ArticleMolecular and cellular biochemistry1998
Sequence of a Menkes-type Cu-transporting ATPase from rat C6 glioma cells: comparison of the rat protein with other mammalian Cu-transporting ATPases.
Article in Molecular and cellular biochemistry, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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
1 citing paper in PubMed, 10 citations in OpenAlex.
- Effect of copper and diethyldithiocarbamate combination therapy on the macular mouse, an animal model of Menkes disease.Journal of inherited metabolic disease · 2005Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Rat Atp7a occupied a single open reading frame (274502) which coded for a protein of 1492 residues. Rat Atp7a was 98% and 95% identical to published sequences for the mouse and Chinese hamster, respectively, and 94% homologous to human ATP7A. Compared to ATP7A, the rat transcript coded for an additional alanine (A446) in the heavy metal binding (Hmb) domain and showed a 34 bp gap in the 3' UTR. Based on published sequence data, hydropathic profiles for rat, mouse, Chinese hamster, and human Cu-ATPases were practically identical with the exception of 8 additional amino acid residues between the 4th and 5th Hmb sites in the human. As deduced from amino acid sequence data, Hmb was predicted to have regions with helical and beta structures. All four species had five of the six metal binding sites centered within hydrophobic regions. The comparative analyses suggested that the Hmb region of the molecule could experience numerous amino acid substitutions with no apparent disruption to theATPase transport function whereas variations to theATPase domain would be more critical.
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