Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2010-5-31
pubmed:abstractText
The membrane-bound mucins, MUC17 (human) and Muc3 (mouse), are highly expressed on the apical surface of intestinal epithelia and have cytoprotective properties. Their extracellular regions contain two EGF-like Cys-rich domains (CRD1 and CRD2) connected by an intervening linker segment with SEA module (L), and may function to stimulate intestinal cell restitution. The purpose of this study was to determine the effect of size, recombinant host source, and external tags on mucin CRD1-L-CRD2 protein activity.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/20332014-10405327, http://linkedlifedata.com/resource/pubmed/commentcorrection/20332014-10512748, http://linkedlifedata.com/resource/pubmed/commentcorrection/20332014-10639160, http://linkedlifedata.com/resource/pubmed/commentcorrection/20332014-10696288, http://linkedlifedata.com/resource/pubmed/commentcorrection/20332014-11986789, http://linkedlifedata.com/resource/pubmed/commentcorrection/20332014-12034770, http://linkedlifedata.com/resource/pubmed/commentcorrection/20332014-14657486, http://linkedlifedata.com/resource/pubmed/commentcorrection/20332014-14760092, http://linkedlifedata.com/resource/pubmed/commentcorrection/20332014-15316018, http://linkedlifedata.com/resource/pubmed/commentcorrection/20332014-15943821, http://linkedlifedata.com/resource/pubmed/commentcorrection/20332014-16369486, http://linkedlifedata.com/resource/pubmed/commentcorrection/20332014-16737958, http://linkedlifedata.com/resource/pubmed/commentcorrection/20332014-17101324, http://linkedlifedata.com/resource/pubmed/commentcorrection/20332014-19561031, http://linkedlifedata.com/resource/pubmed/commentcorrection/20332014-3569771, http://linkedlifedata.com/resource/pubmed/commentcorrection/20332014-4440635, http://linkedlifedata.com/resource/pubmed/commentcorrection/20332014-7502046, http://linkedlifedata.com/resource/pubmed/commentcorrection/20332014-8649852, http://linkedlifedata.com/resource/pubmed/commentcorrection/20332014-9098007, http://linkedlifedata.com/resource/pubmed/commentcorrection/20332014-9334251, http://linkedlifedata.com/resource/pubmed/commentcorrection/20332014-9494100, http://linkedlifedata.com/resource/pubmed/commentcorrection/20332014-9828841, http://linkedlifedata.com/resource/pubmed/commentcorrection/20332014-9832422
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-3002
pubmed:author
pubmed:copyrightInfo
Published by Elsevier B.V.
pubmed:issnType
Print
pubmed:volume
1800
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
629-38
pubmed:dateRevised
2011-9-26
pubmed:meshHeading
pubmed-meshheading:20332014-Amino Acid Sequence, pubmed-meshheading:20332014-Animals, pubmed-meshheading:20332014-Apoptosis, pubmed-meshheading:20332014-Baculoviridae, pubmed-meshheading:20332014-Cell Line, Tumor, pubmed-meshheading:20332014-Cell Movement, pubmed-meshheading:20332014-Chromosome Mapping, pubmed-meshheading:20332014-Chromosomes, Human, Pair 7, pubmed-meshheading:20332014-Colonic Neoplasms, pubmed-meshheading:20332014-Escherichia coli, pubmed-meshheading:20332014-Glutathione Transferase, pubmed-meshheading:20332014-Humans, pubmed-meshheading:20332014-Intestines, pubmed-meshheading:20332014-Mice, pubmed-meshheading:20332014-Molecular Sequence Data, pubmed-meshheading:20332014-Mucins, pubmed-meshheading:20332014-Recombinant Proteins, pubmed-meshheading:20332014-Sequence Alignment, pubmed-meshheading:20332014-Sequence Homology, Amino Acid
pubmed:year
2010
pubmed:articleTitle
Activity of recombinant cysteine-rich domain proteins derived from the membrane-bound MUC17/Muc3 family mucins.
pubmed:affiliation
Department of Medicine, University of California-San Diego, San Diego, CA, USA. samuel.ho2@va.gov
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, N.I.H., Extramural