Zobrazeno 1 - 10
of 135
pro vyhledávání: '"Maurizio Molinari"'
Autor:
Ester Piovesana, Claudia Magrin, Matteo Ciccaldo, Martina Sola, Manolo Bellotto, Maurizio Molinari, Stéphanie Papin, Paolo Paganetti
Publikováno v:
Scientific Reports, Vol 13, Iss 1, Pp 1-14 (2023)
Abstract Neurodegenerative disorders are characterized by the brain deposition of insoluble amyloidogenic proteins, such as α-synuclein or Tau, and the concomitant deterioration of cell functions such as the autophagy-lysosomal pathway (ALP). The AL
Externí odkaz:
https://doaj.org/article/1846b0d20eb74f7f89a1ff35c7714a2b
Autor:
Marika K. Kucińska, Juliette Fedry, Carmela Galli, Diego Morone, Andrea Raimondi, Tatiana Soldà, Friedrich Förster, Maurizio Molinari
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-20 (2023)
Abstract The endoplasmic reticulum (ER) is an organelle of nucleated cells that produces proteins, lipids and oligosaccharides. ER volume and activity are increased upon induction of unfolded protein responses (UPR) and are reduced upon activation of
Externí odkaz:
https://doaj.org/article/776f9f177eb6455eaad59ec9b6588efd
Autor:
Mikhail Rudinskiy, Maria Pons-Vizcarra, Tatiana Soldà, Ilaria Fregno, Timothy Jan Bergmann, Ana Ruano, Aida Delgado, Sara Morales, Xavier Barril, Manolo Bellotto, Elena Cubero, Ana María García-Collazo, Natalia Pérez-Carmona, Maurizio Molinari
Publikováno v:
PLoS ONE, Vol 18, Iss 11 (2023)
Externí odkaz:
https://doaj.org/article/198a5f8d8044421ba9f38e8ce4f93178
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
The ER increases in size upon stress in response to the UPR and is remodelled after the stressor is removed by a process called recov-ER-phagy. Here, the authors show remodelling to pre-stress ER size occurs by micro-ER-phagy requiring ESCRT-III comp
Externí odkaz:
https://doaj.org/article/d6b40ad97a5d4efa9a4258dae758c269
Publikováno v:
AIMS Biophysics, Vol 3, Iss 4, Pp 456-478 (2016)
The biosynthesis of proteins entails a complex series of chemical reactions that transform the information stored in the nucleic acid sequence into a polypeptide chain that needs to properly fold and reach its functional location in or outside the ce
Externí odkaz:
https://doaj.org/article/2464bc2295a34ad184eb1b5c41c1d470
Autor:
Concetta Guerra, Maurizio Molinari
Publikováno v:
Cells, Vol 9, Iss 9, p 2000 (2020)
The endoplasmic reticulum (ER) is site of synthesis and maturation of membrane and secretory proteins in eukaryotic cells. The ER contains more than 20 members of the Protein Disulfide Isomerase (PDI) family. These enzymes regulate formation, isomeri
Externí odkaz:
https://doaj.org/article/4a4a2d3da039466aa08203be91ec2f31
Autor:
Ilaria Fregno, Maurizio Molinari
Publikováno v:
F1000Research, Vol 7 (2018)
The endoplasmic reticulum (ER) is a highly dynamic organelle in eukaryotic cells. It is deputed to lipid and protein biosynthesis, calcium storage, and the detoxification of various exogenous and endogenous harmful compounds. ER activity and size mus
Externí odkaz:
https://doaj.org/article/6d90a3c6604e4801b2e3c3d3f5f9c98a
Publikováno v:
Molecular & Cellular Oncology, Vol 4, Iss 2 (2017)
Amplification of the candidate oncogene TLOC1/SEC62 in tumors correlates with reduced patient survival. The recently reported role of SEC62 as an autophagy receptor that controls endoplasmic reticulum (ER) size and function might open new scenarios f
Externí odkaz:
https://doaj.org/article/2a4b808b24fe409dadf7c52536b9d9af
Unconventional Use of LC3 by Coronaviruses through the Alleged Subversion of the ERAD Tuning Pathway
Publikováno v:
Viruses, Vol 3, Iss 9, Pp 1610-1623 (2011)
Pathogens of bacterial and viral origin hijack pathways operating in eukaryotic cells in many ways in order to gain access into the host, to establish themselves and to eventually produce their progeny. The detailed molecular characterization of the
Externí odkaz:
https://doaj.org/article/ccbf1f68febc4e0489e7a6e26d51d986
Publikováno v:
Swiss Medical Weekly, Vol 144, Iss 3334 (2014)
The endoplasmic reticulum (ER) is an intracellular compartment dedicated to the synthesis and maturation of secretory and membrane proteins, totalling about 30% of the total eukaryotic cells proteome. The capacity to produce correctly folded polypept
Externí odkaz:
https://doaj.org/article/0a8537e5036946629c5ae8cebdd7a693