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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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The AtC-VPS protein complex is localized to the tonoplast and the prevacuolar compartment in arabidopsis.

TL;DR: The first components of the vacuolar biogenesis machinery to be identified in plants are identified, and it is shown that a VCL1-containing complex includes SYP2-type syntaxins and is most likely involved in membrane fusion on both the PVC and tonoplast in vivo.
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Auxin-Mediated Ribosomal Biogenesis Regulates Vacuolar Trafficking in Arabidopsis

TL;DR: It is shown that ribosomal biogenesis can be directly regulated by auxins and that the exogenous application of auxins to wild-type plants results in vacuolar trafficking defects similar to those observed in rpl4a mutants.
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Cloning and Characterization of Root-Specific Barley Lectin

TL;DR: In this paper, a barley (Hordeum vulgare L.) embryo cDNA library was constructed and a clone (BLc3) for barley lectin was isolated, which contained a putative signal peptide of 26 amino acid residues followed by a 186 amino acid polypeptide.
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NPSN11 Is a Cell Plate-Associated SNARE Protein That Interacts with the Syntaxin KNOLLE

TL;DR: The identification and characterization of a novel plant-specific SNARE, NSPN11, a member of a closely related small gene family in Arabidopsis is described, suggesting that NPSN11 is another component of the membrane trafficking and fusion machinery involved in cell plate formation.
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Cloning and characterization of AtRGP1. A reversibly autoglycosylated arabidopsis protein implicated in cell wall biosynthesis.

TL;DR: It is confirmed that AtRGP1 produced in Escherichia coli could be reversibly glycosylated using UDP-glucose and UDP-galactose as substrates.