Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Alexander, Jussupow"'
Autor:
Stefan Riedl, Ecenaz Bilgen, Ganesh Agam, Viivi Hirvonen, Alexander Jussupow, Franziska Tippl, Maximilian Riedl, Andreas Maier, Christian F. W. Becker, Ville R. I. Kaila, Don C. Lamb, Johannes Buchner
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-16 (2024)
Abstract Hsp90 is a molecular chaperone of central importance for protein homeostasis in the cytosol of eukaryotic cells, with key functional and structural traits conserved from yeast to man. During evolution, Hsp90 has gained additional functional
Externí odkaz:
https://doaj.org/article/3fff8661c1de4900a222d6f15df59e1e
Autor:
Hannah R. Bridges, Justin G. Fedor, James N. Blaza, Andrea Di Luca, Alexander Jussupow, Owen D. Jarman, John J. Wright, Ahmed-Noor A. Agip, Ana P. Gamiz-Hernandez, Maxie M. Roessler, Ville R. I. Kaila, Judy Hirst
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-11 (2020)
The respiratory complex I (NADH:ubiquinone oxidoreductase) is a large redox-driven proton pump that initiates respiration in mitochondria. Here, the authors present the 3.0 Å cryo-EM structure of complex I from mouse heart mitochondria with the ubiq
Externí odkaz:
https://doaj.org/article/c67a68fb52d54db99aeb5805317cf695
Autor:
Mustapha Carab Ahmed, Line K. Skaanning, Alexander Jussupow, Estella A. Newcombe, Birthe B. Kragelund, Carlo Camilloni, Annette E. Langkilde, Kresten Lindorff-Larsen
Publikováno v:
Frontiers in Molecular Biosciences, Vol 8 (2021)
The inherent flexibility of intrinsically disordered proteins (IDPs) makes it difficult to interpret experimental data using structural models. On the other hand, molecular dynamics simulations of IDPs often suffer from force-field inaccuracies, and
Externí odkaz:
https://doaj.org/article/86f6af80565f4194b9e0b758008f8a7f
Autor:
Alexander Jussupow, Ville R. I. Kaila
Publikováno v:
Journal of Chemical Theory and Computation. 19:1965-1975
Recent breakthroughs in neural-network based structure prediction methods, such as AlphaFold2 and RoseTTAFold, have dramatically improved the quality of computational protein structure prediction. These models also provide statistical confidence scor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::567a230e1fa72c695be1c3e58ec9b1fc
https://doi.org/10.1021/acs.jctc.2c01027
https://doi.org/10.1021/acs.jctc.2c01027
Autor:
Hamed Kooshapur, Nila Roy Choudhury, Bernd Simon, Max Mühlbauer, Alexander Jussupow, Noemi Fernandez, Alisha N. Jones, Andre Dallmann, Frank Gabel, Carlo Camilloni, Gracjan Michlewski, Javier F. Caceres, Michael Sattler
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-17 (2018)
hnRNP A1 is an auxiliary factor that promotes the Microprocessor-mediated processing of pri-mir-18a, of the oncomiR-1 cluster. Here the authors employ an integrative structural biology approach and provide insights into the molecular mechanism of how
Externí odkaz:
https://doaj.org/article/014a6dc8990b44dca7c25370f4266456
Autor:
Diana C Rodriguez Camargo, Kyle J Korshavn, Alexander Jussupow, Kolio Raltchev, David Goricanec, Markus Fleisch, Riddhiman Sarkar, Kai Xue, Michaela Aichler, Gabriele Mettenleiter, Axel Karl Walch, Carlo Camilloni, Franz Hagn, Bernd Reif, Ayyalusamy Ramamoorthy
Publikováno v:
eLife, Vol 6 (2017)
Membrane-assisted amyloid formation is implicated in human diseases, and many of the aggregating species accelerate amyloid formation and induce cell death. While structures of membrane-associated intermediates would provide tremendous insights into
Externí odkaz:
https://doaj.org/article/83e9a3672fef478bbca4e26152d644a1
Autor:
Alexander Jussupow, Abraham Lopez, Mona Baumgart, Sophie L. Mader, Michael Sattler, Ville R.I. Kaila
Publikováno v:
J. Biol. Chem. 298:102101 (2022)
The heat shock protein 90 (Hsp90) is a molecular chaperone central to client protein folding and maturation in eukaryotic cells. During its chaperone cycle, Hsp90 undergoes ATPase-coupled large-scale conformational changes between open and closed sta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc98b085bfdcf3e153fb745bdf22431b
https://pubmed.ncbi.nlm.nih.gov/35667441
https://pubmed.ncbi.nlm.nih.gov/35667441
Publikováno v:
Journal of Applied Crystallography. 52:394-402
The use of small-angle X-ray scattering (SAXS) in combination with molecular dynamics simulation is hampered by its heavy computational cost. The calculation of SAXS from atomic structures can be speeded up by using a coarse-grain representation of t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0c7eac897d825e78f1b0d9e4a572422f
https://doi.org/10.1107/s1600576719002450
https://doi.org/10.1107/s1600576719002450
Autor:
Verena Bittl, Maximilian Fottner, Anja Bremm, Kathrin Lang, Daniel Horn-Ghetko, Andreas-David Brunner, Alexander Jussupow, Ville R. I. Kaila
Publikováno v:
Nature Chemical Biology. 15:276-284
Post-translational modification of proteins with ubiquitin and ubiquitin-like proteins (Ubls) is central to the regulation of eukaryotic cellular processes. Our ability to study the effects of ubiquitylation, however, is limited by the difficulty to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::121b7e1b01ca9d6017fa6cb2590988e5
https://doi.org/10.1038/s41589-019-0227-4
https://doi.org/10.1038/s41589-019-0227-4
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1863:148663
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1717d919273597af65e723da3ab664d5
https://doi.org/10.1016/j.bbabio.2022.148663
https://doi.org/10.1016/j.bbabio.2022.148663