Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Ludwig Sinn"'
Autor:
Federica Agostini, Ludwig Sinn, Daniel Petras, Christian J. Schipp, Vladimir Kubyshkin, Allison Ann Berger, Pieter C. Dorrestein, Juri Rappsilber, Nediljko Budisa, Beate Koksch
Publikováno v:
ACS Central Science, Vol 7, Iss 1, Pp 81-92 (2020)
Externí odkaz:
https://doaj.org/article/f25c840e9c8042a2ae6989f1c3079b99
Autor:
Sofia Banchenko, Ferdinand Krupp, Christine Gotthold, Jörg Bürger, Andrea Graziadei, Francis J O'Reilly, Ludwig Sinn, Olga Ruda, Juri Rappsilber, Christian M T Spahn, Thorsten Mielke, Ian A Taylor, David Schwefel
Publikováno v:
PLoS Pathogens, Vol 17, Iss 8, p e1009775 (2021)
Viruses have evolved means to manipulate the host's ubiquitin-proteasome system, in order to down-regulate antiviral host factors. The Vpx/Vpr family of lentiviral accessory proteins usurp the substrate receptor DCAF1 of host Cullin4-RING ligases (CR
Externí odkaz:
https://doaj.org/article/b63e6e33cdeb4efb8f380f91c2f56491
We present Slice-PASEF, a novel mass spectrometry technology based on trapped ion mobility separation of ions. Slice-PASEF allows to achieve the theoretical maximum of MS/MS sensitivity and boosts proteomics of low sample amounts. Leveraging Slice-PA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fefc08c9fd9541282441c1b8a77b9299
https://doi.org/10.1101/2022.10.31.514544
https://doi.org/10.1101/2022.10.31.514544
Publikováno v:
Kolbowski, L, Lenz, S, Fischer, L, Sinn, L, O'Reilly, F J & Rappsilber, J 2022, ' Improved peptide backbone fragmentation is the primary advantage of MS-cleavable crosslinkers ', Analytical Chemistry, vol. 94, no. 22, pp. 7779-7786 . https://doi.org/10.1021/acs.analchem.1c05266
Proteome-wide crosslinking mass spectrometry studies have coincided with the advent of mass spectrometry (MS)-cleavable crosslinkers that can reveal the individual masses of the two crosslinked peptides. However, recently, such studies have also been
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7612f8364dacf1a5b83328a6d5e7f504
Autor:
Marta Mendes, Francis J. O’Reilly, Marchel Stuiver, Petra S J Ryl, Juri Rappsilber, Lutz Fischer, Michael Bohlke-Schneider, Lisa Budzinski, Swantje Lenz, Ludwig Sinn
Publikováno v:
Ryl, P S J, Bohlke-schneider, M, Lenz, S, Fischer, L, Budzinski, L, Stuiver, M, Mendes, M M L, Sinn, L, O’reilly, F J & Rappsilber, J 2020, ' In situ structural restraints from cross-linking mass spectrometry in human Mitochondria ', Journal Of Proteome Research, vol. 19, no. 1, pp. 327-336 . https://doi.org/10.1021/acs.jproteome.9b00541
Journal of Proteome Research
Journal of Proteome Research
The field of structural biology is increasingly focusing on studying proteins in situ, i.e., in their greater biological context. Cross-linking mass spectrometry (CLMS) is contributing to this effort, typically through the use of mass spectrometry (M
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d8934297138779f3181fa06fd2447f97
https://doi.org/10.1021/acs.jproteome.9b00541
https://doi.org/10.1021/acs.jproteome.9b00541
Autor:
Byung-Gil Lee, Frank Bürmann, Thane Than, Jan Löwe, Bin Hu, Juri Rappsilber, Ludwig Sinn, Francis J. O’Reilly, Kim Nasmyth, Stanislau Yatskevich
Publikováno v:
Nature Structural & Molecular Biology. 26:227-236
Structural maintenance of chromosomes (SMC)-kleisin complexes organize chromosomal DNAs in all domains of life, where they have key roles in chromosome segregation, DNA repair and regulation of gene expression. They function through topological entra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0eff1abee399e10c48864552ac39b15d
https://doi.org/10.1038/s41594-019-0196-z
