Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Barbara Christen"'
Two lines of transgenic mice expressing mouse/elk and mouse/horse prion protein (PrP) hybrids, which both form a well-structured β2–α2 loop in the NMR structures at 20 °C termed rigid-loop cellular prion proteins (RL-PrP C ), presented with accu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::19ebff781cadc0db12b8e8c157de521b
https://doi.org/10.1142/9789811235795_0016
https://doi.org/10.1142/9789811235795_0016
NMR Structure of the Bank Vole Prion Protein at 20 °C Contains a Structured Loop of Residues 165–171
Publikováno v:
Journal of Molecular Biology. 383:306-312
The recent introduction of bank vole (Clethrionomys glareolus) as an additional laboratory animal for research on prion diseases revealed an important difference when compared to the mouse and the Syrian hamster, since bank voles show a high suscepti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d3cb74f3fc333a5aceace6f8e778889e
https://doi.org/10.1016/j.jmb.2008.08.045
https://doi.org/10.1016/j.jmb.2008.08.045
Publikováno v:
FEBS Journal. 275:263-270
Prion proteins (PrP) of mammals, birds, reptiles and amphibians have been successfully cloned, expressed and purified in sufficient yields to enable 3D structure determination by NMR spectroscopy in solution. More recently, PrP ortholog genes have al
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d111048d50d898eb0667edc10f9fd994
https://doi.org/10.1111/j.1742-4658.2007.06196.x
https://doi.org/10.1111/j.1742-4658.2007.06196.x
Publikováno v:
Journal of Molecular Biology. 322:1117-1133
The pancreatic polypeptide (PP), a 36-residue, C-terminally amidated polypeptide hormone is a member of the neuropeptide Y (NPY) family. Here, we have studied the structure and dynamics of bovine pancreatic polypeptide (bPP) when bound to DPC-micelle
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b29cc76023b9d760c48f575c54151366
https://doi.org/10.1016/s0022-2836(02)00889-6
https://doi.org/10.1016/s0022-2836(02)00889-6
Publikováno v:
Journal of molecular biology. 423(4)
The three-dimensional structures of prion proteins (PrPs) in the cellular form (PrP(C)) include a stacking interaction between the aromatic rings of the residues Y169 and F175, where F175 is conserved in all but two so far analyzed mammalian PrP sequ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8b5d7286c026c84e368e936afbfceb28
https://pubmed.ncbi.nlm.nih.gov/22922482
https://pubmed.ncbi.nlm.nih.gov/22922482
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 108(42)
In the otherwise highly conserved NMR structures of cellular prion proteins (PrP C ) from different mammals, species variations in a surface epitope that includes a loop linking a β-strand, β2, with a helix, α2, are associated with NMR manifestati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fbb3e3067e977f69a702333836e3b6f3
https://pubmed.ncbi.nlm.nih.gov/21987789
https://pubmed.ncbi.nlm.nih.gov/21987789
A survey of plasmids for 51 prion protein constructs from bank vole, cat, cattle, chicken, dog, elk, ferret, frog, fugu, horse, human, pig, sheep, turtle, and wallaby, and for 113 mouse prion protein constructs and variants thereof, is presented. Thi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3da99de657f2e0b6d59d691bac697fc2
https://doi.org/10.5167/uzh-32204
https://doi.org/10.5167/uzh-32204
NMR structures are presented for the recombinant construct of residues 121-230 from the tammar wallaby (Macropus eugenii) prion protein (PrP) twPrP(121-230) and for the variant mouse PrPs mPrP[Y225A,Y226A](121-231) and mPrP[V166A](121-231) at 20 degr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ad4183e76fcb882b243cd378ee71503a
Publikováno v:
The FEBS journal. 275(2)
Prion proteins (PrP) of mammals, birds, reptiles and amphibians have been successfully cloned, expressed and purified in sufficient yields to enable 3D structure determination by NMR spectroscopy in solution. More recently, PrP ortholog genes have al
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b1304020abf8d8633541feb48852df85
https://pubmed.ncbi.nlm.nih.gov/18070106
https://pubmed.ncbi.nlm.nih.gov/18070106
Autor:
Christine von Schroetter, Barbara Christen, Vicent Esteve-Moya, Christian Schorn, Dominikus A. Lysek, Lucas G. Nivón, Torsten Herrmann, Luigi Calzolai, Francesco Fiorito, Peter Güntert, Kurt Wüthrich
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 102(3)
The NMR structures of the recombinant cellular form of the prion proteins (PrP C ) of the cat ( Felis catus ), dog ( Canis familiaris ), and pig ( Sus scrofa ), and of two polymorphic forms of the prion protein from sheep ( Ovis aries ) are presented
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::89026f31e288583470bd2dbec413e4ed
https://pubmed.ncbi.nlm.nih.gov/15647367
https://pubmed.ncbi.nlm.nih.gov/15647367