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ProteomicsA protein adaptor mediating Ap4A-dependent control of protein acetylation.
Reversible lysine acetylation is a highly conserved post-translational modification across all domains of life, modulating diverse cellular processes. However, the regulatory mechanisms governing this modification remain poorly understood. Here, we uncover a novel regulatory system in Bacillus subti...
ORGANISM(S): Geobacillus thermodenitrificans NG80-2 
2026-01-21 | PXD064203 | Pride
Lysine acetylation Cbs Hdx-ms Ap4a 
ProteomicsPseudouridine-modified tRNA fragments repress malignant protein synthesis and predict leukemic progression in myelodysplastic syndrome
Transfer RNA (tRNA)-derived fragments (tRF) are emerging small noncoding (nc) RNAs that, while commonly altered in cancer, have poorly defined roles in tumorigenesis. Here we show that pseudouridylation (Ψ) of a stem-cell-enriched tRF subtype, mTOG, selectively inhibits malignant protein synthesis p...
ORGANISM(S): Homo sapiens (Human) 
2021-12-20 | PXD023122 | Pride
Rna modifications  development  hematopoiesis  pseudouridine  stem cells  trna fragments  translation control. hdx ms 
ProteomicsDynamics and Structural Features of eEF1A1 and eEF1A2 Paralogs
The aim of the project was to compare the structural dynamics of two tissue-specific variants of human translation elongation factors. eEF1A1 and eEF1A2.
ORGANISM(S): Oryctolagus cuniculus (Rabbit) 
2025-05-07 | PXD056814 | Pride
Elogation factors Protein dynamics Hdx-ms Protein structure Split isotopic envelope 
ProteomicsEukaryotic Ribosome GCN2 interaction Hydrogen/Deuterium Exchange Mass Spectrometry
General control nonderepressible 2 (GCN2) phosphorylates eIF2α, regulating translation in response to nutritional stress. Here, we show that mammalian ribosomes are potent GCN2 activators. Hydrogen/deuterium exchange–mass spectrometry (HDX-MS) showed GCN2 interacting with domain II of the uL10 P-sta...
ORGANISM(S): Oryctolagus cuniculus (Rabbit) 
2019-05-24 | PXD013051 | Pride
Ribosome Gcn2 Hdx-ms 
ProteomicsReduced structural rigidity of MDMX protein enhances binding to TP53 mRNA
The two murine double minute (MDM) family members, MDM2 and MDMX are a well-established negative regulator of p53 activity. Under DNA damage conditions, MDM2 and MDMX are phosphorylated near their RING domains (serine 395 at MDM2 and serine 403 at MDMX) and switch to act as p53 positive regulators. ...
ORGANISM(S): Homo sapiens (Human) 
2026-01-05 | PXD060074 | Pride
Human Mdmx-mdm2 interaction P53 mrna stabilization Ring domain Hdx-ms mapping Lc-ms/ms 
UnknownActivation of GCN2 by the ribosomal P-stalk.
Not available
S-EPMC6421407 | biostudies-literature
ProteomicsStructural proteomic analysis of folding intermediates of FLuc on the human ribosome
bRNC HDX-MS: Protein biogenesis begins on the ribosome where nascent chains are expressed vectorially from their N- to C-terminus, and start to fold as mRNA is translated. How the context of protein synthesis influences protein folding is poorly understood, especially in eukaryotes. Here we describe...
ORGANISM(S): Escherichia coli 
2025-08-11 | PXD055476 | Pride
Ribosome Nascent chain Bacteria Hdx-ms Firefly luciferase Protein synthesis Protein folding 
ProteomicsStructural proteomic analysis of folding intermediates of FLuc on the human ribosome
hRNC HDX-MS: Protein biogenesis begins on the ribosome where nascent chains are expressed vectorially from their N- to C-terminus, and start to fold as mRNA is translated. How the context of protein synthesis influences protein folding is poorly understood, especially in eukaryotes. Here we describe...
ORGANISM(S): Homo sapiens (Human) 
2025-08-11 | PXD055280 | Pride
Human Ribosome Nascent chain Hdx-ms Firefly luciferase Protein synthesis Protein folding 
ProteomicsMechanism of chaperone coordination during cotranslational protein folding in bacteria
Protein folding is assisted by molecular chaperones that bind nascent polypeptides during mRNA translation. Several structurally-distinct classes of chaperones promote de novo folding, suggesting that their activity is coordinated at the ribosome. Here we use biochemical reconstitution and structura...
ORGANISM(S): Escherichia coli 
2024-07-03 | PXD048642 | Pride
Nascent chain Ribosomes Hdx-ms Molecular chaperones Protein synthesis Β-galactosidase Protein folding 
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