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Natasha V. Raikhel

Researcher at University of California, Riverside

Publications -  219
Citations -  19035

Natasha V. Raikhel is an academic researcher from University of California, Riverside. The author has contributed to research in topics: Arabidopsis & Vacuole. The author has an hindex of 78, co-authored 218 publications receiving 18121 citations. Previous affiliations of Natasha V. Raikhel include National Academy of Sciences & University of California, Berkeley.

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Journal Article

Molecular basis of post-translational modifications and targeting of barley lectin to the vacuoles in barley and in transgenic tobacco plants

TL;DR: In this article, the 15-amino acid carboxylterminal propeptide (CTPP) of probarley lectin (proBL) was shown to be necessary for the proper sorting of this protein to the plant vacuole.
Journal ArticleDOI

2020 Vision for Biology: The Role of Plants in Addressing Grand Challenges in Biology

TL;DR: The Arabidopsis 2010 Program has funded the generation of a broad range of powerful genetic and genomic resources and technologies and will now facilitate effective studies at all levels of biological organization, including, molecular, cellular, organismal, and ecological.
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Drug Affinity Responsive Target Stability (DARTS) to Resolve Protein–Small Molecule Interaction in Arabidopsis

TL;DR: The protocols outlined in this article describe in detail the DARTS technique applied to plant proteins and propose several detection procedures according to protein abundance.
Book ChapterDOI

1 H NMR-Based Metabolomics Methods for Chemical Genomics Experiments

TL;DR: Methodology is provided for probing the metabolism of Arabidopsis thaliana in a chemical genomics experiment including methods for tissue treatment, tissue collection, metabolite extraction, and methods to minimize variance in biological and technical sample replicates.
Journal ArticleDOI

Isolation and characterization of pro-barley lectin expressed in Escherichia coli.

TL;DR: To analyze the three-dimensional structure of barley lectin with the carboxyl-terminal extension and to investigate whether the conversion of the prolectin into the mature molecule leads to a conformational change, the precursor and the mature forms of barley Lectin were expressed in Escherichia coli.