Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Mikail D. Levasseur"'
Publikováno v:
CHIMIA, Vol 75, Iss 4, Pp 323-328 (2021)
Well-defined containers constructed from multiple protein subunits are a unique class of nanomaterial useful in supramolecular chemistry and biology. These protein cages are widespread in nature, where they are responsible for a diversity of importan
Externí odkaz:
https://doaj.org/article/4c3c8d52ea0144cea67c4591ccb1c8c4
Autor:
Hanne L. P. Tytgat, Chia-wei Lin, Mikail D. Levasseur, Markus B. Tomek, Christoph Rutschmann, Jacqueline Mock, Nora Liebscher, Naohiro Terasaka, Yusuke Azuma, Michael Wetter, Martin F. Bachmann, Donald Hilvert, Markus Aebi, Timothy G. Keys
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-10 (2019)
Established bacterial glycoengineering platforms limit access to protein and glycan substrates. Here the authors design a cytoplasmic protein glycosylation system, Glycoli, to generate a variety of multivalent glycostructures.
Externí odkaz:
https://doaj.org/article/ac3f91e741e14ae68b947f045f6333f3
Autor:
Mikail D. Levasseur, Raphael Hofmann, Thomas G. W. Edwardson, Svenja Hehn, Manutsawee Thanaburakorn, Jeffrey W. Bode, Donald Hilvert
Publikováno v:
Chembiochem : a European journal of chemical biology. 23(20)
Although viruses have been successfully repurposed as vaccines, antibiotics, and anticancer therapeutics, they also raise concerns regarding genome integration and immunogenicity. Virus-like particles and non-viral protein cages represent a potential
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bf7d734d84adb31d9d3d047b1669e448
https://pubmed.ncbi.nlm.nih.gov/35951442
https://pubmed.ncbi.nlm.nih.gov/35951442
Autor:
Thomas G. W. Edwardson, Mikail D. Levasseur, Stephan Tetter, Angela Steinauer, Mao Hori, Donald Hilvert
Publikováno v:
Chemical Reviews, 122 (9)
Proteins that self-assemble into polyhedral shell-like structures are useful molecular containers both in nature and in the laboratory. Here we review efforts to repurpose diverse protein cages, including viral capsids, ferritins, bacterial microcomp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::05693380c022de76a8418e1ead2a29ed
https://pubmed.ncbi.nlm.nih.gov/35394752
https://pubmed.ncbi.nlm.nih.gov/35394752
Autor:
Elodie Pramil, Olivier Lequin, Thomas Denèfle, Pascal Grondin, Ana Carolina Martínez-Torres, H. Merle-Beral, Estelle Odile, Fabrice Viviani, Luis Gómez-Morales, Santos A. Susin, Mikail D. Levasseur, Linda Herbi, Philippe Karoyan, Eva Lardé, Yann Lamotte, Nicolas Ancellin, Kenny Herry, Clara Newton
Publikováno v:
Journal of Medicinal Chemistry. 62:7656-7668
In order to optimize the potency of the first serum-stable peptide agonist of CD47 (PKHB1) in triggering regulated cell death of cancer cells, we designed a maturation process aimed to mimic the trimeric structure of the thrombospondin-1/CD47 binding
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::55e95163835ac5bfa2e82ae0ed04fe81
https://doi.org/10.1021/acs.jmedchem.9b00024
https://doi.org/10.1021/acs.jmedchem.9b00024
Publikováno v:
CHIMIA, Vol 75, Iss 4, Pp 323-328 (2021)
Chimia, 75 (4)
Chimia, 75 (4)
Well-defined containers constructed from multiple protein subunits are a unique class of nanomaterial useful in supramolecular chemistry and biology. These protein cages are widespread in nature, where they are responsible for a diversity of importan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c25758fb1b93d885ca3b96dc7cb3eda5
https://pubmed.ncbi.nlm.nih.gov/33902803
https://pubmed.ncbi.nlm.nih.gov/33902803
Autor:
Takahiro Hayashi, Donald Hilvert, Shiksha Mantri, Maria Reichenbach, Ying Waeckerle-Men, Pål Johansen, Mikail D. Levasseur, Svenja Hehn
Publikováno v:
ACS Chemical Biology, 16 (5)
Nanoparticle-based delivery systems have shown great promise for theranostics and bioimaging on the laboratory scale due to favorable pharmacokinetics and biodistribution. In this study, we examine the utility of a cage-forming variant of the protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::863b516ac81b0758421bd95c52a8600c
https://pubmed.ncbi.nlm.nih.gov/33881303
https://pubmed.ncbi.nlm.nih.gov/33881303
Autor:
Martin F. Bachmann, Markus B. Tomek, Christoph Rutschmann, Yusuke Azuma, Naohiro Terasaka, Markus Aebi, Chia-Wei Lin, Donald Hilvert, Jacqueline Mock, Hanne L. P. Tytgat, Michael Wetter, Mikail D. Levasseur, Nora Liebscher, Timothy G. Keys
Publikováno v:
Nature Communications, 10 (1)
