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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 
UnknownLarge-Scale and Targeted Quantitative Cross-Linking MS Using Isotope-Labeled Protein Interaction Reporter (PIR) Cross-Linkers.
Not available
S-EPMC5513479 | biostudies-literature
UnknownQuantitative Cross-linking/Mass Spectrometry Using Isotope-labeled Cross-linkers and MaxQuant.
Not available
S-EPMC4974350 | biostudies-literature
UnknownDeveloping new isotope-coded mass spectrometry-cleavable cross-linkers for elucidating protein structures.
Not available
S-EPMC3985771 | biostudies-literature
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
UnknownA Study into the Collision-induced Dissociation (CID) Behavior of Cross-Linked Peptides.
Not available
S-EPMC4813691 | biostudies-literature
UnknownMultiplexed Cross-Linking with Isobaric Quantitative Protein Interaction Reporter Technology.
Not available
S-EPMC9014865 | biostudies-literature
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 (Human) 
2016-06-16 | PXD001675 | Pride
Quantitative cross-linking/mass spectrometry  conformation changes  human c3  activation of complement system 
UnknownDeveloping a Multiplexed Quantitative Cross-Linking Mass Spectrometry Platform for Comparative Structural Analysis of Protein Complexes.
Not available
S-EPMC5361889 | biostudies-literature
UnknownProbing Protein 3D Structures and Conformational Changes Using Electrochemistry-Assisted Isotope Labeling Cross-Linking Mass Spectrometry.
Not available
S-EPMC4841728 | biostudies-literature
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