https://doi.org/10.1038/s41594-019-0196-z
Crosslinking mass spectrometry (Crosslinking MS) has developed into a robust technique that is increasingly used to investigate the interactomes of organelles and cells. However, the incomplete and noisy information in the spectra limits the numbers
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5a7eb30b0a0495b2e96672f750ded898
https://doi.org/10.1101/2021.03.08.432999
https://doi.org/10.1101/2021.03.08.432999
Publikováno v:
Nature Communications
Lenz, S, Sinn, L, O'Reilly, F J, Fischer, L, Wegner, F & Rappsilber, J 2021, ' Reliable identification of protein-protein interactions by crosslinking mass spectrometry ', Nature Communications, vol. 12, 3564 . https://doi.org/10.1038/s41467-021-23666-z
Nature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
Lenz, S, Sinn, L, O'Reilly, F J, Fischer, L, Wegner, F & Rappsilber, J 2021, ' Reliable identification of protein-protein interactions by crosslinking mass spectrometry ', Nature Communications, vol. 12, 3564 . https://doi.org/10.1038/s41467-021-23666-z
Nature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
Protein-protein interactions govern most cellular pathways and processes, and multiple technologies have emerged to systematically map them. Assessing the error of interaction networks has been a challenge. Crosslinking mass spectrometry is currently
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::99ca7d1c60995bd53569651de8a82523
https://doi.org/10.1101/2020.05.25.114256
https://doi.org/10.1101/2020.05.25.114256
Autor:
Pilar Gutiérrez-Escribano, Matteo Allegretti, Jan Löwe, Francis J. O’Reilly, Christopher Cawood, Luis Aragón, Ludwig Sinn, Martin Beck, Byung-Gil Lee, Christian H. Haering, Léa Lecomte, Juri Rappsilber, Fabian Merkel, Takanori Nakane, Sol Bravo, Markus Hassler, Marc Kschonsak
Publikováno v:
Nat Struct Mol Biol
Nature Structural & Molecular Biology
Nature Structural & Molecular Biology
Complexes containing a pair of structural maintenance of chromosomes (SMC) family proteins are fundamental for the three-dimensional (3D) organization of genomes in all domains of life. The eukaryotic SMC complexes cohesin and condensin are thought t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9787bd257114a4c8cf8b0299b0ece5c3
https://pubmed.ncbi.nlm.nih.gov/32661420
https://pubmed.ncbi.nlm.nih.gov/32661420
Autor:
Neil Singh, Cedric Blötz, Wim J. H. Hagen, Francis J. O’Reilly, Ludwig Sinn, Swantje Lenz, Jörg Stülke, Andrea Graziadei, Patrick Cramer, Julia Mahamid, Liang Xue, Dimitry Tegunov, Juri Rappsilber
Publikováno v:
Fac Rev
O'Reilly, F J, Xue, L, Graziadei, A, Sinn, L, Lenz, S, Tegunov, D, Blötz, C, Singh, N, Hagen, W J H, Cramer, P, Stülke, J, Mahamid, J & Rappsilber, J 2020, ' In-cell architecture of an actively transcribing-translating expressome ', Science, vol. 369, no. 6503, pp. 554-557 . https://doi.org/10.1126/science.abb3758
Science
bioRxiv
O'Reilly, F J, Xue, L, Graziadei, A, Sinn, L, Lenz, S, Tegunov, D, Blötz, C, Singh, N, Hagen, W J H, Cramer, P, Stülke, J, Mahamid, J & Rappsilber, J 2020, ' In-cell architecture of an actively transcribing-translating expressome ', Science, vol. 369, no. 6503, pp. 554-557 . https://doi.org/10.1126/science.abb3758
Science
bioRxiv
Although much is known about the machinery that executes fundamental processes of gene expression in cells, much also remains to be learned about how that machinery works. A recent paper by O’Reilly et al. reports a major step forward in the direct
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1566ce803de4b7ca020222713aa49e3
https://pubmed.ncbi.nlm.nih.gov/35146496
https://pubmed.ncbi.nlm.nih.gov/35146496