Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Julius Rabl"'
Autor:
Sara Pfister, Julius Rabl, Thomas Wiegand, Simone Mattei, Alexander A. Malär, Lauriane Lecoq, Stefan Seitz, Ralf Bartenschlager, Anja Böckmann, Michael Nassal, Daniel Boehringer, Beat H. Meier
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-15 (2023)
Nackednaviruses and hepatitis B virus (HBV) have a common non-enveloped viral ancestor. While HBV acquired an envelope during evolution, nackednaviruses remained non-enveloped. Here, Pfister et al. apply CryoEM and NMR to characterize the capsid stru
Externí odkaz:
https://doaj.org/article/8c260d6601c645e1a548bd8179f2151e
Autor:
Julius Rabl
Publikováno v:
Biomolecules, Vol 10, Iss 11, p 1503 (2020)
The K63-linkage specific deubiquitinase BRCC36 forms the core of two multi-subunit deubiquitination complexes: BRCA1-A and BRISC. BRCA1-A is recruited to DNA repair foci, edits ubiquitin signals on chromatin, and sequesters BRCA1 away from the site o
Externí odkaz:
https://doaj.org/article/cca7747870ab4c5dbf372af1978c6158
Autor:
Arka Banerjee, Meric Ataman, Maciej Jerzy Smialek, Debdatto Mookherjee, Julius Rabl, Aleksei Mironov, Lea Mues, Ludovic Enkler, Mairene Coto-Llerena, Alexander Schmidt, Daniel Boehringer, Salvatore Piscuoglio, Anne Spang, Nitish Mittal, Mihaela Zavolan
Supplementary materials for the paper "Ribosomal protein RPL39L is an efficiency factor in the cotranslational folding of proteins with alpha helical domains". Analysis of public RNA-seq data The files named "RPL39L_public_rna_seq*" are related to th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::828c05f3ce155f4cd5b336e0b4e3b810
Autor:
Michal Domanski, Emil Dedic, Maria Escura Pérez, Antoine Cléry, Sébastien Campagne, Anne-Christine Uldry, Sophie Braga, Manfred Heller, Julius Rabl, Pavel Afanasyev, Daniel Boehringer, Jiří Nováček, Frédéric T Allain, Oliver Mühlemann
Publikováno v:
Nucleic Acids Research, 50 (11)
Domanski, Michal; Dedic, Emil; Pérez, Maria Escura; Cléry, Antoine; Campagne, Sébastien; Uldry, Anne-Christine; Braga, Sophie; Heller, Manfred; Rabl, Julius; Afanasyev, Pavel; Boehringer, Daniel; Nováček, Jiří; Allain, Frédéric T; Mühlemann, Oliver (2022). 40S hnRNP particles are a novel class of nuclear biomolecular condensates. Nucleic acids research, 50(11), pp. 6300-6312. Oxford University Press 10.1093/nar/gkac457
Domanski, Michal; Dedic, Emil; Pérez, Maria Escura; Cléry, Antoine; Campagne, Sébastien; Uldry, Anne-Christine; Braga, Sophie; Heller, Manfred; Rabl, Julius; Afanasyev, Pavel; Boehringer, Daniel; Nováček, Jiří; Allain, Frédéric T; Mühlemann, Oliver (2022). 40S hnRNP particles are a novel class of nuclear biomolecular condensates. Nucleic acids research, 50(11), pp. 6300-6312. Oxford University Press 10.1093/nar/gkac457
Heterogenous nuclear ribonucleoproteins (hnRNPs) are abundant proteins implicated in various steps of RNA processing that assemble on nuclear RNA into larger complexes termed 40S hnRNP particles. Despite their initial discovery 55 years ago, our unde
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f4ec9c840302de1e53df42302d40f942
Autor:
Andreas D. Schenk, Weaam I. Mohamed, Georg Kempf, Anja Basters, Alessandro Potenza, Simone Cavadini, Kurt M. Reichermeier, Wassim Abdul Rahman, Julius Rabl, Nicolas H. Thomä
Publikováno v:
The EMBO Journal
The EMBO Journal, 40 (22)
The EMBO Journal, 40 (22)
The cullin-4-based RING-type (CRL4) family of E3 ubiquitin ligases functions together with dedicated substrate receptors. Out of the similar to 29 CRL4 substrate receptors reported, the DDB1- and CUL4-associated factor 1 (DCAF1) is essential for cell
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c2fcf45367ecd8e8de975a053e679ff5
https://resolver.caltech.edu/CaltechAUTHORS:20211021-201507835
https://resolver.caltech.edu/CaltechAUTHORS:20211021-201507835
Autor:
Andreas D. Schenk, Julius Rabl, Alessandro Potenza, Junpei Yamamoto, Dirk Schübeler, Ralph S. Grand, Shigenori Iwai, Simone Cavadini, Hitoshi Kurumizaka, Syota Matsumoto, Richard D. Bunker, Kaoru Sugasawa, Nicolas H. Thomä
Publikováno v:
Nature
