Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Kristina Marx"'
Autor:
Hans J.C.T. Wessels, Purva Kulkarni, Maurice van Dael, Anouk Suppers, Esther Willems, Fokje Zijlstra, Else Kragt, Jolein Gloerich, Pierre-Olivier Schmit, Stuart Pengelley, Kristina Marx, Alain J. van Gool, Dirk J. Lefeber
Publikováno v:
Journal of Advanced Research, Vol 61, Iss , Pp 179-192 (2024)
Introduction: The human plasma glycoproteome holds enormous potential to identify personalized biomarkers for diagnostics. Glycoproteomics has matured into a technology for plasma N-glycoproteome analysis but further evolution towards clinical applic
Externí odkaz:
https://doaj.org/article/047479ae6a8b4ca1b4863cf855f7ee50
Autor:
Xu Peng, Isaac Woodhouse, Gemma Hancock, Robert Parker, Kristina Marx, Julius Müller, Silvia Salatino, Thomas Partridge, Annalisa Nicastri, Hanqing Liao, Gary Kruppa, Karin Hellner, Lucy Dorrell, Nicola Ternette
Publikováno v:
iScience, Vol 26, Iss 3, Pp 106101- (2023)
Summary: Current immunotherapeutic approaches for human papillomavirus (HPV)-driven cervical cancer target the viral oncogenes E6 and E7. We report viral canonical and alternative reading frame (ARF)-derived sequences presented on cervical tumor cell
Externí odkaz:
https://doaj.org/article/7a2d88fc08a94b27b6d93df3c7c3919a
Autor:
Hans JCT Wessels, Purva Kulkarni, Maurice van Dael, Anouk Suppers, Esther Willems, Fokje Zijlstra, Else Kragt, Jolein Gloerich, Pierre-Olivier Schmit, Stuart Pengelley, Kristina Marx, Alain J van Gool, Dirk J Lefeber
The human plasma glycoproteome holds enormous potential to identify personalized biomarkers to diagnose and understand disease. Recent advances in mass spectrometry and software development are opening novel avenues to mine the glycoproteome for prot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6306b275feada2f303805853ef690222
https://doi.org/10.1101/2022.05.31.494121
https://doi.org/10.1101/2022.05.31.494121
Publikováno v:
Molecular and Cellular Proteomics
Molecular and Cellular Proteomics, 15(2), 624-641. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Molecular & Cellular Proteomics : MCP
Molecular and Cellular Proteomics, 15(2), 624-641. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Molecular & Cellular Proteomics : MCP
Site-specific glycosylation analysis is key to investigate structure-function relationships of glycoproteins, e.g. in the context of antigenicity and disease progression. The analysis, though, is quite challenging and time consuming, in particular fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6bf4e3cf02414a4d10d851fe0c2ec0de
https://hdl.handle.net/11858/00-001M-0000-0029-48D0-511858/00-001M-0000-0029-B376-7
https://hdl.handle.net/11858/00-001M-0000-0029-48D0-511858/00-001M-0000-0029-B376-7
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1394
Zwitterionic hydrophilic interaction chromatography (ZIC-HILIC) solid-phase extraction (SPE) combined with direct-infusion nanoESI mass spectrometry (MS) and tandem MS/MS is a well-suited method for the analysis of protein N-glycosylation. A site-spe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::70bd5c9cef23a168e6889b47492cac81
https://pubmed.ncbi.nlm.nih.gov/26700048
https://pubmed.ncbi.nlm.nih.gov/26700048
Publikováno v:
Methods in Molecular Biology ISBN: 9781493933396
Zwitterionic hydrophilic interaction chromatography (ZIC-HILIC) solid-phase extraction (SPE) combined with direct-infusion nanoESI mass spectrometry (MS) and tandem MS/MS is a well-suited method for the analysis of protein N-glycosylation. A site-spe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1c65420b3b6a1bcc6f46c30ebcef70c8
https://doi.org/10.1007/978-1-4939-3341-9_12
https://doi.org/10.1007/978-1-4939-3341-9_12
Publikováno v:
Journal of proteome research. 14(6)
Although wild-type hen egg white lysozyme (HEL) is lacking the consensus sequence motif NX(S/T), in 1995 Trudel et al. (Biochem. Cell Biol. 1995, 73, 307-309) proposed the existence of a low abundant N-glycosylated form of HEL; however, the identity
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2361ed487933dd35cbc2decb7a3caa42
https://pubmed.ncbi.nlm.nih.gov/25964011
https://pubmed.ncbi.nlm.nih.gov/25964011
Autor:
Uwe Möginger, Carthene R. Bazemore-Walker, Lauren E. Ball, Benjamin F. Mann, Jan Mirco Schulz, Carina Sihlbom, David Horn, Eden P. Go, Jeffrey S. Rohrer, Lipika Basumallick, Gregory O. Staples, Manfred Wuhrer, Detlev Suckau, Jonas Nilsson, Wolfgang Jabs, Richard R. Drake, Deanna C. Hurum, Christian Neusüβ, Christopher W. Cairo, Bernd Meyer, Leena Valmu, F. Altmann, Petr Pompach, William R. Alley, Michael Blank, Nancy Leymarie, Yoshinao Wada, Adnan Halim, Mellisa Ly, Daniel Kolarich, Randy M. Whittal, Yetrib Hathout, Milos V. Novotny, Jennifer T. Aguilan, Rambod Daneshfar, Joseph Zaia, Svenja-Catharina Bunz, Paul J. Hensbergen, Morten Thaysen-Andersen, Kristy J. Brown, John F. Cipollo, Clemens Gruber, Yehia Mechref, Alexandra Ruthenbeck, Megan T. Watson, Anja Resemann, Yiying Zhu, Radoslav Goldman, Markus Windwarder, Chunxia Zou, Yanming An, Henning N. Behnken, Haixu Tang, Rosa Viner, Béla Reiz, Ulrike Schweiger-Hufnagel, Nicolle H. Packer, Heather Desaire, Paula J. Griffin, Kristina Marx, Miloslav Sanda, Ron Orlando, Göran Larson, Julius O. Nyalwidhe, Karen R. Jonscher, Mark E. McComb, Ehwang Song
Publikováno v:
Molecular and Cellular Proteomics
Molecular and Cellular Proteomics, 12(10), 2935-2951
Molecular and Cellular Proteomics, 12(10), 2935-2951
One of the principal goals of glycoprotein research is to correlate glycan structure and function. Such correlation is necessary in order for one to understand the mechanisms whereby glycoprotein structure elaborates the functions of myriad proteins.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a5a82d518e0571702f3d264e5c3079f
https://hdl.handle.net/1887/100353
https://hdl.handle.net/1887/100353