Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Andreas Kallinos"'
Autor:
Jane Jardine, Michael J. Clague, Sylvie Urbé, Emma V Rusilowicz-Jones, Andreas Kallinos, Elena Marcassa
Publikováno v:
AUTOPHAGY
Mitochondria and peroxisomes have a number of features in common: they each play interconnected roles in fatty acid and reactive oxygen species (ROS) metabolism and, once damaged, need to be removed by specialized autophagic mechanisms, termed mitoph
Autor:
Weiping Wang, Adan Pinto-Fernandez, Caravella Justin Andrew, Stephanos Ioannidis, Claire Heride, Benedikt M. Kessler, David Komander, Michael J. Clague, Simon J. Davis, Marie Katz, Victoria Smith, Hannah Elcocks, Tim Hammonds, Andreas Kallinos, Sylvie Urbé, Bruce Follows, Christopher J. Dinsmore, Sunkyu Kim, Katherine J. Kayser-Bricker, Steven Mischke, Shawn Fessler, Anne Clancy, Neil P. Jones, Axel Behrens, Jonathan O'Connell, Crystal McKinnon
Publikováno v:
The Journal of Cell Biology
When a ribosome stalls during translation, it runs the risk of collision with a trailing ribosome. Such an encounter leads to the formation of a stable di-ribosome complex, which needs to be resolved by a dedicated machinery. The initial stalling and
Autor:
Weiping Wang, Adan Pinto-Fernandez, Simon J. Davis, Katherine J. Kayser-Bricker, Victoria Smith, Jonathan O'Connell, Christopher J. Dinsmore, Crystal McKinnon, Neil P. Jones, Bruce Follows, Marie Katz, Claire Heride, Sylvie Urbé, Anne Clancy, Benedikt M. Kessler, Andreas Kallinos, Sunkyu Kim, Axel Behrens, Steven Mischke, Stephanos Ioannidis, Shawn Fessler, David Komander, Caravella Justin Andrew, Tim Hammonds, Hannah Elcocks, Michael J. Clague
Publikováno v:
The Journal of Cell Biology
Bioxriv
Bioxriv
Clancy et al. develop a specific chemical inhibitor of USP9X and characterize its effects upon the cellular proteome. This analysis reveals a central role in the regulation of ribosomal stalling through control of critical E3 ligases.
When a rib
When a rib
Autor:
Aitor Martinez, Franziska Guenther, Benedikt M. Kessler, Katherine S. England, Elena Marcassa, Malte Gersch, Simon J. Davis, Alejandro Murad, Katherine J. Kayser-Bricker, Frederic Lamoliatte, Andreas Kallinos, Jane Jardine, Sylvie Urbé, Stephanos Ioannidis, Akshada Gajbhiye, Francesco G. Barone, Mariacarmela Giurrandino, Hannah C. Scott, Christopher J. Burke, Katy McCarron, David Komander, Emma J. Murphy, Alexandre J. Buckmelter, Matthias Trost, Michael K. Ahlijanian, Adan Pinto-Fernandez, Emma V Rusilowicz-Jones, Heather Mortiboys, Michael J. Clague
Publikováno v:
LIFE SCIENCE ALLIANCE
Life Science Alliance
Life Science Alliance
A new inhibitor of the deubiquitylase USP30, an actionable target relevant to Parkinson’s Disease, is introduced and characterised for parameters related to mitophagy.
The mitochondrial deubiquitylase USP30 negatively regulates the selective a
The mitochondrial deubiquitylase USP30 negatively regulates the selective a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb623ed1d21051d2610b1c0e5b7d95ea
http://livrepository.liverpool.ac.uk/3093573/1/LSA-2020-00768-TRR_Merged_PDF.pdf
http://livrepository.liverpool.ac.uk/3093573/1/LSA-2020-00768-TRR_Merged_PDF.pdf
Autor:
Adan Pinto-Fernandez, Heather Mortiboys, Christopher J. Burke, Andreas Kallinos, Simon J. Davis, Katherine J. Kayser-Bricker, Akshada Gajbhiye, Jane Jardine, Stephanos Ioannidis, David Komander, Michael J. Clague, Malte Gersch, Hannah C. Scott, Katy McCarron, Francesco G. Barone, Sylvie Urbé, Aitor Martinez, Alejandro Murad, Emma V Rusilowicz-Jones, Mariacarmela Giurrandino, Matthias Trost, Benedikt M. Kessler, Alexandre J. Buckmelter, Michael K. Ahlijanian, Emma J. Murphy, Franziska Guenther, Elena Marcassa, Frederic Lamoliatte, Katherine S. England
The mitochondrial deubiquitylase USP30 negatively regulates the selective autophagy of damaged mitochondria. It has been proposed as an actionable target to alleviate the loss of function of the mitophagy pathway governed by the Parkinson’s Disease
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d5c825509ce20a0d3a235b0e7ffe38de
https://doi.org/10.1101/2020.04.16.044206
https://doi.org/10.1101/2020.04.16.044206