Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Stine Smedegaard"'
Publikováno v:
The Journal of Biological Chemistry
Guérillon, C, Smedegaard, S, Hendriks, I A, Nielsen, M L & Mailand, N 2020, ' Multisite SUMOylation restrains DNA polymerase η interactions with DNA damage sites ', Journal of Biological Chemistry, vol. 295, pp. 8350-8362 . https://doi.org/10.1074/jbc.RA120.013780
Guérillon, C, Smedegaard, S, Hendriks, I A, Nielsen, M L & Mailand, N 2020, ' Multisite SUMOylation restrains DNA polymerase η interactions with DNA damage sites ', Journal of Biological Chemistry, vol. 295, pp. 8350-8362 . https://doi.org/10.1074/jbc.RA120.013780
Translesion DNA synthesis (TLS) mediated by low-fidelity DNA polymerases is an essential cellular mechanism for bypassing DNA lesions that obstruct DNA replication progression. However, the access of TLS polymerases to the replication machinery must
Autor:
Chunaram Choudhary, Petra Beli, Sofie V. Nielsen, Tina Thorslund, Niels Mailand, Anna Mosbech, Konstantinos Kagias, Garry G Sedgwick, Simon Bekker-Jensen, Claudia Lukas, Ian Gibbs-Seymour, Jiri Lukas, Stine Smedegaard, Lou Klitgaard Povlsen, Roger Pocock, Rasmus Hartmann-Petersen
Publikováno v:
Nature Structural & Molecular Biology. 19:1084-1092
Ubiquitin-mediated processes orchestrate critical DNA-damage signaling and repair pathways. We identify human DVC1 (C1orf124; Spartan) as a cell cycle-regulated anaphase-promoting complex (APC) substrate that accumulates at stalled replication forks.
Autor:
Tine K. Nielsen, Charlotte Svensson, Diego Iglesias-Gato, Amilcar Flores-Morales, Giuseppe Cazzamali, Christina Aaen Andresen, Stine Smedegaard, Michael L. Nielsen, Kathrine B. Sylvestersen
Publikováno v:
The Journal of biological chemistry. 289(4)
The ankyrin and SOCS (suppressor of cytokine signaling) box (ASB) family of proteins function as the substrate recognition subunit in a subset of Elongin-Cullin-SOCS (ECS) E3 ubiquitin ligases. Despite counting 18 members in humans, the identity of t
Autor:
Matthias Mann, Francisco J. Blanco, Yasuyoshi Oka, Anja Groth, Kyosuke Nakamura, Niels Mailand, Gulnahar B. Mortuza, Simon Bekker-Jensen, Guillermo Montoya, Markus Räschle, Stine Smedegaard, Saskia Hoffmann, Yunpeng Feng, Alain Ibáñez de Opakua
Publikováno v:
Hoffmann, S, Smedegaard, S, Nakamura, K, Mortuza, G B, Räschle, M, Ibañez de Opakua, A, Oka, Y, Feng, Y, Blanco, F J, Mann, M, Montoya, G, Groth, A, Bekker-Jensen, S & Mailand, N 2016, ' TRAIP is a PCNA-binding ubiquitin ligase that protects genome stability after replication stress ', The Journal of Cell Biology, vol. 212, no. 1, pp. 63-75 . https://doi.org/10.1083/jcb.201506071
The Journal of Cell Biology
The Journal of Cell Biology
The E3 ubiquitin ligase TRAIP associates with replication forks through direct interaction with PCNA, promoting checkpoint signaling and genome stability after replication stress.
Cellular genomes are highly vulnerable to perturbations to chromo
Cellular genomes are highly vulnerable to perturbations to chromo