Zobrazeno 1 - 10
of 36
pro vyhledávání: '"Beth A. Rasala"'
Publikováno v:
PLoS ONE, Vol 9, Iss 4, p e94028 (2014)
Transgenic microalgae have the potential to impact many diverse biotechnological industries including energy, human and animal nutrition, pharmaceuticals, health and beauty, and specialty chemicals. However, major obstacles to sophisticated genetic a
Externí odkaz:
https://doaj.org/article/fa228645b94e4f9b855d40eb9aa8786d
Autor:
Beth A Rasala, Philip A Lee, Zhouxin Shen, Steven P Briggs, Michael Mendez, Stephen P Mayfield
Publikováno v:
PLoS ONE, Vol 7, Iss 8, p e43349 (2012)
Microalgae have recently received attention as a potential low-cost host for the production of recombinant proteins and novel metabolites. However, a major obstacle to the development of algae as an industrial platform has been the poor expression of
Externí odkaz:
https://doaj.org/article/43338d95395841b9b76c2f4fd32022dc
Autor:
Stephen P. Mayfield, Miller Tran, Beth A. Rasala, Shengchun Guo, Ayswarya Ravi, Zivko L. Nikolov
Publikováno v:
International Journal of Molecular Sciences, Vol 19, Iss 2, p 585 (2018)
International journal of molecular sciences, vol 19, iss 2
International Journal of Molecular Sciences; Volume 19; Issue 2; Pages: 585
International Journal of Molecular Sciences
International journal of molecular sciences, vol 19, iss 2
International Journal of Molecular Sciences; Volume 19; Issue 2; Pages: 585
International Journal of Molecular Sciences
Correct folding and post-translational modifications are vital for therapeutic proteins to elicit their biological functions. Osteopontin (OPN), a bone regenerative protein present in a range of mammalian cells, is an acidic phosphoprotein with multi
Autor:
Stephen P. Mayfield, Beth A. Rasala
Publikováno v:
Photosynthesis Research. 123:227-239
Recombinant proteins are widely used for industrial, nutritional, and medical applications. Green microalgae have attracted considerable attention recently as a biomanufacturing platform for the production of recombinant proteins for a number of reas
Publikováno v:
Plant Biotechnology Journal. 9:674-683
Microalgae have the potential to be a valuable biotechnological platform for the production of recombinant proteins. However, because of the complex regulatory network that tightly controls chloroplast gene expression, heterologous protein accumulati
The microalgaChlamydomonas reinhardtiias a platform for the production of human protein therapeutics
Autor:
Stephen P. Mayfield, Beth A. Rasala
Publikováno v:
Bioengineered Bugs. 2:50-54
Microalgae are a diverse group of eukaryotic photosynthetic microorganisms. While microalgae play a crucial role in global carbon fixation and oxygen evolution, these organisms have recently gained much attention for their potential role in biotechno
Publikováno v:
Molecular Biology of the Cell. 21:4197-4211
Nuclear pore complexes (NPCs) are large proteinaceous channels embedded in double nuclear membranes, which carry out nucleocytoplasmic exchange. The mechanism of nuclear pore assembly involves a unique challenge, as it requires creation of a long-liv
Autor:
Stephen P. Mayfield, Craig A. Behnke, Machiko Muto, Roberto Crea, Philip A. Lee, Craig A. Hokanson, Beth A. Rasala, Rosa M.F. Cardoso, Peter B. Kirk, Michael Mendez, Michal Jager
Publikováno v:
Plant Biotechnology Journal. 8:719-733
Recombinant proteins are widely used today in many industries, including the biopharmaceutical industry, and can be expressed in bacteria, yeasts, mammalian and insect cell cultures, or in transgenic plants and animals. In addition, transgenic algae
Publikováno v:
Molecular Biology of the Cell. 19:3982-3996
Assembly of the nuclear pore, gateway to the genome, from its component subunits is a complex process. In higher eukaryotes, nuclear pore assembly begins with the binding of ELYS/MEL-28 to chromatin and recruitment of the large critical Nup107-160 po
Publikováno v:
Molecular and Cellular Biology. 28:1755-1769
Centrins in vertebrates have traditionally been associated with microtubule-nucleating centers such as the centrosome. Unexpectedly, we found centrin 2 to associate biochemically with nucleoporins, including the Xenopus laevis Nup107-160 complex, a c