ArticleThe Biochemical journal1991
Transverse topology of glucose-6-phosphatase in rat hepatic endoplasmic reticulum.
Article in The Biochemical journal, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
6 citing papers in PubMed, 35 citations in OpenAlex.
- Metabolic Transporters in the Peripheral Nerve-What, Where, and Why?Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2021Review
- Fasting hyperglycemia is not associated with increased expression of PEPCK or G6Pc in patients with Type 2 Diabetes.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Aldolase potentiates DIDS activation of the ryanodine receptor in rabbit skeletal sarcoplasmic reticulum.The Biochemical journal · 2006Article
- The gene for glycogen-storage disease type 1b maps to chromosome 11q23.American journal of human genetics · 1998Article
- The hepatic glucose-6-phosphatase system in Ehrlich-ascites-tumour-bearing mice.The Biochemical journal · 1993Article
- Cloning and expression of a hepatic microsomal glucose transport protein. Comparison with liver plasma-membrane glucose-transport protein GLUT 2.The Biochemical journal · 1992Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Antibodies raised against purified components of glucose-6-phosphatase were used to study the transmembrane orientation of the complex. Measurements of glucose-6-phosphatase activities and immunoblot analysis of sealed microsomes and detergent-solubilized microsomes after treatment with proteases suggested that most of the catalytic subunit resides within the lumen of the endoplasmic reticulum. In contrast, other components of glucose-6-phosphatase are accessible to the cytoplasm. Treatment of the partially purified glucose-6-phosphatase enzyme with glycopeptide N-glycosidase indicated that the catalytic subunit of the enzyme was a glycoprotein.
Indexed as
Identifiers
What OpenQuestion holds
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.