Zobrazeno 1 - 10
of 43
pro vyhledávání: '"Johan G. Olsen"'
Autor:
Louise Hamborg, Daniele Granata, Johan G. Olsen, Jennifer Virginia Roche, Lasse Ebdrup Pedersen, Alex Toftgaard Nielsen, Kresten Lindorff-Larsen, Kaare Teilum
Publikováno v:
Communications Biology, Vol 4, Iss 1, Pp 1-9 (2021)
Louise Hamborg et al. use a cell-based screen in E. coli to look for mutants of chymotrypsin inhibitor 2 which are either destabilized or stabilized, in an effort to identify a larger library of mutants which might improve stability prediction. Their
Externí odkaz:
https://doaj.org/article/e62f07713f7946109276026a00012c4c
Autor:
Katrine Bugge, Inna Brakti, Catarina B. Fernandes, Jesper E. Dreier, Jeppe E. Lundsgaard, Johan G. Olsen, Karen Skriver, Birthe B. Kragelund
Publikováno v:
Frontiers in Molecular Biosciences, Vol 7 (2020)
Living organisms depend on timely and organized interactions between proteins linked in interactomes of high complexity. The recent increased precision by which protein interactions can be studied, and the enclosure of intrinsic structural disorder,
Externí odkaz:
https://doaj.org/article/c6455c1ccc2e408fa283986206056610
Autor:
Katrine Bugge, Elena Papaleo, Gitte W. Haxholm, Jonathan T. S. Hopper, Carol V. Robinson, Johan G. Olsen, Kresten Lindorff-Larsen, Birthe B. Kragelund
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-11 (2016)
The prolactin receptor consists of a folded extracellular domain, a transmembrane domain and an intracellular intrinsically disordered domain. Here the authors use a combined experimental and computational approach to obtain a structure of a class I
Externí odkaz:
https://doaj.org/article/d950feac1c4e42839bcfaa0103164780
Publikováno v:
Frontiers in Molecular Biosciences, Vol 2 (2015)
In biology proteins from different structural classes interact across and within classes in ways that are optimized to achieve balanced functional outputs. The interactions between intrinsically disordered proteins (IDPs) and other proteins rely on c
Externí odkaz:
https://doaj.org/article/3745adc6e0a84d569a1783318d4f0408
Autor:
Johan G. Olsen, Andreas Prestel, Noah Kassem, Sebastian S. Broendum, Hossain Mohammad Shamim, Signe Simonsen, Martin Grysbæk, Josefine Mortensen, Louise Lund Rytkjær, Gitte W. Haxholm, Riccardo Marabini, Antony M. Carr, Ramon Crehuet, Olaf Nielsen, Birthe B. Kragelund
DNA regulation, replication and repair are processes fundamental to all known organisms and the sliding clamp proliferating cell nuclear antigen (PCNA) is central to all these processes. S-phase delaying protein 1 (Spd1) fromS. pombe, an intrinsicall
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::190d1efba4b37ac0b8cd7a0bbb64dd0a
https://doi.org/10.1101/2023.05.11.540346
https://doi.org/10.1101/2023.05.11.540346
Publikováno v:
Teilum, K, Olsen, J G & Kragelund, B B 2023, ' Comment on “ Intrinsic protein disorder uncouples affinity from binding specificity ” ', Protein Science, vol. 32, no. 4, e4602 . https://doi.org/10.1002/pro.4602
Autor:
Olav M. Andersen, Giulia Monti, Anne Mette G. Jensen, Matthijs de Waal, Marc Hulsman, Johan G. Olsen, Henne Holstege
SORL1encodes the retromer-associated receptor SORLA that functions in endosomal recycling. Rare variants inSORL1have been associated with Alzheimer’s disease (AD) and rare pathogenic variants are estimated to occur in up to 2.75% of early onset AD
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7e9fc8b6497ff8835ade4f6bd1b938dc
https://doi.org/10.1101/2023.02.27.524103
https://doi.org/10.1101/2023.02.27.524103
Autor:
Francesco Pesce, Estella A. Newcombe, Pernille Seiffert, Emil E. Tranchant, Johan G. Olsen, Christy R. Grace, Birthe B. Kragelund, Kresten Lindorff-Larsen
Publikováno v:
Pesce, F, Newcombe, E A, Seiffert, P, Tranchant, E E, Olsen, J G, Grace, C R, Kragelund, B B & Lindorff-Larsen, K 2023, ' Assessment of models for calculating the hydrodynamic radius of intrinsically disordered proteins ', Biophysical Journal, vol. 122, no. 2, pp. 310-321 . https://doi.org/10.1016/j.bpj.2022.12.013
Diffusion measurements by pulsed-field gradient NMR and fluorescence correlation spectroscopy can be used to probe the hydrodynamic radius of proteins, which contains information about the overall dimension of a protein in solution. The comparison of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4219b34702011c2aa700b4e1102721e6
https://curis.ku.dk/ws/files/334258562/2022.06.11.495732v2.full.pdf
https://curis.ku.dk/ws/files/334258562/2022.06.11.495732v2.full.pdf
Publikováno v:
Teilum, K, Olsen, J G & Kragelund, B B 2021, ' On the specificity of protein-protein interactions in the context of disorder ', Biochemical Journal, vol. 478, no. 11, pp. 2035-2050 . https://doi.org/10.1042/BCJ20200828
Biochemical Journal
Biochemical Journal
With the increased focus on intrinsically disordered proteins (IDPs) and their large interactomes, the question about their specificity — or more so on their multispecificity — arise. Here we recapitulate how specificity and multispecificity are
Autor:
Emilie S Pedersen, Johan G. Olsen, Lise M. Sjøgaard-Frich, Stine F. Pedersen, Andreas Prestel, Marc Severin, Kristian Kølby Kristensen, Birthe B. Kragelund
Publikováno v:
Sjøgaard-Frich, L M, Prestel, A, Pedersen, E S, Severin, M, Kristensen, K K, Olsen, J G, Kragelund, B B & Pedersen, S F 2021, ' Dynamic Na + /H + exchanger 1 (NHE1)-calmodulin complexes of varying stoichiometry and structure regulate Ca 2+-dependent NHE1 activation ', eLife, vol. 10, e60889 . https://doi.org/10.7554/eLife.60889
eLife, Vol 10 (2021)
eLife, Vol 10 (2021)
Calmodulin (CaM) engages in Ca2+-dependent interactions with numerous proteins, including a still incompletely understood physical and functional interaction with the human Na+/H+-exchanger NHE1. Using nuclear magnetic resonance (NMR) spectroscopy, i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::51f7d0525ea785a44ebb5867e45c3c97
https://curis.ku.dk/ws/files/260544981/elife_60889_v2.pdf
https://curis.ku.dk/ws/files/260544981/elife_60889_v2.pdf