Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Caio A. Rebula"'
Autor:
Signe M. Schenstrøm, Caio A. Rebula, Michael H. Tatham, Ruth Hendus-Altenburger, Isabelle Jourdain, Ronald T. Hay, Birthe B. Kragelund, Rasmus Hartmann-Petersen
Publikováno v:
Cell Reports, Vol 25, Iss 4, Pp 862-870 (2018)
Summary: Dss1 (also known as Sem1) is a conserved, intrinsically disordered protein with a remarkably broad functional diversity. It is a proteasome subunit but also associates with the BRCA2, RPA, Csn12-Thp1, and TREX-2 complexes. Accordingly, Dss1
Externí odkaz:
https://doaj.org/article/a5aeda8ecbde481c8d4936444ea5853b
Publikováno v:
Biomolecules, Vol 4, Iss 3, Pp 646-661 (2014)
In their natural environment, cells are regularly exposed to various stress conditions that may lead to protein misfolding, but also in the absence of stress, misfolded proteins occur as the result of mutations or failures during protein synthesis. S
Externí odkaz:
https://doaj.org/article/d4e1404010114cd1991199d8df098471
Autor:
Birthe B. Kragelund, Rasmus Hartmann-Petersen, Caio A. Rebula, Vikram Govind Panse, Signe M. Schenstrøm
Publikováno v:
Trends Biochem Sci.
Trends in Biochemical Sciences
Trends in Biochemical Sciences
DSS1/Sem1 is a versatile intrinsically disordered protein. Besides being a bona fide subunit of the 26S proteasome, DSS1 associates with other protein complexes, including BRCA2-RPA, involved in homologous recombination; the Csn12-Thp3 complex, invol
Autor:
Rasmus Hartmann-Petersen, Ruth Hendus-Altenburger, Michael H. Tatham, Caio A. Rebula, Isabelle Jourdain, Signe M. Schenstrøm, Birthe B. Kragelund, Ronald T. Hay
Publikováno v:
Schenstrøm, S M, Rebula, C A, Tatham, M H, Hendus-Altenburger, R, Jourdain, I, Hay, R T, Kragelund, B B & Hartmann-Petersen, R 2018, ' Expanded Interactome of the Intrinsically Disordered Protein Dss1 ', Cell Reports, vol. 25, no. 4, pp. 862-870 . https://doi.org/10.1016/j.celrep.2018.09.080
Cell Reports
Cell Reports, Vol 25, Iss 4, Pp 862-870 (2018)
Cell Reports
Cell Reports, Vol 25, Iss 4, Pp 862-870 (2018)
Summary Dss1 (also known as Sem1) is a conserved, intrinsically disordered protein with a remarkably broad functional diversity. It is a proteasome subunit but also associates with the BRCA2, RPA, Csn12-Thp1, and TREX-2 complexes. Accordingly, Dss1 f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3e4aeca9a7084ecce156a1cdd738aa5d
https://curis.ku.dk/portal/da/publications/expanded-interactome-of-the-intrinsically-disordered-protein-dss1(35864465-0f92-49cf-b1e0-fe9d263cdfb2).html
https://curis.ku.dk/portal/da/publications/expanded-interactome-of-the-intrinsically-disordered-protein-dss1(35864465-0f92-49cf-b1e0-fe9d263cdfb2).html
Publikováno v:
Biomolecules, Vol 4, Iss 3, Pp 646-661 (2014)
Nielsen, S V, Poulsen, E G, Rebula, C A & Hartmann-Petersen, R 2014, ' Protein quality control in the nucleus ', Biomolecules, vol. 4, no. 3, pp. 646-661 . https://doi.org/10.3390/biom4030646
Biomolecules
Nielsen, S V, Poulsen, E G, Rebula, C A & Hartmann-Petersen, R 2014, ' Protein quality control in the nucleus ', Biomolecules, vol. 4, no. 3, pp. 646-661 . https://doi.org/10.3390/biom4030646
Biomolecules
In their natural environment, cells are regularly exposed to various stress conditions that may lead to protein misfolding, but also in the absence of stress, misfolded proteins occur as the result of mutations or failures during protein synthesis. S