Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Melania Minoia"'
Autor:
Melania Minoia, Jany Quintana-Cordero, Katharina Jetzinger, Ilgin Eser Kotan, Kathryn Jane Turnbull, Michela Ciccarelli, Anna E. Masser, Dorina Liebers, Eloïse Gouarin, Marius Czech, Vasili Hauryliuk, Bernd Bukau, Günter Kramer, Claes Andréasson
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-16 (2024)
Abstract Cotranslational protein folding depends on general chaperones that engage highly diverse nascent chains at the ribosomes. Here we discover a dedicated ribosome-associated chaperone, Chp1, that rewires the cotranslational folding machinery to
Externí odkaz:
https://doaj.org/article/f23814c7fcb4463299135165d37e841c
Autor:
Mahebali Tabusi, Sigrun Thorsdottir, Maria Lysandrou, Ana Rita Narciso, Melania Minoia, Chinmaya Venugopal Srambickal, Jerker Widengren, Birgitta Henriques-Normark, Federico Iovino
Publikováno v:
PLoS Pathogens, Vol 17, Iss 3, p e1009432 (2021)
Neuronal damage is a major consequence of bacterial meningitis, but little is known about mechanisms of bacterial interaction with neurons leading to neuronal cell death. Streptococcus pneumoniae (pneumococcus) is a leading cause of bacterial meningi
Externí odkaz:
https://doaj.org/article/e5d10e3b952945a8928024eeff867695
Autor:
Melanie Meister-Broekema, Rebecca Freilich, Chandhuru Jagadeesan, Jennifer N. Rauch, Rocio Bengoechea, William W. Motley, E. F. Elsiena Kuiper, Melania Minoia, Gabriel V. Furtado, Maria A. W. H. van Waarde, Shawn J. Bird, Adriana Rebelo, Stephan Zuchner, Peter Pytel, Steven S. Scherer, Federica F. Morelli, Serena Carra, Conrad C. Weihl, Steven Bergink, Jason E. Gestwicki, Harm H. Kampinga
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-14 (2018)
BAG3 is a Hsp70 co-chaperone that is highly expressed in muscles. Here the authors show that several myofibrillar myopathy causing BAG3 mutations are not impaired in Hsp70 binding, but rather impair the ADP-ATP exchange step of the Hsp70 cycle, causi
Externí odkaz:
https://doaj.org/article/ddf05b7beeda41dab42d91cc0f57bb70
Publikováno v:
Disease Models & Mechanisms, Vol 7, Iss 4, Pp 421-434 (2014)
There are numerous human diseases that are associated with protein misfolding and the formation of toxic protein aggregates. Activating the heat shock response (HSR) – and thus generally restoring the disturbed protein homeostasis associated with s
Externí odkaz:
https://doaj.org/article/7798815264e14fa3b4d38a541ae6a4e5
Autor:
Federico Iovino, Ana Rita Narciso, Melania Minoia, Sigrun Thorsdottir, Birgitta Henriques-Normark, Maria Lysandrou, Mahebali Tabusi
Neuronal damage is a major consequence of bacterial meningitis, but little is known about mechanisms that lead to neuronal death.Streptococcus pneumoniae(pneumococcus) is a leading cause of bacterial meningitis and many survivors develop neurological
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dd9a8267aea3eea71d1adcc990b30933
https://doi.org/10.1101/2020.08.20.258681
https://doi.org/10.1101/2020.08.20.258681
Autor:
Laura K. Herzog, Klára Ács, Annika Pfeiffer, Martijn S. Luijsterburg, Claudia Böttcher, Florian A. Salomons, Angela Helfricht, Haico van Attikum, Nico P. Dantuma, Melania Minoia, Wouter W. Wiegant
Publikováno v:
The EMBO Journal. 36:1066-1083
The SUMO‐targeted ubiquitin ligase RNF4 functions at the crossroads of the SUMO and ubiquitin systems. Here, we report that the deubiquitylation enzyme (DUB) ataxin‐3 counteracts RNF4 activity during the DNA double‐strand break (DSB) response.
Autor:
Jennifer N. Rauch, Melania Minoia, Peter Pytel, Rebecca Freilich, Steven Bergink, E. F. Elsiena Kuiper, Shawn J. Bird, Adriana P. Rebelo, William W. Motley, Melanie Meister-Broekema, Gabriel Vasata Furtado, Chandhuru Jagadeesan, Steven S. Scherer, Conrad C. Weihl, Rocio Bengoechea, Stephan Züchner, Jason E. Gestwicki, Maria A.W.H. van Waarde, Harm H. Kampinga, Serena Carra, Federica Francesca Morelli
Publikováno v:
Nature communications, vol 9, iss 1
Nature Communications
Nature Communications, Vol 9, Iss 1, Pp 1-14 (2018)
Nature Communications, 9(1):5342. Nature Publishing Group
Nature Communications
Nature Communications, Vol 9, Iss 1, Pp 1-14 (2018)
Nature Communications, 9(1):5342. Nature Publishing Group
BAG3 is a multi-domain hub that connects two classes of chaperones, small heat shock proteins (sHSPs) via two isoleucine-proline-valine (IPV) motifs and Hsp70 via a BAG domain. Mutations in either the IPV or BAG domain of BAG3 cause a dominant form o
HSPA1A-Independent Suppression of PARK2 C289G Protein Aggregation by Human Small Heat Shock Proteins
Publikováno v:
Molecular and Cellular Biology, 34(19), 3570-3578. AMER SOC MICROBIOLOGY
The C289G mutation of the parkin E3-ubiquitin protein ligase (PARK2) is associated with autosomal recessive juvenile onset Parkinson's disease and was found to be associated with protein aggregation. Members of the human small heat shock proteins (HS
Publikováno v:
Disease Models & Mechanisms
Disease Models & Mechanisms, Vol 7, Iss 4, Pp 421-434 (2014)
Disease Models & Mechanisms, Vol 7, Iss 4, Pp 421-434 (2014)
There are numerous human diseases that are associated with protein misfolding and the formation of toxic protein aggregates. Activating the heat shock response (HSR) – and thus generally restoring the disturbed protein homeostasis associated with s
Autor:
Annika, Pfeiffer, Martijn S, Luijsterburg, Klara, Acs, Wouter W, Wiegant, Angela, Helfricht, Laura K, Herzog, Melania, Minoia, Claudia, Böttcher, Florian A, Salomons, Haico, van Attikum, Nico P, Dantuma
Publikováno v:
The EMBO Journal
The SUMO‐targeted ubiquitin ligase RNF4 functions at the crossroads of the SUMO and ubiquitin systems. Here, we report that the deubiquitylation enzyme (DUB) ataxin‐3 counteracts RNF4 activity during the DNA double‐strand break (DSB) response.