Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Ainhoa, Lezamiz"'
Autor:
Elvira Infante, Yongjian Wang, Catherine M. Shanahan, Stephanie Board, Andrew Stannard, Samuel A. Gulaidi Breen, Ainhoa Lezamiz, Palma Rico-Lastres, Fani Panagaki, Vinoth Sundar Rajan, Elena Rostkova, Pere Roca-Cusachs, Sergi Garcia-Manyes, Amy E. M. Beedle
Publikováno v:
Infante, E, Stannard, A, Board, S J, Rico-Lastres, P, Rostkova, E, Beedle, A E M, Lezamiz, A, Wang, Y J, Gulaidi Breen, S, Panagaki, F, Sundar Rajan, V, Shanahan, C, Roca-Cusachs, P & Garcia-Manyes, S 2019, ' The mechanical stability of proteins regulates their translocation rate into the cell nucleus ', Nature Physics, vol. 15, no. 9, pp. 973-981 . https://doi.org/10.1038/s41567-019-0551-3
Publons
Nature Physics
Publons
Nature Physics
A cell’s ability to react to mechanical stimuli is known to be affected by the transport of transcription factors, the proteins responsible for regulating transcription of DNA into RNA, across the membrane enveloping its nucleus. Yet the molecular
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::44c515c138bed1ed5dac5723562d2c70
https://kclpure.kcl.ac.uk/ws/files/113466324/The_mechanical_stability_of_INFANTE_Published_1_July_2019_GREEEN_AAM.pdf
https://kclpure.kcl.ac.uk/ws/files/113466324/The_mechanical_stability_of_INFANTE_Published_1_July_2019_GREEEN_AAM.pdf
Publikováno v:
The journal of physical chemistry letters. 6(17)
Zinc fingers are highly ubiquitous structural motifs that provide stability to proteins, thus contributing to their correct folding. Despite the high thermodynamic stability of the ZnCys4 centers, their kinetic properties display remarkable lability.
Autor:
Palma Rico-Lastres, Anita Joanna Kosmalska, Daniel Navajas, Ainhoa Lezamiz, Jenny Z. Kechagia, Ion Andreu, Sergi Garcia-Manyes, Anabel-Lise Le Roux, Roger Oria, Catherine M. Shanahan, Amy E. M. Beedle, Pere Roca-Cusachs, Xavier Trepat, Alberto Elosegui-Artola, Marina Uroz
Publikováno v:
Cell
Elosegui-Artola, A, Andreu, I, Beedle, A E M, Lezamiz, A, Uroz, M, Kosmalska, A J, Oria, R, Kechagia, J Z, Rico-Lastres, P, Le Roux, A-L, Shanahan, C M, Trepat, X, Navajas, D, Garcia-Manyes, S & Roca-Cusachs, P 2017, ' Force Triggers YAP Nuclear Entry by Regulating Transport across Nuclear Pores ', Cell, vol. 171, no. 6, pp. 1397-1410.e14 . https://doi.org/10.1016/j.cell.2017.10.008
Elosegui-Artola, A, Andreu, I, Beedle, A E M, Lezamiz, A, Uroz, M, Kosmalska, A J, Oria, R, Kechagia, J Z, Rico-Lastres, P, Le Roux, A-L, Shanahan, C M, Trepat, X, Navajas, D, Garcia-Manyes, S & Roca-Cusachs, P 2017, ' Force Triggers YAP Nuclear Entry by Regulating Transport across Nuclear Pores ', Cell, vol. 171, no. 6, pp. 1397-1410.e14 . https://doi.org/10.1016/j.cell.2017.10.008
YAP is a mechanosensitive transcriptional activator with a critical role in cancer, regeneration, and organ size control. Here, we show that force applied to the nucleus directly drives YAP nuclear translocation by decreasing the mechanical restricti
Autor:
Palma Rico-Lastres, Marc Mora, Guillaume Stirnemann, Carles Solsona, Sergi Garcia-Manyes, Yongjian Wang, Ainhoa Lezamiz
Publikováno v:
Recercat. Dipósit de la Recerca de Catalunya
instname
The Journal of Physical Chemistry Letters
Dipòsit Digital de la UB
Universidad de Barcelona
Wang, Y J, Rico-Lastres, P, Lezamiz, A, Mora, M, Solsona, C, Stirnemann, G & Garcia-Manyes, S 2018, ' DNA Binding Induces a Nanomechanical Switch in the RRM1 Domain of TDP-43 ', Journal of physical chemistry letters, vol. 9, no. 14, pp. 3800-3807 . https://doi.org/10.1021/acs.jpclett.8b01494
instname
The Journal of Physical Chemistry Letters
Dipòsit Digital de la UB
Universidad de Barcelona
Wang, Y J, Rico-Lastres, P, Lezamiz, A, Mora, M, Solsona, C, Stirnemann, G & Garcia-Manyes, S 2018, ' DNA Binding Induces a Nanomechanical Switch in the RRM1 Domain of TDP-43 ', Journal of physical chemistry letters, vol. 9, no. 14, pp. 3800-3807 . https://doi.org/10.1021/acs.jpclett.8b01494
Understanding the molecular mechanisms governing protein-nucleic acid interactions is fundamental to many nuclear processes. However, how nucleic acid binding affects the conformation and dynamics of the substrate protein remains poorly understood. H
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1554211b6ca1eccda14b5c811e153c1a
http://hdl.handle.net/2445/140129
http://hdl.handle.net/2445/140129
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