Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Melissa Baerenfaenger"'
Autor:
Peter T. A. Linders, Eveline C. F. Gerretsen, Angel Ashikov, Mari-Anne Vals, Rinse de Boer, Natalia H. Revelo, Richard Arts, Melissa Baerenfaenger, Fokje Zijlstra, Karin Huijben, Kimiyo Raymond, Kai Muru, Olga Fjodorova, Sander Pajusalu, Katrin Õunap, Martin ter Beest, Dirk Lefeber, Geert van den Bogaart
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-15 (2021)
Mutations in genes critical for proper intra-Golgi transport can cause human syndromes due to defects in glycosylation of proteins. Here, the authors identify a human variant of Syntaxin-5 that causes fatal multisystem disease and mislocalization of
Externí odkaz:
https://doaj.org/article/a484fd5da84a4c6e8dc6c4421c08bd42
Autor:
Melissa Baerenfaenger, Merel A. Post, Pieter Langerhorst, Karin Huijben, Fokje Zijlstra, Joannes F. M. Jacobs, Marcel M. Verbeek, Hans J. C. T. Wessels, Dirk J. Lefeber
Publikováno v:
International Journal of Molecular Sciences, Vol 24, Iss 3, p 1937 (2023)
The glycosylation of proteins plays an important role in neurological development and disease. Glycoproteomic studies on cerebrospinal fluid (CSF) are a valuable tool to gain insight into brain glycosylation and its changes in disease. However, it is
Externí odkaz:
https://doaj.org/article/445be050d41c439e9627ca4db0d8114e
Autor:
Agnes L. Hipgrave Ederveen, Noortje de Haan, Melissa Baerenfaenger, Dirk J. Lefeber, Manfred Wuhrer
Publikováno v:
International Journal of Molecular Sciences, Vol 21, Iss 20, p 7635 (2020)
Protein N-glycosylation is a multifactorial process involved in many biological processes. A broad range of congenital disorders of glycosylation (CDGs) have been described that feature defects in protein N-glycan biosynthesis. Here, we present insig
Externí odkaz:
https://doaj.org/article/4e4cd11078cc4910bdde8d0f8a6a3c95
Autor:
Pieter Langerhorst, Melissa Baerenfaenger, Purva Kulkarni, Simon Nadal, Charissa Wijnands, Merel A. Post, Somayya Noori, Martijn M. vanDuijn, Irma Joosten, Thomas Dejoie, Alain J. van Gool, Jolein Gloerich, Dirk J. Lefeber, Hans J.C.T. Wessels, Joannes F.M. Jacobs
Multiple Myeloma (MM) is a plasma cell malignancy characterized by a monoclonal expansion of plasma cells that secrete a characteristic M-protein. This M-protein is crucial for diagnosis and monitoring of MM in the blood of patients. Recent evidence
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2543ddfa7c93b5037f7327209bda7328
https://doi.org/10.1101/2023.04.05.535540
https://doi.org/10.1101/2023.04.05.535540
Autor:
Rita Barone, Filippo Vairo, Bobby G. Ng, Jaak Jaeken, Gert Matthijs, James Pitt, Thierry Dupré, Lyndon Gallacher, Liesbeth Keldermans, Helen Michelakakis, Marina Ventouratou, Susan M. White, Sze Chern Lim, Melissa Baerenfaenger, Mirian C. H. Janssen, Angel Ashikov, Karin Huijben, Sandrine Vuillaumier-Barrot, Diana Ballhausen, Daisy Rymen, Agustí Rodríguez-Palmero, Blai Morales-Romero, Antonia Ribes, Peter Witters, Heidi Peters, Erika Souche, Eva Morava, Agata Fiumara, Pascale de Lonlay, Matthew P. Wilson, Dirk Lefeber, Wasantha Ranatunga, Alejandro Garanto, Hudson H. Freeze, Christian Thiel
Publikováno v:
American Journal of Human Genetics
r-IGTP. Repositorio Institucional de Producción Científica del Instituto de Investigación Germans Trias i Pujol
instname
The American Journal of Human Genetics
Wilson, M P, Garanto, A, Pinto e Vairo, F, Ng, B G, Ranatunga, W K, Ventouratou, M, Baerenfaenger, M, Huijben, K, Thiel, C, Ashikov, A, Keldermans, L, Souche, E, Vuillaumier-Barrot, S, Dupré, T, Michelakakis, H, Fiumara, A, Pitt, J, White, S M, Lim, S C, Gallacher, L, Peters, H, Rymen, D, Witters, P, Ribes, A, Morales-Romero, B, Rodríguez-Palmero, A, Ballhausen, D, de Lonlay, P, Barone, R, Janssen, M C H, Jaeken, J, Freeze, H H, Matthijs, G, Morava, E & Lefeber, D J 2021, ' Active site variants in STT3A cause a dominant type I congenital disorder of glycosylation with neuromusculoskeletal findings ', American Journal of Human Genetics, vol. 108, no. 11, pp. 2130-2144 . https://doi.org/10.1016/j.ajhg.2021.09.012
American Journal of Human Genetics, 108(11), 2130-2144. Cell Press
American Journal of Human Genetics, 108, 11, pp. 2130-2144
American Journal of Human Genetics, 108, 2130-2144
Am J Hum Genet
r-IGTP. Repositorio Institucional de Producción Científica del Instituto de Investigación Germans Trias i Pujol
instname
The American Journal of Human Genetics
Wilson, M P, Garanto, A, Pinto e Vairo, F, Ng, B G, Ranatunga, W K, Ventouratou, M, Baerenfaenger, M, Huijben, K, Thiel, C, Ashikov, A, Keldermans, L, Souche, E, Vuillaumier-Barrot, S, Dupré, T, Michelakakis, H, Fiumara, A, Pitt, J, White, S M, Lim, S C, Gallacher, L, Peters, H, Rymen, D, Witters, P, Ribes, A, Morales-Romero, B, Rodríguez-Palmero, A, Ballhausen, D, de Lonlay, P, Barone, R, Janssen, M C H, Jaeken, J, Freeze, H H, Matthijs, G, Morava, E & Lefeber, D J 2021, ' Active site variants in STT3A cause a dominant type I congenital disorder of glycosylation with neuromusculoskeletal findings ', American Journal of Human Genetics, vol. 108, no. 11, pp. 2130-2144 . https://doi.org/10.1016/j.ajhg.2021.09.012
American Journal of Human Genetics, 108(11), 2130-2144. Cell Press
American Journal of Human Genetics, 108, 11, pp. 2130-2144
American Journal of Human Genetics, 108, 2130-2144
Am J Hum Genet
Congenital disorders of glycosylation (CDGs) form a group of rare diseases characterized by hypoglycosylation. We here report the identification of 16 individuals from nine families who have either inherited or de novo heterozygous missense variants
Publikováno v:
Strecker, C, Bärenfänger, M, Miehe, M, Spillner, E & Meyer, B 2020, ' In Silico Evaluation of the Binding Site of Fucosyltransferase 8 and First Attempts to Synthesize an Inhibitor with Drug-Like Properties ', ChemBioChem, vol. 21, no. 13, pp. 1923-1931 . https://doi.org/10.1002/cbic.201900289
Bärenfänger, J M 2019, ' In silico evaluation of the binding site of fucosyltransferase 8 and first attempts of synthesizing an inhibitor with drug-like properties ', ChemBioChem, vol. 21, no. 13, pp. 1923-1931 . https://doi.org/10.1002/cbic.201900289
ChemBioChem, 21(13), 1923-1931. Wiley-VCH Verlag
Bärenfänger, J M 2019, ' In silico evaluation of the binding site of fucosyltransferase 8 and first attempts of synthesizing an inhibitor with drug-like properties ', ChemBioChem, vol. 21, no. 13, pp. 1923-1931 . https://doi.org/10.1002/cbic.201900289
ChemBioChem, 21(13), 1923-1931. Wiley-VCH Verlag
Core fucosylation of N-glycans is catalyzed by fucosyltransferase 8 and is associated with various types of cancer. Most reported fucosyltransferase inhibitors contain non-drug-like features, such as charged groups. New starting points for the develo
Autor:
Melissa Baerenfaenger, Bernd Meyer
Publikováno v:
Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics, 1867(6), 556-564. Elsevier
Bärenfänger, J M 2019, ' Simultaneous characterization of SNPs and N-glycans from multiple glycosylation sites of intact β-2-glycoprotein-1 (B2GP1) by ESI-qTOF-MS ', Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics, vol. 1867, no. 6, pp. 556-564 . https://doi.org/10.1016/j.bbapap.2019.03.007
Bärenfänger, J M 2019, ' Simultaneous characterization of SNPs and N-glycans from multiple glycosylation sites of intact β-2-glycoprotein-1 (B2GP1) by ESI-qTOF-MS ', Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics, vol. 1867, no. 6, pp. 556-564 . https://doi.org/10.1016/j.bbapap.2019.03.007
The highly glycosylated s-2-glycoprotein-1 (B2GP1), also called apolipoprotein H, is a 50 kDa human plasma protein with four or five N-glycosylation sites. Glycosylation of B2GP1 can impact auto antibody recognition leading to the development of anti
Publikováno v:
Glycoconjugate Journal, 36(1), 13-26. Springer Netherlands
Bärenfänger, J M 2019, ' Quantitation of Glycopeptides by ESI/MS-size of the peptide part strongly affects the relative proportions and allows discovery of new glycan compositions of Ceruloplasmin ', Glycoconjugate Journal, vol. 36, no. 1, pp. 13-26 . https://doi.org/10.1007/s10719-018-9852-5
Bärenfänger, J M 2019, ' Quantitation of Glycopeptides by ESI/MS-size of the peptide part strongly affects the relative proportions and allows discovery of new glycan compositions of Ceruloplasmin ', Glycoconjugate Journal, vol. 36, no. 1, pp. 13-26 . https://doi.org/10.1007/s10719-018-9852-5
Significant changes of glycan structures are observed in humans if diseases like cancer, arthritis or inflammation are present. Thus, interest in biomarkers based on glycan structures has rapidly emerged in recent years and monitoring disease specifi
Autor:
Sanne Ruigrok, Hans J. C. T. Wessels, Eiko K. de Jong, Susette Lauwen, Dirk Lefeber, Melissa Baerenfaenger, Anneke I. den Hollander
Publikováno v:
Experimental Eye Research, 213:108798. Academic Press Inc.
Lauwen, S, Baerenfaenger, M, Ruigrok, S, Jong, E K D, Wessels, H J C T, Hollander, A I D & Lefeber, D J 2021, ' Loss of the AMD-associated B3GLCT gene affects glycosylation of TSP1 without impairing secretion in retinal pigment epithelial cells ', Experimental Eye Research, vol. 213, 108798 . https://doi.org/10.1016/j.exer.2021.108798
Experimental Eye Research, 213
Lauwen, S, Baerenfaenger, M, Ruigrok, S, Jong, E K D, Wessels, H J C T, Hollander, A I D & Lefeber, D J 2021, ' Loss of the AMD-associated B3GLCT gene affects glycosylation of TSP1 without impairing secretion in retinal pigment epithelial cells ', Experimental Eye Research, vol. 213, 108798 . https://doi.org/10.1016/j.exer.2021.108798
Experimental Eye Research, 213
Age-related macular degeneration (AMD) has been associated with protective genetic variants in the β1-3 glucosyltransferase (B3GLCT) locus through genome-wide association studies. B3GLCT mediates modification of proteins with thrombospondin type I r
Autor:
Olga Fjodorova, Natalia H. Revelo, Eveline C F Gerretsen, Richard Arts, Kimiyo Raymond, Fokje Zijlstra, Martin ter Beest, Karin Huijben, Rinse de Boer, Angel Ashikov, Katrin Õunap, Mari-Anne Vals, Kai Muru, Geert van den Bogaart, Melissa Baerenfaenger, Peter T. A. Linders, Dirk Lefeber, Sander Pajusalu
Publikováno v:
Nature Communications, 12
Nature Communications
Nature Communications, Vol 12, Iss 1, Pp 1-15 (2021)
Nature Communications, 12, 1
Nature Communications, 12(1):6227. Nature Publishing Group
Nature Communications
Nature Communications, Vol 12, Iss 1, Pp 1-15 (2021)
Nature Communications, 12, 1
Nature Communications, 12(1):6227. Nature Publishing Group
The SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) protein syntaxin-5 (Stx5) is essential for Golgi transport. In humans, the STX5 mRNA encodes two protein isoforms, Stx5 Long (Stx5L) from the first starting methionine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::37a224e59f6199469bd35cf1f6d3b7e5
http://hdl.handle.net/2066/239969
http://hdl.handle.net/2066/239969