Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Emma V Rusilowicz-Jones"'
Publikováno v:
Molecular cell. 82(8)
Protein degradation occurs through proteasomal, endosomal, and lysosomal pathways. Technological advancements have allowed for the determination of protein copy numbers and turnover rates on a global scale, which has provided an overview of trends an
Autor:
Sylvie Urbé, Elezabeth Stephen, Michael J. Clague, Francesco G. Barone, Heather Mortiboys, Fernanda Martins Lopes, Emma V Rusilowicz-Jones
Publikováno v:
Life Science Alliance
LIFE SCIENCE ALLIANCE
LIFE SCIENCE ALLIANCE
A detailed look at the properties of a novel USP30 inhibitor applied to studies of mitophagy and pexophagy.
The deubiquitylase USP30 is an actionable target considered for treatment of conditions associated with defects in the PINK1-PRKN pathway
The deubiquitylase USP30 is an actionable target considered for treatment of conditions associated with defects in the PINK1-PRKN pathway
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:
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
Autor:
Andrew B, Fielding, Matthew, Concannon, Sarah, Darling, Emma V, Rusilowicz-Jones, Joseph J, Sacco, Ian A, Prior, Michael J, Clague, Sylvie, Urbé, Judy M, Coulson
Publikováno v:
Oncogene
Ubiquitin-specific protease 15 (USP15) is a widely expressed deubiquitylase that has been implicated in diverse cellular processes in cancer. Here we identify topoisomerase II (TOP2A) as a novel protein that is regulated by USP15. TOP2A accumulates d
Autor:
Emma V. Rusilowicz-Jones, Ailbhe J. Brazel, Francesca Frigenti, Sylvie Urbé, Michael J. Clague
Publikováno v:
Seminars in Cell & Developmental Biology.
We now have a comprehensive inventory of ubiquitin system components. Understanding of any system also needs an appreciation of how components are organised together. Quantitative proteomics has provided us with a census of their relative populations