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Статті в журналах з теми "Lysosomal storage disorder (LSD)"
Kuk, Myeong Uk, Yun Haeng Lee, Jae Won Kim, Su Young Hwang, Joon Tae Park, and Sang Chul Park. "Potential Treatment of Lysosomal Storage Disease through Modulation of the Mitochondrial—Lysosomal Axis." Cells 10, no. 2 (February 17, 2021): 420. http://dx.doi.org/10.3390/cells10020420.
Повний текст джерелаHayashi, Okamoto, Kawano, and Iwasaki. "Development of Organelle Replacement Therapy Using a Stearyl-Polyhistidine Peptide against Lysosomal Storage Disease Cells." Molecules 24, no. 16 (August 18, 2019): 2995. http://dx.doi.org/10.3390/molecules24162995.
Повний текст джерелаGorbunova, Victoria N. "Congenital metabolic diseases. Lysosomal storage diseases." Pediatrician (St. Petersburg) 12, no. 2 (August 11, 2021): 73–83. http://dx.doi.org/10.17816/ped12273-83.
Повний текст джерелаBlumenreich, Shani, Or B. Barav, Bethan J. Jenkins, and Anthony H. Futerman. "Lysosomal Storage Disorders Shed Light on Lysosomal Dysfunction in Parkinson’s Disease." International Journal of Molecular Sciences 21, no. 14 (July 14, 2020): 4966. http://dx.doi.org/10.3390/ijms21144966.
Повний текст джерелаOnyenwoke, Rob U., Jonathan Z. Sexton, Feng Yan, María Cristina Huertas Díaz, Lawrence J. Forsberg, Michael B. Major, and Jay E. Brenman. "The mucolipidosis IV Ca2+ channel TRPML1 (MCOLN1) is regulated by the TOR kinase." Biochemical Journal 470, no. 3 (September 4, 2015): 331–42. http://dx.doi.org/10.1042/bj20150219.
Повний текст джерелаDe Filippis, Concetta, Barbara Napoli, Laura Rigon, Giulia Guarato, Reinhard Bauer, Rosella Tomanin, and Genny Orso. "Drosophila D-idua Reduction Mimics Mucopolysaccharidosis Type I Disease-Related Phenotypes." Cells 11, no. 1 (December 31, 2021): 129. http://dx.doi.org/10.3390/cells11010129.
Повний текст джерелаAltarescu, Gheona, Rachel Beeri, Rachel Eiges, Silvina Epsztejn-Litman, Talia Eldar-Geva, Deborah Elstein, Ari Zimran, Ehud J. Margalioth, Ephrat Levy-Lahad, and Paul Renbaum. "Prevention of Lysosomal Storage Diseases and Derivation of Mutant Stem Cell Lines by Preimplantation Genetic Diagnosis." Molecular Biology International 2012 (December 26, 2012): 1–9. http://dx.doi.org/10.1155/2012/797342.
Повний текст джерелаAmodio, Federica, Martina Caiazza, Emanuele Monda, Marta Rubino, Laura Capodicasa, Flavia Chiosi, Vincenzo Simonelli, et al. "An Overview of Molecular Mechanisms in Fabry Disease." Biomolecules 12, no. 10 (October 12, 2022): 1460. http://dx.doi.org/10.3390/biom12101460.
Повний текст джерелаMeikle, Peter J., Doug A. Brooks, Elaine M. Ravenscroft, Miao Yan, Ruth E. Williams, Alvis E. Jaunzems, Timothy K. Chataway, et al. "Diagnosis of lysosomal storage disorders: evaluation of lysosome-associated membrane protein LAMP-1 as a diagnostic marker." Clinical Chemistry 43, no. 8 (August 1, 1997): 1325–35. http://dx.doi.org/10.1093/clinchem/43.8.1325.
Повний текст джерелаLa Cognata, Valentina, Maria Guarnaccia, Agata Polizzi, Martino Ruggieri, and Sebastiano Cavallaro. "Highlights on Genomics Applications for Lysosomal Storage Diseases." Cells 9, no. 8 (August 14, 2020): 1902. http://dx.doi.org/10.3390/cells9081902.
