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The Family of Glycogen Phosphorylases: Structure and Functio
Abstract
Glycogen phosphorylase plays a central role in the mobilization of carbohydrate reserves in a wide variety of organisms and tissues. While rabbit muscle phosphorylase remains the most studied and best characterized of phosphorylases, recombinant DNA techniques have led to the recent appearance of primary sequence data for a wide variety of phosphorylase enzymes. The functional properties of rabbit muscle phosphorylases are reviewed and then compared to properties of phosphorylases from other tissues and organisms. Tissue expression patterns and the chromosomal localization of mammalian phosphorylases are described. Differences in functional properties among phosphorylases are related to new structural information. Evolutionary relationships among phosphorylases as afforded by comparative analysis of proteins and gene sequences are discussed.
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CEREBRAL ENERGY METABOLISM DURING EXPERIMENTAL STATUS EPILEPTICUS 1
Duffy, T. E., Howse, D. C., & Plum, F. (1975) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1975.tb03657.x · Cited by 220
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Pyridoxine dependent epilepsy and antiquitin deficiency
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Sheng, H., & Sun, H. (2011) · Natural Product Reports · doi:10.1039/c0np00059k · Cited by 289
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Metadata
- Authors
- Newgard, C. B., Hwang, P. K., & Fletterick, R. J.
- Venue
- Critical Reviews in Biochemistry and Molecular Biology
- Publisher
- Informa UK Limited
- Published
- 1989-01
- Volume
- 24
- Issue
- 1
- Pages
- 69-99
- ISSN
- 0045-6411 (ISSN-L)
- 1040-9238
- 1549-7798
- OpenAlex
- W2073887637
- Cited by
- 397
- References
- 1
- FWCI
- 5.20
- Type
- journal article
- Language
- en
- Open access
- closed
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- Newgard, C. B., Hwang, P. K., & Fletterick, R. J. (1989). The Family of Glycogen Phosphorylases: Structure and Functio. Critical Reviews in Biochemistry and Molecular Biology. https://doi.org/10.3109/10409238909082552
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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