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D esign: We administered questionnaires regarding maize storage and consumption and obtained maize and blood samples from participants.
We developed a questionnaire to elicit information about maize and protein consumption, the quality of home-grown and purchased maize products, maize storage and cooking practices, and associated illness and death of family members and pet dogs.
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Alligator pepper, Aframomum melegueta (Roscoe) K. Schum, and ginger, Zingiber officinale Roscoe were tested for their efficacy in protecting stored maize cobs (Zea mays L). against the maize weevil, Sitophilus zeamais Motschulsky, in traditional maize storage barn conditions, from November 2006 to February 2007, and November 2009 to February 2010 in Obudu, Southeast Nigeria.
High expression levels have been obtained by using fusion protein technologies such as elastin-like polypeptides (ELPs) [14] [16], hydrophobin [17], zeolin [18] and Zera, a proline-rich domain of the maize storage protein γ-zein [19].
A large-scale experiment on maize storage systems was carried out in Atakpamé (Plateaux region of Togo), between autumn 1996 and spring 1997.
However, in some African countries knowledge gaps exist on the effectiveness of hermetic maize storage, particularly where the Larger Grain Borer (LGB), Prostephanus truncatus occurs.
We have developed here an efficient system for the production of an active xylanase in tobacco plants fused to a proline-rich domain (Zera) of the maize storage protein γ-zein.
Total maize storage proteins are made of more than 60% zeins, of which about 70% are α-zeins [ 23].
The proline-rich N-terminal domain derived from the maize storage protein γ zein (Zera) is sufficient to induce PBs in non-seed tissues of Arabidopsis and tobacco.
The N-terminal proline-rich domain (Zera) of the maize storage protein γ-zein, is able to induce the formation of endoplasmic reticulum (ER -derived protER -derived(proteinen fused to proteins of interest.
Zera, a domain of prolamine-rich (gamma) maize storage protein accumulated inside the ER, can form stable supramolecular aggregates of polyproline structure bodies in plant cells, which allow the high accumulation of recombinant proteins in the ER and, thus, facilitates protein recovery through simple homogenization and centrifugation, enabling efficient purification [ 81].
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