| pubmed-article:10029548 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10029548 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:10029548 | lifeskim:mentions | umls-concept:C0997362 | lld:lifeskim |
| pubmed-article:10029548 | lifeskim:mentions | umls-concept:C0040679 | lld:lifeskim |
| pubmed-article:10029548 | lifeskim:mentions | umls-concept:C1171362 | lld:lifeskim |
| pubmed-article:10029548 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:10029548 | lifeskim:mentions | umls-concept:C1515670 | lld:lifeskim |
| pubmed-article:10029548 | lifeskim:mentions | umls-concept:C0206755 | lld:lifeskim |
| pubmed-article:10029548 | lifeskim:mentions | umls-concept:C0037813 | lld:lifeskim |
| pubmed-article:10029548 | lifeskim:mentions | umls-concept:C0332462 | lld:lifeskim |
| pubmed-article:10029548 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:10029548 | pubmed:dateCreated | 1999-3-16 | lld:pubmed |
| pubmed-article:10029548 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10029548 | pubmed:abstractText | The ferric form of the N-lobe of human serum transferrin (Fe(III)-hTF/2N) has been expressed at high levels in Pichia pastoris. The Fe(III)-hTF/2N was crystallized in the space group P41212, and X-ray crystallography was used to solve the structure of the recombinant protein at 2.5 A resolution. This represents only the second P. pastoris-derived protein structure determined to date, and allows the comparison of the structures of recombinant Fe(III)-hTF/2N expressed in P. pastoris and mammalian cells with serum-derived transferrin. The polypeptide folding pattern is essentially identical in all of the three proteins. Mass spectroscopic analyses of P. pastoris- hTF/2N and proteolytically derived fragments revealed glycosylation of Ser-32 with a single hexose. This represents the first localization of an O-linked glycan in a P. pastoris-derived protein. Because of its distance from the iron-binding site, glycosylation of Ser-32 should not affect the iron-binding properties of hTF/2N expressed in P. pastoris, making this an excellent expression system for the production of hTF/2N. | lld:pubmed |
| pubmed-article:10029548 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10029548 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10029548 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10029548 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10029548 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10029548 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10029548 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10029548 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10029548 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10029548 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10029548 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10029548 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10029548 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:10029548 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:10029548 | pubmed:author | pubmed-author:BakerE NEN | lld:pubmed |
| pubmed-article:10029548 | pubmed:author | pubmed-author:WoodworthR... | lld:pubmed |
| pubmed-article:10029548 | pubmed:author | pubmed-author:MurphyM EME | lld:pubmed |
| pubmed-article:10029548 | pubmed:author | pubmed-author:MacGillivrayR... | lld:pubmed |
| pubmed-article:10029548 | pubmed:author | pubmed-author:GoFF | lld:pubmed |
| pubmed-article:10029548 | pubmed:author | pubmed-author:MasonA BAB | lld:pubmed |
| pubmed-article:10029548 | pubmed:author | pubmed-author:GrewalJJ | lld:pubmed |
| pubmed-article:10029548 | pubmed:author | pubmed-author:TanB LBL | lld:pubmed |
| pubmed-article:10029548 | pubmed:author | pubmed-author:BewleyM CMC | lld:pubmed |
| pubmed-article:10029548 | pubmed:author | pubmed-author:ShewrySS | lld:pubmed |
| pubmed-article:10029548 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10029548 | pubmed:day | 23 | lld:pubmed |
| pubmed-article:10029548 | pubmed:volume | 38 | lld:pubmed |
| pubmed-article:10029548 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10029548 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10029548 | pubmed:pagination | 2535-41 | lld:pubmed |
| pubmed-article:10029548 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
| pubmed-article:10029548 | pubmed:meshHeading | pubmed-meshheading:10029548... | lld:pubmed |
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| pubmed-article:10029548 | pubmed:meshHeading | pubmed-meshheading:10029548... | lld:pubmed |
| pubmed-article:10029548 | pubmed:meshHeading | pubmed-meshheading:10029548... | lld:pubmed |
| pubmed-article:10029548 | pubmed:meshHeading | pubmed-meshheading:10029548... | lld:pubmed |
| pubmed-article:10029548 | pubmed:meshHeading | pubmed-meshheading:10029548... | lld:pubmed |
| pubmed-article:10029548 | pubmed:meshHeading | pubmed-meshheading:10029548... | lld:pubmed |
| pubmed-article:10029548 | pubmed:meshHeading | pubmed-meshheading:10029548... | lld:pubmed |
| pubmed-article:10029548 | pubmed:meshHeading | pubmed-meshheading:10029548... | lld:pubmed |
| pubmed-article:10029548 | pubmed:meshHeading | pubmed-meshheading:10029548... | lld:pubmed |
| pubmed-article:10029548 | pubmed:meshHeading | pubmed-meshheading:10029548... | lld:pubmed |
| pubmed-article:10029548 | pubmed:meshHeading | pubmed-meshheading:10029548... | lld:pubmed |
| pubmed-article:10029548 | pubmed:meshHeading | pubmed-meshheading:10029548... | lld:pubmed |
| pubmed-article:10029548 | pubmed:meshHeading | pubmed-meshheading:10029548... | lld:pubmed |
| pubmed-article:10029548 | pubmed:meshHeading | pubmed-meshheading:10029548... | lld:pubmed |
| pubmed-article:10029548 | pubmed:meshHeading | pubmed-meshheading:10029548... | lld:pubmed |
| pubmed-article:10029548 | pubmed:meshHeading | pubmed-meshheading:10029548... | lld:pubmed |
| pubmed-article:10029548 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10029548 | pubmed:articleTitle | X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32. | lld:pubmed |
| pubmed-article:10029548 | pubmed:affiliation | Institute of Molecular Biosciences, College of Sciences, Massey University, Palmerston North, New Zealand. | lld:pubmed |
| pubmed-article:10029548 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10029548 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10029548 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:7018 | entrezgene:pubmed | pubmed-article:10029548 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10029548 | lld:pubmed |
