Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Anna Maria Eisele-Bürger"'
Autor:
Anna Maria Eisele-Bürger, Frederik Eisele, Sandra Malmgren Hill, Xinxin Hao, Kara L. Schneider, Rahmi Imamoglu, David Balchin, Beidong Liu, F. Ulrich Hartl, Peter V. Bozhkov, Thomas Nyström
Publikováno v:
Cell Reports, Vol 42, Iss 11, Pp 113372- (2023)
Summary: Metacaspases are ancestral homologs of caspases that can either promote cell death or confer cytoprotection. Furthermore, yeast (Saccharomyces cerevisiae) metacaspase Mca1 possesses dual biochemical activity: proteolytic activity causing cel
Externí odkaz:
https://doaj.org/article/9af3080157bc43d7b143e62b2b0ce9aa
Autor:
Frederik Eisele, Anna Maria Eisele-Bürger, Xinxin Hao, Lisa Larsson Berglund, Johanna L. Höög, Beidong Liu, Thomas Nyström
Publikováno v:
Cell Reports, Vol 35, Iss 13, Pp 109328- (2021)
Summary: In this paper, we show that the essential Hsp90 co-chaperone Sgt1 is a member of a general protein quality control network that links folding and degradation through its participation in the degradation of misfolded proteins both in the cyto
Externí odkaz:
https://doaj.org/article/10d8f3ae433d4bc2bc959b564eba6d35
Autor:
Rebecca Andersson, Anna Maria Eisele-Bürger, Sarah Hanzén, Katarina Vielfort, David Öling, Frederik Eisele, Gustav Johansson, Tobias Gustafsson, Kristian Kvint, Thomas Nyström
Publikováno v:
PLoS Genetics, Vol 17, Iss 1, p e1008951 (2021)
70 kDa heat shock proteins (Hsp70) are essential chaperones of the protein quality control network; vital for cellular fitness and longevity. The four cytosolic Hsp70's in yeast, Ssa1-4, are thought to be functionally redundant but the absence of Ssa
Externí odkaz:
https://doaj.org/article/5f0b7cbabc894c19a94e21e6c7bda430
Autor:
Kara L, Schneider, Doryaneh, Ahmadpour, Katharina S, Keuenhof, Anna Maria, Eisele-Bürger, Lisa Larsson, Berglund, Frederik, Eisele, Roja, Babazadeh, Johanna L, Höög, Thomas, Nyström, Per O, Widlund
Publikováno v:
The Journal of biological chemistry. 298(11)
The accumulation of misfolded proteins is a hallmark of aging and many neurodegenerative diseases, making it important to understand how the cellular machinery recognizes and processes such proteins. A key question in this respect is whether misfolde
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::372db26dfbe4b5ba1f941c7fb3deef76
https://pubmed.ncbi.nlm.nih.gov/36096201
https://pubmed.ncbi.nlm.nih.gov/36096201
Autor:
Lisa Larsson Berglund, Frederik Eisele, Anna Maria Eisele-Bürger, Xinxin Hao, Johanna L. Höög, Beidong Liu, Thomas Nyström
Publikováno v:
Cell Reports, Vol 35, Iss 13, Pp 109328-(2021)
Summary: In this paper, we show that the essential Hsp90 co-chaperone Sgt1 is a member of a general protein quality control network that links folding and degradation through its participation in the degradation of misfolded proteins both in the cyto
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d49140a575b472a94186f99ae1b831ef
https://pub.epsilon.slu.se/27146/
https://pub.epsilon.slu.se/27146/
Autor:
Gustav Johansson, Tobias Gustafsson, David Öling, Thomas Nyström, Rebecca Andersson, Katarina Vielfort, Sarah Hanzén, Frederik Eisele, Kristian Kvint, Anna Maria Eisele-Bürger
Publikováno v:
PLoS Genetics
PLoS Genetics, Vol 17, Iss 1, p e1008951 (2021)
PLoS Genetics, Vol 17, Iss 1, p e1008951 (2021)
70 kDa heat shock proteins (Hsp70) are essential chaperones of the protein quality control network; vital for cellular fitness and longevity. The four cytosolic Hsp70’s in yeast, Ssa1-4, are thought to be functionally redundant but the absence of S
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1122bbc935c929e7d837f6710dae53e1
https://doi.org/10.1101/2020.06.25.170670
https://doi.org/10.1101/2020.06.25.170670