Zobrazeno 1 - 10 of 24 pro vyhledávání: '"metabolism [RNA-Binding Protein FUS]"'
1
Cytoplasmic FUS triggers early behavioral alterations linked to cortical neuronal hyperactivity and inhibitory synaptic defects
Autor: Scekic-Zahirovic, Jelena, Sanjuan-Ruiz, Inmaculada, Kan, Vanessa, Megat, Salim, De Rossi, Pierre, Dieterlé, Stéphane, Cassel, Raphaelle, Jamet, Marguerite, Kessler, Pascal, Wiesner, Diana, Tzeplaeff, Laura, Demais, Valérie, Sahadevan, Sonu, Hembach, Katharina M, Muller, Hans-Peter, Picchiarelli, Gina, Mishra, Nibha, Antonucci, Stefano, Dirrig-Grosch, Sylvie, Kassubek, Jan, Rasche, Volker, Ludolph, Albert, Boutillier, Anne-Laurence, Roselli, Francesco, Polymenidou, Magdalini, Lagier-Tourenne, Clotilde, Liebscher, Sabine, Dupuis, Luc
Publikováno v: Nature Communications
Nature Communications, Nature Publishing Group, 2021, 12 (1), pp.3028. ⟨10.1038/s41467-021-23187-9⟩
Nature Communications, Vol 12, Iss 1, Pp 1-19 (2021)
Nature Communications 12(1), 3028 (2021). doi:10.1038/s41467-021-23187-9
Nature Communications, Nature Publishing Group, 2021, 12 (1), ⟨10.1038/s41467-021-23187-9⟩
Nature Communications, 2021, 12 (1), ⟨10.1038/s41467-021-23187-9⟩
Nature Communications, 2021, 12 (1), pp.3028. ⟨10.1038/s41467-021-23187-9⟩
Gene mutations causing cytoplasmic mislocalization of the RNA-binding protein FUS lead to severe forms of amyotrophic lateral sclerosis (ALS). Cytoplasmic accumulation of FUS is also observed in other diseases, with unknown consequences. Here, we sho
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::c8536f94d17455134cebd44e2729e13b
https://www.hal.inserm.fr/inserm-03376335
Zobrazit plný text záznamu
2
Multi-omics profiling identifies a deregulated FUS-MAP1B axis in ALS/FTD–associated UBQLN2 mutants
Autor: Laura Strohm, Zehan Hu, Yongwon Suk, Alina Rühmkorf, Erin Sternburg, Vanessa Gattringer, Henrick Riemenschneider, Riccardo Berutti, Elisabeth Graf, Jochen H Weishaupt, Monika S Brill, Angelika B Harbauer, Dorothee Dormann, Jörn Dengjel, Dieter Edbauer, Christian Behrends
Publikováno v: Life science alliance 5(11), e202101327 (2022). doi:10.26508/lsa.202101327
Ubiquilin-2 (UBQLN2) is a ubiquitin-binding protein that shuttles ubiquitinated proteins to proteasomal and autophagic degradation. UBQLN2 mutations are genetically linked to the neurodegenerative disorders amyotrophic lateral sclerosis and frontotem
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::999c052f873cd378aead73b0b3b1e8b6
https://doi.org/10.26508/lsa.202101327
Zobrazit plný text záznamu
3
The ALS-Associated FUS (P525L) Variant Does Not Directly Interfere with Microtubule-Dependent Kinesin-1 Motility
Autor: Seifert, Anne, Drechsler, Hauke, Japtok, Julia, Korten, Till, Diez, Stefan, Hermann, Andreas
Publikováno v: International Journal of Molecular Sciences, Vol 22, Iss 2422, p 2422 (2021)
International journal of molecular sciences 22(5), 2422-(2021). doi:10.3390/ijms22052422
International Journal of Molecular Sciences
Volume 22
Issue 5
Deficient intracellular transport is a common pathological hallmark of many neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS). Mutations in the fused-in-sarcoma (FUS) gene are one of the most common genetic causes for familial
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::ef91019ea3d39d68003d57630d8e5536
https://www.mdpi.com/1422-0067/22/5/2422
Zobrazit plný text záznamu
4
Genome Wide Analysis Points towards Subtype-Specific Diseases in Different Genetic Forms of Amyotrophic Lateral Sclerosis
Autor: Marcel Naumann, Andreas Hermann, Banaja P. Dash, Jared Sterneckert
Publikováno v: International journal of molecular sciences 21(18), 6938-(2020). doi:10.3390/ijms21186938
