Zobrazeno 1 - 10
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pro vyhledávání: '"Hans-Dieter Liebig"'
Autor:
Nicola J. Baxter, Svetlana E. Sedelnikova, Jonathan P. Waltho, Andreas Roetzer, Tim Skern, Andrea M. Hounslow, Hans-Dieter Liebig
Publikováno v:
Journal of Virology. 80:1451-1462
The 2A proteinases (2A pro ) from the picornavirus family are multifunctional cysteine proteinases that perform essential roles during viral replication, involving viral polyprotein self-processing and shutting down host cell protein synthesis throug
This chapter discusses the strategy used by picornaviruses belonging to the genera of enteroviruses, rhinoviruses, and aphthoviruses to interfere with host cell protein synthesis. First it describes the mechanism of initiation of capped mRNA and comp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b1c2a76e5a7f0a450c4d7f26a38fd0f0
https://doi.org/10.1128/9781555817916.ch24
https://doi.org/10.1128/9781555817916.ch24
Autor:
Jens Petersen, Michael N.G. James, Hans-Dieter Liebig, Tim Skern, Ernst Kuechler, Maia M. Cherney
Publikováno v:
The EMBO Journal. 18:5463-5475
The crystal structure of the 2A proteinase from human rhinovirus serotype 2 (HRV2-2A(pro)) has been solved to 1.95 A resolution. The structure has an unusual, although chymotrypsin-related, fold comprising a unique four-stranded beta sheet as the N-t
Autor:
Friederike Fessl, G. Casari, Wolfgang Sommergruber, Hans-Dieter Liebig, Tim Skern, J. Seipelt
Publikováno v:
Virology. 234:203-214
The proteinase 2A of human rhinovirus 2 is a cysteine proteinase which contains a tightly bound Zn ion thought to be required for structural integrity. A three-dimensional model for human rhinovirus type 2 proteinase 2A (HRV2 2A) was established usin
Publikováno v:
Virology. 220:109-118
During the replication of rhino- and enteroviruses, the translation initiation factor elF-4 gamma is specifically cleaved by the virally encoded 2 A proteinase. This cleavage has been proposed to lead to the inability of the host cell to translate it
Autor:
Andrew M. Borman, E Ziegler, F G Deliat, Hans-Dieter Liebig, Tim Skern, Katherine M. Kean, Ernst Kuechler, D Jugovic
Publikováno v:
Virology. 213:549-557
Poliovirus and human rhinovirus 2A proteinases are known to stimulate translation initiation on the cognate viral Internal Ribosome Entry Segments (IRESes). The molecular mechanism of this translational transactivation was investigated in vitro using
Autor:
Hans Dieter Liebig, Fang Yang, Barry J. Lamphear, Hannes Klump, Robert E. Rhoads, Riqiang Yan, Tim Skern, Debra A. Waters, Ernst Kuechler
Publikováno v:
Journal of Biological Chemistry. 268:19200-19203
The rate-limiting step of eukaryotic protein synthesis is the binding of mRNA to the 40 S ribosomal subunit, a step which is catalyzed by initiation factors of the eIF-4 (eukaryotic initiation factor 4) group: eIF-4A, eIF-4B, eIF-4E, and eIF-4 gamma.
Autor:
Hartmuth K, Yan R, Sommergruber W, Dieter Blaas, E Ziegler, Kowalski H, Frasel L, Klump H, Hans-Dieter Liebig, Barry J. Lamphear
Publikováno v:
Biochemistry. 32:7581-7588
A mammalian cell infected with a human rhinovirus or enterovirus has a much reduced capability to translate capped mRNAs (the host cell shutoff), while still allowing translation of uncapped viral RNA. Biochemical and genetic evidence suggests that t
Autor:
Friederike Fessl, Dieter Blaas, Ingrid Maurer-Fogy, G Schnorrenberg, Ernst Kuechler, A Zöphel, Horst Ahorn, Wolfgang Sommergruber, Tim Skern, Hans-Dieter Liebig
Publikováno v:
Europe PubMed Central
Proteinase 2A of human rhinovirus serotype 2 (HRV2 2A) was expressed in Escherichia coli and partially purified; the preparation was used to study various enzymatic parameters. Using a 16-amino acid peptide representing the native cleavage region of
Autor:
M. Luderer, Dieter Blaas, Tim Skern, Ernst Kuechler, Wolfgang Sommergruber, Hans-Dieter Liebig
Publikováno v:
Proceedings of the National Academy of Sciences. 88:5979-5983
Many virally encoded proteinases cleave themselves out of a polyprotein, with cleavage occurring usually at their own N terminus. This property was used to develop an in vivo screening system using the lacZ gene fragment of M13mp18. When a fusion pro