Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Friederike Fessl"'
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
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
Publikováno v:
Virology. 204(2)
The 2A proteinase of human rhinovirus (HRV) 2 is a cysteine proteinase which is not inhibited by metal chelating agents. However, total hydrolysis of highly purified HRV2 2A followed by atom emission spectroscopy demonstrated that HRV2 2A contains I
Autor:
Wolfgang Sommergruber, Friederike Fessl, Hans-Dieter Liebig, H. Ahorn, Joachim Seipelt, H. Klump, Ernst Kuechler, E. Krystek, A. Zoephel, Dieter Blaas, Tim Skern
Publikováno v:
Virology. 198(2)
The cleavage specificities of the 2A proteinases from coxsackievirus B4 (CVB4) and human rhinovirus 2 (HRV2) on oligopeptide substrates have been determined. Comparison of the specificity of CVB4 2A proteinase with that of HRV2 2A proteinase allowed
Autor:
Manfred Zorn, Ernst Kuechler, Wolfgang Sommergruber, Hans-Dieter Liebig, Dieter Blaas, Friederike Fessl, Herbert Auer, Tim Skern, Peter Volkmann
Publikováno v:
Virology. 181(1)
The genetic information contained within the RNA genome of picornaviruses is expressed as a single large open reading frame; processing of the primary translation product begins while translation is still in progress. In rhinoviruses and enteroviruse
Publikováno v:
European Journal of Biochemistry. 122:199-203
A cell-free protein-synthesizing system has been prepared from Saccharomyces cerevisiae by mechanical breakage of cells, isolation of a 30000 x g supernatant fraction and removal of endogenous mRNA by treatment with micrococcal nuclease. The system t
Publikováno v:
Hoppe-Seyler´s Zeitschrift für physiologische Chemie. 357:961-970
The subcellular distribution of catalase A in the yeast Saccharomyces cerevisiae has been investigated. The enzyme was found to be bound to large particles, whereas most of the activity of catalase T was located in a 38 000 X g supernatant. Under var
Autor:
Manfred Zorn, Ingrid Maurer-Fogy, Peter Pallai, Wolfgang Sommergruber, Peter Volkmann, Vincent J. Merluzzi, Martha Matteo, Friederike Fessl, Tim Skern, Ernst Kuechler, Dieter Blaas
Publikováno v:
Virology. 169(1)
Evidence is presented that the protein 2A of human rhinovirus serotype 2 (HRV2) is a protease. On expression of the VP1-2A region of HRV2 in bacteria, protein 2A was capable of acting on its own N-terminus; derived extracts specifically cleaved a 16
Isolation of the catalase A gene of Saccharomyces cerevisiae by complementation of the cta1 mutation
Publikováno v:
Moleculargeneral genetics : MGG. 200(1)
As a first step in an analysis of the DNA regions involved in the control of the catalase A gene of Saccharomyces cerevisiae by glucose, heme, and oxygen this gene has been cloned. Catalase A-deficient mutants were obtained by UV mutagenesis of a ctt