Letteratura scientifica selezionata sul tema "CHCHD10"
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Articoli di riviste sul tema "CHCHD10":
Zhou, Wei, Dongrui Ma e Eng-King Tan. "Mitochondrial CHCHD2 and CHCHD10: Roles in Neurological Diseases and Therapeutic Implications". Neuroscientist 26, n. 2 (16 settembre 2019): 170–84. http://dx.doi.org/10.1177/1073858419871214.
Liu, Tian, Liam Wetzel, Zexi Zhu, Pavan Kumaraguru, Viraj Gorthi, Yan Yan, Mohammed Zaheen Bukhari et al. "Disruption of Mitophagy Flux through the PARL-PINK1 Pathway by CHCHD10 Mutations or CHCHD10 Depletion". Cells 12, n. 24 (7 dicembre 2023): 2781. http://dx.doi.org/10.3390/cells12242781.
Imai, Yuzuru, Hongrui Meng, Kahori Shiba-Fukushima e Nobutaka Hattori. "Twin CHCH Proteins, CHCHD2, and CHCHD10: Key Molecules of Parkinson’s Disease, Amyotrophic Lateral Sclerosis, and Frontotemporal Dementia". International Journal of Molecular Sciences 20, n. 4 (20 febbraio 2019): 908. http://dx.doi.org/10.3390/ijms20040908.
Gomez, Adriana Morales, Nathan Staff e Stephen C. Ekker. "288 Harnessing the potential of transcriptional adaptation as a mechanism for Amyotrophic lateral sclerosis". Journal of Clinical and Translational Science 7, s1 (aprile 2023): 86. http://dx.doi.org/10.1017/cts.2023.344.
Gomez, Adriana Morales, Nathan Staff e Stephen C. Ekker. "320 Genetic Compensation as a mechanism underlying patients with Rare ALS". Journal of Clinical and Translational Science 6, s1 (aprile 2022): 57. http://dx.doi.org/10.1017/cts.2022.178.
Gomez, Adriana Morales, Nathan Staff e Stephen C. Ekker. "393 Harnessing the potential of transcriptional adaptation as a mechanism for rare Amyotrophic lateral sclerosis". Journal of Clinical and Translational Science 8, s1 (aprile 2024): 117. http://dx.doi.org/10.1017/cts.2024.343.
Keith, Julia L., Emily Swinkin, Andrew Gao, Samira Alminawi, Ming Zhang, Philip McGoldrick, Paul McKeever, Janice Robertson, Ekaterina Rogaeva e Lorne Zinman. "Neuropathologic description of CHCHD10 mutated amyotrophic lateral sclerosis". Neurology Genetics 6, n. 1 (13 gennaio 2020): e394. http://dx.doi.org/10.1212/nxg.0000000000000394.
McCann, Emily P., Jennifer A. Fifita, Natalie Grima, Jasmin Galper, Prachi Mehta, Sarah E. Freckleton, Katharine Y. Zhang et al. "Genetic and immunopathological analysis of CHCHD10 in Australian amyotrophic lateral sclerosis and frontotemporal dementia and transgenic TDP-43 mice". Journal of Neurology, Neurosurgery & Psychiatry 91, n. 2 (5 novembre 2019): 162–71. http://dx.doi.org/10.1136/jnnp-2019-321790.
Xiao, Yatao, Jianmin Zhang, Xiaoqiu Shu, Lei Bai, Wentao Xu, Ailian Wang, Aizhong Chen et al. "Loss of mitochondrial protein CHCHD10 in skeletal muscle causes neuromuscular junction impairment". Human Molecular Genetics 29, n. 11 (2 luglio 2019): 1784–96. http://dx.doi.org/10.1093/hmg/ddz154.
Grossman, Lawrence I., Neeraja Purandare, Rooshan Arshad, Stephanie Gladyck, Mallika Somayajulu, Maik Hüttemann e Siddhesh Aras. "MNRR1, a Biorganellar Regulator of Mitochondria". Oxidative Medicine and Cellular Longevity 2017 (2017): 1–12. http://dx.doi.org/10.1155/2017/6739236.
Tesi sul tema "CHCHD10":
Ropert, Baptiste. "Stratégie de repositionnement thérapeutique pour la SLA/DFT liée à la mutation p.Ser59Leu dans le gène CHCHD10". Electronic Thesis or Diss., Université Côte d'Azur, 2021. http://www.theses.fr/2021COAZ6037.
