ArticlePlant physiology1996
Cytoplasmic Orientation of the Naphthylphthalamic Acid-Binding Protein in Zucchini Plasma Membrane Vesicles.
Article in Plant physiology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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Who cites it
12 citing papers in PubMed, 34 citations in OpenAlex.
- Review
- A Retro-Perspective on Auxin Transport.Frontiers in plant science · 2021Article
- Inhibitors of plant hormone transport.Protoplasma · 2016Review
- TWISTED DWARF1 Mediates the Action of Auxin Transport Inhibitors on Actin Cytoskeleton Dynamics.The Plant cell · 2016Article
- Mutation of the rice Narrow leaf1 gene, which encodes a novel protein, affects vein patterning and polar auxin transport.Plant physiology · 2008Article
- The transparent testa4 mutation prevents flavonoid synthesis and alters auxin transport and the response of Arabidopsis roots to gravity and light.The Plant cell · 2004Article
- Do phytotropins inhibit auxin efflux by impairing vesicle traffic?Plant physiology · 2003Article
- Genetic and chemical reductions in protein phosphatase activity alter auxin transport, gravity response, and lateral root growth.The Plant cell · 2001Article
- Alteration of auxin polar transport in the Arabidopsis ifl1 mutants.Plant physiology · 2001Article
- Flavonoids act as negative regulators of auxin transport in vivo in arabidopsis.Plant physiology · 2001Article
- Going the distance with auxin: unravelling the molecular basis of auxin transport.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 1998Review
- Reduced naphthylphthalamic acid binding in the tir3 mutant of Arabidopsis is associated with a reduction in polar auxin transport and diverse morphological defects.The Plant cell · 1997Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Polar transport of the plant hormone auxin is blocked by substances such as N-1-naphthylphthalamic acid (NPA), which inhibit auxin efflux and block polar auxin transport. To understand how auxin transport is regulated in vivo, it is necessary to discern whether auxin transport inhibitors act at the intra- or extracellular side of the plasma membrane. Populations of predominantly in-side-in plasma membrane vesicles were subjected to treatments that reverse the orientation. These treatments, which included osmotic shock, cycles of freezing and thawing, and incubation with 0.05% Brij-58, all increased NPA-binding activity and the accessibility of the binding protein to protease digestion. Marker activities for inside-out vesicles also increased, indicating that these treatments act by altering the membrane orientation. Finally, binding data were analyzed by multiple analyses and indicated that neither the affinity nor abundance of binding sites changed. Kinetic analyses indicated that the change in NPA-binding activity by Brij-58 treatment was due to an increase in the initial rates of both association and dissociation of this ligand. These experiments indicated that the NPA-binding site is on the cytoplasmic face of the plasma membrane in zucchini (Cucurbita pepo L. cv Burpee Fordhook).
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.