Zobrazeno 1 - 10
of 53
pro vyhledávání: '"Jens Danielsson"'
Autor:
Mia L. Abramsson, Cagla Sahin, Jonathan T. S. Hopper, Rui M. M. Branca, Jens Danielsson, Mingming Xu, Shane A. Chandler, Nicklas Österlund, Leopold L. Ilag, Axel Leppert, Joana Costeira-Paulo, Lisa Lang, Kaare Teilum, Arthur Laganowsky, Justin L. P. Benesch, Mikael Oliveberg, Carol V. Robinson, Erik G. Marklund, Timothy M. Allison, Jakob R. Winther, Michael Landreh
Publikováno v:
JACS Au, Vol 1, Iss 12, Pp 2385-2393 (2021)
Externí odkaz:
https://doaj.org/article/7f0e3b6cb2494cfdaa4cfb5acec6a09a
Publikováno v:
Current Research in Structural Biology, Vol 2, Iss , Pp 68-78 (2020)
Random encounters between proteins in crowded cells are by no means passive, but found to be under selective control. This control enables proteome solubility, helps to optimise the diffusive search for interaction partners, and allows for adaptation
Externí odkaz:
https://doaj.org/article/3acb138201b246a3805b50163ab91356
Autor:
Ann-Sofi Johansson, Monika Vestling, Per Zetterström, Lisa Lang, Lina Leinartaitė, Mikael Karlström, Jens Danielsson, Stefan L Marklund, Mikael Oliveberg
Publikováno v:
PLoS ONE, Vol 7, Iss 4, p e36104 (2012)
Neurodegeneration in protein-misfolding disease is generally assigned to toxic function of small, soluble protein aggregates. Largely, these assignments are based on observations of cultured neural cells where the suspect protein material is titrated
Externí odkaz:
https://doaj.org/article/042651e0e7974a7f9a75648bce24bfc8
Autor:
Ulrika Nordström, Lisa Lang, Elaheh Ekhtiari Bidhendi, Per Zetterström, Mikael Oliveberg, Jens Danielsson, Peter M. Andersen, Stefan L. Marklund
Publikováno v:
Journal of Neurochemistry. 164:77-93
Mutations in the human Superoxide dismutase 1 (hSOD1) gene are well-established cause of the motor neuron disease ALS. Patients and transgenic (Tg) ALS model mice carrying mutant variants develop hSOD1 aggregates in the CNS. We have identified two hS
Autor:
Kenji Sugase, Masahiro Shirakawa, Daichi Morimoto, Erik Walinda, Sarah Leeb, Jens Danielsson, Naoto Iwakawa
Publikováno v:
The Journal of Physical Chemistry B. 125:2521-2532
Aggregate formation of superoxide dismutase 1 (SOD1) inside motor neurons is known as a major factor in onset of amyotrophic lateral sclerosis. The thermodynamic stability of the SOD1 β-barrel has been shown to decrease in crowded environments such
Publikováno v:
The Journal of Physical Chemistry. B
In the cytosolic environment, protein crowding and Brownian motions result in numerous transient encounters. Each such encounter event increases the apparent size of the interacting molecules, leading to slower rotational tumbling. The extent of tran
Publikováno v:
Current Research in Structural Biology, Vol 2, Iss, Pp 68-78 (2020)
Current Research in Structural Biology
Current Research in Structural Biology
Random encounters between proteins in crowded cells are by no means passive, but found to be under selective control. This control enables proteome solubility, helps to optimise the diffusive search for interaction partners, and allows for adaptation
Publikováno v:
Journal of the American Chemical Society. 140:16570-16579
A conspicuous feature of the amyotrophic lateral sclerosis (ALS)-associated protein SOD1 is that its maturation into a functional enzyme relies on local folding of two disordered loops into a catalytic subdomain. To drive the disorder-to-order transi
Publikováno v:
Biochemistry
The structural stability of proteins is found to markedly change upon their transfer to the crowded interior of live cells. For some proteins, the stability increases, while for others, it decreases, depending on both the sequence composition and the
Autor:
Arthur Laganowsky, Kaare Teilum, Mikael Oliveberg, Justin L. P. Benesch, Rui M. M. Branca, Erik G. Marklund, Joana Costeira-Paulo, Mia L Abramsson, Mingming Xu, Lisa Lang, Michael Landreh, Leopold L. Ilag, Carol V. Robinson, Axel Leppert, Jonathan T. S. Hopper, Shane A. Chandler, Timothy M. Allison, Nicklas Österlund, Cagla Sahin, Jens Danielsson, Jakob R. Winther
Publikováno v:
JACS Au
Abramsson, M L, Sahin, C, Hopper, J T S, Branca, R M M, Danielsson, J, Xu, M, Chandler, S A, Österlund, N, Ilag, L L, Leppert, A, Costeira-Paulo, J, Lang, L, Teilum, K, Laganowsky, A, Benesch, J L P, Oliveberg, M, Robinson, C V, Marklund, E G, Allison, T M, Winther, J R & Landreh, M 2021, ' Charge Engineering Reveals the Roles of Ionizable Side Chains in Electrospray Ionization Mass Spectrometry ', JACS Au, vol. 1, no. 12, pp. 2385-2393 . https://doi.org/10.1021/jacsau.1c00458
JACS Au, Vol 1, Iss 12, Pp 2385-2393 (2021)
Abramsson, M L, Sahin, C, Hopper, J T S, Branca, R M M, Danielsson, J, Xu, M, Chandler, S A, Österlund, N, Ilag, L L, Leppert, A, Costeira-Paulo, J, Lang, L, Teilum, K, Laganowsky, A, Benesch, J L P, Oliveberg, M, Robinson, C V, Marklund, E G, Allison, T M, Winther, J R & Landreh, M 2021, ' Charge Engineering Reveals the Roles of Ionizable Side Chains in Electrospray Ionization Mass Spectrometry ', JACS Au, vol. 1, no. 12, pp. 2385-2393 . https://doi.org/10.1021/jacsau.1c00458
JACS Au, Vol 1, Iss 12, Pp 2385-2393 (2021)
In solution, the charge of a protein is intricately linked to its stability, but electrospray ionization distorts this connection, potentially limiting the ability of native mass spectrometry to inform about protein structure and dynamics. How the be