Zobrazeno 1 - 10
of 27
pro vyhledávání: '"Claudia Rato"'
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-15 (2019)
The role of mesencephalic astrocyte-derived neurotrophic factor (MANF) in maintenance of protein folding homeostasis inside the ER has remained unclear. Here the authors determine the structure of the complex between MANF and the ER-localized chapero
Externí odkaz:
https://doaj.org/article/29a9184db10c451b966d07b035dde1b3
Publikováno v:
eLife, Vol 9 (2020)
The metazoan endoplasmic reticulum (ER) serves both as a hub for maturation of secreted proteins and as an intracellular calcium storage compartment, facilitating calcium-release-dependent cellular processes. ER calcium depletion robustly activates t
Externí odkaz:
https://doaj.org/article/2df68a40864044a2966b41fdb69dcf50
Autor:
Milena Vitale, Anush Bakunts, Andrea Orsi, Federica Lari, Laura Tadè, Alberto Danieli, Claudia Rato, Caterina Valetti, Roberto Sitia, Andrea Raimondi, John C Christianson, Eelco van Anken
Publikováno v:
eLife, Vol 8 (2019)
How endoplasmic reticulum (ER) stress leads to cytotoxicity is ill-defined. Previously we showed that HeLa cells readjust homeostasis upon proteostatically driven ER stress, triggered by inducible bulk expression of secretory immunoglobulin M heavy c
Externí odkaz:
https://doaj.org/article/1fadbf5d07454278a95cd18f5e2395cb
Autor:
Meral Tunc-Ozdemir, Claudia Rato, Elizabeth Brown, Stephanie Rogers, Amanda Mooneyham, Sabine Frietsch, Candace T Myers, Lisbeth Rosager Poulsen, Rui Malhó, Jeffrey F Harper
Publikováno v:
PLoS ONE, Vol 8, Iss 2, p e55277 (2013)
The Arabidopsis thaliana genome contains 20 CNGCs, which are proposed to encode cyclic nucleotide gated, non-selective, Ca²⁺-permeable ion channels. CNGC7 and CNGC8 are the two most similar with 74% protein sequence identity, and both genes are pr
Externí odkaz:
https://doaj.org/article/a16dde603bbc447a88044de56bd5083f
Publikováno v:
Nature structural & molecular biology
The enzyme FICD was previously known to AMPylate the ER-resident chaperone BiP, inactivating the chaperone. Mammalian FICD is now shown to catalyze the removal of the AMP group from BiP. Protein folding homeostasis in the endoplasmic reticulum (ER) i
Autor:
Randy J. Read, Luke A. Perera, Yahui Yan, Claudia Rato, David Ron, Lisa Neidhardt, Stephen H. McLaughlin, Steffen Preissler
Publikováno v:
The EMBO Journal
AMPylation is an inactivating modification that alters the activity of the major endoplasmic reticulum (ER) chaperone BiP to match the burden of unfolded proteins. A single ER‐localised Fic protein, FICD (HYPE), catalyses both AMPylation and deAMPy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::466986deec02fe8a92a607c5bdc4eaca
Autor:
David Ron, Steffen Preissler, Randy J. Read, Luke A. Perera, Lisa Neidhardt, Claudia Rato, Stephen H. McLaughlin, Yahui Yan
AMPylation is an inactivating modification that matches the activity of the major endoplasmic reticulum (ER) chaperone BiP to the burden of unfolded proteins. A single ER-localised Fic protein, FICD (HYPE), catalyses both AMPylation and deAMPylation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed1ad99ccf5230ad496fbf2cb613e179
Autor:
Anush Bakunts, Andrea Orsi, Alberto Danieli, Laura Tadè, Roberto Sitia, Andrea Raimondi, Milena Vitale, Eelco van Anken, Federica Lari, Claudia Rato, John C. Christianson, Caterina Valetti
Publikováno v:
eLife, Vol 8 (2019)
eLife
eLife
How endoplasmic reticulum (ER) stress leads to cytotoxicity is ill-defined. Previously we showed that HeLa cells readjust homeostasis upon proteostatically driven ER stress, triggered by inducible bulk expression of secretory immunoglobulin M heavy c
Autor:
Federica Lari, Roberto Sitia, John C. Christianson, Milena Vitale, Anush Bakunts, Claudia Rato, Andrea Orsi, Alberto Danieli, Caterina Valetti, Eelco van Anken, Laura Tadè, Andrea Raimondi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b501376335bad4bb211e290a9a0c3efa
https://doi.org/10.7554/elife.41168.024
https://doi.org/10.7554/elife.41168.024