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UnknownDesign of CID-cleavable protein cross-linkers: identical mass modifications for simpler sequence analysis.
Not available
S-EPMC4581996 | biostudies-literature
UnknownAn isotopically coded CID-cleavable biotinylated cross-linker for structural proteomics.
Not available
S-EPMC3033670 | biostudies-literature
UnknownAn enhanced protein crosslink identification strategy using CID-cleavable chemical crosslinkers and LC/MS(n) analysis.
Not available
S-EPMC3426502 | biostudies-literature
ProteomicsMapping of nanobody binding sites on human LRRK2 by CX-MS
As part of an in-depth characterization of nanobodies directed against the human Leucine-rich repeat kinase 2 (LRRK2), epitopes of the nanobodies bound to LRRK2 were mapped by chemical crosslinking combined with mass spectrometry using the CID-cleavable crosslinker disuccinimidyl sulfoxide (DSSO).
ORGANISM(S): Homo sapiens (Human) 
2022-02-27 | PXD030063 | Pride
Cl-ms Lrrk2 Dsso Nanobodies Cx-ms Crosslinking Cid-cleavable 
ProteomicsA Glycosidic-Bond-Based Mass-Spectrometry-Cleavable Cross-linker Enables In Vivo Cross-linking for Protein Complex Analysis
Chemical cross-linking mass spectrometry (CXMS) has emerged as a powerful technology to analyze protein complex structure and interaction. However, the spectral fragmentation behavior and spectral data retrieval of cross-linked peptides are more complex than single peptides. In this study, we design...
ORGANISM(S): Homo Sapiens Saccharomyces Cerevisiae 
2023-12-06 | PXD047554 |
ProteomicsAnalysis of conformational changes induced by binding of allosteric nanobodies to a bacterial LRRK2 homologue by CX-MS
As part of an in-depth characterization of nanobodies directed against the Chlorobium tepidum protein CtRoco, a bacterial LRRK2 homologue, chemical crosslinking combined with mass spectrometry (CX-MS) was performed. Two allosteric nanobodies binding to two different epitopes in the LRR and the Roc d...
ORGANISM(S): Chlorobium tepidum 
2024-04-23 | PXD046634 | Pride
Lrrk2 Dsso Nanobodies Crosslinking Ctroco 
UnknownSynthesis of CID-cleavable protein crosslinking agents containing quaternary amines for structural mass spectrometry.
Not available
S-EPMC6138586 | biostudies-literature
ProteomicsA Collision-induced Dissociation Cleavable Isobaric Tag for Peptide Fragment Ion-based Quantification in Proteomics
Fragment ion-based proteome quantification methods quantify peptides based on unique peptide fragment ions avoiding the issue of ratio distortion that is commonly observed for reporter ion-based quantification approaches. Herein, we present a novel approach that relies on a collision-induced dissoci...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2020-08-17 | PXD018790 | Pride
Isotopic labelling Proteomics Cid cleavable tag Fragment ion-based quantification Isobaric labelling 
ProteomicsFinding and using Diagnostic Ions in Collisional Induced Crosslinked Peptide Fragmentation Spectra
Crosslinking mass spectrometry (XL-MS) has emerged as a powerful tool in its own right for the investigation of protein structures and interactions. Utilizing standard shotgun MS mass spectrometry equipment and specialized database search software, crosslinked peptide-pairs can be identified and dir...
ORGANISM(S): Bos taurus (Bovine) 
2019-07-16 | PXD013083 | Pride
Xlinkx Crosslinking mass spectrometry Gas phase fragmentation of crosslinks 
ProteomicsHigher dimensional cross-linking with a tetra-reactive cross-linker
A tetrameric CID-cleavable cross-linker was synthesized and applied to BSA and isolated mitochondria from mouse hearts. A real-time instrument method was developed to dynamically target released peptides from cross-linked species, enabling their characterization through a series of ms3 scans.
ORGANISM(S): Bos taurus (Bovine) Mus musculus (Mouse) 
2023-11-27 | PXD032222 | Pride
Mitochondria Cross-linking 
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