Results 31 to 40 of about 21,397 (220)

Multi-Temperature Crystallography of Polyamine Biosynthesis Enzymes Reveals Differing Active Site Conformations at RT than 100K [PDF]

open access: yesStructural Dynamics
The polyamine biosynthetic pathway synthesizes the polyamines putrescine, spermidine, and spermine from ornithine and S-adenosyl methionine. These polyamines are important molecules in metabolism and are associated with growth and proliferation of cells ...
Jonathan A Clinger
doaj   +1 more source

Determinants of the differential antizyme-binding affinity of ornithine decarboxylase. [PDF]

open access: yesPLoS ONE, 2011
Ornithine decarboxylase (ODC) is a ubiquitous enzyme that is conserved in all species from bacteria to humans. Mammalian ODC is degraded by the proteasome in a ubiquitin-independent manner by direct binding to the antizyme (AZ).
Yen-Chin Liu   +5 more
doaj   +1 more source

Melatonin treatment induces chilling tolerance by regulating the contents of polyamine, γ-aminobutyric acid, and proline in cucumber fruit

open access: yesJournal of Integrative Agriculture, 2021
The mechanism of melatonin (MT) induced chilling tolerance in harvested cucumber fruit was investigated at commercial maturity. In this study, cucumber fruits were treated with 100 µmol L–1 MT at 4°C and 90% relative humidity for 15 d of storage.
Miilion P MADEBO   +4 more
doaj   +1 more source

Regulation of ovarian ornithine decarboxylase by human chorionic gonadotrophin [PDF]

open access: yes, 1987
Treatment of 29-day-old female Sprague-Dawley rats with human chorionic gonadotrophin (hCG) produced a large and rapid increase in the activity of ornithine decarboxylase.
A. E. Pegg, G. J. Sertich, L. Persson
core   +1 more source

Hydroxylamine Analogue of Agmatine: Magic Bullet for Arginine Decarboxylase

open access: yesBiomolecules, 2020
The biogenic polyamines, spermine, spermidine (Spd) and putrescine (Put) are present at micro-millimolar concentrations in eukaryotic and prokaryotic cells (many prokaryotes have no spermine), participating in the regulation of cellular proliferation and
Mervi T. Hyvönen   +9 more
doaj   +1 more source

A quantitative cytochemical method for ornithine decarboxylase activity. [PDF]

open access: yes, 1990
Although decarboxylases, particularly ornithine decarboxylase, are of considerable importance in cell metabolism, it has been impossible to demonstrate their activity histochemically, as this depends on trapping carbon dioxide at neutral pH values.
R A Dodds, G T Frost, A A Pitsillides
core   +1 more source

Putrescine Biosynthesis Inhibition in Tomato by DFMA and DFMO Treatment

open access: yesBio-Protocol, 2016
This protocol can be used to inhibit the biosynthesis of polyamines, specifically putrescine, in tomato plants grown with NH4+ as a solely N source. In general, polyamines are positively charged small metabolites implicated in physiological processes ...
Emma Fernández-Crespo   +5 more
doaj   +1 more source

Phosphorylation of ornithine decarboxylase in intact erythroleukemia cells [PDF]

open access: yes, 1990
32P-labeled ornithine decarboxylase was isolated by immunoprecipitation from murine erythroleukemia cells incubated in a medium containing [32P]ortophosphoric acid.
Meggio F.   +4 more
core   +1 more source

Characterization of the Entamoeba histolytica ornithine decarboxylase-like enzyme. [PDF]

open access: yesPLoS Neglected Tropical Diseases, 2008
BACKGROUND: The polyamines putrescine, spermidine, and spermine are organic cations that are required for cell growth and differentiation. Ornithine decarboxylase (ODC), the first and rate-limiting enzyme in the polyamine biosynthetic pathway, is a ...
Anupam Jhingran   +8 more
doaj   +1 more source

In vivo hormonal induction of ornithine decarboxylase in rat kidney [PDF]

open access: yes, 1976
Single pharmacological doses of parathyroid hormone, calcitonin, vasopressin, d-aldosterone, or L-triiodothyronine produced a significant increase in the ornithine decarboxylase activity of rat kidney.
M. E. Ferioli, G. Scalabrino
core   +1 more source

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