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ProteomicsQuantitative cross-linking/mass spectrometry
Dynamic proteins and multi-protein complexes govern most biological processes. Cross-linking/mass spectrometry (CLMS) is increasingly successful in providing residue- resolution data on static proteinaceous structures. Here we investigate the technical feasibility of recording dynamic processes usin...
ORGANISM(S): Homo sapiens (Human) 
2015-06-08 | PXD002142 | Pride
Protein dynamics Structual biology Quantitation Cross-linking 
ProteomicsA model dataset for quantitative cross-linking/mass spectrometry using isotope-labeled cross-linkers
Dynamic proteins and multi-protein complexes govern most biological processes. Cross-linking/mass spectrometry (CLMS) is increasingly successful in providing residue-resolution data on static proteinaceous structures. In order to investigate the technical feasibility of recording dynamic processes u...
ORGANISM(S): Homo sapiens (Human) 
2016-05-06 | PXD004107 | Pride
Model dataset Isotope-labeled cross-linkers Hsa Quantitative cross-linking/mass spectromentry 
ProteomicsQuantitative cross-linking/mass spectrometry reveals subtle protein conformational changes
We have developed quantitative cross-linking/mass spectrometry (QCLMS) to interrogate conformational rearrangements of proteins in solution. Our workflow was tested using a structurally well-described reference system, the human complement protein C3 and its activated cleavage product C3b. We found ...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2016-06-16 | MSV000079827 | MassIVE
UnknownIdentification of novel interferon responsive protein partners of human leukocyte antigen A (HLA-A) using cross-linking mass spectrometry (CLMS) approach.
Not available
S-EPMC9653400 | biostudies-literature
ProteomicsIdentifying and characterising Thrap3, Bclaf1 and Erh direct interactions using cross-linking mass spectrometry
Cross-linking mass spectrometry (XL-MS) is a powerful technology capable of yielding structural insights across the complex cellular protein interaction network. We performed XL-MS using MS-cleavable cross-linker disuccinimidyl sulfoxide (DSSO) on endogenous affinity-purified BAF complex. We identif...
ORGANISM(S): Mus musculus (Mouse) 
2021-09-24 | PXD027611 | Pride
Clms cross-linking mass spectrometry Endogenous complexes Erh Dsso Xl-ms Thrap3 Bclaf1 
Proteomics3D topology of the SMC2/SMC4 sub-complex from chicken condensin I revealed by cross-linking and molecular modelling
SMC proteins are essential components of three protein complexes that are important for chromosome structure and function. The cohesin complex holds replicated sister chromatids together, whereas the condensin complex has an essential role in mitotic chromosome architecture. Both are involved in int...
ORGANISM(S): Gallus gallus (Chicken) 
2015-07-13 | PXD001835 | Pride
Condensin Cross-linking Mass spectrometry Smc Structure Coiled-coil 
UnknownQuantitative cross-linking/mass spectrometry using isotope-labelled cross-linkers.
Not available
S-EPMC3714596 | biostudies-literature
ProteomicsCross-Linking/mass spectrometry (CLMS) analysis of RNA polymerase II
The mass spectrometry data of a previous publication (Chen et.al. 2009 doi:10.1038/emboj.2009.401) were reprocesed and is used for method developing, teaching and training purpose.
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2018-07-20 | PXD010481 | Pride
Cross-linking/mass spectrometry Mult-iprotein complex 
ProteomicsCross-linking/mass spectrometry analysis of the AOC complex
As a part of a study on how kinetochors are assembled at the centromeres of the chromosomes, cross-linking/mass spectrometry has been applied to investigate interactions between Okp1/ Ame1 heterodimer, which is part of the COMA complex, and CENP-A from Saccharomyces cerevisiae.
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2018-10-30 | PXD009648 | Pride
Protein interaction Cenp-a Okp1 Centromere Cross-linking/mass spectrometry Ame1 
ProteomicsFacilitating in situ cross-linking and mass spectrometry by antibody-based protein enrichment
Cross-linking of living cells followed by mass spectrometry identification of cross-linked peptides (in situ CLMS) is an emerging technology to study protein structures in their native environment. One of the inherent difficulties of this approach is the high complexity of the samples following cell...
ORGANISM(S): Homo sapiens (Human) 
2022-06-09 | PXD025099 | Pride
Cl-ms Antibody 
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