Dicarboxylic acid dietary supplementation protects against acute kidney injury

ACS Barbosa, KE Pfister, T Chiba, J Bons… - Journal of the …, 2024 - journals.lww.com
Methods and Results: Mice were fed with either a control diet or diet enriched with
dicarboxylic acids, which are peroxisome-specific FAO substrates, then subjected to either …

[HTML][HTML] Perspectives and opinions from scientific leaders on the evolution of data-independent acquisition for quantitative proteomics and novel biological …

CL Hunter, J Bons, B Schilling - Australian Journal of Chemistry, 2023 - CSIRO Publishing
The methodology of data-independent acquisition (DIA) within mass spectrometry (MS) was
developed into a method of choice for quantitative proteomics, to capture the depth and …

Succinylation of Park 7 Activates a Protective Metabolic Response to Acute Kidney Injury

K Pfister, V Young, B Frankel… - American Journal …, 2024 - journals.physiology.org
Acute Kidney Injury (AKI) is extremely prevalent among hospitalizations and presents a
significant risk for the development of chronic kidney disease and increased mortality …

[HTML][HTML] Protocol for mass spectrometric profiling of lysine malonylation by lysine acetyltransferase in CRISPRi K562 cell lines

R Zhang, J Bons, JP Rose, B Schilling, E Verdin - STAR protocols, 2024 - Elsevier
Lysine malonylation is a protein posttranslational modification. We present a protocol to
generate stable gene-knockdown K562 cell lines through lentiviral infection of a CRISPR …

Dicarboxylic acid supplementation protects from acute kidney injury via stimulation of renal peroxisomal activity

ACS Barbosa, KE Pfister, T Chiba, J Bons, JP Rose… - bioRxiv, 2023 - biorxiv.org
Introduction Lysine succinylation is a post-translational modification associated with the
control of several diseases, including acute kidney injury (AKI). It is suggested that …

[引用][C] Post‐translational modification and phenotype

B Salovska, Y Liu - Proteomics, 2023 - Wiley Online Library
Post-translational modification (PTM) greatly expands the molecular diversity of a protein.
The dynamic decoration of PTMs during the protein lifespan, normally in an amino acid site …