| pubmed-article:16401092 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16401092 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:16401092 | lifeskim:mentions | umls-concept:C1171362 | lld:lifeskim |
| pubmed-article:16401092 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:16401092 | lifeskim:mentions | umls-concept:C1421866 | lld:lifeskim |
| pubmed-article:16401092 | lifeskim:mentions | umls-concept:C1515670 | lld:lifeskim |
| pubmed-article:16401092 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:16401092 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:16401092 | lifeskim:mentions | umls-concept:C0443199 | lld:lifeskim |
| pubmed-article:16401092 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:16401092 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:16401092 | lifeskim:mentions | umls-concept:C0591833 | lld:lifeskim |
| pubmed-article:16401092 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:16401092 | pubmed:dateCreated | 2006-1-10 | lld:pubmed |
| pubmed-article:16401092 | pubmed:abstractText | Murine sperm initiate fertilization by binding to the zona pellucida (mZP), the specialized extracellular matrix of their homologous eggs. O-Glycans occupying two highly conserved vicinal glycosylation sites (Ser-332 and Ser-334) on the mZP glycoprotein designated mZP3 were previously implicated in this interaction. However, recent biophysical analyses confirm that neither site is occupied, implying that an alternate O-glycosylation domain may be operational in native mZP3. Since human ZP3 (huZP3) can substitute for mZP3 in rescue mice to mediate sperm binding, the site specificity of O-glycosylation in both native mZP3 and huZP3 was analyzed using ultrasensitive mass spectrometric techniques. Two O-glycosylation sites in native mZP3, one at Thr-155 and the other within the glycopeptide at positions 161-168 (ATVSSEEK), are conserved in huZP3 derived from transgenic mice. Thus, there is a specific O-glycosylation domain within native mZP3 expressing two closely spaced O-glycans that is very well conserved in an evolutionarily related glycoprotein. In native mZP3, core 2 O-glycans predominate at both sites. However, in huZP3 derived from rescue mice, the O-glycans associated with Thr-156 (analogous to Thr-155 in mZP3) are exclusively core 1 and related Tn sequences, whereas core 2 O-glycans predominate at the other conserved site. This unique restriction of O-glycan expression suggests that sequence differences in the conserved O-glycosylation domains of mZP3 and huZP3 affect the ability of core 2 N-acetylglucosaminyltransferase(s) to extend the core 1 sequence. However, this difference in O-glycosylation at Thr-156 does not affect the fertility or the sperm binding phenotype of eggs derived from female huZP3 rescue mice. | lld:pubmed |
| pubmed-article:16401092 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16401092 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16401092 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16401092 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16401092 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16401092 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16401092 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16401092 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16401092 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16401092 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16401092 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16401092 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:16401092 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:16401092 | pubmed:author | pubmed-author:PanicoMariaM | lld:pubmed |
| pubmed-article:16401092 | pubmed:author | pubmed-author:MorrisHoward... | lld:pubmed |
| pubmed-article:16401092 | pubmed:author | pubmed-author:DellAnneA | lld:pubmed |
| pubmed-article:16401092 | pubmed:author | pubmed-author:ChalabiSaraS | lld:pubmed |
| pubmed-article:16401092 | pubmed:author | pubmed-author:PatankarManis... | lld:pubmed |
| pubmed-article:16401092 | pubmed:author | pubmed-author:LattanzioFran... | lld:pubmed |
| pubmed-article:16401092 | pubmed:author | pubmed-author:ClarkGary FGF | lld:pubmed |
| pubmed-article:16401092 | pubmed:author | pubmed-author:HaslamStuart... | lld:pubmed |
| pubmed-article:16401092 | pubmed:author | pubmed-author:Sutton-SmithM... | lld:pubmed |
| pubmed-article:16401092 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16401092 | pubmed:day | 17 | lld:pubmed |
| pubmed-article:16401092 | pubmed:volume | 45 | lld:pubmed |
| pubmed-article:16401092 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16401092 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16401092 | pubmed:pagination | 637-47 | lld:pubmed |
| pubmed-article:16401092 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:16401092 | pubmed:meshHeading | pubmed-meshheading:16401092... | lld:pubmed |
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| pubmed-article:16401092 | pubmed:meshHeading | pubmed-meshheading:16401092... | lld:pubmed |
| pubmed-article:16401092 | pubmed:meshHeading | pubmed-meshheading:16401092... | lld:pubmed |
| pubmed-article:16401092 | pubmed:meshHeading | pubmed-meshheading:16401092... | lld:pubmed |
| pubmed-article:16401092 | pubmed:meshHeading | pubmed-meshheading:16401092... | lld:pubmed |
| pubmed-article:16401092 | pubmed:meshHeading | pubmed-meshheading:16401092... | lld:pubmed |
| pubmed-article:16401092 | pubmed:meshHeading | pubmed-meshheading:16401092... | lld:pubmed |
| pubmed-article:16401092 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16401092 | pubmed:articleTitle | Differential O-glycosylation of a conserved domain expressed in murine and human ZP3. | lld:pubmed |
| pubmed-article:16401092 | pubmed:affiliation | Division of Molecular Biosciences, Imperial College London, London SW7 2AZ, UK. | lld:pubmed |
| pubmed-article:16401092 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16401092 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:16401092 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:16401092 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16401092 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16401092 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:16401092 | lld:pubmed |
