Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Helena Steinocher"'
Autor:
Li He, Helena Steinocher, Ashish Shelar, Emily B Cohen, Erin N Heim, Birthe B Kragelund, Gevorg Grigoryan, Daniel DiMaio
Publikováno v:
eLife, Vol 6 (2017)
Transmembrane domains (TMDs) engage in protein-protein interactions that regulate many cellular processes, but the rules governing the specificity of these interactions are poorly understood. To discover these principles, we analyzed 26-residue model
Externí odkaz:
https://doaj.org/article/0c943039475e4f7da16907be3642d2a5
Autor:
Jennifer Mehlhorn, Helena Steinocher, Sebastian Beck, John T M Kennis, Peter Hegemann, Tilo Mathes
Publikováno v:
PLoS ONE, Vol 8, Iss 11, p e79006 (2013)
Biological reactions are facilitated by delicate molecular interactions between proteins, cofactors and substrates. To study and understand their dynamic interactions researchers have to take great care not to influence or distort the object of study
Externí odkaz:
https://doaj.org/article/aee3a6e42e1344e9b8a985f9dc7b1a39
Autor:
Helena Steinocher, Raul Araya-Secchi, Maikel C. Rheinstädter, Yong Wang, Noah Kassem, Martin Cramer Pedersen, Anne S. Ulrich, Katrine Bugge, Jochen Bürck, Abigail Barclay, Birthe B. Kragelund, Aneta J. Lenard, Michael Landreh, Cagla Sahin, Lise Arleth, Kresten Lindorff-Larsen, Per Amstrup Pedersen, Adree Khondker
Publikováno v:
'Science Advances ', vol: 7, pages: eabh3805-1-eabh3805-20 (2021)
Science Advances, 7 (27), Art.-Nr.: eabh3805
Kassem, N, Araya-Secchi, R, Bugge, K, Barclay, A, Steinocher, H, Khondker, A, Wang, Y, Lenard, A J, Bürck, J, Sahin, C, Ulrich, A S, Landreh, M, Pedersen, M C, Rheinstädter, M C, Pedersen, P A, Lindorff-Larsen, K, Arleth, L & Kragelund, B B 2021, ' Order and disorder-An integrative structure of the full-length human growth hormone receptor ', Science Advances, vol. 7, no. 27, eabh3805 . https://doi.org/10.1126/sciadv.abh3805
Science advances 7(27), eabh3805 (1-19) (2021). doi:10.1126/sciadv.abh3805
'Science Advances ', vol: 7, pages: eabh3805-1-eabh3805-19 (2021)
Science Advances
Science Advances, 7 (27), Art.-Nr.: eabh3805
Kassem, N, Araya-Secchi, R, Bugge, K, Barclay, A, Steinocher, H, Khondker, A, Wang, Y, Lenard, A J, Bürck, J, Sahin, C, Ulrich, A S, Landreh, M, Pedersen, M C, Rheinstädter, M C, Pedersen, P A, Lindorff-Larsen, K, Arleth, L & Kragelund, B B 2021, ' Order and disorder-An integrative structure of the full-length human growth hormone receptor ', Science Advances, vol. 7, no. 27, eabh3805 . https://doi.org/10.1126/sciadv.abh3805
Science advances 7(27), eabh3805 (1-19) (2021). doi:10.1126/sciadv.abh3805
'Science Advances ', vol: 7, pages: eabh3805-1-eabh3805-19 (2021)
Science Advances
Science advances 7(27), eabh3805 (1-19) (2021). doi:10.1126/sciadv.abh3805
Because of its small size (70 kilodalton) and large content of structural disorder (>50%), the human growth hormone receptor (hGHR) falls between the cracks of convention
Because of its small size (70 kilodalton) and large content of structural disorder (>50%), the human growth hormone receptor (hGHR) falls between the cracks of convention
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::657169a20ecc942385443443830c63df
Autor:
Abigail Barclay, Birthe B. Kragelund, Lise Arleth, Jochen Bürck, Kresten Lindorff-Larsen, Maikel C. Rheinstädter, Anne S. Ulrich, Yong Wang, Per Amstrup Pedersen, Martin Cramer Pedersen, Helena Steinocher, Katrine Bugge, Aneta J. Lenard, Raul Araya-Secchi, Adree Khondker, Noah Kassem
Despite the many physiological and pathophysiological functions of the human growth hormone receptor (hGHR), a detailed understanding of itsmodus operandiis hindered by the lack of structural information of the entire receptor at the molecular level.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6d2bc0d12242844a9209af99ebd6d8e4
https://doi.org/10.1101/2020.06.25.171116
https://doi.org/10.1101/2020.06.25.171116
Autor:
