Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Joshua J. Peter"'
Publikováno v:
The FEBS Journal.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::02770120a75954d8ae3d6cb4b020bf4c
https://doi.org/10.1111/febs.16730
https://doi.org/10.1111/febs.16730
Autor:
Joshua J Peter, Helge M Magnussen, Paul A DaRosa, David Millrine, Stephen P Matthews, Frederic Lamoliatte, Ramasubramanian Sundaramoorthy, Ron R Kopito, Yogesh Kulathu
Publikováno v:
The EMBO Journal. 41
Protein UFMylation, i.e., post-translational modification with ubiquitin-fold modifier 1 (UFM1), is essential for cellular and endoplasmic reticulum homeostasis. Despite its biological importance, we have a poor understanding of how UFM1 is conjugate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::35f13c92b89b4f7e58893f4e768a971d
https://doi.org/10.15252/embj.2022111015
https://doi.org/10.15252/embj.2022111015
Autor:
David Millrine, Thomas Cummings, Stephen P. Matthews, Joshua J. Peter, Helge Magnussen, Thomas Macartney, Frederic Lamoliatte, Axel Knebel, Yogesh Kulathu
An essential first step in the posttranslational modification of proteins with UFM1, UFMylation, is the proteolytic cleavage of pro-UFM1 to expose a C-terminal glycine. Of the two UFM1-specific proteases (UFSPs) identified in humans, only UFSP2 is re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::200f779f47f0cc6fb3b9f60bf35b7886
https://doi.org/10.1101/2022.02.28.482207
https://doi.org/10.1101/2022.02.28.482207
Autor:
Joshua J. Peter, Helge M. Magnussen, Paul Anthony DaRosa, David Millrine, Stephen P Matthews, Frederic Lamoliatte, Ramasubramanian Sundaramoorthy, Ron R Kopito, Yogesh Kulathu
Protein UFMylation is emerging as a posttranslational modification essential for endoplasmic reticulum and cellular homeostasis. Despite its biological importance, we have a poor understanding of how UFM1 is conjugated onto substrates. Here, we use a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d3819ab41288e8e19a2c2323d5d08546
https://doi.org/10.1101/2022.01.31.478489
https://doi.org/10.1101/2022.01.31.478489
Autor:
David Millrine, Thomas Cummings, Stephen P. Matthews, Joshua J. Peter, Helge M. Magnussen, Sven M. Lange, Thomas Macartney, Frederic Lamoliatte, Axel Knebel, Yogesh Kulathu
Publikováno v:
Cell reports. 40(5)
An essential first step in the post-translational modification of proteins with UFM1, UFMylation, is the proteolytic cleavage of pro-UFM1 to expose a C-terminal glycine. Of the two UFM1-specific proteases (UFSPs) identified in humans, only UFSP2 is r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a5bcd4b20509cf2819421ac72b06319
https://pubmed.ncbi.nlm.nih.gov/35926457
https://pubmed.ncbi.nlm.nih.gov/35926457
Autor:
Grant J. Herrington, Joshua J. Peterson, Linhai Cheng, Benjamin M. Allington, Renato D. Jensen, Heather S. Healy, Marcelo L. G. Correia
Publikováno v:
Obesity Science & Practice, Vol 8, Iss 4, Pp 510-524 (2022)
Abstract This scoping review synthesizes the existing research on the use of very low‐calorie diets (VLCDs) in subjects with nonalcoholic fatty liver disease (NAFLD) and end‐stage liver disease (ESLD). 19 studies were included, of which 5 were cl
Externí odkaz:
https://doaj.org/article/d29df8a94d684a569fa0d1a0e4402f6d
Autor:
Lee L; Aix-Marseille Univ, INSERM, CNRS, Institut Paoli-Calmettes, CRCM, Marseille, France., Perez Oliva AB; Hospital Clínico Universitario Virgen de la Arrixaca, IMIB-Arrixaca, Centro de Investigación Biomédica en Red de Enfermedades Raras, Murcia, Spain.; Departamento de Biología Celular e Histología, Facultad de Biología, Universidad de Murcia, IMIB-Arrixaca, Centro de Investigación Biomédica en Red de Enfermedades Raras, Murcia, Spain., Martinez-Balsalobre E; Hospital Clínico Universitario Virgen de la Arrixaca, IMIB-Arrixaca, Centro de Investigación Biomédica en Red de Enfermedades Raras, Murcia, Spain., Churikov D; Aix-Marseille Univ, INSERM, CNRS, Institut Paoli-Calmettes, CRCM, Marseille, France., Peter J; MRC Protein Phosphorylation & Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, UK., Rahmouni D; Aix-Marseille Univ, INSERM, CNRS, Institut Paoli-Calmettes, CRCM, Marseille, France., Audoly G; Aix-Marseille Univ, INSERM, CNRS, Institut Paoli-Calmettes, CRCM, Marseille, France., Azzoni V; Aix-Marseille Univ, INSERM, CNRS, Institut Paoli-Calmettes, CRCM, Marseille, France., Audebert S; Aix-Marseille Univ, INSERM, CNRS, Institut Paoli-Calmettes, CRCM, Marseille, France., Camoin L; Aix-Marseille Univ, INSERM, CNRS, Institut Paoli-Calmettes, CRCM, Marseille, France., Mulero V; Hospital Clínico Universitario Virgen de la Arrixaca, IMIB-Arrixaca, Centro de Investigación Biomédica en Red de Enfermedades Raras, Murcia, Spain.; Departamento de Biología Celular e Histología, Facultad de Biología, Universidad de Murcia, IMIB-Arrixaca, Centro de Investigación Biomédica en Red de Enfermedades Raras, Murcia, Spain., Cayuela ML; Hospital Clínico Universitario Virgen de la Arrixaca, IMIB-Arrixaca, Centro de Investigación Biomédica en Red de Enfermedades Raras, Murcia, Spain., Kulathu Y; MRC Protein Phosphorylation & Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, UK., Geli V; Aix-Marseille Univ, INSERM, CNRS, Institut Paoli-Calmettes, CRCM, Marseille, France., Lachaud C; Aix-Marseille Univ, INSERM, CNRS, Institut Paoli-Calmettes, CRCM, Marseille, France.
Publikováno v:
Science advances [Sci Adv] 2021 Sep 24; Vol. 7 (39), pp. eabc7371. Date of Electronic Publication: 2021 Sep 24.