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Numerous reagents have been developed to enable chemical proteomic analysis of small molecule-protein interactomes. However, the performance of these reagents has not been systematically evaluated and compared. Herein, we report our efforts to conduct a parallel assessment of two widely-used chemica...
ORGANISM(S): Homo sapiens (Human) 
2019-08-21 | PXD014066 | Pride
Protein biotinylation via chemical or enzymatic reactions is often coupled with streptavidin-based enrichment and on-beads digestion in numerous biological applications. However, the popular on-beads digestion method faces major challenges of streptavidin contamination, the lost information of bioti...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2021-04-21 | MSV000087256 | MassIVE
the performance of five common cleavable biotin linkers are assessed parallelly by using commercially available thiol-reactive probe IPM (2-iodo-N-(prop-2-yn-1-yl)acetamide) in profiling cysteinome
ORGANISM(S): Homo Sapiens 
2022-01-16 | PXD031019 |
The present work describes a novel search program for the detection of both MS-cleavable and non-cleavable crosslinked peptides and it is the first software program reported with both capacities. The search strategy has been implemented in the computer program MetaMorpheus, which has a user-friendly...
ORGANISM(S): Escherichia coli 
2018-07-16 | PXD009000 | Pride
Cleavable crosslinking has traditionally been employed in bottom-up mass spectrometry to elucidate protein structure and protein-protein interactions through identification of peptides bearing characteristic mass adducts. Here, we demonstrate the application of cleavable crosslinking in top-down mas...
ORGANISM(S): Homo Sapiens (human) Equus Caballus 
Identification of SortaseA cleavable MHC class I proteins (CD1d, H2Kb) for shotgun lipidomics
ORGANISM(S): Mus musculus (Mouse) 
2022-07-08 | PXD034366 | Pride
Proteome-wide crosslinking mass spectrometry studies have coincided with the advent of MS-cleavable crosslinkers that can reveal the individual masses of the two crosslinked peptides. However, recently such studies have also been published with non-cleavable crosslinkers suggesting that MS-cleavabil...
ORGANISM(S): Mus musculus (Mouse) Escherichia coli Drosophila melanogaster (Fruit fly) 
2022-06-24 | PXD032821 | Pride
Reanalysis of a synthetic crosslinked peptide library datasets with DSS (non-cleavable), DSSO and DSBU (MS-cleavable) cross linkers from Beveridge et al., Nat. Commun., 2020 (PXD014337)
ORGANISM(S): Streptococcus pyogenes ABC020006030 
2022-01-11 | PXD027159 | Pride
Cross-linking mass spectrometry (XLMS) is becoming increasingly popular, and current advances are widening the applicability of the technique so that it can be utilized by non-specialist laboratories. Specifically, the use of novel mass spectrometry-cleavable (MS-cleavable) reagents dramatically red...
ORGANISM(S): Bos taurus (Bovine) Cicer arietinum (Chickpea) (Garbanzo) Streptococcus pyogenes serotype M2 Candida albicans (Yeast) Homo sapiens (Human) Oryctolagus cuniculus (Rabbit) Escherichia coli Equus caballus (Horse) 
2019-02-01 | PXD011861 | Pride
Herein, a cleavable hydrophobic derivatization (CHD) strategy was established for the enrichment and identification of pLys peptides. By CHD, 2,5-dioxopyrrolidin-1-yl-3-(decyldisulfanyl)propanoate (Dec-disulf-NHS) was synthesized to react with lysine dephosphorylated peptides, and then the derived p...
ORGANISM(S): Escherichia Coli 
2019-02-12 | PXD012682 |
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