Reports, Vol 11, Iss 1, Pp 1-13 (2021)
Scientific Reports, Vol 11, Iss 1, Pp 1-13 (2021)
The TRDC-locus encodes the T cell receptor delta constant region, one component of the γδ T cell receptor which is essential for development of γδ T cells. In contrast to peptide recognition by αβ T cells, antigens activating γδ T cells are m
Publikováno v:
International Journal of Molecular Sciences
International Journal of Molecular Sciences, Vol 22, Iss 7285, p 7285 (2021)
Volume 22
Issue 14
International Journal of Molecular Sciences, Vol 22, Iss 7285, p 7285 (2021)
Volume 22
Issue 14
Pestiviruses contain three envelope proteins: Erns, E1, and E2. Expression of HA-tagged E1 or mutants thereof showed that E1 forms homodimers and -trimers. C123 and, to a lesser extent, C171, affected the oligomerization of E1 with a double mutant C1
Publikováno v:
Nucleic Acids Research
Caliciviruses use a termination/reinitiation mechanism for translation of their minor capsid protein VP2. A sequence element of about 80 nucleotides denoted ‘termination upstream ribosomal binding site’ (TURBS) is crucial for reinitiation. RNA se