Повний текст джерелаДисертації з теми "Lysosomal storage disorder (LSD)"
Roy, Elise. "Cell disorders in lysosomal storage diseases." Phd thesis, Université René Descartes - Paris V, 2012. http://tel.archives-ouvertes.fr/tel-00683248.
Повний текст джерелаMason, Lyndel Ann. "Expression variation in lysosomal storage disorder genes." Thesis, Queensland University of Technology, 2006. https://eprints.qut.edu.au/16240/1/Lyndel_Mason_Thesis.pdf.
Повний текст джерелаMason, Lyndel Ann. "Expression variation in lysosomal storage disorder genes." Queensland University of Technology, 2006. http://eprints.qut.edu.au/16240/.
Повний текст джерелаLangford-Smith, Alexander William Walker. "Lentiviral vector mediated haematopoietic stem cell gene therapy for mucopolysaccharidosis type IIIA." Thesis, University of Manchester, 2012. https://www.research.manchester.ac.uk/portal/en/theses/lentiviral-vector-mediated-haematopoietic-stem-cell-gene-therapy-for-mucopolysaccharidosis-type-iiia(89f8e108-58f3-42bb-8b80-0e0a1fe45fd7).html.
Повний текст джерелаMauri, Victor [Verfasser]. "Trehalose mediated enhancement of glycosaminoglycan degradation in the lysosomal storage disorder Mucopolysaccharidosis III / Victor Mauri." Köln : Deutsche Zentralbibliothek für Medizin, 2014. http://d-nb.info/1047324342/34.
Повний текст джерелаHuynh, Julie. "ESCRT-Dependent Cell Death in a Caenorhabditis elegans Model of the Lysosomal Storage Disorder Mucolipidosis Type IV." Thesis, The University of Arizona, 2015. http://hdl.handle.net/10150/595811.
Повний текст джерелаDe, Silva Weerakonda Arachchige Bhagya Nilukshi. "A study of neuronal ceroid lipofuscinosis proteins CLN5 and CLN8." Thesis, Kansas State University, 2015. http://hdl.handle.net/2097/35749.
Повний текст джерелаBiochemistry and Molecular Biophysics Interdepartmental Program
Stella Yu-Chien Lee
Neuronal ceroid lipofuscinoses (NCLs) are a group of neurodegenerative lysosomal storage disorders which is the most frequent group of inherited neurodegenerative disorders that affect children leading to severe pathological conditions such as progressive loss of motor neuron functions, loss of vision, mental retardation, epilepsy, ataxia and atrophy in cerebral, cerebella cortex and retina and eventually premature death. Among the many genes that cause NCL, mutations in CLN5 leads to different forms of NCL (infantile, late infantile, juvenile and adult) and mutations in CLN8 leads to progressive epilepsy with mental retardation (EPMR) and a variant late infantile form of NCL. The function(s) of both CLN5 and CLN8 proteins remain elusive. CLN5 is a glycosylated soluble protein that resides in the lysosome. We observed that endogenous CLN5 protein exist in two forms and identified a previously unknown C-terminal proteolytic processing event of CLN5. Using a cycloheximide chase experiment we demonstrated that the proteolytic processing of CLN5 is a post-translational modification. Furthermore treatment with chloroquine showed the processing occurs in low pH cellular compartments. After treatment with different protease inhibitors our results suggested the protease involved in the processing of CLN5 could be a cysteine protease. Using two glycosylation mutants of CLN5, retained in the endoplasmic reticulum (ER) or the Golgi we showed the proteolytic processing occurs in an organelle beyond the ER. This study contributes to understanding the characteristics of the CLN5 protein. CLN8 is an ER resident transmembrane protein that shuttles between the ER and the ER-Golgi intermediate compartment (ERGIC). In our study we identified a potential interaction between CLN8 and a PP2A holoenzyme complex consisting regulatory subunit A α isoform and regulatory subunit B α isoform. Using two CLN8 patient derived fibroblast cell lines we were able to show that the phosphorylated levels of PP2A target kinase Akt was reduced at both of its regulatory sites Ser473 and Thr308 and the activity of PP2A was increased. A delay of ceramide transport from ER to Golgi in CLN8 deficient patient cell lines was observed using BODIPY FL C5-Ceramide staining. Our results provide evidence for CLN8 protein being involved in the regulation of PP2A activity and trafficking of ceramide from ER to Golgi.
