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ProteomicsNeissLock: an inducible protein anhydride for covalent targeting of endogenous proteins
Effective and convenient covalent protein conjugation could benefit diverse biological systems, stabilizing key protein protein interactions which are otherwise reversible. Neisseria meningitidis contains a protein which undergoes autoproteolysis via an anhydride. Here, we harness this spontaneously...
ORGANISM(S): Escherichia coli 
2021-02-01 | PXD023073 | Pride
Protein engineering Proximity labeling Chemical biology Synthetic biology Nanoassembly Protein conjugation 
ProteomicsUbiquitin-based pathway acts inside chloroplasts to regulate photosynthesis
Photosynthesis is the energetic basis for most life on Earth, and in plants it operates inside double-membrane-bound organelles called chloroplasts. The photosynthetic apparatus comprises numerous proteins encoded by the nuclear and organellar genomes. Maintenance of this apparatus requires the acti...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2022-12-06 | PXD031388 | Pride
Ubiquitinome Chloroplast Organelle Chlorad Proteolysis Ubiquitin 
ProteomicsRepurposed 3D Printer Allows Economical and Programmable Fraction Collection for Proteomics of Nanogram Scale Samples
In this work we describe the construction and application of a repurposed 3D-printer as a fraction collector. We utilise a nanoLC to ensure minimal volumes and surfaces although any LC can be coupled. The setup operates as a high-pH fractionation system capable of effectively working with nanogram s...
ORGANISM(S): Homo sapiens (Human) 
2024-07-12 | PXD051148 | Pride
Dda dia wwa lc-ms/ms Phosphoproteome Proteomics Two-dimensional peptide separation Rna-binding protein 
ProteomicsLarge scale ubiquitination in doxorubicin treated cells
Protein post-translational modification (PTM) plays a central role in the DNA damage response. In particular protein phosphorylation and ubiquitination have been shown to play a major role in the signalling cascade that coordinates break repair with cell cycle progression. Here we performed large-sc...
ORGANISM(S): Homo sapiens (Human) 
2018-02-23 | PXD004445 | Pride
Proteomics Dna damage Ubiquitin Lc-ms/ms 
ProteomicsUVPD of peptides modified with N-terminal UV-absorbing chromophores
Ultraviolet photodissociation (UVPD) has emerged as a powerful alternative to conventional collision-induced dissociation (CID) for peptide and protein sequencing in mass spectrometry–based proteomics. However, UVPD efficiency depends on the presence of UV-absorbing chromophores within analytes.The ...
ORGANISM(S): Homo sapiens (Human) 
2026-06-08 | PXD075227 | Pride
Chromophores Lc-ms Proteomics Nhs chemistry Uvpd 
ProteomicsSystem-wide analyses of the fission yeast poly(A)+ RNA interactome reveal insights into organisation and function of RNA-protein complexes
Production, function, and turnover of mRNA are orchestrated by multi-subunit machineries that play a central role in gene expression. Within these molecular machines, interactions with the target mRNA are mediated by RNA-binding proteins (RBPs), and the accuracy and dynamics of these RNA-protein int...
ORGANISM(S): Schizosaccharomyces pombe OY26 
2021-09-09 | PXD016741 | Pride
Rna exosome complex  rna interactome capture  rna-binding proteins  rna-protein crosslinking  ribonucleoprotein complexes 
ProteomicsEvaluating the performance of photon- and electron-based fragmentation methods in Omnitrap-LCMS analysis of N-glycopeptides
To date, collision-induced dissociation and methods based on electron transfer dissociation are considered the standard approaches for the mass spectrometry analysis of N- and O-glycopeptides, respectively, allowing for identification of both peptide and glycan compositions. In recent years, alterna...
ORGANISM(S): Homo sapiens (Human) 
2026-09-07 | PXD071023 | Pride
Glycopeptides Omnitrap Ecd Uvpd Eid 
ProteomicsDeposition for: Mild and Chemoselective, Light-Driven Post-translational Editing Allows Installation of Reactive Side-Chains into Proteins
MS/MS characterisation data of the publication: Mild anChemoselective, Light-Driven Post-Translational Editing Allows Installation of Reactive Side Chains into Proteins.
ORGANISM(S): Homo sapiens (Human) 
2020-09-24 | PXD019565 | Pride
Synthetic protein modification Chemical biology Photocatalysis 
Proteomicstrypsin_AHSG_Hec293
Refined version of low-pH strong cation exchange, Trypsin r1
ORGANISM(S): Homo Sapiens (human) 
2009-12-31 | PAe005306 | PeptideAtlas
ProteomicsLysN_AHSG_Hec293
Refined version of low-pH strong cation exchange, LysN
ORGANISM(S): Homo Sapiens (human) 
2009-12-31 | PAe005309 | PeptideAtlas
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