Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Beatrix Kuen"'
Publikováno v:
Archives of Microbiology. 174:97-103
Cell surface (S)-layer protein synthesis in Bacillus stearothermophilus PV72/p6 is blocked when cells are grown at elevated temperature. From a culture exhibiting the S-layer-negative phenotype, the S-layer deficient mutant T5 (SbsA-) was isolated. G
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78e0a8238b41f6ca53adc5c66f58ea42
https://doi.org/10.1007/s002030000181
https://doi.org/10.1007/s002030000181
Autor:
Beatrix Kuen, W. Haidinger, M. Kamal, Angela Witte, Peter Mayrhofer, H. Mader, Sonja Lechleitner, Stephanie Resch, Diana Felnerova, Wolfgang Jechlinger, Michael P. Szostak, B. Mayr, N. Stralis-Alves, Veronika Huter, Francis O. Eko, Andreas Hensel, Edith Brand, H. Melzer, Alexander G. Haslberger, J. Marchart, R. Geretschläger, Werner Lubitz
Publikováno v:
Journal of Biotechnology. 73:261-273
Controlled expression of cloned PhiX174 gene E in Gram-negative bacteria results in lysis of the bacteria by formation of an E-specific transmembrane tunnel structure built through the cell envelope complex. Bacterial ghosts from a variety of bacteri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df5d96fd3b6d72ea168bcfb5557b5e33
https://doi.org/10.1016/s0168-1656(99)00144-3
https://doi.org/10.1016/s0168-1656(99)00144-3
Autor:
S. Fürst-Ladani, Andreas Hensel, A. Katinger, W. Haidinger, Edith Brand, Alexander G. Haslberger, Veronika Huter, Werner Lubitz, Wolfgang Jechlinger, Stephanie Resch, Beatrix Kuen, Angela Witte, Michael P. Szostak, Francis O. Eko, P. Raza, J. Marchart, H. Mader
Publikováno v:
Vaccine. 17:1643-1649
Controlled expression of cloned PhiX174 gene E in Gram-negative bacteria results in lysis of the bacteria by formation of an E-specific transmembrane tunnel structure built through the cell envelope complex. Bacterial ghosts have been produced from a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d895e3703c6c83725ec4e0349df2b49a
https://doi.org/10.1016/s0264-410x(98)00423-x
https://doi.org/10.1016/s0264-410x(98)00423-x
Autor:
Holger Scholz, Michèle Mock, Werner Lubitz, Stephan Howorka, Thaddée Gulik-Krzywicki, Hein J. Boot, José Berenguer, Peter H. Pouwels, Beatrix Kuen, Alberto J.L. Macario, Sonja Lechleitner, Carin P. A. M. Kolen, Stéphane Mesnage, Luis Angel Fernández-Herrero, Airi Palva, Gerhard Schroll, Nicolas Bayan, Martin J. Blaser, Margit Sára, Agnès Fouet, Gérard Leblon, Mohamed Chami, Stephanie Resch, Evelyne Tosi-Couture, G Olabarría, Michaela Truppe, Hubert Bahl, Everly Conway de Macario, Pierre Gounon, Emanuel Shechter
Publikováno v:
FEMS Microbiology Reviews. 20:47-98
In this chapter we report on the molecular biology of crystalline surface layers of different bacterial groups. The limited information indicates that there are many variations on a common theme. Sequence variety, antigenic diversity, gene expression
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::305b66e60c62c360dae566ebc547e1a3
https://doi.org/10.1111/j.1574-6976.1997.tb00304.x
https://doi.org/10.1111/j.1574-6976.1997.tb00304.x
Publikováno v:
Journal of Bacteriology. 179:1664-1670
S-layer protein variation from a hexagonally ordered (SbsA; 130 kDa) to a obliquely ordered (SbsB; 98 kDa) protein in Bacillus stearothermophilus PV72 is mediated by an increased oxygen supply. To elucidate the molecular basis of S-layer protein vari
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9accb82001d9fcea983e2fc108d14c15
https://doi.org/10.1128/jb.179.5.1664-1670.1997
https://doi.org/10.1128/jb.179.5.1664-1670.1997
Publikováno v:
Journal of Bacteriology. 178:2108-2117
Stable synthesis of the hexagonally ordered (p6) S-layer protein from the wild-type strain of Bacillus stearothermophilus PV72 could be achieved in continuous culture on complex medium only under oxygen-limited conditions when glucose was used as the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d38181128179566ee908156ec5cf1cd
https://doi.org/10.1128/jb.178.7.2108-2117.1996
https://doi.org/10.1128/jb.178.7.2108-2117.1996
Autor:
Athanasios Makristathis, Jutta Burghardt, Hans-Jürgen Busse, Friedrich Hollaus, Andrea Scheberl, Katharina Meier-Stauffer, Uwe B. Sleytr, Frederick A. Rainey, Beatrix Kuen, Paul Messner
Publikováno v:
International Journal of Systematic Bacteriology. 46:532-541
Isolates of thermophilic bacteria obtained from an Austrian beet sugar factory were screened by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and freeze-fracture electron microscopy for the presence of glycosylated crystalline
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::21d41192a2ce251cae6e35a304a05485
https://doi.org/10.1099/00207713-46-2-532
https://doi.org/10.1099/00207713-46-2-532
Publikováno v:
Journal of bacteriology. 183(5)
Bacillus stearothermophilus PV72 expresses different S-layer genes ( sbsA and sbsB ) under different growth conditions. No stretches of significant sequence identity between sbsA and sbsB were detected. In order to investigate S-layer gene regulation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f0e689c677fa5677b1c7085abc5e6a1b
https://pubmed.ncbi.nlm.nih.gov/11160098
https://pubmed.ncbi.nlm.nih.gov/11160098
Autor:
Werner Lubitz, Yunjuan Wang, Stefan Howorka, Beatrix Kuen, Uwe B. Sleytr, Hagan Bayley, Margit Sára
Publikováno v:
The Journal of biological chemistry. 275(48)
The S-layer protein SbsB of the thermophilic, Gram-positive organism Bacillus stearothermophilus PV72/p2 forms a crystalline, porous array constituting the outermost component of the cell envelope. SbsB has a molecular mass of 98 kDa, and the corresp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8aa0d0ea7f5d88a3808a80d7a62fcd36
https://pubmed.ncbi.nlm.nih.gov/10969072
https://pubmed.ncbi.nlm.nih.gov/10969072
Publikováno v:
FEMS microbiology letters. 172(2)
In order to achieve high level expression and to study the release of a protein capable of self-assembly, the gene encoding the crystalline cell surface (S-layer) protein SbsA of Bacillus stearothermophilus PV72/p6, including its signal sequence, was
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3c8059d9890c56023895a90c5fa085d
https://pubmed.ncbi.nlm.nih.gov/10188248
https://pubmed.ncbi.nlm.nih.gov/10188248