Zobrazeno 1 - 10
of 61
pro vyhledávání: '"Josée N. Lavoie"'
Autor:
Sara L. Banerjee, Frédéric Lessard, François J.M. Chartier, Kévin Jacquet, Ana I. Osornio-Hernandez, Valentine Teyssier, Karim Ghani, Noémie Lavoie, Josée N. Lavoie, Manuel Caruso, Patrick Laprise, Sabine Elowe, Jean-Philippe Lambert, Nicolas Bisson
Publikováno v:
Cell Reports, Vol 40, Iss 1, Pp 111031- (2022)
Summary: EPH receptors (EPHRs) constitute the largest family among receptor tyrosine kinases in humans. They are mainly involved in short-range cell-cell communication events that regulate cell adhesion, migration, and boundary formation. However, th
Externí odkaz:
https://doaj.org/article/8fd2c903558b408894f403b0c0bd57f6
Autor:
Carole Luthold, Herman Lambert, Solenn M. Guilbert, Marc-Antoine Rodrigue, Margit Fuchs, Alice-Anaïs Varlet, Amélie Fradet-Turcotte, Josée N. Lavoie
Publikováno v:
Cells, Vol 10, Iss 10, p 2638 (2021)
The cochaperone BCL2-associated athanogene 3 (BAG3), in complex with the heat shock protein HSPB8, facilitates mitotic rounding, spindle orientation, and proper abscission of daughter cells. BAG3 and HSPB8 mitotic functions implicate the sequestosome
Externí odkaz:
https://doaj.org/article/6f8aa7adb1fb49bba81b2d28869a7b5c
Publikováno v:
International Journal of Molecular Sciences, Vol 22, Iss 1, p 142 (2020)
The fidelity of actin dynamics relies on protein quality control, but the underlying molecular mechanisms are poorly defined. During mitosis, the cochaperone BCL2-associated athanogene 3 (BAG3) modulates cell rounding, cortex stability, spindle orien
Externí odkaz:
https://doaj.org/article/82fb81a571ee4d889a67b91ce1fb6dda
Autor:
Mirella Meregalli, Josée N. Lavoie, Viola Oorschot, Keith E. Schulze, Emily A. McKaige, Emily C. Baxter, Emmanuelle Lacène, Keyne Monro, Margit Fuchs, Rita J. Serrano, Avnika A. Ruparelia, Clara Yun Qi Lee, Caitlin Williams, Robert J. Bryson-Richardson, Georg Ramm, Yvan Torrente, Tanya Stojkovic
Publikováno v:
Autophagy
Dominant de novo mutations in the co-chaperone BAG3 cause a severe form of myofibrillar myopathy, exhibiting progressive muscle weakness, muscle structural failure, and protein aggregation. To elucidate the mechanism of disease in, and identify thera
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::88e16895245d610b66231b5d46a9172c
https://doi.org/10.1080/15548627.2020.1833500
https://doi.org/10.1080/15548627.2020.1833500
Autor:
Erin K. O'Ferrall, Vladimir V. Rymar, Abbas F. Sadikot, Bernard Brais, Marie Josée Dicaire, Rebecca Robertson, Robert J. Bryson-Richardson, Talita C. Conte, Jason C. Young, Josée N. Lavoie
Publikováno v:
The American Journal of Pathology. 190:554-562
BCL-2-associated athanogene 3 (BAG3) is a co-chaperone to heat shock proteins important in degrading misfolded proteins through chaperone-assisted selective autophagy. The recurrent dominant BAG3-P209L mutation results in a severe childhood-onset myo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d9a37286fea4b97516e6f1760c753751
https://doi.org/10.1016/j.ajpath.2019.11.005
https://doi.org/10.1016/j.ajpath.2019.11.005
Autor:
Herman Lambert, Marc-Antoine Rodrigue, Amélie Fradet-Turcotte, Solenn M. Guilbert, Josée N. Lavoie, Alice-Anaïs Varlet, Margit Fuchs, Carole Luthold
Publikováno v:
Cells; Volume 10; Issue 10; Pages: 2638
Cells, Vol 10, Iss 2638, p 2638 (2021)
Cells
Cells, Vol 10, Iss 2638, p 2638 (2021)
Cells
The cochaperone BCL2-associated athanogene 3 (BAG3), in complex with the heat shock protein HSPB8, facilitates mitotic rounding, spindle orientation, and proper abscission of daughter cells. BAG3 and HSPB8 mitotic functions implicate the sequestosome
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0b66dfc728c4dcf37cb1d762f928411b
Autor:
Margit Fuchs, Carole Luthold, Solenn M Guilbert, Alice Anaïs Varlet, Herman Lambert, Alexandra Jetté, Sabine Elowe, Jacques Landry, Josée N Lavoie
Publikováno v:
PLoS Genetics, Vol 11, Iss 10, p e1005582 (2015)
The co-chaperone BAG3, in complex with the heat shock protein HSPB8, plays a role in protein quality control during mechanical strain. It is part of a multichaperone complex that senses damaged cytoskeletal proteins and orchestrates their seclusion a
Externí odkaz:
https://doaj.org/article/523288e564ad48df9ff97d2de4d343aa
Publikováno v:
International Journal of Molecular Sciences
Volume 22
Issue 1
International Journal of Molecular Sciences, Vol 22, Iss 142, p 142 (2021)
Volume 22
Issue 1
International Journal of Molecular Sciences, Vol 22, Iss 142, p 142 (2021)
The fidelity of actin dynamics relies on protein quality control, but the underlying molecular mechanisms are poorly defined. During mitosis, the cochaperone BCL2-associated athanogene 3 (BAG3) modulates cell rounding, cortex stability, spindle orien
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::596f44b6a65d9a77ecdc8e282b776ed7
https://pubmed.ncbi.nlm.nih.gov/33375626
https://pubmed.ncbi.nlm.nih.gov/33375626
Publikováno v:
Cell Cycle
The human adenovirus (Ad) type 2/5 early region 4 (E4) ORF4 protein (E4orf4) exerts a remarkable tumor cell-selective killing activity in mammalian cells. This indicates that E4orf4 can target tumor cell-defining features and is a unique tool to prob
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aea7dc3d93b3002643f4530260f72da1
https://pubmed.ncbi.nlm.nih.gov/33103553
https://pubmed.ncbi.nlm.nih.gov/33103553
Autor:
Josée N. Lavoie, Ana I. Osornio-Hernandez, Nicolas Bisson, Jean-Philippe Lambert, Sabine Elowe, Kévin Jacquet, Frédéric Lessard, Sara L. Banerjee, Patrick Laprise, Noémie Lavoie
SUMMARYThe EPH family is the largest among receptor tyrosine kinases (RTKs) in humans. In contrast to other RTKs, EPH receptors (EPHRs) cognate ligands, ephrins, are tethered to the cell surface. This results in EPHR-ephrin signaling being mainly inv
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9bb8a3eb31896985b704b825eb08df08
https://doi.org/10.1101/2020.09.06.285270
https://doi.org/10.1101/2020.09.06.285270