Mitochondrial diseases are metabolic diseases characterized by a deficit of the respiratory chain, implicating a deficit in the production of energy under the form of ATP. In 2014, Pr. Paquis-Flucklinger’s team analysed several families suffering from mitochondrial myopathy coupled to a motor neuron disorder resembling Amyotrophic Lateral Sclerosis/FrontoTemporal Dementia. By exome sequencing, the team discovered the point mutation p.Ser59Leu in the gene CHCHD10. This gene codes for the mitochondrial protein CHCHD10, which function was unknown. Our team showed that the p.Ser59Leu mutation induces the disorganisation of the MICOS complex, a multiproteic complex which major role is to maintain mitochondrial cristae structure, leading to the mitochondrial myopathy and the motor neuron disease. It was the first evidence of a causal link between a mitochondrial disorder and a motor neuron loss. Amyotrophic Lateral Sclerosis is a terrible disease that provokes the death of motor neurons, inducing a progressive paralysis and patient death, two to three years after onset when the paralysis affects the respiratory system. Today, no curative treatment exists. This led us to start this PhD project: To try to find a molecule able to counter the symptoms due to the p.Ser59Leu mutation in CHCHD10 that could become a drug against the disease. For that, we screened two libraries of molecules containing repurposable drugs, the Prestwick library and the Selleckchem library. We chose this approach to reduce as much as possible the time between a potential discovery and the placing on the market of the new drug. First, we carried out a high throughput screening on an S.cerevisiae mutant that mimics the MICOS complex disassembly. This first screen allowed us to test more than 1500 molecules and to find two efficient molecules in this model. After the first toxicological tests performed on human cells, we decided to focus on one drug: the Nifuroxazide. We have been able to show that Nifuroxazide improves the deleterious phenotypes linked to the p.Ser59Leu mutation in patient fibroblasts but also in motor neurons derived from IPSCs carrying the p.Ser59Leu mutation. Notably, treatment with Nifuroxazide increases the number of normal mitochondrial cristae and elongates the mitochondrial network. We tried to understand the mechanism of action of the Nifuroxazide. We showed that the mechanism of action of the Nifuroxazide does not depend on STAT3 but it increases the interaction between two major actors of the maintaining of mitochondrial cristae structure: Mic60, the main component of the MICOS complex and OPA1. Investigation are still ongoing. The next step will be the pre-clinical analysis in mouse. For that, we will use the mutant murine model CHCHD10S59L/+ that we characterized and that recapitulates the phenotypes observed in patients carrying the p.Ser59Leu mutation. We also worked on the understanding of the molecular cascade that leads to the disorganisation of mitochondrial cristae. We showed that CHCHD10 interacts with SLP2 and that they stabilize the PHB1/PHB2 complex. We demonstrated that in mutant conditions, SLP2/PHB aggregates and the destabilisation of the PHB1/PHB2 complex trigger the activation the protease OMA1 that will cleave OPA1 and provoke the disorganisation of the MICOS complex and the loss of mitochondrial cristae.The work done during this PhD project allowed us to better understand the mechanisms linked to CHCHD10 and to set the bases of what we hope will become, in the future, a new treatment for ALS/FTD linked to the p.Ser59Leu mutation in CHCHD10
Bourefis, Annis-Rayan. "Novel FUS and CHCHD10 models to investigate pathogenic mechanisms in Amyotrophic Lateral Sclerosis". Thesis, Sorbonne université, 2019. http://www.theses.fr/2019SORUS177.
Amyotrophic Lateral Sclerosis (ALS) is a devastating neurodegenerative disorder caused by progressive degeneration of upper and lower motor neurons (MNs), with a very rapid clinical course. It leads to muscle weakness and atrophy progressing to paralysis, with respiratory failure being the major cause of death within years following clinical diagnosis. Two major genes mutated in ALS patients are the RNA-binding protein FUS (FUSed in sarcoma), implicated in RNA metabolism, and coiled-coil-helix-coiled-coil-helix domain 10 (CHCHD10), which plays a role in mitochondria stability. Both these genes have been investigated through different model systems, from small invertebrate models to patient biopsies. However, the major phenotypic features obtained in these models are complex and often controversial. The objective of this work is to provide new insights on the implication of these genes in ALS through the use of new models.To investigate the pathogenic mechanisms induced by FUS and CHCHD10, we generated and characterized two novel stable non-sense mutant zebrafish models for the orthologues of these genes and highlighted several ALS phenotypic features. We demonstrated, for the FUS model but not for CHCHD10, reduced lifespan, locomotor disabilities, aberrant motor axons, disorganized neuromuscular junction (NMJ), muscle and mitochondrial alteration, as well as molecular changes. These findings indicate that loss of fus expression is responsible for the occurrence of distal pathological signs at the NMJ, thus supporting a “dying-back” neuronopathy, in which early disease hallmarks start at the level of the NMJ and progress towards MN cell bodies
Teyssou, Elisa. "Analyses génétiques et fonctionnelles de nouveaux gènes incriminés dans la Sclérose Latérale Amyotrophique (SLA) Genetic analysis of matrin 3 gene in French amyotrophic lateral sclerosis patients and frontotemporal lobar degeneration with amyotrophic lateral sclerosis patients Genetic analysis of CHCHD10 in French familial amyotrophic lateral sclerosis patients". Thesis, Paris 6, 2017. http://www.theses.fr/2017PA066738.
