Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Esben G. Poulsen"'
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:
Rasmus Hartmann-Petersen, Maher M. Kassem, Esben G. Poulsen, Michael H. Tatham, Lene Juel Rasmussen, Sofie V. Nielsen, Elena Papaleo, Kresten Lindorff-Larsen, Amelie Stein, Alexander B. Dinitzen
Publikováno v:
Nielsen, S V, Stein, A, Dinitzen, A B, Papaleo, E, Tatham, M H, Poulsen, E G, Kassem, M M, Rasmussen, L J, Lindorff-Larsen, K & Hartmann-Petersen, R 2017, ' Predicting the impact of Lynch syndrome-causing missense mutations from structural calculations ', PLoS Genetics, vol. 13, no. 4, e1006739 . https://doi.org/10.1371/journal.pgen.1006739
PLoS Genetics
PLoS Genetics, Vol 13, Iss 4, p e1006739 (2017)
PLoS Genetics
PLoS Genetics, Vol 13, Iss 4, p e1006739 (2017)
Accurate methods to assess the pathogenicity of mutations are needed to fully leverage the possibilities of genome sequencing in diagnosis. Current data-driven and bioinformatics approaches are, however, limited by the large number of new variations
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c867fd9ea723449e8858c1aaae828719
https://curis.ku.dk/ws/files/179882467/Nielsen_2017_Predicting_the_impact.pdf
https://curis.ku.dk/ws/files/179882467/Nielsen_2017_Predicting_the_impact.pdf
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
Autor:
Kay Hofmann, Jens Vilstrup Johansen, Rasmus Hartmann-Petersen, Esben G. Poulsen, Christian Holmberg, Caroline Kampmeyer, Franziska Kriegenburg
Publikováno v:
Cell stresschaperones. 22(1)
As a result of exposure to stress conditions, mutations, or defects during synthesis, cellular proteins are prone to misfold. To cope with such partially denatured proteins, cells mount a regulated transcriptional response involving the Hsf1 transcri
Autor:
Esben G, Poulsen, Sofie V, Nielsen, Elin J, Pietras, Jens V, Johansen, Cornelia, Steinhauer, Rasmus, Hartmann-Petersen
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1449
The ubiquitin-proteasome system is the major pathway for intracellular protein degradation in eukaryotic cells. Due to the large number of genes dedicated to the ubiquitin-proteasome system, mapping degradation pathways for short lived proteins is a
Autor:
Jens Vilstrup Johansen, Cornelia Steinhauer, Elin J. Pietras, Rasmus Hartmann-Petersen, Esben G. Poulsen, Sofie V. Nielsen
Publikováno v:
Methods in Molecular Biology ISBN: 9781493937547
The ubiquitin-proteasome system is the major pathway for intracellular protein degradation in eukaryotic cells. Due to the large number of genes dedicated to the ubiquitin-proteasome system, mapping degradation pathways for short lived proteins is a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dd7a1c049c396ea5c89474c11364edec
https://doi.org/10.1007/978-1-4939-3756-1_28
https://doi.org/10.1007/978-1-4939-3756-1_28
Publikováno v:
Antioxidants & Redox Signaling. 15:2265-2299
In their natural environments, cells are regularly exposed to oxidizing conditions that may lead to protein misfolding. If such misfolded proteins are allowed to linger, they may form insoluble aggregates and pose a serious threat to the cell. Accumu
Autor:
Christian Madsen, Franziska Kriegenburg, Birthe B. Kragelund, Kresten Lindorff-Larsen, Søs Grønbæk Mathiassen, Elena Papaleo, Rasmus Hartmann-Petersen, Ida Signe Bohse Larsen, Esben G. Poulsen, Michael L. Nielsen
