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UnknownProXL (Protein Cross-Linking Database): A Platform for Analysis, Visualization, and Sharing of Protein Cross-Linking Mass Spectrometry Data.
Not available
S-EPMC4977572 | biostudies-literature
ProteomicsTaf2 mediates DNA binding of Taf14
The assembly and function of the yeast general transcription factor TFIID complex requires specific contacts between its Taf14 and Taf2 subunits, however, the mechanism underlying these contacts remains unclear. Here, we determined the molecular and structural basis by which the YEATS and ET domains...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2022-08-12 | PXD033397 | Pride
Taf2 mediates dna binding of taf14 
ProteomicsBRCA1/BARD1 intrinsically disordered regions facilitate chromatin recruitment and ubiquitylation
BRCA1/BARD1 is a tumor suppressor E3 ubiquitin (Ub) ligase with roles in DNA damage repair and in transcriptional regulation. BRCA1/BARD1 RING domains interact with nucleosomes to facilitate mono-ubiquitylation of distinct residues on the C-terminal tail of histone H2A. These enzymatic domains const...
ORGANISM(S): Homo sapiens (Human) 
2023-06-21 | PXD035345 | Pride
Kojak Brca1 Cancer Nucleosome Cross-linking mass spectrometry Proxl H2a Xl-ms Bard1 Tumor Ubiquitin ligase 
ProteomicsCullin-independent recognition of HHARI substrates by a dynamic RBR catalytic domain
RING-Between-RING (RBR) E3 ligases mediate ubiquitin transfer through an obligate E3- ubiquitin thioester intermediately prior to substrate ubiquitination. While RBRs share a conserved catalytic module, substrate recruitment mechanisms remain enigmatic and the relevant domains have yet to be identi...
ORGANISM(S): Homo sapiens (Human) 
2023-05-24 | PXD030849 | Pride
Kojak Cross-linking mass spectrometry Proxl Skyline Cullin Xl-ms Hhari Ubiquitin Rbr E3 ligase 
UnknownDetermination of the glycoprotein specificity of lectins on cell membranes through oxidative proteomics.
Not available
S-EPMC8162070 | biostudies-literature
ProteomicsDeciphering the interaction between TopBP1 and GINS using crosslinking mass spectrometry
Recombinant TopBP1 and GINS were cross linked using the MS non-cleavable crosslinker BS3. Crosslinked proteins were then subsequently either digested directly using the SP3 strategy or first seperated on SDS-PAGE and then in-gel digested. cross-linked peptides were identified by LC-MS. The informati...
ORGANISM(S): Homo sapiens (Human) 
2024-05-24 | PXD040156 | Pride
Cross linking Gins Topbp1 Bs3 
ProteomicsDisulfide mapping of J-chain by crosslinking MS
Here we show how J-chain (JC) outcompetes the sixth IgM subunit during assembly. We looked at the disulfide re-arrangements in JC and showed that it exists as an unstructured protein with non-native disulfides before its insertion into IgM.
ORGANISM(S): Mus musculus (Mouse) 
2024-12-04 | PXD048614 | Pride
Disulfide J-chain Crosslinking 
ProteomicsPhosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble
Hsp26 is a small heat shock protein (sHsp) from S. cerevisiae. It is known to be activated by dissociation of the oligomer at heat shock temperatures. We wondered whether phosphorylation regulates its activity at physiological temperatures. In Hsp26, 9 phosphorylation sites which are located in diff...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2021-12-17 | PXD025314 | Pride
Hsp26 Phosphorylation Shsp 
ProteomicsA direct interplay between the co-chaperones Hop and p23 regulates cycle progression and client folding in the Hsp70/Hsp90 chaperone machineries
Folding of stringent clients requires transfer from Hsp70 to Hsp90. The co-chaperone Hop physically connects the chaperone machineries. Here we define its role from the remodeling of Hsp70/40-client complexes to the mechanism of client transfer and the conformational switching from stalled to active...
ORGANISM(S): Homo sapiens (Human) Saccharomyces cerevisiae (Baker's yeast) 
2022-02-24 | PXD027413 | Pride
Hsp90 P23 Hop Hsp70 
ProteomicsChemical and photo-Crosslinking experiments of the BAX/BNIP3/PeptideB interaction
In these experiments we try to show by cross-linking MS how BAX and BNIP3 interact (DSSO cross-linking) and how Peptide B (an octapeptide that prevents mitochondrial damage and cell death induced by BNIP3/BAX activity) interacts with the BNIP3/BAX complex (BPA cross-linking; BPA on Peptide B).
ORGANISM(S): Homo sapiens (Human) 
2026-05-22 | PXD056758 | Pride
Bnip3 Bax Mitochondrial damage Cell death 
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