Linked Life Data

21370056

Source:http://linkedlifedata.com/resource/pubmed/id/21370056

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2011-3-3
pubmed:abstractText
The complexity of carbohydrate structures and their derivatives makes the study of the glycome a challenging subset of proteomic research. The microarray platform has become an essential tool to characterize glycan structure and to study glycosylation-related biological interactions, by using probes as a means to interrogate the spotted or captured glycosylated molecules on the arrays. The high-throughput and reproducible nature of microarray platforms have been highlighted by their extensive applications in the field of biomarker validation, where a large number of samples must be analyzed multiple times. This chapter presents an antibody-lectin microarray approach, which allows the efficient, multiplexed study of the glycosylation of multiple individual proteins from complex mixtures with both fluorescence labeling detection and label-free detection based on mass spectrometry.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1940-6029
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
723
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
15-28
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Analysis of serum protein glycosylation with antibody-lectin microarray for high-throughput biomarker screening.
pubmed:affiliation
Department of Chemistry, The University of Michigan, Ann Arbor, MI, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural