Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Ida Signe Bohse Larsen"'
Publikováno v:
eLife, Vol 9 (2020)
UDP-glucose:glycoprotein glucosyltransferase (UGGT) 1 and 2 are central hubs in the chaperone network of the endoplasmic reticulum (ER), acting as gatekeepers to the early secretory pathway, yet little is known about their cellular clients. These two
Externí odkaz:
https://doaj.org/article/e9b749e658c04d258b97db0520436f21
Autor:
Katarina Valoskova, Julia Biebl, Marko Roblek, Shamsi Emtenani, Attila Gyoergy, Michaela Misova, Aparna Ratheesh, Patricia Reis-Rodrigues, Kateryna Shkarina, Ida Signe Bohse Larsen, Sergey Y Vakhrushev, Henrik Clausen, Daria E Siekhaus
Publikováno v:
eLife, Vol 8 (2019)
Aberrant display of the truncated core1 O-glycan T-antigen is a common feature of human cancer cells that correlates with metastasis. Here we show that T-antigen in Drosophila melanogaster macrophages is involved in their developmentally programmed t
Externí odkaz:
https://doaj.org/article/f6c7c1be67ed4f21b72e54f2ceaf8ed1
Autor:
Ida Signe Bohse Larsen, Lorenzo Povolo, Luping Zhou, Weihua Tian, Kasper Johansen Mygind, John Hintze, Chen Jiang, Verity Hartill, Katrina Prescott, Colin A. Johnson, Sureni V. Mullegama, Allyn McConkie-Rosell, Marie McDonald, Lars Hansen, Sergey Y. Vakhrushev, Katrine T. Schjoldager, Henrik Clausen, Thomas Worzfeld, Hiren J. Joshi, Adnan Halim
Publikováno v:
Larsen, I S B, Povolo, L, Zhou, L, Tian, W, Mygind, K J, Hintze, J, Jiang, C, Hartill, V, Prescott, K, Johnson, C A, Mullegama, S V, McConkie-Rosell, A, McDonald, M, Hansen, L, Vakhrushev, S Y, Schjoldager, K T, Clausen, H, Worzfeld, T, Joshi, H J & Halim, A 2023, ' The SHDRA syndrome-associated gene TMEM260 encodes a protein-specific O-mannosyltransferase ', Proceedings of the National Academy of Sciences of the United States of America, vol. 120, no. 21, pp. e2302584120 . https://doi.org/10.1073/pnas.2302584120
Mutations in the TMEM260 gene cause structural heart defects and renal anomalies syndrome, but the function of the encoded protein remains unknown. We previously reported wide occurrence of O-mannose glycans on extracellular immunoglobulin, plexin, t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::002d22943d971c680b2f7b4e379c7c4f
https://doi.org/10.1073/pnas.2302584120
https://doi.org/10.1073/pnas.2302584120
Autor:
Ida Signe Bohse Larsen, Adnan Halim, Jill B. Graham, Johan C. Sunryd, Dominque Alfandari, Ketan Mathavan, Daniel N. Hebert, Emma Weir, Hélène Cousin, Henrik Clausen
Publikováno v:
Molecular Biology of the Cell
Graham, J B, Sunryd, J C, Mathavan, K, Weir, E, Larsen, I S B, Halim, A, Clausen, H, Cousin, H, Alfandari, D & Hebert, D N 2020, ' Endoplasmic reticulum transmembrane protein TMTC3 contributes to O-mannosylation of E-cadherin, cellular adherence, and embryonic gastrulation ', Molecular Biology of the Cell, vol. 31, no. 3, pp. 167-183 . https://doi.org/10.1091/mbc.E19-07-0408
Graham, J B, Sunryd, J C, Mathavan, K, Weir, E, Larsen, I S B, Halim, A, Clausen, H, Cousin, H, Alfandari, D & Hebert, D N 2020, ' Endoplasmic reticulum transmembrane protein TMTC3 contributes to O-mannosylation of E-cadherin, cellular adherence, and embryonic gastrulation ', Molecular Biology of the Cell, vol. 31, no. 3, pp. 167-183 . https://doi.org/10.1091/mbc.E19-07-0408
Protein glycosylation plays essential roles in protein structure, stability, and activity such as cell adhesion. The cadherin superfamily of adhesion molecules carry O-linked mannose glycans at conserved sites and it was recently demonstrated that th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cd3b870848eea9554fa6de1f97dfbb1d
http://europepmc.org/articles/PMC7001481
http://europepmc.org/articles/PMC7001481
Publikováno v:
eLife, Vol 9 (2020)
Adams, B M, Canniff, N P, Guay, K P, Larsen, I S B & Hebert, D N 2020, ' Quantitative glycoproteomics reveals cellular substrate selectivity of the ER protein quality control sensors UGGT1 and UGGT2 ', eLife, vol. 9 . https://doi.org/10.7554/eLife.63997
eLife
Adams, B M, Canniff, N P, Guay, K P, Larsen, I S B & Hebert, D N 2020, ' Quantitative glycoproteomics reveals cellular substrate selectivity of the ER protein quality control sensors UGGT1 and UGGT2 ', eLife, vol. 9 . https://doi.org/10.7554/eLife.63997
eLife
UDP-glucose: glycoprotein glucosyltransferase (UGGT) 1 and 2 are central hubs in the chaperone network of the endoplasmic reticulum (ER), acting as gatekeepers to the early secretory pathway yet little is known about their cellular clients. These two
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b6fb830043097b9444d088afd4a3bfc
https://doi.org/10.7554/elife.63997
https://doi.org/10.7554/elife.63997
Autor:
Shengjun Wang, Zhang Yang, Yoshiki Narimatsu, Katrine T. Schjoldager, Christoffer K. Goth, Sarah L. King, Tongzhong Ju, Lars Hansen, Eric P. Bennett, María F Festari, Malene Bech Vester-Christensen, Ulla Mandel, Catharina Steentoft, Kelley W. Moremen, Ida Signe Bohse Larsen
Publikováno v:
Glycobiology
Complex carbohydrates serve a wide range of biological functions in cells and tissues, and their biosynthesis involves more than 200 distinct glycosyltransferases (GTfs) in human cells. The kinetic properties, cellular expression patterns and subcell
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dfe415f18163a1fd4f628b304d97221c
https://pubmed.ncbi.nlm.nih.gov/31172184
https://pubmed.ncbi.nlm.nih.gov/31172184
Autor:
Attila Gyoergy, Sergey Y. Vakhrushev, Marko Roblek, Patricia Reis-Rodrigues, Henrik Clausen, Aparna Ratheesh, Michaela Misova, Kateryna Shkarina, Daria E Siekhaus, Katarina Valoskova, Emtenani S, Julia Biebl, Ida Signe Bohse Larsen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f011b126ebadcab85ac48f66b42f38bc
https://doi.org/10.7554/elife.41801.032
https://doi.org/10.7554/elife.41801.032
Publikováno v:
Current Opinion in Structural Biology
Larsen, I S B, Narimatsu, Y, Clausen, H, Joshi, H J & Halim, A 2019, ' Multiple distinct O-Mannosylation pathways in eukaryotes ', Current Opinion in Structural Biology, vol. 56, pp. 171-178 . https://doi.org/10.1016/j.sbi.2019.03.003
Larsen, I S B, Narimatsu, Y, Clausen, H, Joshi, H J & Halim, A 2019, ' Multiple distinct O-Mannosylation pathways in eukaryotes ', Current Opinion in Structural Biology, vol. 56, pp. 171-178 . https://doi.org/10.1016/j.sbi.2019.03.003
Protein O-mannosylation (O-Man), originally discovered in yeast five decades ago, is an important post-translational modification (PTM) conserved from bacteria to humans, but not found in plants or nematodes. Until recently, the homologous family of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b8c9a8df107b9372b2c43a93fb28d19f
https://pubmed.ncbi.nlm.nih.gov/30999272
https://pubmed.ncbi.nlm.nih.gov/30999272
Autor:
Ewa Zatorska, Sabine Strahl, Henrik Clausen, Martin Loibl, Markus Aebi, Adnan Halim, Ida Signe Bohse Larsen, Joan Castells-Ballester, Martin Zauser, Andreas Essig, Hiren J. Joshi, Patrick Neubert
Publikováno v:
Molecular & Cellular Proteomics : MCP
Molecular & Cellular Proteomics, 15 (4)
Neubert, P, Halim, A, Zauser, M, Essig, A, Joshi, H J, Zatorska, E, Larsen, I S B, Loibl, M, Castells-Ballester, J, Aebi, M, Clausen, H & Strahl, S 2016, ' Mapping the O-Mannose Glycoproteome in Saccharomyces cerevisiae ', Molecular and Cellular Proteomics, vol. 15, no. 4, pp. 1323-37 . https://doi.org/10.1074/mcp.M115.057505
Molecular & Cellular Proteomics, 15 (4)
Neubert, P, Halim, A, Zauser, M, Essig, A, Joshi, H J, Zatorska, E, Larsen, I S B, Loibl, M, Castells-Ballester, J, Aebi, M, Clausen, H & Strahl, S 2016, ' Mapping the O-Mannose Glycoproteome in Saccharomyces cerevisiae ', Molecular and Cellular Proteomics, vol. 15, no. 4, pp. 1323-37 . https://doi.org/10.1074/mcp.M115.057505
O-Mannosylation is a vital protein modification conserved from fungi to humans. Yeast is a perfect model to study this post-translational modification, because in contrast to mammals O-mannosylation is the only type of O-glycosylation. In an essentia
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::564ab2670f9d15934acc105eda9a8cde
http://europepmc.org/articles/PMC4824858
http://europepmc.org/articles/PMC4824858