Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Fabian Seyffer"'
Autor:
Gaetan Barbet, Michael Schotsaert, Angela Choi, Giorgi Metreveli, J. Magarian Blander, Priyanka Nair-Gupta, Fabian Seyffer, Stephen T. Yeung, Adolfo García-Sastre, Robert Tampé, Domenico Tortorella, Kamal M. Khanna, Julien Moretti, Thomas J. Gardner
Publikováno v:
Nature immunology. 22(4)
Classic major histocompatibility complex class I (MHC-I) presentation relies on shuttling cytosolic peptides into the endoplasmic reticulum (ER) by the transporter associated with antigen processing (TAP). Viruses disable TAP to block MHC-I presentat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a4f3921d8115fcddc8d4aac4a83d297
https://pubmed.ncbi.nlm.nih.gov/33790474
https://pubmed.ncbi.nlm.nih.gov/33790474
Autor:
Michael Overholtzer, Meenakshi Banerjee, Yunjie Huang, Priyanka Nair-Gupta, Derk Amsen, J. Magarian Blander, Navpreet Tung, Sidney W. Whiteheart, Brian D. Brown, Alessia Baccarini, Fabian Seyffer, Paul A. Roche, Oliver Florey, Robert Tampé
Publikováno v:
Cell, 158(3), 506-521. Cell Press
SummaryAdaptation of the endoplasmic reticulum (ER) pathway for MHC class I (MHC-I) presentation in dendritic cells enables cross-presentation of peptides derived from phagocytosed microbes, infected cells, or tumor cells to CD8 T cells. How these pe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2de4e2badf4a41206eba03057c1e708d
https://doi.org/10.1016/j.cell.2014.04.054
https://doi.org/10.1016/j.cell.2014.04.054
Publikováno v:
FEBS Letters. 587:810-817
The Saccharomyces cerevisiae AAA+ protein Hsp104 and its Escherichia coli counterpart ClpB cooperate with Hsp70 chaperones to refold aggregated proteins and fragment prion fibrils. Hsp104/ClpB activity is regulated by interaction of the M-domain with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f26d2de29833cb7db4a1e19ac749d1a4
https://doi.org/10.1016/j.febslet.2013.02.011
https://doi.org/10.1016/j.febslet.2013.02.011
Autor:
Axel Mogk, Fabian Seyffer, Ingrid Hausser, Gabriele Bönemann, Jacomine Krijnse Locker, Nicole Kapitein, Aleksandra Pietrosiuk
Publikováno v:
Molecular Microbiology. 87:1013-1028
The multicomponent type VI secretion system (T6SS) mediates the transport of effector proteins by puncturing target membranes. T6SSs are suggested to form a contractile nanomachine, functioning similar to the cell-puncturing device of tailed bacterio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::160a12259b72295a302a8d7174c0b2a7
https://doi.org/10.1111/mmi.12147
https://doi.org/10.1111/mmi.12147
Autor:
Fabian Seyffer, Benjamin Anstett, Yuki Oguchi, Eva Kummer, Rebecca C. Wade, Regina Zahn, Bernd Bukau, Axel Mogk, Mykhaylo Berynskyy
Publikováno v:
Nature Structural & Molecular Biology. 19:1338-1346
The ring-forming AAA+ protein ClpB cooperates with the DnaK chaperone system to refold aggregated proteins in Escherichia coli. The M domain, a ClpB-specific coiled-coil structure with two wings, motif 1 and motif 2, is essential to disaggregation, b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a97b256f55c6e84e09638c66c64bc217
https://doi.org/10.1038/nsmb.2441
https://doi.org/10.1038/nsmb.2441
Autor:
Fabian Seyffer, Robert Tampé
Publikováno v:
Biochimica et biophysica acta. 1850(3)
Background ABC transporters ubiquitously found in all kingdoms of life move a broad range of solutes across membranes. Crystal structures of four distinct types of ABC transport systems have been solved, shedding light on different conformational sta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b1e47eeccadfad0222d59e57badf84ee
https://pubmed.ncbi.nlm.nih.gov/24923865
https://pubmed.ncbi.nlm.nih.gov/24923865
Autor:
Nicole, Kapitein, Gabriele, Bönemann, Aleksandra, Pietrosiuk, Fabian, Seyffer, Ingrid, Hausser, Jacomine Krijnse, Locker, Axel, Mogk
Publikováno v:
Molecular microbiology. 87(5)
The multicomponent type VI secretion system (T6SS) mediates the transport of effector proteins by puncturing target membranes. T6SSs are suggested to form a contractile nanomachine, functioning similar to the cell-puncturing device of tailed bacterio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::947865373e92fdabd7b08a70d1d5b9af
https://pubmed.ncbi.nlm.nih.gov/23289512
https://pubmed.ncbi.nlm.nih.gov/23289512
Autor:
Fabian Seyffer, Bernd Bukau, Yuki Oguchi, Eva Kummer, Axel Mogk, Victor Sourjik, Juliane Winkler, Regina Zahn, Mohit Kumar
Publikováno v:
Nat Struct Mol Biol
Bacteria, fungi and plants rescue aggregated proteins using a powerful bichaperone system composed of an Hsp70 chaperone and an Hsp100 AAA+ disaggregase. In Escherichia coli, the Hsp70 chaperone DnaK binds aggregates and targets the disaggregase ClpB
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8b768b21d7d2b60448dad321c46d2ac5
https://hdl.handle.net/21.11116/0000-000A-DDA0-8
https://hdl.handle.net/21.11116/0000-000A-DDA0-8
