Temporal dynamics of liver mitochondrial protein acetylation and succinylation and metabolites due to high fat diet and/or excess glucose or fructose.

Autor: Jesse G Meyer, Samir Softic, Nathan Basisty, Matthew J Rardin, Eric Verdin, Bradford W Gibson, Olga Ilkayeva, Christopher B Newgard, C Ronald Kahn, Birgit Schilling

Publikováno v: PLoS ONE, Vol 13, Iss 12, p e0208973 (2018)

Dietary macronutrient composition alters metabolism through several mechanisms, including post-translational modification (PTM) of proteins. To connect diet and molecular changes, here we performed short- and long-term feeding of mice with standard c

Externí odkaz: https://doaj.org/article/cf66df9a1835494b885242f765b83e95

A novel splice variant of Elp3/Kat9 regulates mitochondrial tRNA modification and function

Autor: Rachid Boutoual, Hyunsun Jo, Indra Heckenbach, Ritesh Tiwari, Herbert Kasler, Chad A. Lerner, Samah Shah, Birgit Schilling, Vincenzo Calvanese, Matthew J. Rardin, Morten Scheibye-Knudsen, Eric Verdin

Publikováno v: Scientific Reports, Vol 12, Iss 1, Pp 1-14 (2022)

Abstract Post-translational modifications, such as lysine acetylation, regulate the activity of diverse proteins across many cellular compartments. Protein deacetylation in mitochondria is catalyzed by the enzymatic activity of the NAD+-dependent dea

Externí odkaz: https://doaj.org/article/b028fc2b6f7e4beeb56bfa8dbba5cc9e

Human Elp3/Kat9 is a mitochondrial tRNA modifying enzyme

Autor: Rachid Boutoual, Hyunsun Jo, Indra Heckenbach, Ritesh Tiwari, Herbert Kasler, Chad A. Lerner, Samah Shah, Birgit Schilling, Vincenzo Calvanese, Matthew J. Rardin, Morten Scheibye-Knudsen, Eric Verdin

Post-translational modifications, such as lysine acetylation, regulate the activity of diverse proteins across many cellular compartments. Protein deacetylation in mitochondria is catalyzed by the enzymatic activity of the NAD+-dependent deacetylase

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40987a70136da768018c1476d0800456
https://doi.org/10.1101/2022.03.24.485634

SUCLA2 mutations cause global protein succinylation contributing to the pathomechanism of a hereditary mitochondrial disease

Autor: Matthew J. Rardin, Gabriele Civiletto, Philipp Gut, Reem A. Alkhater, Pieti Pällijeff, Jonathan Thevenet, Stefan Christen, Wenjuan He, Anu Suomalainen, Jesse G. Meyer, Xiaojing Liu, Yuya Nishida, John C. Newman, Berge A. Minassian, Elsebet Ostergaard, Alice Parisi, Christopher B. Jackson, Liliya Euro, Christopher Carroll, Eric Verdin, Sanna Matilainen, Joy Richard, Pirjo Isohanni, Jason W. Locasale, Birgit Schilling, Sofia Moco

Publikováno v: Gut, P, Matilainen, S, Meyer, J G, Pällijeff, P, Richard, J, Carroll, C J, Euro, L, Jackson, C B, Isohanni, P, Minassian, B A, Alkhater, R A, Østergaard, E, Civiletto, G, Parisi, A, Thevenet, J, Rardin, M J, He, W, Nishida, Y, Newman, J C, Liu, X, Christen, S, Moco, S, Locasale, J W, Schilling, B, Suomalainen, A & Verdin, E 2020, ' SUCLA2 mutations cause global protein succinylation contributing to the pathomechanism of a hereditary mitochondrial disease ', Nature Communications, vol. 11, no. 1, 5927 . https://doi.org/10.1038/s41467-020-19743-4
Nature Communications
Nature Communications, Vol 11, Iss 1, Pp 1-14 (2020)

Mitochondrial acyl-coenzyme A species are emerging as important sources of protein modification and damage. Succinyl-CoA ligase (SCL) deficiency causes a mitochondrial encephalomyopathy of unknown pathomechanism. Here, we show that succinyl-CoA accum

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::627067377d873bdec12a0ec3223fba08
https://curis.ku.dk/portal/da/publications/sucla2-mutations-cause-global-protein-succinylation-contributing-to-the-pathomechanism-of-a-hereditary-mitochondrial-disease(3eed9d20-a055-4e59-abcf-f469a814ed8f).html

MS1 Peptide Ion Intensity Chromatograms in MS2 (SWATH) Data Independent Acquisitions. Improving Post Acquisition Analysis of Proteomic Experiments

Autor: Olga Vitek, Alexandria K. Sahu, Matthew J. Rardin, Brendan MacLean, Dylan J. Sorensen, Bradford W. Gibson, Lin-Yang Cheng, Michael J. MacCoss, Birgit Schilling

Publikováno v: Molecular & Cellular Proteomics : MCP

Quantitative analysis of discovery-based proteomic workflows now relies on high-throughput large-scale methods for identification and quantitation of proteins and post-translational modifications. Advancements in label-free quantitative techniques, u

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12f8165ec66fce56e061adca80d0be77
https://doi.org/10.1074/mcp.o115.048181