International Journal of Molecular Sciences
Volume 21
Issue 18
International Journal of Molecular Sciences, Vol 21, Iss 6938, p 6938 (2020)
Amyotropic lateral sclerosis (ALS) is a lethally progressive and irreversible neurodegenerative disease marked by apparent death of motor neurons present in the spinal cord, brain stem and motor cortex. While more and more gene mutants being establis
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0d29795516a3bf903129529c3d5293e1
Zobrazit plný text záznamu
5
FUS-mediated regulation of acetylcholine receptor transcription at neuromuscular junctions is compromised in amyotrophic lateral sclerosis
Autor: Chantal Sellier, Nick H.M. van Bakel, Amila Zuko, Céline Sijlmans, Sina Mersmann, Anne-Laurence Boutillier, Annemarie Hübers, Amr Aly, Marina Wagner, Stéphane Dieterlé, Moushami Mallik, Marc-Antoine Goy, Clotilde Lagier-Tourenne, Gina Picchiarelli, Albert C. Ludolph, Luc Dupuis, Erik Storkebaum, Julia Higelin, Angela Rosenbohm, Li Zhang, Tobias M. Boeckers, Marije Been, Maria Demestre, Jelena Scekic-Zahirovic, Nadia Messaddeq, Inmaculada Sanjuan-Ruiz
Publikováno v: Nature Neuroscience
Nature Neuroscience, Nature Publishing Group, 2019, 22 (11), pp.1793-1805. ⟨10.1038/s41593-019-0498-9⟩
Nature neuroscience
Nature Neuroscience, 22, 1793-1805
Nature reviews / Neuroscience 22(11), 1793-1805 (2019). doi:10.1038/s41593-019-0498-9
Nature Neuroscience, 22, 11, pp. 1793-1805
Neuromuscular junction (NMJ) disruption is an early pathogenic event in amyotrophic lateral sclerosis (ALS). Yet, direct links between NMJ pathways and ALS-associated genes such as FUS, whose heterozygous mutations cause aggressive forms of ALS, rema
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a29ee2725324cd47aad72a1d21ded34f
https://hal.archives-ouvertes.fr/hal-02406369
Zobrazit plný text záznamu
6
FUS (fused in sarcoma) is a component of the cellular response to topoisomerase I–induced DNA breakage and transcriptional stress
Autor: Fernando Gómez-Herreros, Philip Van Damme, Marcel Naumann, Duncan A. Q. Moore, María Isabel Martínez-Macías, Ryan L. Green, Majid Hafezparast, Andreas Hermann, Keith W. Caldecott
Publikováno v: Life Science Alliance
idUS. Depósito de Investigación de la Universidad de Sevilla
instname
Digital.CSIC. Repositorio Institucional del CSIC
Life science alliance 2(2), e201800222 (2019). doi:10.26508/lsa.201800222
FUS (fused in sarcoma) plays a key role in several steps of RNA metabolism, and dominant mutations in this protein are associated with neurodegenerative diseases. Here, we show that FUS is a component of the cellular response to topoisomerase I (TOP1
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a997c0650dddf63f90e8dfd173f3753
http://europepmc.org/articles/PMC6391683
Zobrazit plný text záznamu
7
Impaired DNA damage response signaling by FUS-NLS mutations leads to neurodegeneration and FUS aggregate formation
Autor: Susanne Petri, Florian Wegner, Axel Freischmidt, Albert C. Ludolph, Peter Reinhardt, Arun Pal, Karlheinz Holzmann, Joachim Weis, Anthony A. Hyman, Anand Goswami, Andreas Hermann, Stephan W. Grill, Xenia Lojewski, Marcel Naumann, Anne Vehlow, Julia Japtok, Alexander Storch, Nils Cordes, Francisco Pan-Montojo, Dirk Troost, Mengmeng Jin, Jared Sterneckert, Ina Poser, René Günther, Tobias M. Boeckers, Jochen H. Weishaupt, Erik Storkebaum, Maximilian Naujock, Nancy Stanslowsky, Stefan Liebau, Marie Frickenhaus
Publikováno v: Nature Communications 9, 335 (2018). doi:10.1038/s41467-017-02299-1
Nature Communications
Nature Communications 9(1), 335 (2018). doi:10.1038/s41467-017-02299-1
