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ProteomicsIn Situ Cross-linking Based Co-Fractionation Mass Spectrometry (XL-CoFrac-MS)
We developed an in situ cross-linking coupled reversed-phase liquid chromatography-based co-fractionation mass spectrometry (XL-CoFrac-MS) platform to analyze drug-induced protein complex changes. A software tool, ChromaQuant, was built to automate chromatographic peak quantification. Using RS4;11 l...
ORGANISM(S): Homo Sapiens 
PXD067673 |
UnknownProtein complexes in cells by AI-assisted structural proteomics.
Not available
S-EPMC10090944 | biostudies-literature
ProteomicsProtein complexes in cells by AI-assisted structural proteomics (Cofractionation MS)
Accurately modeling the structures of proteins and their complexes using artificial intelligence is revolutionizing molecular biology. Experimental data enable a candidate-based approach to systematically model novel protein assemblies. Here, we use a combination of in-cell crosslinking mass spectro...
ORGANISM(S): Bacillus Subtilis Subsp. Subtilis Str. 168 
2023-02-16 | PXD035520 | JPOST Repository
ProteomicsProtein complexes in cells by AI-assisted structural proteomics (Proteomics)
Accurately modeling the structures of proteins and their complexes using artificial intelligence is revolutionizing molecular biology. Experimental data enable a candidate-based approach to systematically model novel protein assemblies. Here, we use a combination of in-cell crosslinking mass spectro...
ORGANISM(S): Bacillus Subtilis Subsp. Subtilis Str. 168 
2023-02-16 | PXD035521 | JPOST Repository
ProteomicsQuantative pTyr protein complex
Our current research focuses on the complex-centric quantification of pTyr protein complexes. We initially constructed a tri-functional probe based on pTyr superbinder (SH2-S) for the enrichment of pTyr protein complexes. The pTyr protein complexes were separated by ion exchange chromatography (IEC)...
ORGANISM(S): Homo Sapiens 
PXD052742 |
ProteomicsNative SEC-MS of the human HT29 colon adenocarcinoma cell line treated with the HSP90 inhibitor tanespimycin (17-AAG)
The molecular chaperone heat shock protein 90 (HSP90) works in concert with its co-chaperones to stabilize its client proteins, which include several drivers of oncogenesis and malignant progression. Pharmacologic inhibitors of HSP90 are proposed to trigger widespread remodeling of cellular protein ...
ORGANISM(S): Homo sapiens (Human) 
2022-12-20 | PXD033459 | Pride
Human Lc-msms Colon Cofrac-ms Hsp90 Adenocarcinoma Cancer Sec-ms Colorectal Pharmacology Protein complexes 
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