Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2008-7-23
pubmed:abstractText
Glycosylation is the most common post-translational modification of proteins. The protein sequence data suggested that more than half of all proteins produced in mammalian cells are glycoproteins. Glycans of secreted glycoproteins affect many protein properties such as solubility, stability, protease sensitivity, and polarity, while glycans on cell surface glycoproteins are involved in various cellular functions including cell-cell and cell-matrix interactions during embryogenesis, immune reactions, and tumor development. The past decade of research on glycan function has revealed the etiology of a growing number of human genetic diseases with aberrant glycan formation. This review focuses upon the involvement of O-mannosylglycan in the molecular and cellular mechanisms of muscular dystrophies. Advances in glycobiology are expected to result in a better understanding and in improved treatments of a class of muscular dystrophies called alpha-dystroglycanopathies.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/18646566-10580125, http://linkedlifedata.com/resource/pubmed/commentcorrection/18646566-10610181, http://linkedlifedata.com/resource/pubmed/commentcorrection/18646566-11294909, http://linkedlifedata.com/resource/pubmed/commentcorrection/18646566-11524432, http://linkedlifedata.com/resource/pubmed/commentcorrection/18646566-11709191, http://linkedlifedata.com/resource/pubmed/commentcorrection/18646566-12091319, http://linkedlifedata.com/resource/pubmed/commentcorrection/18646566-12140559, http://linkedlifedata.com/resource/pubmed/commentcorrection/18646566-12230980, http://linkedlifedata.com/resource/pubmed/commentcorrection/18646566-12369018, http://linkedlifedata.com/resource/pubmed/commentcorrection/18646566-12441301, http://linkedlifedata.com/resource/pubmed/commentcorrection/18646566-12464682, http://linkedlifedata.com/resource/pubmed/commentcorrection/18646566-12551906, http://linkedlifedata.com/resource/pubmed/commentcorrection/18646566-12716890, http://linkedlifedata.com/resource/pubmed/commentcorrection/18646566-12797959, http://linkedlifedata.com/resource/pubmed/commentcorrection/18646566-12907685, http://linkedlifedata.com/resource/pubmed/commentcorrection/18646566-14699049, http://linkedlifedata.com/resource/pubmed/commentcorrection/18646566-15377669, http://linkedlifedata.com/resource/pubmed/commentcorrection/18646566-15467391, http://linkedlifedata.com/resource/pubmed/commentcorrection/18646566-15894594, http://linkedlifedata.com/resource/pubmed/commentcorrection/18646566-16251947, http://linkedlifedata.com/resource/pubmed/commentcorrection/18646566-16410545, http://linkedlifedata.com/resource/pubmed/commentcorrection/18646566-16427280, http://linkedlifedata.com/resource/pubmed/commentcorrection/18646566-16464857, http://linkedlifedata.com/resource/pubmed/commentcorrection/18646566-16550917, http://linkedlifedata.com/resource/pubmed/commentcorrection/18646566-16698797, http://linkedlifedata.com/resource/pubmed/commentcorrection/18646566-16704966, http://linkedlifedata.com/resource/pubmed/commentcorrection/18646566-17024709, http://linkedlifedata.com/resource/pubmed/commentcorrection/18646566-17034757, http://linkedlifedata.com/resource/pubmed/commentcorrection/18646566-17452335, http://linkedlifedata.com/resource/pubmed/commentcorrection/18646566-17470820, http://linkedlifedata.com/resource/pubmed/commentcorrection/18646566-17502374, http://linkedlifedata.com/resource/pubmed/commentcorrection/18646566-17869517
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1128-2460
pubmed:author
pubmed:issnType
Print
pubmed:volume
26
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
165-70
pubmed:dateRevised
2011-7-28
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Dystroglycan glycosylation and its role in alpha-dystroglycanopathies.
pubmed:affiliation
Tokyo Metropolitan Institute of Gerontology, Foundation for Research on Aging and Promotion of Human Welfare, Itabashi-ku, Tokyo, Japan. endo@tmig.or.jp
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't