Di, Malta Chiara. "The analysis of a mouse model of Lysosomal Storage Disorder uncovers a role for astrocyte dysfunction in neurodegeneration." Thesis, Open University, 2012. http://oro.open.ac.uk/54503/.
Повний текст джерелаHersh, Bradley Michael 1973. "C. elegans apoptosis : CED-4 translocation and involvement in a model of mucolipidosis type IV human lysosomal storage disorder." Thesis, Massachusetts Institute of Technology, 2001. http://hdl.handle.net/1721.1/8305.
Повний текст джерелаIncludes bibliographical references.
The process of programmed cell death is important in the development and homeostasis of multicellular organisms. The conserved morphological events of this process have been termed apoptosis. The molecular mechanisms of apoptosis execution are also conserved. We have investigated the behavior of these shared components during programmed cell death in the nematode Caenorhabditis elegans. We have found that the CED-9 protein, an anti-apoptotic member of the Bcl-2 family of apoptotic regulators, is required for the sequestering of the CED-4 cell-death activator to mitochondria. In the absence of CED-9 in C. elegans embryos, we found that CED-4 protein translocates to the nuclear membrane. In addition, inducing excess programmed cell death by expression of the EGL-1 cell-death activator triggers the translocation of CED-4 from mitochondria to the nuclear membrane. We performed a genetic screen for mutations that trigger programmed cell death in ced-9 gain-of-function animals where cell death is blocked. We identified a mutation in cup-5, the C. elegans homolog of the human mucolipidosis type IV gene, which is mutated in a lysosomal storage disorder. We found that cup-5 is required for viability and that excess lysosomes accumulate in cup-5 mutants. In addition, cup--5 mutants contain excess programmed cell deaths, suggesting that apoptosis may play a role in the pathology of mucolipidosis type IV.
by Bradley Michael Hersh.
Ph.D.
Budden, Theodore. "CLN5 deficiency results in alterations in the activation of autophagy." Thesis, Kansas State University, 2014. http://hdl.handle.net/2097/20473.
Повний текст джерелаDepartment of Biology
Stella Y. Lee
CLN5 is one of several proteins that when mutated result in the lysosomal storage disorder (LSD) Neuronal Ceroid Lipofuscinosis (NCL). CLN5 is a soluble lysosomal protein that has no known function at this time. Previously we showed that eight asparagine residues in CLN5 are N-glycosylated, and that this modification is important for the protein’s transport and function. Now, we have identified a link between the activation of autophagy and CLN5 deficiency. The autophagy-lysosomal protein degradation system is one of the major pathways the cell uses to degrade intracellular material and recycle cellular building blocks. It was recently shown that other CLN proteins affect the relative level of autophagy, indicating a potential link between the autophagy pathway and the NCLs. By knocking down endogenous CLN5 in HeLa we showed that, upon stress induction, cells responded with higher levels of autophagy activation. Consistent with these knockdown experiments, there is a higher level of the autophagy marker protein, LC3-II, in CLN5 patient cells that are naturally deficient for the CLN5 protein. Pharmaceutical induction of autophagy through different means also showed higher LC3-II levels compared to control, though patterns differed in the type of autophagy induced. In summary, we discovered that the autophagy pathway is altered in CLN5 deficient cells, indicating a potential role for CLN5 in autophagy. Further analyses of the autophagy pathway will shed light on where CLN5 is acting and the mechanism by which defective CLN5 causes NCL.
Книги з теми "Lysosomal storage disorder (LSD)"
Maegawa, Gustavo H. B. Lysosomal Storage Disorders. Oxford University Press, 2017. http://dx.doi.org/10.1093/med/9780199937837.003.0068.
Повний текст джерелаHollak, Carla E. M. Cholesteryl Ester Storage Disease. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780199972135.003.0058.
Повний текст джерелаCassiman, David, and Carla E. M. Hollak. Approach to the Patient with Hepato-Gastroenterological or Abdominal Signs and Symptoms. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780199972135.003.0074.
