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A putative lipopeptide biosynthetic gene cluster is conserved in many species of Actinobacteria, including Mycobacterium tuberculosis and Mycobacterium marinum, but the specific function of the encoding proteins has been elusive. Using both in vivo heterologous reconstitution and in vitro biochemica...
2017-07-18 | MTBLS454 | MetaboLights
High Throughput pMHC-I Tetramer Library Production Using Chaperone Mediated Peptide Exchange
Human TAPBPR is known to function as a Major Histocompatibility Complex class I (MHC-I) peptide exchange catalyst which shapes the peptide repertoire presented to immune cells. Never14theless, investigations characterizing TAPBPR from other species are limited. Here, we characterize mouse TAPBPR, ex...
ORGANISM(S): Mus musculus (Mouse) 
2026-03-23 | PXD069965 | Pride
Human TAPBPR is known to function as a Major Histocompatibility Complex class I (MHC-I) peptide exchange catalyst which shapes the peptide repertoire presented to immune cells. Never14theless, investigations characterizing TAPBPR from other species are limited. Here, we characterize mouse TAPBPR, ex...
ORGANISM(S): Mus musculus (Mouse) 
2026-03-23 | PXD068540 | Pride
Data from ProteomeXchange, PXD ID: PXD001333. File: Amanda ms1-8ppm ms2-20ppm 20130219_QEx3_RSLC-4_Mischerikow_Peters_IMP_shotgun_s2324.msf.mgf. Published as part of Anal Chem. 2015 Apr 17 . From the Abstract: {{i}} ... Weak anion-exchange (WAX) and strong anion-exchange (SAX) columns were compared...
ORGANISM(S): Homo_sapiens_viruses, Human_female 
At a pH > 5, phosphopeptides have two negative charges per residue and are well-retained in anion-exchange chromatography. However, the peptides with one or two phosphate groups are not separated from the peptides with multiple Asp or Glu residues, which interfere with the identification of phosph...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080774 | MassIVE
Peptide exchange technologies are essential for the generation of pMHC-multimer libraries for probing diverse, polyclonal TCR repertoires in various settings. Here we report, using the molecular chaperone TAPBPR, a robust method for the capture of stable, empty MHC-I molecules, which can be readily ...
ORGANISM(S): synthetic construct Homo sapiens 
2020-03-12 | GSE146826 | GEO
We have developed a one-step method to isolate protein C-terminal peptides from V8-digested proteins by metal oxide-based ligand-exchange (MOLEX) chromatography. V8 protease cleaves the C-terminal side of Asp and Glu, and the resulting digested peptide has two carboxy groups at the C-terminus, where...
ORGANISM(S): Homo Sapiens (human) 
We investigated the conformational dynamics of the LPS translocon LptDE was using hydrogen-deuterium exchange mass spectrometry. We evaluated the conformational changes of LptDE upon binding of LPS, Re-LPS (an LPS substructure), thanatin, and the membrane lipid POPG. Our data reveal that LPS induces...
ORGANISM(S): Klebsiella pneumoniae 
2020-11-16 | PXD021743 | Pride
Building on the insights gained from systematically investigating of aromatic nucleophilic substitution (SNAr) and thiol-exchange, we identified the highly electron-deficient halopyridiniums as a tunable and predictable reaction platform for adjusting electrophilicity and thiol-cleavability by follo...
ORGANISM(S): Homo Sapiens 
2023-09-25 | PXD045683 |
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