Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Anna-Liisa Hänninen"'
Autor:
Christopher P Landowski, Anne Huuskonen, Ramon Wahl, Ann Westerholm-Parvinen, Anne Kanerva, Anna-Liisa Hänninen, Noora Salovuori, Merja Penttilä, Jari Natunen, Christian Ostermeier, Bernhard Helk, Juhani Saarinen, Markku Saloheimo
Publikováno v:
PLoS ONE, Vol 10, Iss 8, p e0134723 (2015)
The filamentous fungus Trichoderma reesei has tremendous capability to secrete proteins. Therefore, it would be an excellent host for producing high levels of therapeutic proteins at low cost. Developing a filamentous fungus to produce sensitive ther
Externí odkaz:
https://doaj.org/article/ed9e1da5f3cc47a1ad32b7da38c7f35f
Autor:
Timo T. Myöhänen, Marjo Piltonen, O. Leskelä, P. Auvinen, Kari Alitalo, Anu Planken, Mart Saarma, Anna-Liisa Hänninen, Pekka T. Männistö, Jaan-Olle Andressoo
Publikováno v:
Neuroscience. 192:550-563
Neurotrophic factors regulate the development and maintenance of the nervous system and protect and repair dopaminergic neurons in animal models of Parkinson's disease (PD). Vascular endothelial growth factors A (VEGF-A) and B have also neurotrophic
Publikováno v:
Biotechnology Progress. 19:1368-1371
Heterologous glycoproteins usually do not fold properly in yeast cells and fail to leave the endoplasmic reticulum. Here we show that the Hsp150Delta polypeptide carrier promoted proper folding and secretion of the catalytic ectodomain of rat alpha2,
Autor:
Merja Penttilä, Juhani Saarinen, Christopher P. Landowski, Anne Kanerva, Jari Natunen, Bernhard Helk, Markku Saloheimo, Noora Salovuori, Christian Ostermeier, Ann Westerholm-Parvinen, Anna-Liisa Hänninen, Anne Huuskonen, Ramon Wahl
Publikováno v:
PLoS ONE, Vol 10, Iss 8, p e0134723 (2015)
PLoS ONE
Landowski, C P, Huuskonen, A, Wahl, R, Westerholm-Parvinen, A, Kanerva, A, Hänninen, A-L, Salovuori, N, Penttilä, M, Natunen, J, Ostermeier, C, Helk, B, Saarinen, J & Saloheimo, M 2015, ' Enabling low cost biopharmaceuticals : A systematic approach to delete proteases from a well-known protein production host trichoderma reesei ', PLoS ONE, vol. 10, no. 8, e0134723 . https://doi.org/10.1371/journal.pone.0134723
PLoS ONE
Landowski, C P, Huuskonen, A, Wahl, R, Westerholm-Parvinen, A, Kanerva, A, Hänninen, A-L, Salovuori, N, Penttilä, M, Natunen, J, Ostermeier, C, Helk, B, Saarinen, J & Saloheimo, M 2015, ' Enabling low cost biopharmaceuticals : A systematic approach to delete proteases from a well-known protein production host trichoderma reesei ', PLoS ONE, vol. 10, no. 8, e0134723 . https://doi.org/10.1371/journal.pone.0134723
The filamentous fungus Trichoderma reesei has tremendous capability to secrete proteins. Therefore, it would be an excellent host for producing high levels of therapeutic proteins at low cost. Developing a filamentous fungus to produce sensitive ther
Publikováno v:
Molecular Microbiology. 52:217-225
Thermal insult at 50 degrees C causes protein denaturation in yeast, but the cells survive if preconditioned at 37 degrees C. Survival depends on refolding of heat-denatured proteins. Refolding of cytoplasmic proteins requires Hsp104, the expression
Publikováno v:
Scopus-Elsevier
Severe heat stress causes protein denaturation in various cellular compartments. If Saccharomyces cerevisiae cells grown at 24 degrees C are preconditioned at 37 degrees C, proteins denatured by subsequent exposure to 48-50 degrees C can be renatured
Autor:
Javier Caldentey, Juha M. Holopainen, Jaana K. H. Bamford, Dennis H. Bamford, Paavo K.J. Kinnunen, Anna-Liisa Hänninen
Publikováno v:
European Journal of Biochemistry. 260:549-558
Assembly factors, proteins assisting the formation of viral structures, have been found in many viral systems. The gene encoding the assembly factor P17 of bacteriophage PRD1 has been cloned and expressed in Escherichia coli. P17 acts late in phage a
Publikováno v:
Virology. 227:207-210
Assembly of the broad-host-range bacteriophage PRD1 involves translocation of the virus-specific membrane to the inside of the icosahedral protein shell formed of trimeric coat proteins. The formation of PRD1 particles is, in addition to the virus-en
Publikováno v:
Virology. 227(1):198-206
Four new specificity class MAbs against PRD1 proteins (P6, P7/14, P11, P18) and polyclonal antiserum against the minor capsid protein P5 were produced. The antibodies were used to analyze the phage protein distribution inside the host cell during inf
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 313
Proper folding, and consequently exit from the endoplasmic reticulum (ER) and secretion of heterologous exocytic proteins in yeast can be rescued by fusing the proteins to certain yeast-derived polypeptides. Biologically active mammalian glycoprotein