Nature Communications, Vol 10, Iss 1, Pp 1-10 (2019)
Tytgat, Hanne L P; Lin, Chia-Wei; Levasseur, Mikail D; Tomek, Markus B; Rutschmann, Christoph; Mock, Jacqueline; Liebscher, Nora; Terasaka, Naohiro; Azuma, Yusuke; Wetter, Michael; Bachmann, Martin F.; Hilvert, Donald; Aebi, Markus; Keys, Timothy G (2019). Cytoplasmic glycoengineering enables biosynthesis of nanoscale glycoprotein assemblies. Nature communications, 10(1), p. 5403. Springer Nature 10.1038/s41467-019-13283-2
Nature Communications 10 (2019) 1
Nature Communications, 10(1)
Nature Communications
Nature Communications, Vol 10, Iss 1, Pp 1-10 (2019)
Tytgat, Hanne L P; Lin, Chia-Wei; Levasseur, Mikail D; Tomek, Markus B; Rutschmann, Christoph; Mock, Jacqueline; Liebscher, Nora; Terasaka, Naohiro; Azuma, Yusuke; Wetter, Michael; Bachmann, Martin F.; Hilvert, Donald; Aebi, Markus; Keys, Timothy G (2019). Cytoplasmic glycoengineering enables biosynthesis of nanoscale glycoprotein assemblies. Nature communications, 10(1), p. 5403. Springer Nature 10.1038/s41467-019-13283-2
Nature Communications 10 (2019) 1
Nature Communications, 10(1)
Nature Communications
Glycosylation of proteins profoundly impacts their physical and biological properties. Yet our ability to engineer novel glycoprotein structures remains limited. Established bacterial glycoengineering platforms require secretion of the acceptor prote
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5b83ff2af8fa8f17889cae3c4ac46b8e
https://hdl.handle.net/20.500.11850/383659
https://hdl.handle.net/20.500.11850/383659
Autor:
Petra Lukacik, Shabaz Mohammed, Lucia Marti, James Patrick McIvor, Andrea Lia, Abhinav Kumar, Alessandro T. Caputo, Snežana Vasiljević, Kristin Qian, Angelo Santino, Martin A. Walsh, Souradeep Basu, Johan C. Hill, Kyle Dent, Colette B. Lipp, Pietro Roversi, Dritan Siliqi, Mikail D. Levasseur, Dominic S. Alonzi, Thomas Waksman, Yentli Soto Albrecht, Nicole Zitzmann
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America 114 (2017): 8544–8549. doi:10.1073/pnas.1703682114
info:cnr-pdr/source/autori:Roversi P.; Marti L.; Caputo A.T.; Alonzi D.S.; Hill J.C.; Dent K.C.; Kumar A.; Levasseur M.D.; Lia A.; Waksman T.; Basu S.; Soto Albrecht Y.; Qian K.; McIvor J.P.; Lipp C.B.; Siliqi D.; Vasiljevic S.; Mohammed S.; Lukacik P.; Walsh M.A.; Santino A.; Zitzmann N./titolo:Interdomain conformational flexibility underpins the activity of UGGT, the eukaryotic glycoprotein secretion checkpoint/doi:10.1073%2Fpnas.1703682114/rivista:Proceedings of the National Academy of Sciences of the United States of America/anno:2017/pagina_da:8544/pagina_a:8549/intervallo_pagine:8544–8549/volume:114
info:cnr-pdr/source/autori:Roversi P.; Marti L.; Caputo A.T.; Alonzi D.S.; Hill J.C.; Dent K.C.; Kumar A.; Levasseur M.D.; Lia A.; Waksman T.; Basu S.; Soto Albrecht Y.; Qian K.; McIvor J.P.; Lipp C.B.; Siliqi D.; Vasiljevic S.; Mohammed S.; Lukacik P.; Walsh M.A.; Santino A.; Zitzmann N./titolo:Interdomain conformational flexibility underpins the activity of UGGT, the eukaryotic glycoprotein secretion checkpoint/doi:10.1073%2Fpnas.1703682114/rivista:Proceedings of the National Academy of Sciences of the United States of America/anno:2017/pagina_da:8544/pagina_a:8549/intervallo_pagine:8544–8549/volume:114
Glycoproteins traversing the eukaryotic secretory pathway begin life in the endoplasmic reticulum (ER), where their folding is surveyed by the 170 kDa UDP-glucose:glycoprotein glucosyltransferase (UGGT). The enzyme acts as the single glycoprotein fol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::92a7783e7d55e7e326dc2c215686d665
Autor:
Peer-Hendrik Kuhn, Mikail D. Levasseur, Kathryn M. Munro, Iryna Voytyuk, Bart De Strooper, Regina Feederle, Stefan F. Lichtenthaler, Johanna Wanngren, Martina Pigoni, Stephan A. Müller, Hiroshi Takeshima, Brian Joel Hrupka, Jenny M. Gunnersen
Publikováno v:
Molecular Neurodegeneration
Molecular neurodegeneration 11(1), 67 (2016). doi:10.1186/s13024-016-0134-z
Molecular neurodegeneration 11(1), 67 (2016). doi:10.1186/s13024-016-0134-z
Background The protease BACE1 (beta-site APP cleaving enzyme) is a major drug target in Alzheimer’s disease. However, BACE1 therapeutic inhibition may cause unwanted adverse effects due to its additional functions in the nervous system, such as in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b381cbe1dab3cd910ed4eb42e020cef
https://doi.org/10.1186/s13024-016-0134-z
https://doi.org/10.1186/s13024-016-0134-z