L
Larry R. Beach
Researcher at DuPont Pioneer
Publications - 24
Citations - 1113
Larry R. Beach is an academic researcher from DuPont Pioneer. The author has contributed to research in topics: Gene & Amino acid. The author has an hindex of 15, co-authored 24 publications receiving 1111 citations.
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A Regulatory Gene as a Novel Visible Marker for Maize Transformation
TL;DR: Microprojectiles were used to introduce into maize cells a vector containing the transcription unit from one of these genes (Lc) fused to a constitutive promoter, which induces cell autonomous pigmentation in tissues that are not normally pigmented by the Lc gene.
Patent
High lysine derivatives of alpha-hordothionin
A. Gururaj Rao,Larry R. Beach +1 more
TL;DR: In this article, position-specific substitution with lysine residues provided the enrichment of α-hordothionin while retaining the antifungal activity of the parent compound.
Patent
Alteration of amino acid compositions in seeds
Rudolf Jung,Larry R. Beach,Virginia M. Dress,A. Gururaj Rao,Jerome P. Ranch,David S. Ertl,Regina K. Higgins +6 more
TL;DR: In this article, the endosperm of a plant seed is characterized as having an elevated level of a preselected amino acid and a method for enhancing the nutritional value of seeds is presented.
Patent
Genes controlling phytate metabolism in plants and uses thereof
TL;DR: In this paper, newly identified polynucleotides and polypeptides, variants and derivatives of same; methods for making the polynuclidean nucleotides, polyprotein derivatives, variants, derivatives and antagonists.
Patent
Methods of increasing accumulation of essential amino acids in seeds
TL;DR: In this paper, a method for increasing the levels of essential amino acids in seeds of plants, thereby enhancing the nutritional value of the seeds, is presented, which comprises manipulating the metabolic pathway of the amino acid to provide an increased source of the target free amino acid and, concomitantly, over-expressing a preselected gene coding for the protein containing the target amino acid, such that there is accumulation of protein-bound target amino acids.