Повний текст джерелаWaldek, Stephen. Fabry disease. Edited by Neil Turner. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780199592548.003.0335_update_001.
Повний текст джерелаSedel, Frédéric. Niemann-Pick Disease Type C. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780199972135.003.0053.
Повний текст джерелаFrawley, Geoff. Mucopolysaccharidoses. Oxford University Press, 2013. http://dx.doi.org/10.1093/med/9780199764495.003.0064.
Повний текст джерелаWaldek, Stephen. Fabry disease. Edited by Neil Turner. Oxford University Press, 2015. http://dx.doi.org/10.1093/med/9780199592548.003.0337.
Повний текст джерелаServais, Aude. Nephropathic Cystinosis in Adults. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780199972135.003.0060.
Повний текст джерелаWaldek, Stephen. Fabry disease. Edited by Neil Turner. Oxford University Press, 2015. http://dx.doi.org/10.1093/med/9780199592548.003.0336.
Повний текст джерелаvan der Ploeg, Ans T., and Pascal Laforêt. Pompe Disease. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780199972135.003.0055.
Повний текст джерелаЧастини книг з теми "Lysosomal storage disorder (LSD)"
Patel, Shutish C., Peter G. Pentchev, Howard S. Kruth, Margaret L. Grunnet, and Sundar Suresh. "Abnormal Cholesterol Metabolism in Primary Brain Cultures of the Lysosomal Cholesterol Storage Disorder (LCSD) Murine Mutant." In Lipid Storage Disorders, 193–200. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4613-1029-7_23.
Повний текст джерелаEllsworth, Katarzyna A., Laura M. Pollard, Sara Cathey, and Tim Wood. "Measurement of Elevated Concentrations of Urine Keratan Sulfate by UPLC-MSMS in Lysosomal Storage Disorders (LSDs): Comparison of Urine Keratan Sulfate Levels in MPS IVA Versus Other LSDs." In JIMD Reports, 11–18. Berlin, Heidelberg: Springer Berlin Heidelberg, 2016. http://dx.doi.org/10.1007/8904_2016_1.
Повний текст джерела"Lysosomal Storage Disease (LSD)." In Clinical Atlas of Canine and Feline Ophthalmic Disease, 308–9. Chichester, UK: John Wiley & Sons, Inc, 2015. http://dx.doi.org/10.1002/9781118840801.ch145.
Повний текст джерела"Lysosomal Lipid Storage Disorder." In Encyclopedia of Autism Spectrum Disorders, 2769. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-319-91280-6_300973.
Повний текст джерелаLinhart, Ales. "The heart in inherited metabolic disorders: lysosomal and glycogen storage diseases." In ESC CardioMed, 1540–45. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780198784906.003.0372.
Повний текст джерелаSyed Haneef, S. A., and C. George Priya Doss. "Personalized Pharmacoperones for Lysosomal Storage Disorder." In Advances in Protein Chemistry and Structural Biology, 225–65. Elsevier, 2016. http://dx.doi.org/10.1016/bs.apcsb.2015.10.001.
Повний текст джерелаHoover, Kevin B. "Lipidoses." In Musculoskeletal Imaging Volume 2, edited by Kevin B. Hoover, 73–78. Oxford University Press, 2019. http://dx.doi.org/10.1093/med/9780190938178.003.0083.
Повний текст джерелаSawaf, Hanny, Angelika L. Erwin, Fang Zhao, Tushar J. Vachharajani, and Xiangling Wang. "Enzyme-Replacement Therapy in Fabry Disease." In Multidisciplinary Experiences in Renal Replacement Therapy [Working Title]. IntechOpen, 2022. http://dx.doi.org/10.5772/intechopen.103799.
Повний текст джерелаTrauner, Doris A. "Neurological and Cognitive Consequences of Nephropathic Cystinosis." In Cognitive and Behavioral Abnormalities of Pediatric Diseases. Oxford University Press, 2010. http://dx.doi.org/10.1093/oso/9780195342680.003.0039.
Повний текст джерелаKåks, Ida, and Peter Magnusson. "Fabry Disease." In Cardiomyopathy - Disease of the Heart Muscle [Working Title]. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.99142.
Повний текст джерела