Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Roman Lyakhovetsky"'
Autor:
Ruth Belostotsky, Michael Y. Sherman, Roi Bar, Bodo B. Beck, Yaacov Frishberg, Fanny Shkedy, Shimrit Tzvi-Behr, Bernd Hoppe, Roman Lyakhovetsky, Björn Reusch
Publikováno v:
Journal of molecular medicine (Berlin, Germany). 96(7)
Primary hyperoxaluria type 1 is a severe kidney stone disease caused by abnormalities of the peroxisomal alanine-glyoxylate aminotransferase (AGT). The most frequent mutation G170R results in aberrant mitochondrial localization of the active enzyme.
Publikováno v:
Journal of Medical Genetics. 51:526-529
Background The primary hyperoxalurias are a group of recessive kidney diseases, characterised by extensive accumulation of calcium oxalate that progressively coalesces into kidney stones. Oxalate overproduction is facilitated by perturbations in the
Autor:
Daniel Kaganovich, Triana Amen, Roman Lyakhovetsky, Joanna Turkowska, Ayelet-chen Abraham, Hanna Salmonowicz, Mikolaj Ogrodnik, Władysław Średniawa, Noam Eichler, Rachel Brown, Sundararaghavan Pattabiraman
Publikováno v:
Proceedings of the National Academy of Sciences. 111:8049-8054
Aging is associated with the accumulation of several types of damage: in particular, damage to the proteome. Recent work points to a conserved replicative rejuvenation mechanism that works by preventing the inheritance of damaged and misfolded protei
Autor:
Peter J. Peters, George A. Carlson, Susan F. Godsave, Gabriela Warburg, Krister Kristensson, Janine Kutzsche, Albert Taraboulos, Katarina M. Luhr, Sanaa Moussa, Dulce Papy-Garcia, Miri D. Goldberg, Alexander Rouvinski, Maria Kounin, Sharon Karniely, Carsten Korth, Roman Lyakhovetsky
Publikováno v:
The Journal of Cell Biology
Journal of Cell Biology, 204(3), 423-441. Rockefeller University Press
Journal of Cell Biology, 204(3), 423-441. Rockefeller University Press
PrPSc forms micrometer long amyloidic strings that can congregate in clusters and webs at the surface of living cells.
Mammalian prions refold host glycosylphosphatidylinositol-anchored PrPC into β-sheet–rich PrPSc. PrPSc is rapidly truncated
Mammalian prions refold host glycosylphosphatidylinositol-anchored PrPC into β-sheet–rich PrPSc. PrPSc is rapidly truncated
Autor:
Yoav Soen, Roman Lyakhovetsky, Daniel Kaganovich, Ayelet-chen Werdiger, Aaron D. Gitler, Sarah J. Weisberg
Publikováno v:
Proceedings of the National Academy of Sciences. 109:15811-15816
Neurodegenerative diseases constitute a class of illnesses marked by pathological protein aggregation in the brains of affected individuals. Although these disorders are invariably characterized by the degeneration of highly specific subpopulations o
Autor:
Daniel Kaganovich, Tziona Ben-Gedalya, Michal Bejerano-Sagie, Natalya M. Kogan, Yifat Yedidia, Roman Lyakhovetsky, Marcela Karpuj, Ehud Cohen
Publikováno v:
Journal of Cell Science. 124:1891-1902
Despite the activity of cellular quality-control mechanisms, subsets of mature and newly synthesized polypeptides fail to fold properly and form insoluble aggregates. In some cases, protein aggregation leads to the development of human neurodegenerat
Autor:
Roman, Lyakhovetsky, Yosef, Gruenbaum
Publikováno v:
Advances in experimental medicine and biology. 773
Lamins are nuclear intermediate filament proteins that are conserved in all multicellular animals. Proteins that resemble lamins are also found in unicellular organisms and in plants. Lamins form a proteinaceous meshwork that outlines the nucleoplasm
Autor:
Roman Lyakhovetsky, Yosef Gruenbaum
Publikováno v:
Cancer Biology and the Nuclear Envelope ISBN: 9781489980311
Lamins are nuclear intermediate filament proteins that are conserved in all multicellular animals. Proteins that resemble lamins are also found in unicellular organisms and in plants. Lamins form a proteinaceous meshwork that outlines the nucleoplasm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6606e114bcef694df9e0c109704308e7
https://doi.org/10.1007/978-1-4899-8032-8_11
https://doi.org/10.1007/978-1-4899-8032-8_11
Publikováno v:
Genetics. 156:983-994
REII is a Schizosaccharomyces pombe repression element located at the centromere-proximal end of the mat silent domain. Here we show that inversion of REII enhances silencing on its centromere-proximal side while suppressing silencing on its centrome