Academic literature on the topic 'Complexe C9ORF72'
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Journal articles on the topic "Complexe C9ORF72":
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, no. 18 (April 17, 2020): 9876–83. http://dx.doi.org/10.1073/pnas.2002110117.
Alvarez-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, no. 6 (June 8, 2022): 1129. http://dx.doi.org/10.3390/antiox11061129.
Nörpel, Julia, Simone Cavadini, Andreas D. Schenk, Alexandra Graff-Meyer, Daniel Hess, Jan Seebacher, Jeffrey A. Chao, and Varun Bhaskar. "Structure of the human C9orf72-SMCR8 complex reveals a multivalent protein interaction architecture." PLOS Biology 19, no. 7 (July 23, 2021): e3001344. http://dx.doi.org/10.1371/journal.pbio.3001344.
Amick, Joseph, Arun Kumar Tharkeshwar, Catherine Amaya,, and Shawn M. Ferguson. "WDR41 supports lysosomal response to changes in amino acid availability." Molecular Biology of the Cell 29, no. 18 (September 2018): 2213–27. http://dx.doi.org/10.1091/mbc.e17-12-0703.
Yang, Mei, Chen Liang, Kunchithapadam Swaminathan, Stephanie Herrlinger, Fan Lai, Ramin Shiekhattar, and Jian-Fu Chen. "A C9ORF72/SMCR8-containing complex regulates ULK1 and plays a dual role in autophagy." Science Advances 2, no. 9 (September 2016): e1601167. http://dx.doi.org/10.1126/sciadv.1601167.
Amick, Joseph, Agnes Roczniak-Ferguson, and Shawn M. Ferguson. "C9orf72 binds SMCR8, localizes to lysosomes, and regulates mTORC1 signaling." Molecular Biology of the Cell 27, no. 20 (October 15, 2016): 3040–51. http://dx.doi.org/10.1091/mbc.e16-01-0003.
Iyer, Shalini, Vasanta Subramanian, and K. Ravi Acharya. "C9orf72, a protein associated with amyotrophic lateral sclerosis (ALS) is a guanine nucleotide exchange factor." PeerJ 6 (October 17, 2018): e5815. http://dx.doi.org/10.7717/peerj.5815.
Chandra, Sunandini, and C. Patrick Lusk. "Emerging Connections between Nuclear Pore Complex Homeostasis and ALS." International Journal of Molecular Sciences 23, no. 3 (January 25, 2022): 1329. http://dx.doi.org/10.3390/ijms23031329.
Ababneh, Nidaa A., Jakub Scaber, Rowan Flynn, Andrew Douglas, Paola Barbagallo, Ana Candalija, Martin R. Turner, et al. "Correction of amyotrophic lateral sclerosis related phenotypes in induced pluripotent stem cell-derived motor neurons carrying a hexanucleotide expansion mutation in C9orf72 by CRISPR/Cas9 genome editing using homology-directed repair." Human Molecular Genetics 29, no. 13 (June 5, 2020): 2200–2217. http://dx.doi.org/10.1093/hmg/ddaa106.
Liang, Chen, Qiang Shao, Wei Zhang, Mei Yang, Qing Chang, Rong Chen, and 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, no. 23 (October 18, 2019): 3940–53. http://dx.doi.org/10.1093/hmg/ddz230.
Dissertations / Theses on the topic "Complexe C9ORF72":
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.
Amyotrophic 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