Linked Life Data

20353490

Source:http://linkedlifedata.com/resource/pubmed/id/20353490

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2010-7-19
pubmed:abstractText
Despite decades of studying muscle glycogen in many metabolic situations, surprisingly little is known regarding its regulation. Glycogen is a dynamic and vital metabolic fuel that has very limited energetic capacity. Thus its regulation is highly complex and multifaceted. The stores in muscle are not homogeneous and there appear to be various metabolic pools. Each granule is capable of independent regulation and fundamental aspects of the regulation appear to be associated with a complex set of proteins (some are enzymes and others serve scaffolding roles) that associate both with the granule and with each other in a dynamic fashion. The regulation includes altered phosphorylation status and often translocation as well. The understanding of the roles and the regulation of glycogenin, protein phosphatase 1, glycogen targeting proteins, laforin and malin are in their infancy. These various processes appear to be the mechanisms that give the glycogen granule precise, yet dynamic regulation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1748-1716
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
199
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
489-98
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
The regulation of muscle glycogen: the granule and its proteins.
pubmed:affiliation
Human Health and Nutritional Sciences, University of Guelph, Guelph, ON, Canada. terrygra@uoguelph.ca
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't