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ProteomicsRecommendations for Automating Hydrogen/Deuterium Exchange Mass Spectrometry Measurements using Data-Independent Acquisition Methods
Two test HX-DIA datasets, Phosphorylase B kinetics and nanobody binding, that can be used to explore the features of DIA-HX and the AutoHX software.
ORGANISM(S): Homo sapiens (Human) 
2025-01-22 | PXD060028 | Pride
Autohx Data-independent acquistion Hx-ms2 Hydrogen deuterium exchange Hx-dia 
ProteomicsAutomating data analysis for hydrogen/deuterium exchange mass spectrometry using data-independent acquisition methodology
We developed an HX-MS2 strategy that supports the acquisition of CID-generated fragment ions alongside their peptide precursors. The approach enables true auto-validation of HX data by mining the rich set of deuterated fragments, using the extra dimension of data to simultaneously confirm the peptid...
ORGANISM(S): Homo sapiens (Human) Oryctolagus cuniculus (Rabbit) 
2023-09-08 | PXD045012 | Pride
Dia Lc-ms Swath-ms Dna-pk Hx-ms 
UnknownAutomating data analysis for hydrogen/deuterium exchange mass spectrometry using data-independent acquisition methodology.
Not available
S-EPMC10928179 | biostudies-literature
ProteomicsThe HisRS-like domain of GCN2 is a pseudoenzyme that can bind uncharged tRNA - HX-MS Data
GCN2 is a stress response kinase that phosphorylates the translation initiation factor eIF2to inhibit general protein synthesis when activated by uncharged tRNA and stalled ribosomes. The presence of a HisRS-like domain in GCN2, normally associated with the ability to bind and aminoacylate tRNAs, le...
ORGANISM(S): Homo sapiens (Human) 
2024-02-01 | PXD049090 | Pride
Hdx-ms 
ProteomicsImmunoproximity biotinylation reveals the axon initial segment proteome
The axon initial segment (AIS) is a specialized neuronal compartment required for action potential generation and neuronal polarity. However, understanding the mechanisms regulating AIS structure and function has been hindered by an incomplete knowledge of its molecular composition. Here, using immu...
ORGANISM(S): Rattus norvegicus (Rat) 
2024-01-02 | PXD045921 | Pride
Axon initial segment Neuron Proteomics Proximity labeling Scrib Ankyring 
ProteomicsA multiplexed microflow LC-MS/MS-PRM assay for serologic quantification of IgG N- and HPX O- glycoforms in liver fibrosis
In this study, we introduce a targeted microflow LC-MS/MS-PRM method for the quantification of multiple glycopeptides in unfractionated serum samples. The entire preparation of 16 samples in a batch is completed within 3 h, and the LC-MS quantification of all the glycoforms in a sample is completed ...
ORGANISM(S): Homo Sapiens (human) 
2023-10-25 | PXD037687 | JPOST Repository
ProteomicsStructural analysis of the interaction between M-PMV matrix protein and human calmodulin – HDX-MS dataset
Calmodulin serves as a regulator for various proteins, such as enzymes, kinases or phosphatases. It can also serve as Ca2+-dependent adaptor protein. Due to the previous evidence that retroviruses use host cell calmodulin for their proliferation, we focused on the description of functional and struc...
ORGANISM(S): Homo sapiens (Human) Mason-Pfizer monkey virus 
2025-12-29 | PXD067350 | Pride
Calmodulin Hydrogen deuterium exchange Structural proteomics Mason-pfizer monkey protein 
ProteomicsThe Mammalian Cytosolic Thioredoxin Reductase Pathway Acts via a Membrane Protein to Reduce ER-localised Proteins
Folding of proteins entering the mammalian secretory pathway requires the insertion of the correct disulfide bonds. Disulfide formation involves both an oxidative pathway for their insertion and a reductive pathway to remove incorrectly formed disulfides. Reduction of these disulfides is critical ...
ORGANISM(S): Homo sapiens (Human) 
2020-04-09 | PXD017923 | Pride
Thioredoxin reductase system Endoplasmic reticulum Sicylia redox proteomics Protein folding 
ProteomicsEnamel proteins from six Homo erectus specimens across China
Homo erectus remains have been found in Africa, Eurasia and Southeast Asia, dating back to 2 million years (Ma), but due to their age and preservation, obtaining informative molecular data from them his been difficult. We successfully extracted ancient enamel proteins from six Middle Pleistocene H. ...
ORGANISM(S): Homo sapiens (Human) 
2026-03-22 | PXD068897 | Pride
ProteomicsIdentification of SpySystem-linked CYP73A5-ATR2 by LC-MSMS
Eukaryotic cytochrome P450 enzymes, generally colocalizing with their redox partner cytochrome P450 reductase (CPR) on the cytoplasmic surface of organelle membranes, often perform poorly in prokaryotic cells, whether expressed with CPR as a tandem chimera or free-floating individuals, causing a low...
ORGANISM(S): Escherichia Coli 
PXD056592 |
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