The fatal Amyotrophic Lateral Sclerosis (ALS) motor neuron disease is characterized by the degeneration of upper and lower motor neurons. Most ALS cases are sporadic (SALS) whereas ~10% are familial (FALS). A growing number of genes has been identified in ALS and represent 70% of FALS and 10% of SALS. The aims of this project were to analyze the contribution of 6 rare genes in a large population of French ALS patients and to study the pathogenic impact of some identified variants.The first part of this work was dedicated to the genetic analysis of MATR3, CHCHD10, SS18L1, SQSTM1, UBQLN2 and PFN1 genes. No causing variants were identified for MATR3 and CHCHD10 while 2 new variants, probably pathogenic, were identified for SS18L1, as well as 4 mutations for SQSTM1, 5 for UBQLN2 and 2 already reported mutations for PFN1. These analyses also highlighted a genetic overlap between ALS and other diseases: the Paget disease of bone for SQSTM1 and spastic paraplegia for UBQLN2. The second part of this work was to study the pathogenicity of some of the mutations identified in SQSTM1, UBQLN2 and PFN1 genes using analyses of (i) inclusions in ALS patient post-mortem tissue, (ii) protein expression and degradation pathways in patient lymphoblasts and/or (iii) cellular consequences after in vitro and in vivo overexpression. Our results showed prominent aggregation of mutant SQSTM1 (involved in autophagosomes formation), impaired lysosomal degradation and disrupted protein binding to HSP70 for mutant UBQLN2 and deregulated alternative autophagy and mitophagy pathways for mutant PFN1. Our results (i) precised the contribution of several genes in French ALS patients, (i) documented the genetic overlap between ALS and other diseases and (iii) highlighted the role of protein degradation pathways, especially autophagy, in the pathogenesis of ALS
COCOMAZZI, PAOLO GIUSEPPE. "THE DOUBLE LIFE OF THE APOPTOSIS INDUCING FACTOR (AIF): THE PRO-VITAL ROLE OF A PRO-DEATH PROTEIN". Doctoral thesis, Università degli Studi di Milano, 2020. http://hdl.handle.net/2434/712701.
Nedara, Kenza. "Impact de l'expression de TRIAP1, substrat de la voie d'import AIF/CHCHD4, sur la prolifération des cellules cancéreuses et leur réponse au stress métabolique". Thesis, université Paris-Saclay, 2022. http://www.theses.fr/2022UPASL032.
