Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Melissa A. Scranton"'
Publikováno v:
PLoS ONE, Vol 12, Iss 10, p e0185492 (2017)
M18 aspartyl aminopeptidases (DAPs) are well characterized in microbes and animals with likely functions in peptide processing and vesicle trafficking. In contrast, there is a dearth of knowledge on plant aminopeptidases with a preference for protein
Externí odkaz:
https://doaj.org/article/715f3c16a089493a89b07505bdcc9174
Publikováno v:
PLoS ONE, Vol 8, Iss 10, p e77889 (2013)
Wounding due to mechanical injury or insect feeding causes a wide array of damage to plant cells including cell disruption, desiccation, metabolite oxidation, and disruption of primary metabolism. In response, plants regulate a variety of genes and m
Externí odkaz:
https://doaj.org/article/c99e23aee5914846bf438e57b50225ae
Autor:
Daphne Li, Shane Lofgren, Rosalie C. Ellis, Joseph T. Ostrand, Andreas Dräger, David L. Masica, David N. Carruthers, Stephen P. Mayfield, Melissa A. Scranton, D. Ryan Georgianna
Publikováno v:
Algal Research. 15:135-142
Algae have enormous potential as bio-factories for the efficient production of a wide array of high-value products, and eventually as a source of renewable biofuels. However, tools for engineering the nuclear genomes of algae remain scarce and limite
Publikováno v:
ACS Synthetic Biology. 5:589-596
Oxygenic photosynthesis provides the energy to produce all food and most of the fuel on this planet. Photosystem II (PSII) is an essential and rate-limiting component of this process. Understanding and modifying PSII function could provide an opportu
Publikováno v:
PLoS ONE, Vol 12, Iss 10, p e0185492 (2017)
PLoS ONE
Park, S-Y; Scranton, MA; Stajich, JE; Yee, A; & Walling, LL. (2017). Chlorophyte aspartyl aminopeptidases: Ancient origins, expanded families, new locations, and secondary functions. PLOS ONE, 12(10), e0185492. doi: 10.1371/journal.pone.0185492. UC Riverside: Retrieved from: http://www.escholarship.org/uc/item/5kz714mf
PLoS ONE
Park, S-Y; Scranton, MA; Stajich, JE; Yee, A; & Walling, LL. (2017). Chlorophyte aspartyl aminopeptidases: Ancient origins, expanded families, new locations, and secondary functions. PLOS ONE, 12(10), e0185492. doi: 10.1371/journal.pone.0185492. UC Riverside: Retrieved from: http://www.escholarship.org/uc/item/5kz714mf
M18 aspartyl aminopeptidases (DAPs) are well characterized in microbes and animals with likely functions in peptide processing and vesicle trafficking. In contrast, there is a dearth of knowledge on plant aminopeptidases with a preference for protein
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 70:1649-1658
The acidic leucine aminopeptidase (LAP-A) from tomato is induced in response to wounding and insect feeding. Although LAP-A showsin vitropeptidase activity towards peptides and peptide analogs, it is not clear what kind of substrates LAP-A hydrolyzes
Publikováno v:
Acta crystallographica. Section D, Structural biology. 72(Pt 5)
Tomato plants express acidic leucine aminopeptidase (LAP-A) in response to various environmental stressors. LAP-A not only functions as a peptidase for diverse peptide substrates, but also displays chaperone activity. A K354E mutation has been shown
Publikováno v:
Journal of Biological Chemistry. 287:18408-18417
Leucine aminopeptidases (LAPs) are present in animals, plants, and microbes. In plants, there are two classes of LAPs. The neutral LAPs (LAP-N and its orthologs) are constitutively expressed and detected in all plants, whereas the stress-induced acid
Publikováno v:
The Plant journal : for cell and molecular biology. 82(3)
Developing renewable energy sources is critical to maintaining the economic growth of the planet while protecting the environment. First generation biofuels focused on food crops like corn and sugarcane for ethanol production, and soybean and palm fo