Access to DNA packaged in nucleosomes is critical for gene regulation, DNA replication and DNA repair. In humans, the UV-damaged DNA-binding protein (UV-DDB) complex detects UV-light-induced pyrimidine dimers throughout the genome; however, it remain
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2402a0720129232461f395c4e1eec490
https://hdl.handle.net/20.500.14094/90006047
https://hdl.handle.net/20.500.14094/90006047
Autor:
Daniel Boehringer, Weaam I. Mohamed, Alexander Leitner, Julius Rabl, Matthias Peter, Sophia L Park
Publikováno v:
EMBO reports
EMBO Reports
EMBO Reports, 22 (11)
EMBO Reports
EMBO Reports, 22 (11)
The human GID (hGID) complex is a conserved E3 ubiquitin ligase regulating diverse biological processes, including glucose metabolism and cell cycle progression. However, the biochemical function and substrate recognition of the multi-subunit complex
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e0e309cf3c4fda4cf4a3f4adb7066636
Autor:
Shigenori Iwai, Nicolas H. Thomä, Kaoru Sugasawa, Simone Cavadini, Dirk Schübeler, Julius Rabl, Hitoshi Kurumizaka, Junpei Yamamoto, Andreas D. Schenk, Richard D. Bunker, Alessandro Potenza, Ralph S. Grand, Syota Matsumoto
Publikováno v:
Nature. 571:E6-E6
In this Article, in Fig. 1a, the 5' and 3' labels were reversed in the DNA sequence, and Fig. 4 was missing panel labels a-e. These errors have been corrected online.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::af97daaef4613d4b00e868952bbf6e18
https://doi.org/10.1038/s41586-019-1343-8
https://doi.org/10.1038/s41586-019-1343-8
Autor:
W. Abdulrahman, Adel F. M. Ibrahim, Ronald T. Hay, Martin Renatus, Aimee H. Marceau, Ulrich Hassiepen, Simone Cavadini, Antoine H.F.M. Peters, Seth M. Rubin, Julius Rabl, Jacob D. Aguirre, Tewis Bouwmeester, Richard D. Bunker, Nicolas H. Thomä, H. van Attikum, Niels Mailand, M.E. Gill, Andreas D. Schenk, Emma Branigan, Claire Guérillon, A. Andres-Pons, L. Gelman, Luijsterburg
Publikováno v:
Molecular Cell
Molecular Cell, 75 (3)
Molecular Cell, 75(3), 483-+. CELL PRESS
Rabl, J, Bunker, R D, Schenk, A D, Cavadini, S, Gill, M E, Abdulrahman, W, Andrés-Pons, A, Luijsterburg, M S, Ibrahim, A F M, Branigan, E, Aguirre, J D, Marceau, A H, Guérillon, C, Bouwmeester, T, Hassiepen, U, Peters, A H F M, Renatus, M, Gelman, L, Rubin, S M, Mailand, N, van Attikum, H, Hay, R T & Thomä, N H 2019, ' Structural Basis of BRCC36 Function in DNA Repair and Immune Regulation ', Molecular Cell, vol. 75, no. 3, pp. 483-497.e9 . https://doi.org/10.1016/j.molcel.2019.06.002
Molecular Cell, 75 (3)
Molecular Cell, 75(3), 483-+. CELL PRESS
Rabl, J, Bunker, R D, Schenk, A D, Cavadini, S, Gill, M E, Abdulrahman, W, Andrés-Pons, A, Luijsterburg, M S, Ibrahim, A F M, Branigan, E, Aguirre, J D, Marceau, A H, Guérillon, C, Bouwmeester, T, Hassiepen, U, Peters, A H F M, Renatus, M, Gelman, L, Rubin, S M, Mailand, N, van Attikum, H, Hay, R T & Thomä, N H 2019, ' Structural Basis of BRCC36 Function in DNA Repair and Immune Regulation ', Molecular Cell, vol. 75, no. 3, pp. 483-497.e9 . https://doi.org/10.1016/j.molcel.2019.06.002
Summary In mammals, ∼100 deubiquitinases act on ∼20,000 intracellular ubiquitination sites. Deubiquitinases are commonly regarded as constitutively active, with limited regulatory and targeting capacity. The BRCA1-A and BRISC complexes serve in D
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7932a90a03964af070a66d7ce8ca586b
http://europepmc.org/articles/PMC6695476
http://europepmc.org/articles/PMC6695476
Autor:
Susanne A. Kassube, Nicolas H. Thomä, Julius Rabl, Eric S. Fischer, Kerstin Böhm, Simone Cavadini, Gondichatnahalli M. Lingaraju
Publikováno v:
DNA Replication, Recombination, and Repair ISBN: 9784431558712
The timely repair of DNA damage is crucial to the maintenance of genome integrity. The DNA damage response relies on the cross talk between a large number of protein complexes and is subject to regulation by posttranslational modifications. Ubiquitin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bb720e826c0759db8d27c9efd0e5cd6d
https://doi.org/10.1007/978-4-431-55873-6_9
https://doi.org/10.1007/978-4-431-55873-6_9