Nature communications, 9(1). Nature Publishing Group
Nature Communications, Vol 9, Iss 1, Pp 1-17 (2018)
Nature Communications 9(2018), 335
Nature Communications, 9, pp. 1-17
Nature Communications, 9, 1-17
Amyotrophic lateral sclerosis (ALS) is the most frequent motor neuron disease. Cytoplasmic fused in sarcoma (FUS) aggregates are pathological hallmarks of FUS-ALS. Proper shuttling between the nucleus and cytoplasm is essential for physiological cell
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e83528d7f7c7ee164b556332b6e9382
https://publications.rwth-aachen.de/record/757240
Zobrazit plný text záznamu
8
Stepwise acquirement of hallmark neuropathology in FUS-ALS iPSC models depends on mutation type and neuronal aging
Autor: Albert C. Ludolph, Tobias M. Boeckers, Stefan Liebau, Moritz Klingenstein, Julia Japtok, Stefan Putz, Xenia Lojewski, Marcel Naumann, Alexander Storch, Jared Sterneckert, Peter Reinhardt, Andreas Hermann, Maria Demestre
Publikováno v: Neurobiology of Disease, Vol 82, Iss, Pp 420-429 (2015)
Neurobiology of disease 82, 420-429 (2015). doi:10.1016/j.nbd.2015.07.017
Autosomal-dominant mutations within the gene FUS (fused in sarcoma) are responsible for 5% of familial cases of amyotrophic lateral sclerosis (ALS). The FUS protein is physiologically mainly located in the nucleus, while cytoplasmic FUS aggregates ar
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6df30cb25e4b5550e91a70d2f177333f
http://www.sciencedirect.com/science/article/pii/S0969996115300218
Zobrazit plný text záznamu
9
TDP-43 and FUS: a nuclear affair
Autor: Christian Haass, Dorothee Dormann
Publikováno v: Trends in neurosciences 34(7), 339-348 (2011). doi:10.1016/j.tins.2011.05.002
Misfolded TAR DNA binding protein 43 (TDP-43) and Fused-In-Sarcoma (FUS) protein have recently been identified as pathological hallmarks of the neurodegenerative disorders amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTL
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eded261c91757806c4528bcf4f196d1f
https://doi.org/10.1016/j.tins.2011.05.002
Zobrazit plný text záznamu
10
Monomethylated and unmethylated FUS exhibit increased binding to Transportin and distinguish FTLD-FUS from ALS-FUS
Autor: Claudia Abou-Ajram, Tobias Madl, Dorothee Dormann, Christian Haass, Marc Suárez-Calvet, Stefan Reber, Manuela Neumann, Benjamin Bourgeois, Moritz Resch, Marc-David Ruepp, Eva B. E. Funk, Christoph Göbl, Olaf Ansorge, Ian R. A. Mackenzie, Thomas Arzberger, Dieter Edbauer, Daniel Jutzi, Hannelore Hartmann, Elisabeth Kremmer
Publikováno v: Suárez-Calvet, Marc; Neumann, Manuela; Arzberger, Thomas; Abou-Ajram, Claudia; Funk, Eva; Hartmann, Hannelore; Edbauer, Dieter; Kremmer, Elisabeth; Göbl, Christoph; Resch, Moritz; Bourgeois, Benjamin; Madl, Tobias; Reber, Stefan; Jutzi, Daniel; Ruepp, Marc-David; Mackenzie, Ian R. A.; Ansorge, Olaf; Dormann, Dorothee; Haass, Christian (2016). Monomethylated and unmethylated FUS exhibit increased binding to Transportin and distinguish FTLD-FUS from ALS-FUS. Acta neuropathologica, 131(4), pp. 587-604. Springer 10.1007/s00401-016-1544-2
Acta neuropathologica 131(4), 587-604 (2016). doi:10.1007/s00401-016-1544-2
Deposition of the nuclear DNA/RNA-binding protein Fused in sarcoma (FUS) in cytosolic inclusions is a common hallmark of some cases of frontotemporal lobar degeneration (FTLD-FUS) and amyotrophic lateral sclero- sis (ALS-FUS). Whether both diseases a
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a4154823d5e62b824899d61b961d8bc8
https://pubmed.ncbi.nlm.nih.gov/26895297
Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání

Omezení vyhledávání
Plný text Recenzováno Digitální knihovna AV ČR
Zdroje