Linked Life Data

20197635

Source:http://linkedlifedata.com/resource/pubmed/id/20197635

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2010-3-19
pubmed:abstractText
GM130 is a peripheral membrane protein strongly attached to the Golgi membrane and is isolated from the detergent and salt resistant Golgi matrix. GM130 is rich in coiled-coil structures and predicted to take a rod-like shape. Together with p115, giantin, and GRASP65, GM130 facilitates vesicle fusion to the Golgi membrane as a vesicle "tethering factor". GM130 is also involved in the maintenance of the Golgi structure and plays a major role in the disassembly and reassembly of the Golgi apparatus during mitosis. Emerging evidence suggests that GM130 is involved in the control of glycosylation, cell cycle progression, and higher order cell functions such as cell polarization and directed cell migration. This creates the potential for novel Golgi-targeted drugs and treatments for various diseases including glycosylation defects, immune diseases, and cancer.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1347-8648
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
112
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
255-64
pubmed:dateRevised
2011-6-20
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Emerging new roles of GM130, a cis-Golgi matrix protein, in higher order cell functions.
pubmed:affiliation
Cell Biology, Division of Life Science, Graduate School of Natural Science and Technologies, Kanazawa University, Japan. osaru3@kenroku.kanazawa-u.ac.jp
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't