Zobrazeno 1 - 10
of 24
pro vyhledávání: '"Fionna E, Loughlin"'
Autor:
Malgorzata M. Duszczyk, Harry Wischnewski, Tamara Kazeeva, Rajika Arora, Fionna E. Loughlin, Christine von Schroetter, Ugo Pradère, Jonathan Hall, Constance Ciaudo, Frédéric H.-T. Allain
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-17 (2022)
The authors report an unusual mode of AU-rich RNA recognition by the RNA recognition motifs of DND1, a protein essential for germline development, in a 27.5 kDa NMR structure and provide additional insight on DND1 function from cell-based experiments
Externí odkaz:
https://doaj.org/article/e56fd6d7edc04090b57e471e350a8a05
Autor:
Danella L. West, Fionna E. Loughlin, Francisco Rivero-Rodríguez, Naveen Vankadari, Alejandro Velázquez-Cruz, Laura Corrales-Guerrero, Irene Díaz-Moreno, Jacqueline A. Wilce
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
Stress granules are non-membrane bound RNA-protein granules essential for survival during acute cellular stress. TIA-1 is a key protein in the formation of stress granules that undergoes liquid-liquid phase separation by association with specific RNA
Externí odkaz:
https://doaj.org/article/bf0cd7cd38eb4ba49b0ba209b963deb4
Autor:
Daniel Jutzi, Sébastien Campagne, Ralf Schmidt, Stefan Reber, Jonas Mechtersheimer, Foivos Gypas, Christoph Schweingruber, Martino Colombo, Christine von Schroetter, Fionna E. Loughlin, Anny Devoy, Eva Hedlund, Mihaela Zavolan, Frédéric H.-T. Allain, Marc-David Ruepp
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
Mutations in the RNA binding protein FUS cause amyotrophic lateral sclerosis (ALS). Here the authors characterize FUS-binding to U1 snRNP and show that ALS-associated FUS aberrantly contacts U1 snRNA which interferes with its biogenesis pathway.
Externí odkaz:
https://doaj.org/article/29a7f401a44547198252c6ea20fa553a
Publikováno v:
Current Opinion in Structural Biology. 59:134-142
RNA-binding proteins TDP-43 and FUS play essential roles in pre-mRNA splicing, localization, granule formation and other aspects of RNA metabolism. Both proteins are implicated in neurodegenerative diseases amyotrophic lateral sclerosis (ALS) and fro
Autor:
Malgorzata M, Duszczyk, Harry, Wischnewski, Tamara, Kazeeva, Rajika, Arora, Fionna E, Loughlin, Christine, von Schroetter, Ugo, Pradère, Jonathan, Hall, Constance, Ciaudo, Frédéric H-T, Allain
Publikováno v:
Nature communications. 13(1)
Dead End (DND1) is an RNA-binding protein essential for germline development through its role in post-transcriptional gene regulation. The molecular mechanisms behind selection and regulation of its targets are unknown. Here, we present the solution
Autor:
Matthew C.J. Wilce, Danella L West, Simon Crawford, Fionna E. Loughlin, Jacqueline A. Wilce, Saboora Waris, Menachem J. Gunzburg
Publikováno v:
Nucleic Acids Research
TIA-1 is an RNA-binding protein that sequesters target RNA into stress granules under conditions of cellular stress. Promotion of stress granule formation by TIA-1 depends upon self-association of its prion-like domain that facilitates liquid-liquid
Autor:
Christoph Schweingruber, Christine von Schroetter, Anny Devoy, Eva Hedlund, Mihaela Zavolan, Martino Colombo, Sébastien Campagne, Frédéric H.-T. Allain, Fionna E. Loughlin, Marc-David Ruepp, Daniel Jutzi, Stefan Reber, Ralf Schmidt, Jonas Mechtersheimer, Foivos Gypas
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
Nature Communications, 11 (1)
Nature Communications
Nature Communications, 11 (1)
Nature Communications
Mutations in the RNA-binding protein Fused in Sarcoma (FUS) cause early-onset amyotrophic lateral sclerosis (ALS). However, a detailed understanding of central RNA targets of FUS and their implications for disease remain elusive. Here, we use a uniqu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5f5ba1552aeeab3822fc0f3b0a4f7b47
Autor:
Jonathan Hall, Constance Ciaudo, Harry Wischnewski, Fionna E. Loughlin, von Schroetter C, Frédéric Ha, Ugo Pradere, Kazeeva T, Duszczyk Mm
Dead End (DND1) is an RNA-binding protein essential for germline development through its role in post-transcriptional gene regulation. The molecular mechanisms behind selection and regulation of its targets are unknown. Here, we present the solution
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b2503ffde8dcd7e7222c289f41325d6a
Autor:
Christian G. Huber, Pierre Barraud, Mario Schubert, Fionna E. Loughlin, David Schweida, Chiara Cabrele, Christof Regl
Publikováno v:
Journal of Biomolecular Nmr
Journal of Biomolecular NMR
Journal of Biomolecular NMR, Springer Verlag, 2019, 73 (1-2), pp.71-79. ⟨10.1007/s10858-019-00228-6⟩
Journal of Biomolecular NMR, 73 (1-2)
Journal of Biomolecular NMR
Journal of Biomolecular NMR, Springer Verlag, 2019, 73 (1-2), pp.71-79. ⟨10.1007/s10858-019-00228-6⟩
Journal of Biomolecular NMR, 73 (1-2)
N-terminal gluconoylation is a moderately widespread modification in recombinant proteins expressed in Escherichia coli, in particular in proteins bearing an N-terminal histidine-tag. This post-translational modification has been investigated mainly
Autor:
Christine von Schroetter, Antoine Cléry, Peter J. Lukavsky, Magdalini Polymenidou, Eva Maria Hock, Oliver Mühlemann, Tamara Kazeeva, Marc-David Ruepp, Fionna E. Loughlin, Frédéric H.-T. Allain, Martino Colombo, Stefan Reber, Phillip Pauli
Publikováno v:
Molecular Cell
Loughlin, F E, Lukavsky, P J, Kazeeva, T, Reber, S, Hock, E-M, Colombo, M, Von Schroetter, C, Pauli, P, Cléry, A, Mühlemann, O, Polymenidou, M, Ruepp, M-D & Allain, F H-T 2019, ' The Solution Structure of FUS Bound to RNA Reveals a Bipartite Mode of RNA Recognition with Both Sequence and Shape Specificity ', MOLECULAR CELL, vol. 73, no. 3, pp. 490-504.e6 . https://doi.org/10.1016/j.molcel.2018.11.012
Loughlin, F E, Lukavsky, P J, Kazeeva, T, Reber, S, Hock, E-M, Colombo, M, Von Schroetter, C, Pauli, P, Cléry, A, Mühlemann, O, Polymenidou, M, Ruepp, M-D & Allain, F H-T 2019, ' The Solution Structure of FUS Bound to RNA Reveals a Bipartite Mode of RNA Recognition with Both Sequence and Shape Specificity ', MOLECULAR CELL, vol. 73, no. 3, pp. 490-504.e6 . https://doi.org/10.1016/j.molcel.2018.11.012
Fused in sarcoma (FUS) is an RNA binding protein involved in regulating many aspects of RNA process- ing and linked to several neurodegenerative dis- eases. Transcriptomics studies indicate that FUS binds a large variety of RNA motifs, suggesting tha