Literatura científica selecionada sobre o tema "C9ORF72 complex"
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Artigos de revistas sobre o assunto "C9ORF72 complex"
Tang, Dan, Jingwen Sheng, Liangting Xu, Xiechao Zhan, Jiaming Liu, Hui Jiang, Xiaoling Shu et al. "Cryo-EM structure of C9ORF72–SMCR8–WDR41 reveals the role as a GAP for Rab8a and Rab11a". Proceedings of the National Academy of Sciences 117, n.º 18 (17 de abril de 2020): 9876–83. http://dx.doi.org/10.1073/pnas.2002110117.
Texto completo da fonteNörpel, Julia, Simone Cavadini, Andreas D. Schenk, Alexandra Graff-Meyer, Daniel Hess, Jan Seebacher, Jeffrey A. Chao e Varun Bhaskar. "Structure of the human C9orf72-SMCR8 complex reveals a multivalent protein interaction architecture". PLOS Biology 19, n.º 7 (23 de julho de 2021): e3001344. http://dx.doi.org/10.1371/journal.pbio.3001344.
Texto completo da fonteYang, Mei, Chen Liang, Kunchithapadam Swaminathan, Stephanie Herrlinger, Fan Lai, Ramin Shiekhattar e Jian-Fu Chen. "A C9ORF72/SMCR8-containing complex regulates ULK1 and plays a dual role in autophagy". Science Advances 2, n.º 9 (setembro de 2016): e1601167. http://dx.doi.org/10.1126/sciadv.1601167.
Texto completo da fonteAmick, Joseph, Arun Kumar Tharkeshwar, Catherine Amaya, e Shawn M. Ferguson. "WDR41 supports lysosomal response to changes in amino acid availability". Molecular Biology of the Cell 29, n.º 18 (setembro de 2018): 2213–27. http://dx.doi.org/10.1091/mbc.e17-12-0703.
Texto completo da fonteAmick, Joseph, Agnes Roczniak-Ferguson e Shawn M. Ferguson. "C9orf72 binds SMCR8, localizes to lysosomes, and regulates mTORC1 signaling". Molecular Biology of the Cell 27, n.º 20 (15 de outubro de 2016): 3040–51. http://dx.doi.org/10.1091/mbc.e16-01-0003.
Texto completo da fonteChandra, Sunandini, e C. Patrick Lusk. "Emerging Connections between Nuclear Pore Complex Homeostasis and ALS". International Journal of Molecular Sciences 23, n.º 3 (25 de janeiro de 2022): 1329. http://dx.doi.org/10.3390/ijms23031329.
Texto completo da fonteAlvarez-Mora, Maria Isabel, Gloria Garrabou, Tamara Barcos, Francisco Garcia-Garcia, Ruben Grillo-Risco, Emma Peruga, Laura Gort et al. "Bioenergetic and Autophagic Characterization of Skin Fibroblasts from C9orf72 Patients". Antioxidants 11, n.º 6 (8 de junho de 2022): 1129. http://dx.doi.org/10.3390/antiox11061129.
Texto completo da fonteMcAlpine, William, Lei Sun, Kuan-wen Wang, Aijie Liu, Ruchi Jain, Miguel San Miguel, Jianhui Wang et al. "Excessive endosomal TLR signaling causes inflammatory disease in mice with defective SMCR8-WDR41-C9ORF72 complex function". Proceedings of the National Academy of Sciences 115, n.º 49 (15 de novembro de 2018): E11523—E11531. http://dx.doi.org/10.1073/pnas.1814753115.
Texto completo da fonteLiang, Chen, Qiang Shao, Wei Zhang, Mei Yang, Qing Chang, Rong Chen e Jian-Fu Chen. "Smcr8 deficiency disrupts axonal transport-dependent lysosomal function and promotes axonal swellings and gain of toxicity in C9ALS/FTD mouse models". Human Molecular Genetics 28, n.º 23 (18 de outubro de 2019): 3940–53. http://dx.doi.org/10.1093/hmg/ddz230.
Texto completo da fonteTalaia, Gabriel, Joseph Amick e Shawn M. Ferguson. "Receptor-like role for PQLC2 amino acid transporter in the lysosomal sensing of cationic amino acids". Proceedings of the National Academy of Sciences 118, n.º 8 (17 de fevereiro de 2021): e2014941118. http://dx.doi.org/10.1073/pnas.2014941118.
Texto completo da fonteTeses / dissertações sobre o assunto "C9ORF72 complex"
Pietri, David. "Structure and function of the C9ORF72-SMCR8-WDR41 complex and its implication for Amyotrophic Lateral Sclerosis (ALS)". Electronic Thesis or Diss., Strasbourg, 2023. http://www.theses.fr/2023STRAJ087.
Texto completo da fonteAmyotrophic lateral sclerosis (ALS or Charcot disease) is the third most common neurodegenerative disease. The main genetic cause of ALS is an expansion of GGGGCC repeats in the C9ORF72 gene which protein forms a complex with the SMCR8 and WDR41 proteins. To better understand its molecular functions, solving its structure was a main goal of my thesis. In parallel, we discovered that C9ORF72 regulates a newly described mechanism of biogenesis of newly-formed lysosomes, called autophagic lysosome reformation (ALR). This process has been extensively investigated during my thesis, in order to better understand its regulation, particularly for the regeneration of lysosomes in basal conditions and amino acid deprivation. My work reveals a new partner of the C9ORF72 complex as a novel function in lysosome biogenesis. These results could thus explain the dysfunction of lysosomes and neurodegeneration observed in ALS, which open new therapeutic ways for this devastating disease