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David A. Morris

Researcher at University of Southampton

Publications -  38
Citations -  2254

David A. Morris is an academic researcher from University of Southampton. The author has contributed to research in topics: Auxin & Invertase. The author has an hindex of 23, co-authored 38 publications receiving 2207 citations. Previous affiliations of David A. Morris include Academy of Sciences of the Czech Republic.

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Auxin inhibits endocytosis and promotes its own efflux from cells

TL;DR: The data imply a previously undescribed mode of plant hormone action: by modulating PIN protein trafficking, auxin regulates PIN abundance and activity at the cell surface, providing a mechanism for the feedback regulation of auxin transport.
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Do Phytotropins Inhibit Auxin Efflux by Impairing Vesicle Traffic

TL;DR: No evidence is found to support recent suggestions that the action of auxin transport inhibitors is mediated by a general inhibition of vesicle-mediated protein traffic to the plasma membrane, and a proportion of the NPA-sensitive auxin efflux carriers may be protected from theaction of BFA.
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The transport and metabolism of (14)C-labelled indoleacetic acid in intact pea seedlings.

TL;DR: Together, the decarboxylation of IAA and the formation of IAAsp operated to maintain a relatively constant level of free IAA-14C in the root system.
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A Microautoradiographic Study of Auxin Transport in the Stem of Intact Pea Seedlings (Pisum sativum L.)

TL;DR: Results are consistent with the conclusions drawn from earlier transport experiments which indicated that in the intact plant the long-distance basipetal transport of auxin from the apical bud takes place in a system which is separated from the phloem transport system and suggests that the vascular cambium and its immediate derivatives may function as the normal pathway for the long distance movement of Auxin in the plant.
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Transmembrane auxin carrier systems--dynamic regulators of polar auxin transport.

TL;DR: Investigation of the turn-over and Golgi-mediated trafficking of auxin carrier proteins have revealed that essential components of at least the efflux carrier have a very short half-life in the plasma membrane and are replaced without the need for concurrent protein synthesis, leading to speculation that they might cycle between internal stores and the plasma membranes.