Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Birgit Tiemann"'
Autor:
Aleksandra Shcherbakova, Matthias Preller, Manuel H Taft, Jordi Pujols, Salvador Ventura, Birgit Tiemann, Falk FR Buettner, Hans Bakker
Publikováno v:
eLife, Vol 8 (2019)
Previous studies demonstrated importance of C-mannosylation for efficient protein secretion. To study its impact on protein folding and stability, we analyzed both C-mannosylated and non-C-mannosylated thrombospondin type 1 repeats (TSRs) of netrin r
Externí odkaz:
https://doaj.org/article/573919a03a124259935a6d4050ce1cfe
Autor:
Hermann J. Hütte, Birgit Tiemann, Aleksandra Shcherbakova, Valerian Grote, Marcus Hoffmann, Lorenzo Povolo, Mark Lommel, Sabine Strahl, Sergey Y. Vakhrushev, Erdmann Rapp, Falk F. R. Buettner, Adnan Halim, Anne Imberty, Hans Bakker
Publikováno v:
Hütte, H J, Tiemann, B, Shcherbakova, A, Grote, V, Hoffmann, M, Povolo, L, Lommel, M, Strahl, S, Vakhrushev, S Y, Rapp, E, Buettner, F F R, Halim, A, Imberty, A & Bakker, H 2022, ' A Bacterial Mannose Binding Lectin as a Tool for the Enrichment of C-and O-Mannosylated Peptides ', Analytical Chemistry, vol. 94, no. 20, pp. 7329–7338 . https://doi.org/10.1021/acs.analchem.2c00742
Mass spectrometry (MS) easily detects C-mannosylated peptides from purified proteins but not from complex biological samples. Enrichment of specific glycopeptides by lectin affinity prior to MS analysis has been widely applied to support glycopeptide
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::046722a0a56b15903ff6c4991963c793
https://pubmed.ncbi.nlm.nih.gov/35549177
https://pubmed.ncbi.nlm.nih.gov/35549177
Autor:
Hendrik R. A. Jonker, Birgit Tiemann, Hans Bakker, Aleksandra Shcherbakova, Krishna Saxena, Harald Schwalbe
Publikováno v:
Angewandte Chemie (International Ed. in English)
Despite the great interest in glycoproteins, structural information reporting on conformation and dynamics of the sugar moieties are limited. We present a new biochemical method to express proteins with glycans that are selectively labeled with NMR
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::39c59af00da3de409dd111d0fea04af5
https://doi.org/10.1002/ange.202009489
https://doi.org/10.1002/ange.202009489
Autor:
Hans Bakker, Birgit Tiemann, Falk F. R. Buettner, Jordi Pujols, Aleksandra Shcherbakova, Salvador Ventura, Manuel H. Taft, Matthias Preller
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8e0993319c335d5abbd4693590688ee4
https://doi.org/10.7554/elife.52978.sa2
https://doi.org/10.7554/elife.52978.sa2
Autor:
Falk F. R. Buettner, Jordi Pujols, Matthias Preller, Salvador Ventura, Hans Bakker, Manuel H. Taft, Birgit Tiemann, Aleksandra Shcherbakova
Publikováno v:
eLife, Vol 8 (2019)
Dipòsit Digital de Documents de la UAB
Universitat Autònoma de Barcelona
eLife
Recercat: Dipósit de la Recerca de Catalunya
Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Recercat. Dipósit de la Recerca de Catalunya
instname
Dipòsit Digital de Documents de la UAB
Universitat Autònoma de Barcelona
eLife
Recercat: Dipósit de la Recerca de Catalunya
Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Recercat. Dipósit de la Recerca de Catalunya
instname
Previous studies demonstrated importance of C-mannosylation for efficient protein secretion. To study its impact on protein folding and stability, we analyzed both C-mannosylated and non-C-mannosylated thrombospondin type 1 repeats (TSRs) of netrin r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e8700f36a4267067e2435b45e4ca59b9
https://elifesciences.org/articles/52978
https://elifesciences.org/articles/52978
Publikováno v:
Molecular Cell, 50, 2, pp. 295-302
Molecular Cell, 50, 295-302
Molecular Cell, 50, 295-302
Item does not contain fulltext Among the different types of protein glycosylation, C-mannosylation of tryptophan residues stands out because of the unique linkage formed between sugar and protein. Instead of the typical O- or N-glycosidic linkage, a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5df63985ebdb5a6d655a9ec7b1a05077
https://doi.org/10.1016/j.molcel.2013.03.003
https://doi.org/10.1016/j.molcel.2013.03.003
Publikováno v:
Glycobiology, 23, 303-9
Glycobiology, 23, 3, pp. 303-9
Glycobiology, 23, 3, pp. 303-9
Item does not contain fulltext LARGE (like-glycosyltransferase) and LARGE2 (glycosyltransferase-like 1B (GYLTL1B)) are homologous Golgi glycosyltransferases possessing two catalytic domains with homology to members of glycosyltransferase families GT8
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e1b36ac57e9de37f61ca60c49f6187e
http://hdl.handle.net/2066/126006
http://hdl.handle.net/2066/126006