J
John C. Rogers
Researcher at Washington State University
Publications - 64
Citations - 5335
John C. Rogers is an academic researcher from Washington State University. The author has contributed to research in topics: Vacuole & Hordeum vulgare. The author has an hindex of 36, co-authored 64 publications receiving 5220 citations. Previous affiliations of John C. Rogers include University of Missouri & Washington University in St. Louis.
Papers
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Journal ArticleDOI
Plant Cells Contain Two Functionally Distinct Vacuolar Compartments
TL;DR: It is demonstrated that antibodies to two different tonoplast intrinsic proteins, alpha-TIP and TIP-Ma27, label vacuole membranes of two different compartments within the same cell, suggesting that as cells develop large vacuoles, the two compartments merge.
Journal ArticleDOI
cis-acting DNA elements responsive to gibberellin and its antagonist abscisic acid.
TL;DR: The effect on transcription from both hormone response elements was orientation-independent, indicating that they function as inducible enhancers in their native genes.
Journal ArticleDOI
Tonoplast Intrinsic Protein Isoforms as Markers for Vacuolar Functions
TL;DR: It is argued that plant cells have the ability to generate and maintain three separate vacuole organelles, with each being marked by a different TIP, and that the functional diversity of the vacuolar system may be generated from different combinations of the three basic types.
Book ChapterDOI
Sorting of proteins to vacuoles in plant cells
Jean-Marc Neuhaus,John C. Rogers +1 more
TL;DR: The emerging picture of how separate plant vacuoles are organized structurally and how proteins are recognized and sorted to each type is reviewed.
Journal ArticleDOI
Integral Membrane Protein Sorting to Vacuoles in Plant Cells: Evidence for Two Pathways
Liwen Jiang,John C. Rogers +1 more
TL;DR: A chimeric integral membrane reporter protein expressed in tobacco suspension culture protoplasts whose traffic was assessed biochemically by following acquisition of complex Asn-linked glycan modifications and proteolytic processing and whose intracellular localization was determined with confocal immunofluorescence is studied.