Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Cecilie L Søltoft"'
Autor:
Lene Clausen, Amelie Stein, Martin Grønbæk-Thygesen, Lasse Nygaard, Cecilie L Søltoft, Sofie V Nielsen, Michael Lisby, Tommer Ravid, Kresten Lindorff-Larsen, Rasmus Hartmann-Petersen
Publikováno v:
PLoS Genetics, Vol 16, Iss 11, p e1009187 (2020)
Germline mutations in the folliculin (FLCN) tumor suppressor gene are linked to Birt-Hogg-Dubé (BHD) syndrome, a dominantly inherited genetic disease characterized by predisposition to fibrofolliculomas, lung cysts, and renal cancer. Most BHD-linked
Externí odkaz:
https://doaj.org/article/aa4119d02042406da6db2f208f892697
Publikováno v:
International journal of molecular sciences. 23(5)
The human Fic domain-containing protein (FICD) is a type II endoplasmic reticulum (ER) membrane protein that is important for the maintenance of ER proteostasis. Structural and in vitro biochemical characterisation of FICD AMPylase and deAMPylase act
Autor:
Henning G. Hansen, Cecilie L. Søltoft, Jonas D. Schmidt, Julia Birk, Christian Appenzeller‑Herzog, Lars Ellgaard
Publikováno v:
Bioscience Reports, Vol 34, Iss 2, p e00103 (2014)
In the ER (endoplasmic reticulum) of human cells, disulfide bonds are predominantly generated by the two isoforms of Ero1 (ER oxidoreductin-1): Ero1α and Ero1β. The activity of Ero1α is tightly regulated through the formation of intramolecular dis
Externí odkaz:
https://doaj.org/article/470fffb88d094a78a98a8441a7f7608e
Autor:
Anastasia Albert, Lars Ellgaard, Mads M. Foged, Terje Vasskog, Samuel D. Robinson, Cecilie L. Søltoft, Raymond S. Norton, Baldomero M. Olivera, Kaare Teilum, Andreas B. Bertelsen, Anthony W. Purcell, Lau Dalby Nielsen, Steen V. Petersen, Helena Safavi-Hemami
Publikováno v:
Nielsen, L D, Foged, M M, Albert, A, Bertelsen, A B, Søltoft, C L, Robinson, S D, Petersen, S V, Purcell, A W, Olivera, B M, Norton, R S, Vasskog, T, Safavi-Hemami, H, Teilum, K & Ellgaard, L 2019, ' The three-dimensional structure of an H-superfamily conotoxin reveals a granulin fold arising from a common ICK cysteine framework ', The Journal of Biological Chemistry, vol. 294, no. 22, pp. 8745-8759 . https://doi.org/10.1074/jbc.RA119.007491
Nielsen, L D, Foged, M M, Albert, A, Bertelsen, A B, Søltoft, C L, Robinson, S D, Petersen, S V, Purcell, A W, Olivera, B M, Norton, R S, Vasskog, T, Safavi-Hemami, H, Teilum, K & Ellgaard, L 2019, ' The three-dimensional structure of an H-superfamily conotoxin reveals a granulin fold arising from a common ICK cysteine framework ', The Journal of biological chemistry . https://doi.org/10.1074/jbc.RA119.007491
J Biol Chem
Nielsen, L D, Foged, M M, Albert, A, Bertelsen, A B, Søltoft, C L, Robinson, S D, Petersen, S V, Purcell, A W, Olivera, B M, Norton, R S, Vasskog, T, Safavi-Hemami, H, Teilum, K & Ellgaard, L 2019, ' The three-dimensional structure of an H-superfamily conotoxin reveals a granulin fold arising from a common ICK cysteine framework ', Journal of Biological Chemistry, vol. 294, no. 22, pp. 8745-8759 . https://doi.org/10.1074/jbc.RA119.007491
Nielsen, L D, Foged, M M, Albert, A, Bertelsen, A B, Søltoft, C L, Robinson, S D, Petersen, S V, Purcell, A W, Olivera, B M, Norton, R S, Vasskog, T, Safavi-Hemami, H, Teilum, K & Ellgaard, L 2019, ' The three-dimensional structure of an H-superfamily conotoxin reveals a granulin fold arising from a common ICK cysteine framework ', The Journal of biological chemistry . https://doi.org/10.1074/jbc.RA119.007491
J Biol Chem
Nielsen, L D, Foged, M M, Albert, A, Bertelsen, A B, Søltoft, C L, Robinson, S D, Petersen, S V, Purcell, A W, Olivera, B M, Norton, R S, Vasskog, T, Safavi-Hemami, H, Teilum, K & Ellgaard, L 2019, ' The three-dimensional structure of an H-superfamily conotoxin reveals a granulin fold arising from a common ICK cysteine framework ', Journal of Biological Chemistry, vol. 294, no. 22, pp. 8745-8759 . https://doi.org/10.1074/jbc.RA119.007491
Venomous marine cone snails produce peptide toxins (conotoxins) that bind ion channels and receptors with high specificity and therefore are important pharmacological tools. Conotoxins contain conserved cysteine residues that form disulfide bonds tha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6471de4fea35e43d0dc539f45f90b2ee
https://curis.ku.dk/portal/da/publications/the-threedimensional-structure-of-an-hsuperfamily-conotoxin-reveals-a-granulin-fold-arising-from-a-common-ick-cysteine-framework(9a6f9a14-de9a-4f62-adfb-2ff58a676733).html
