Zobrazeno 1 - 10
of 24
pro vyhledávání: '"Nina O.L. Seto"'
Autor:
H.P. Nguyen, L Brade, Nina O.L. Seto, Helmut Brade, Paul Kosma, Stephen V. Evans, C.R. MacKenzie
Publikováno v:
Nature Structural & Molecular Biology. 10:1019-1025
High-resolution structures reveal how a germline antibody can recognize a range of clinically relevant carbohydrate epitopes. The germline response to a carbohydrate immunogen can be critical to survivability, with selection for antibody gene segment
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bba3a7edf8061640d5d51720b2f99e09
https://doi.org/10.1038/nsb1014
https://doi.org/10.1038/nsb1014
Autor:
Nina O.L. Seto, Sandra L. Marcus, Monica M. Palcic, Adam Szpacenko, Sonia I. Patenaude, Svetlana N. Borisova, Stephen V. Evans
Publikováno v:
Nature Structural Biology. 9:685-690
The human ABO(H) blood group antigens are produced by specific glycosyltransferase enzymes. An N-acetylgalactosaminyltransferase (GTA) uses a UDP-GalNAc donor to convert the H-antigen acceptor to the A antigen, whereas a galactosyltransferase (GTB) u
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0fd3430711b96e8db5d09fd1bbce141f
https://doi.org/10.1038/nsb832
https://doi.org/10.1038/nsb832
Autor:
Saran A. Narang, Catherine A. Compston, David R. Bundle, Monica M. Palcic, Nina O.L. Seto, Stephen V. Evans
Publikováno v:
European Journal of Biochemistry. 259:770-775
The human blood group A and B glycosyltransferases catalyze the transfer of GalNAc and Gal, to the (O)H-precursor structure Fucα(1–2)Galβ-OR to form the blood group A and B antigens, respectively. Changing four amino acids (176, 235, 266 and 268)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4e5562e8b31c95f59898520e530b2692
https://doi.org/10.1046/j.1432-1327.1999.00086.x
https://doi.org/10.1046/j.1432-1327.1999.00086.x
Publikováno v:
Carbohydrate Research. 324:161-169
Glycosyltransferases A and B utilize the donor substrates UDP-GalNAc and UDP-Gal, respectively, in the biosynthesis of the human blood group A and B trisaccharide antigens from the O(H)-acceptor substrates. These enzymes were cloned as synthetic gene
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be909ae4f478618117117438e94e4a49
https://doi.org/10.1016/s0008-6215(99)00297-9
https://doi.org/10.1016/s0008-6215(99)00297-9
Publikováno v:
Journal of Mass Spectrometry. 35:990-1002
Cysteine residues and disulfide bonds are important for protein structure and function. We have developed a simple and sensitive method for determining the presence of free cysteine (Cys) residues and disulfide bonded Cys residues in proteins (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::759ae4d639042d60be5882e52bda86ee
https://doi.org/10.1002/1096-9888(200008)35:8<990::aid-jms27>3.0.co
https://doi.org/10.1002/1096-9888(200008)35:8<990::aid-jms27>3.0.co
Publikováno v:
Glycoconjugate Journal. 16:599-606
We report the chemical synthesis of αFuc(1→2)αGal-O(CH2)7CH3 (1) an analog of the natural blood group (O)H disaccharide αFuc(1→2)βGal-OR. Compound 1 was a good substrate for recombinant blood group B glycosyltransferase (GTB) and was used as
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e0ad81bd773022ba189fd53f68583815
https://doi.org/10.1023/a:1007072832421
https://doi.org/10.1023/a:1007072832421
Autor:
Brock Schuman, Svetlana N. Borisova, Javier A. Alfaro, Asha R Johal, Nina O.L. Seto, Stephen V. Evans
The human ABO(H) A and B blood group glycosyltransferases GTA and GTB differ by only four amino acids, yet this small dissimilarity is responsible for significant differences in biosynthesis, kinetics and structure. Like other glycosyltransferases, t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::762a9772791f9a2f1941b8668818a3f3
https://doi.org/10.1107/s0907444912001801
https://doi.org/10.1107/s0907444912001801
Autor:
Stephen V. Evans, Robert Polakowski, Svetlana N. Borisova, Monica M. Palcic, Brock Schuman, Nina O.L. Seto, Mattias Persson, Roxanne C Landry, Joel T. Weadge
A common feature in the structures of GT-A-fold-type glycosyltransferases is a mobile polypeptide loop that has been observed to participate in substrate recognition and enclose the active site upon substrate binding. This is the case for the human A
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0e8d793f6cb10fba49bc2ade2c2427c1
https://europepmc.org/articles/PMC3069981/
https://europepmc.org/articles/PMC3069981/
Autor:
Robert Polakowski, Svetlana N. Borisova, Javier A. Alfaro, Stephen V. Evans, Ruixiang Blake Zheng, Yu Bai, Todd L. Lowary, Nina O.L. Seto, Mattias Persson, Monica M. Palcic, James A. Letts
Publikováno v:
The Journal of biological chemistry. 283(15)
The final step in the enzymatic synthesis of the ABO(H) blood group A and B antigens is catalyzed by two closely related glycosyltransferases, an alpha-(1-->3)-N-acetylgalactosaminyltransferase (GTA) and an alpha-(1-->3)-galactosyltransferase (GTB).
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::550391378ec68003fe0220f49a2fb23e
https://pubmed.ncbi.nlm.nih.gov/18192272
https://pubmed.ncbi.nlm.nih.gov/18192272
Autor:
Ying R. Fang, Christopher H. Barry, Svetlana N. Borisova, Monica M. Palcic, Nina O.L. Seto, James A. Letts, Natisha L. Rose, Stephen V. Evans
Publikováno v:
The Journal of biological chemistry. 281(6)
The human ABO(H) blood group A and B antigens are generated by the homologous glycosyltransferases A (GTA) and B (GTB), which add the monosaccharides GalNAc and Gal, respectively, to the cell-surface H antigens. In the first comprehensive structural
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d924549cafcfc9fd49ee8abcb792889
https://pubmed.ncbi.nlm.nih.gov/16326711
https://pubmed.ncbi.nlm.nih.gov/16326711