Frederic A. Meunier, Andreas Papadopulos, Michael J. Waters, Yash Chhabra, Birthe B. Kragelund, Ho Yi Wong, Helena Steinocher, Louise F. Nikolajsen, Kathryn A. Tunny, Aaron G. Smith, Andrew J. Brooks
Publikováno v:
Oncogene
Chhabra, Y, Wong, H Y, Nikolajsen, L F, Steinocher, H, Papadopulos, A, Tunny, K A, Meunier, F A, Smith, A G, Kragelund, B B, Brooks, A J & Waters, M J 2018, ' A growth hormone receptor SNP promotes lung cancer by impairment of SOCS2-mediated degradation ', Oncogene, vol. 37, pp. 489-501 . https://doi.org/10.1038/onc.2017.352
Chhabra, Y, Wong, H Y, Nikolajsen, L F, Steinocher, H, Papadopulos, A, Tunny, K A, Meunier, F A, Smith, A G, Kragelund, B B, Brooks, A J & Waters, M J 2018, ' A growth hormone receptor SNP promotes lung cancer by impairment of SOCS2-mediated degradation ', Oncogene, vol. 37, pp. 489-501 . https://doi.org/10.1038/onc.2017.352
Both humans and mice lacking functional growth hormone (GH) receptors are known to be resistant to cancer. Further, autocrine GH has been reported to act as a cancer promoter. Here we present the first example of a variant of the GH receptor (GHR) as
Autor:
Andrew J. Brooks, Birthe B. Kragelund, Kresten Lindorff-Larsen, Katrine Bugge, Helena Steinocher
Publikováno v:
Analytical Chemistry. 87:9126-9131
Despite the biological and pharmaceutical significance of membrane proteins, their tertiary structures constitute less than 3% of known structures. One of the major obstacles for initiating structural studies of membrane proteins by NMR spectroscopy
Autor:
Peter Hegemann, Sebastian Beck, John T. M. Kennis, Kathrin Glass, Tom Lindtner, Jennifer Mehlhorn, Helena Steinocher, Florian Richter, Tilo Mathes
Publikováno v:
Journal of Physical Chemistry Letters, 6(27), 4749-4753. American Chemical Society
Mehlhorn, J, lindtner, T, glass, K, Steinocher, H, Beck, S, Hegemann, P, Kennis, J T M & Mathes, T 2015, ' Light-Induced Rearrangement of the β5 Strand in the BLUF Photoreceptor SyPixD (Slr1694) ', Journal of Physical Chemistry Letters, vol. 6, no. 27, pp. 4749-4753 . https://doi.org/10.1021/acs.jpclett.5b02245
Mehlhorn, J, lindtner, T, glass, K, Steinocher, H, Beck, S, Hegemann, P, Kennis, J T M & Mathes, T 2015, ' Light-Induced Rearrangement of the β5 Strand in the BLUF Photoreceptor SyPixD (Slr1694) ', Journal of Physical Chemistry Letters, vol. 6, no. 27, pp. 4749-4753 . https://doi.org/10.1021/acs.jpclett.5b02245
The structural changes that facilitate signal transduction in blue light sensors using FAD (BLUF) photoreceptors and confer the stability of the rearranged hydrogen bond network between flavin and protein in the signaling state are still poorly under
Autor:
Daniel DiMaio, Helena Steinocher, Erin N. Heim, Birthe B. Kragelund, Emily B. Cohen, Gevorg Grigoryan, Ashish Shelar, Li He
Publikováno v:
eLife
eLife, Vol 6 (2017)
He, L, Steinocher, H, Shelar, A, Cohen, E B, Heim, E N, Kragelund, B B, Grigoryan, G & DiMaio, D 2017, ' Single methyl groups can act as toggle switches to specify transmembrane protein-protein interactions ', eLife, vol. 6, e27701 . https://doi.org/10.7554/eLife.27701
eLife, Vol 6 (2017)
He, L, Steinocher, H, Shelar, A, Cohen, E B, Heim, E N, Kragelund, B B, Grigoryan, G & DiMaio, D 2017, ' Single methyl groups can act as toggle switches to specify transmembrane protein-protein interactions ', eLife, vol. 6, e27701 . https://doi.org/10.7554/eLife.27701
Transmembrane domains (TMDs) engage in protein-protein interactions that regulate many cellular processes, but the rules governing the specificity of these interactions are poorly understood. To discover these principles, we analyzed 26-residue model
Autor:
Helena Steinocher, Andrew J. Brooks, Kresten Lindorff-Larsen, Birthe B. Kragelund, Katrine Bugge, Louise F. Nikolajsen
Publikováno v:
Biophysical Journal. 112:171a
The Growth Hormone Receptor (GHR) is a member of the Class I Cytokine Receptor family and comprises three different domains, an extracellular domain (ECD), a cell membrane spanning helix constituting the transmembrane domain (TMD) and an intracellula