Sort   by:  
 Page size 

Aortic disease poses a significant mortality risk in adults, yet many of its underlying factors remain undiscovered. In this study, we identify mitochondrial NAD⁺ deficiency as a causal factor. Metabolomics analysis of 73 surgical aortic specimens revealed impaired NAD⁺ salvage and mitochondrial ...

2024-12-04 | MTBLS8062 | MetaboLights
We present XL-MS data of the trigger factor:GAPDH complex to define the interaction sites for GAPDH on trigger factor.
ORGANISM(S): Escherichia coli 
2022-06-07 | PXD029365 | Pride
We present HDX-MS data of the trigger factor:GAPDH complex to define the interaction sites for GAPDH on trigger factor and the structure of GAPDH in the bound state.
ORGANISM(S): Escherichia coli 
2022-06-07 | PXD029364 | Pride
As nascent polypeptides exit ribosomes, they are engaged by a series of processing, targeting and folding factors. Here we present a selective ribosome profiling strategy that enables global monitoring of when these factors engage polypeptides in the complex cellular environment. Studies of the Esch...
ORGANISM(S): Escherichia coli 
Molecular chaperones are essential throughout a protein's life and act already during protein synthesis. Bacteria and chloroplasts of plant cells share the ribosome-associated chaperone trigger factor (Tig1 in plastids), facilitating maturation of emerging nascent polypeptides. While typical trigger...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2025-03-11 | PXD052583 | Pride
Molecular chaperones are essential throughout a protein's life and act already during protein synthesis. Bacteria and chloroplasts of plant cells share the ribosome-associated chaperone trigger factor (Tig1 in plastids), facilitating maturation of emerging nascent polypeptides. While typical trigger...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2025-03-11 | PXD052586 | Pride
The cellular environment is critical for efficient protein maturation, but how proteins fold during biogenesis remains poorly understood. We used hydrogen/deuterium exchange (HDX) mass spectrometry (MS) to define, at peptide resolution, the cotranslational chaperone-assisted folding pathway of Esche...
ORGANISM(S): Escherichia coli 
2024-07-12 | PXD036945 | Pride
Peptidyl-prolyl cis/trans isomerases (PPIases) are enzymes that assist in protein folding around proline-peptide bonds, and often possess chaperone activity. Staphylococcus aureus encodes three PPIases; PrsA, PpiB and Trigger factor (TF). Previous work by our group demonstrated a role for both PrsA ...
ORGANISM(S): Staphylococcus aureus 
2021-01-28 | PXD023811 | Pride
Molecular chaperones are essential throughout a protein's life and act already during protein synthesis. Bacteria and chloroplasts of plant cells share the ribosome-associated chaperone trigger factor (Tig1 in plastids), facilitating maturation of emerging nascent polypeptides. While typical trigger...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2024-12-09 | PXD057264 | Pride
Melioidosis is a potentially fatal infection caused by Burkholderia pseudomallei, a bacterium that is intrinsically resistant to many commonly used antibiotics. Therefore, the identification of new drug targets is essential for the development of new and effective therapies. This study demonstrates...
ORGANISM(S): Burkholderia pseudomallei (strain K96243) 
2026-04-07 | PXD067556 | Pride
Sort   by:  
 Page size