Publikováno v:
The Journal of biological chemistry. 290(34)
A mutation, L166P, in the cytosolic protein, PARK7/DJ-1, causes protein misfolding and is linked to Parkinson disease. Here, we identify the fission yeast protein Sdj1 as the orthologue of DJ-1 and calculate by in silico saturation mutagenesis the ef
Autor:
Visnja Jakopec, Colin Gordon, Rasmus Hartmann-Petersen, Esben G. Poulsen, Sofie V. Nielsen, Nevan J. Krogan, Ursula Fleig, Assen Roguev, Franziska Kriegenburg
Publikováno v:
PLoS Genetics, Vol 10, Iss 1, p e1004140 (2014)
Krogan, Nevan; Kriegenburg, F; Jakopec, V; Poulsen, EG; Nielsen, SV; Roguev, A; et al.(2014). A chaperone-assisted degradation pathway targets kinetochore proteins to ensure genome stability.. UC San Francisco: Retrieved from: http://www.escholarship.org/uc/item/8qs114dw
Kriegenburg, F, Jakopec, V, Poulsen, E G, Nielsen, S V, Roguev, A, Krogan, N, Gordon, C, Fleig, U & Hartmann-Petersen, R 2014, ' A chaperone-assisted degradation pathway targets kinetochore proteins to ensure genome stability ', P L o S Genetics, vol. 10, no. 1, e1004140 . https://doi.org/10.1371/journal.pgen.1004140
PLoS Genetics
Krogan, Nevan; Kriegenburg, F; Jakopec, V; Poulsen, EG; Nielsen, SV; Roguev, A; et al.(2014). A chaperone-assisted degradation pathway targets kinetochore proteins to ensure genome stability.. UC San Francisco: Retrieved from: http://www.escholarship.org/uc/item/8qs114dw
Kriegenburg, F, Jakopec, V, Poulsen, E G, Nielsen, S V, Roguev, A, Krogan, N, Gordon, C, Fleig, U & Hartmann-Petersen, R 2014, ' A chaperone-assisted degradation pathway targets kinetochore proteins to ensure genome stability ', P L o S Genetics, vol. 10, no. 1, e1004140 . https://doi.org/10.1371/journal.pgen.1004140
PLoS Genetics
Cells are regularly exposed to stress conditions that may lead to protein misfolding. To cope with this challenge, molecular chaperones selectively target structurally perturbed proteins for degradation via the ubiquitin-proteasome pathway. In mammal
Autor:
Esben G. Poulsen, Anne-Marie B. Lauridsen, Michael Lees, Cornelia Steinhauer, Lars Ellgaard, Rasmus Hartmann-Petersen
Publikováno v:
Poulsen, E G, Steinhauer, C, Lees, M, Lauridsen, A-M, Ellgaard, L & Hartmann-Petersen, R 2012, ' HUWE1 and TRIP12 Collaborate in Degradation of Ubiquitin-Fusion Proteins and Misframed Ubiquitin ', P L o S One, vol. 7, no. 11 . https://doi.org/10.1371/journal.pone.0050548
PLoS ONE, Vol 7, Iss 11, p e50548 (2012)
PLoS ONE
PLoS ONE, Vol 7, Iss 11, p e50548 (2012)
PLoS ONE
In eukaryotic cells an uncleavable ubiquitin moiety conjugated to the N-terminus of a protein signals the degradation of the fusion protein via the proteasome-dependent ubiquitin fusion degradation (UFD) pathway. In yeast the molecular mechanism of t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2905f14c557ded4ff3c1f8ae7cd9ce41
https://curis.ku.dk/portal/da/publications/huwe1-and-trip12-collaborate-in-degradation-of-ubiquitinfusion-proteins-and-misframed-ubiquitin(efa9e7ce-56d8-44f7-b984-36905bde2f84).html
https://curis.ku.dk/portal/da/publications/huwe1-and-trip12-collaborate-in-degradation-of-ubiquitinfusion-proteins-and-misframed-ubiquitin(efa9e7ce-56d8-44f7-b984-36905bde2f84).html