Under physiological conditions, mitochondria play a fundamental role in cell survival, differentiation and activation by participating in bioenergetic metabolism, synthesis of macromolecules, regulation of signaling pathways or control of the epigenome. This organelle is bifunctional as its involvement is also well established in the cellular response to stress or apoptotic signals. The regulation of the mitochondrial activity is closely linked to its morphology, which is controlled by a set of proteins involved in the remodeling of its ultrastructure and fusion/fission dynamics. These proteins are crucial for the adaptation of mitochondrial biogenesis and activity to the bioenergetic needs of the cell. They are also key players in the regulation of cellular processes and signaling pathways that require the interaction of mitochondria with other cellular compartments such as the endoplasmic reticulum.Recently, a new class of mitochondria shaping proteins (TRIAP1, CHCHD2, CHCHD3, CHCHD6 and CHCHD10) was described. These proteins contain a coiled-coil-helix (CHCHD) domain and are imported into the intermembrane space of the organelle through the activity of the redox-dependent Mia40/CHCHD4 import machinery. They represent potential therapeutic targets as their abnormal expression or deficient activity has been associated with various human pathologies such as neurodegenerative diseases and cancer. During my thesis I studied the TRIAP1 protein which is overexpressed in many types of cancers. RNA interference or recombinant protein overexpression experiments , in a colorectal cancer model, showed that TRIAP1 expression promotes cell proliferation and tumor growth. Our results show that TRIAP1 depletion alters mitochondrial ultrastructure, impacts the metabolomic and lipidomic profile of the cells and induces a retrograde signaling to the nucleus that modifies the gene expression program. Furthermore, our results show that loss of TRIAP1 alters the response of cancer cells to metabolic stress conditions. Overall, our results highlight the relevance of TRIAP1 in the metabolic plasticity of cancer cells. A better understanding of the molecular basis of the mitochondrial activity of TRIAP1 in cancer cells should provide a better understanding of the selective advantage that its overexpression provides to tumor cells
Reinhardt, Camille. "Impact de la voie d’import mitochondrial contrôlée par le complexe AIF/CHCHD4 sur la survie des cellules cancéreuses et la réponse aux traitements anticancéreux". Thesis, Université Paris-Saclay (ComUE), 2019. http://www.theses.fr/2019SACLS542.
In the vast majority of cases, mitochondria are required for tumorigenesis and also for the tumoral response to signals generated by the microenvironmental factors (e.g. nutrient deprivation, hypoxia) or to the effects of anti-cancer treatments (e.g. chemotherapy, radiotherapy). As almost all mitochondrial proteins are nuclear-encoded and imported into the organelle, specialized import machineries have evolved in order to meet the need for protein import. Among these machineries, the one that operates in the intermembrane space and is controlled by CHCHD4/Mia40, regulates the import of a group of proteins (substrates) that play important roles in survival and stress response. Substrates of CHCHD4/Mia40 are involved in a broad panel of mitochondrial activities that includes the biogenesis of respiratory chain complexes, lipid homeostasis, calcium storage, as well as ultrastructure and mitochondrial dynamics. This thesis program was dedicated to the study of the CHCHD4/Mia40 import pathway in cancer cells, with a particular interest for one of the CHCHD4/Mia40 substrates that shapes mitochondrial ultrastructure. Using RNA interference approach and recombinant protein overexpression technique, in a colon cancer model, we showed that the expression of this substrate had a crucial effect on proliferation and tumor growth. Our data also involved this protein in the response to anti-cancer treatments. All together, this work opens a new field of investigations that will not only shed new lights on the metabolic plasticity of cancer cells but also help to identify new metabolic biomarkers
Libri sul tema "CHCHD10":
Huang, Jinfan. Gaseous electron-diffraction investigations: I. Molecular structures of Os(CO)₅, Ru(CO)₅, and CrOF₄. II. Molecular structures and anti-gauche compositions of BrCH₂,CH₂,F, BrCH₂CH₂C1, C1CH₂CH₂F,C1₂CHCHC1₂, and FCH₂CH₂OH. 1989.
Atti di convegni sul tema "CHCHD10":
Souto, Emília Correia, Carolina Maria Marin, Gustavo Carvalho Costa, Igor Braga Farias, Bruno de Mattos Lombardi Badia, Icaro França Navarro Pinto, Roberta Ismael Lacerda Machado, Paulo Victor Sgobbi de Souza, Wladimir Bocca Vieira de Rezende Pinto e Acary Souza Bulle Oliveira. "Family with atypical Parkinsonism due to CHCHD10 gene mutation". In XIII Congresso Paulista de Neurologia. Zeppelini Editorial e Comunicação, 2021. http://dx.doi.org/10.5327/1516-3180.502.
Lumibao, Jan C., e H. Rex Gaskins. "Abstract 2650: Characterizing CHCHD2 subcellular localization in response to hypoxia and redox perturbations in glioblastoma cells". In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-2650.
Lumibao, Jan C., e H. Rex Gaskins. "Abstract 2650: Characterizing CHCHD2 subcellular localization in response to hypoxia and redox perturbations in glioblastoma cells". In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-2650.
Rapporti di organizzazioni sul tema "CHCHD10":
Wei, Huijie, Xin Mu, Yu Li, Hua Lei, De Yang, Tian Li e Junwei Ren. Meta-analysis of the association between CHCHD10 Pro34Ser variant and the risk of frontotemporal dementia. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, maggio 2021. http://dx.doi.org/10.37766/inplasy2021.5.0090.