Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Mateusz Dyla"'
Publikováno v:
Cell Regeneration, Vol 3, Iss 1 (2014)
Genomic datasets and the tools to analyze them have proliferated at an astonishing rate. However, such tools are often poorly integrated with each other: each program typically produces its own custom output in a variety of non-standard file formats.
Externí odkaz:
https://doaj.org/article/2be3b0ef84934491aff883468c27b9ae
Publikováno v:
Dyla, M, González Foutel, N S, Otzen, D E & Kjaergaard, M 2022, ' The optimal docking strength for reversibly tethered kinases ', Proceedings of the National Academy of Sciences of the United States of America, vol. 119, no. 25, e2203098119 . https://doi.org/10.1073/pnas.2203098119
Many kinases use reversible docking interactions to augment the specificity of their catalytic domains. Such docking interactions are often structurally independent of the catalytic domain, which allow for flexible combination of modules in evolution
Publikováno v:
Dyla, M, Kjærgaard, M, Poulsen, H & Nissen, P 2020, ' Structure and Mechanism of P-Type ATPase Ion Pumps ', Annual Review of Biochemistry, vol. 89, pp. 583-603 . https://doi.org/10.1146/annurev-biochem-010611-112801
P-type ATPases are found in all kingdoms of life and constitute a wide range of cation transporters, primarily for H+, Na+, K+, Ca2+, and transition metal ions such as Cu(I), Zn(II), and Cd(II). They have been studied through a wide range of techniqu
Autor:
Mateusz, Dyla, Magnus, Kjaergaard
Publikováno v:
Progress in molecular biology and translational science. 183
Protein kinase A (PKA) is regulated by a diverse class of anchoring proteins known as AKAPs that target PKA to subsets of its activators and substrates. Recently, it was reported that PKA can remain bound to its regulatory subunit after activation in
Autor:
C. Neumann, Poul Nissen, Sara Basse Hansen, Mateusz Dyla, Magnus Kjaergaard, Esben M. Quistgaard, Jacob Andersen
Publikováno v:
Hansen, S B, Dyla, M, Neumann, C, Quistgaard, E M H, Andersen, J L, Kjaergaard, M & Nissen, P 2021, ' The Crystal Structure of the Ca 2+-ATPase 1 from Listeria monocytogenes reveals a Pump Primed for Dephosphorylation ', Journal of Molecular Biology, vol. 433, no. 16, 167015 . https://doi.org/10.1016/j.jmb.2021.167015
Journal of molecular biology 433(16), 167015 (2021). doi:10.1016/j.jmb.2021.167015
Journal of molecular biology 433(16), 167015 (2021). doi:10.1016/j.jmb.2021.167015
Journal of molecular biology 433(16), 167015 (2021). doi:10.1016/j.jmb.2021.167015
Many bacteria export intracellular calcium using active transporters homologous to the sarco/endoplasmic reticulum Ca$^{2+}$-ATPase (SERCA). Here we present three
Many bacteria export intracellular calcium using active transporters homologous to the sarco/endoplasmic reticulum Ca$^{2+}$-ATPase (SERCA). Here we present three
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::10d984167e0419d960771583d5accdfc
https://pure.au.dk/portal/da/publications/the-crystal-structure-of-the-ca2atpase-1-from-listeria-monocytogenes-reveals-a-pump-primed-for-dephosphorylation(0f720282-27dd-4d8f-8b0c-3ac08bac9f0b).html
https://pure.au.dk/portal/da/publications/the-crystal-structure-of-the-ca2atpase-1-from-listeria-monocytogenes-reveals-a-pump-primed-for-dephosphorylation(0f720282-27dd-4d8f-8b0c-3ac08bac9f0b).html
Autor:
Sara Basse, Hansen, Mateusz, Dyla, Caroline, Neumann, Esben Meldgaard Hoegh, Quistgaard, Jacob Lauwring, Andersen, Magnus, Kjaergaard, Poul, Nissen
Publikováno v:
Journal of molecular biology. 433(16)
Many bacteria export intracellular calcium using active transporters homologous to the sarco/endoplasmic reticulum Ca
Autor:
Mateusz Dyla, Magnus Kjaergaard
Publikováno v:
Dyla, M & Kjaergaard, M 2021, Intrinsic disorder in protein kinase A anchoring proteins signaling complexes . in V N Uversky & V N Uversky (eds), Dancing Protein Clouds : Intrinsically Disordered Proteins in the Norm and Pathology, Part C . Elsevier, Amsterdam, Progress in Molecular Biology and Translational Science, vol. 183, pp. 271-294 . https://doi.org/10.1016/bs.pmbts.2021.06.005
Progress in Molecular Biology and Translational Science ISBN: 9780323852999
Progress in Molecular Biology and Translational Science ISBN: 9780323852999
Protein kinase A (PKA) is regulated by a diverse class of anchoring proteins known as AKAPs that target PKA to subsets of its activators and substrates. Recently, it was reported that PKA can remain bound to its regulatory subunit after activation in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e4382982f801a5af8e2137dfe488e547
https://pure.au.dk/portal/da/publications/intrinsic-disorder-in-protein-kinase-a-anchoring-proteins-signaling-complexes(b1232825-a697-40c1-96d6-84fc1a886279).html
https://pure.au.dk/portal/da/publications/intrinsic-disorder-in-protein-kinase-a-anchoring-proteins-signaling-complexes(b1232825-a697-40c1-96d6-84fc1a886279).html
Autor:
Magnus Kjaergaard, Mateusz Dyla
Publikováno v:
Proc Natl Acad Sci U S A
Dyla, M & Kjaergaard, M 2020, ' Intrinsically disordered linkers control tethered kinases via effective concentration ', Proceedings of the National Academy of Sciences of the United States of America, vol. 117, no. 35 . https://doi.org/10.1073/pnas.2006382117
Dyla, M & Kjaergaard, M 2020, ' Intrinsically disordered linkers control tethered kinases via effective concentration ', Proceedings of the National Academy of Sciences of the United States of America, vol. 117, no. 35 . https://doi.org/10.1073/pnas.2006382117
Kinase specificity is crucial to the fidelity of signalling pathways, yet many pathways use the same kinases to achieve widely different effects. Specificity arises in part from the enzymatic domain, but also from the physical tethering of kinases to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a15af08ca4becb40d57e447a1a2c3ca0
https://doi.org/10.1101/2020.04.04.023713
https://doi.org/10.1101/2020.04.04.023713
Autor:
Magnus Kjaergaard, Mateusz Dyla
Publikováno v:
Biophysical Journal. 120:305a-306a
Publikováno v:
Dyla, M, Basse Hansen, S, Nissen, P & Kjaergaard, M 2019, ' Structural dynamics of P-type ATPase ion pumps ', Biochemical Society Transactions, vol. 47, no. 5, pp. 1247-1257 . https://doi.org/10.1042/BST20190124
P-type ATPases transport ions across biological membranes against concentration gradients and are essential for all cells. They use the energy from ATP hydrolysis to propel large intramolecular movements, which drive vectorial transport of ions. Tigh