ArticleJournal of protein chemistry1990
Characterization of a GDP-sensitive phosphorylation in plasma membranes of D. discoideum.
Article in Journal of protein chemistry, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
4 citing papers in PubMed, 4 citations in OpenAlex.
- Regulatory role of GDP in the phosphoenzyme formation of guanine nucleotide: specific forms of succinyl coenzyme A synthetase.Journal of protein chemistry · 1994Article
- Evidence for allosteric regulation of succinyl-CoA synthetase.The Biochemical journal · 1993Article
- Dual role of GDP in the regulation of the levels of p36 phosphorylation in Dictyostelium discoideum.Journal of protein chemistry · 1991Article
- Properties of CAR-kinase: the enzyme that phosphorylates the cAMP chemotactic receptor of D. discoideum.Journal of protein chemistry · 1990Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
In a previous study, we reported the GDP-dependent phosphorylation of a 36 kD membrane protein, p36, in D. discoideum membranes prepared from starved (aggregation competent) cells (Anschutz et al., 1989). Here we show that p36 can be phosphorylated when membranes are supplied either ATP or GTP as the phosphate donor, but that a greater level of p36 phosphorylation is achieved with GTP. The rate of phosphorylation of p36, using either nucleotide triphosphate, is enhanced by GDP. This reflects a decrease in the apparent Km of the enzyme for the particular nucleotide triphosphate. p36 can also be phosphorylated in membranes prepared from vegetative cells. However, the ability of GDP to stimulate p36 phosphorylation is not observed in vegetative cell membranes. Competition experiments indicate that there are also developmental differences in the nucleotide triphosphate site(s) available to phosphorylate p36.
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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.