https://curis.ku.dk/portal/da/publications/the-threedimensional-structure-of-an-hsuperfamily-conotoxin-reveals-a-granulin-fold-arising-from-a-common-ick-cysteine-framework(9a6f9a14-de9a-4f62-adfb-2ff58a676733).html
Autor:
Kresten Lindorff-Larsen, Lene Clausen, Rasmus Hartmann-Petersen, Cecilie L. Søltoft, Michael Lisby, Sofie V. Nielsen, Amelie Stein, Tommer Ravid, Martin Grønbæk-Thygesen, Lasse Nygaard
Publikováno v:
PLoS Genetics, Vol 16, Iss 11, p e1009187 (2020)
Clausen, L, Stein, A, Grønbæk-Thygesen, M, Nygaard, L, Søltoft, C L, Nielsen, S V, Lisby, M, Ravid, T, Lindorff-Larsen, K & Hartmann-Petersen, R 2020, ' Folliculin variants linked to Birt-Hogg-Dubé syndrome are targeted for proteasomal degradation ', PLOS Genetics, vol. 16, no. 11, e1009187 . https://doi.org/10.1371/journal.pgen.1009187
PLoS Genetics
Clausen, L, Stein, A, Grønbæk-Thygesen, M, Nygaard, L, Søltoft, C L, Nielsen, S V, Lisby, M, Ravid, T, Lindorff-Larsen, K & Hartmann-Petersen, R 2020, ' Folliculin variants linked to Birt-Hogg-Dubé syndrome are targeted for proteasomal degradation ', PLOS Genetics, vol. 16, no. 11, e1009187 . https://doi.org/10.1371/journal.pgen.1009187
PLoS Genetics
Germline mutations in the folliculin (FLCN) tumor suppressor gene are linked to Birt-Hogg-Dubé (BHD) syndrome, a dominantly inherited genetic disease characterized by predisposition to fibrofolliculomas, lung cysts, and renal cancer. Most BHD-linked
Autor:
Celeste Menuet Hackney, Minttu S Virolainen, James C. Paton, Esben S. Sørensen, Raffaella Magnoni, Jan J. Enghild, Ana P Cordeiro, Cecilie L. Søltoft, Carsten Scavenius, Brian Christensen, Yun Liu, Lars Ellgaard, Adrienne W. Paton
Endoplasmic reticulum (ER) stress that leads to the accumulation of misfolded proteins in the ER initiates the unfolded protein response (UPR). This homeostatic response activates signaling pathways that seek to reinstate a proper ER protein folding
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5f37e711301b3b53d2c3cd9bca251992
https://doi.org/10.1101/126516
https://doi.org/10.1101/126516
Autor:
Thomas Ramming, Jonas D. Schmidt, Cecilie L. Søltoft, Agnieszka S. Juncker, Esben S. Sørensen, Henning Gram Hansen, Christian Appenzeller-Herzog, Brian Christensen, Henrik Marcus Geertz-Hansen, Lars Ellgaard
Publikováno v:
The Journal of biological chemistry
Hansen, H G, Schmidt, J D, Søltoft, C L, Ramming, T, Geertz-Hansen, H M, Christensen, B, Sørensen, E S, Juncker, A S, Appenzeller-Herzog, C & Ellgaard, L 2012, ' Hyperactivity of the Ero1α oxidase elicits endoplasmic reticulum stress but no broad antioxidant response ', Journal of Biological Chemistry, vol. 287, no. 47, pp. 39513-39523 . https://doi.org/10.1074/jbc.M112.405050
Hansen, H G, Schmidt, J D, Søltoft, C L, Ramming, T, Geertz-Hansen, H M, Christensen, B, Sørensen, E S, Juncker, A S, Appenzeller-Herzog, C & Ellgaard, L 2012, ' Hyperactivity of the Ero1α oxidase elicits endoplasmic reticulum stress but no broad antioxidant response ', Journal of Biological Chemistry, vol. 287, no. 47, pp. 39513-39523 . https://doi.org/10.1074/jbc.M112.405050
Oxidizing equivalents for the process of oxidative protein folding in the endoplasmic reticulum (ER) of mammalian cells are mainly provided by the Ero1α oxidase. The molecular mechanisms that regulate Ero1α activity in order to harness its oxidativ
Autor:
Cecilie L. Søltoft, Christian Appenzeller-Herzog, Jonas D. Schmidt, Julia Birk, Henning Gram Hansen, Lars Ellgaard
Publikováno v:
Bioscience reports
Bioscience Reports, Vol 34, Iss 2, p e00103 (2014)
Hansen, H G, Søltoft, C L, Schmidt, J D, Birk, J, Appenzeller-Herzog, C & Ellgaard, L 2014, ' Biochemical evidence that regulation of Ero1β activity in human cells does not involve the isoform-specific cysteine 262 ', Bioscience Reports, vol. 34, no. 2 . https://doi.org/10.1042/BSR20130124
Bioscience Reports
Bioscience Reports, Vol 34, Iss 2, p e00103 (2014)
Hansen, H G, Søltoft, C L, Schmidt, J D, Birk, J, Appenzeller-Herzog, C & Ellgaard, L 2014, ' Biochemical evidence that regulation of Ero1β activity in human cells does not involve the isoform-specific cysteine 262 ', Bioscience Reports, vol. 34, no. 2 . https://doi.org/10.1042/BSR20130124
Bioscience Reports
In the ER (endoplasmic reticulum) of human cells, disulfide bonds are predominantly generated by the two isoforms of Ero1 (ER oxidoreductin-1): Ero1α and Ero1β. The activity of Ero1α is tightly regulated through the formation of intramolecular dis