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ProteomicsSupplementary Dataset 77 - Trypsin and Glu-C reference data for PILS experiments
This dataset contains trypsin and Glu-C reference peptides used for PILS analysis.
ORGANISM(S): Escherichia Coli (ncbitaxon:562) 
2017-07-12 | MSV000081316 | MassIVE
ProteomicsHuman Bone Morphogenetic Protein Receptor 2 (BMPR2) N-Glycopeptides
Trypsin,Glu-C and trypsin-Glu-C N-glycopeptides spanning all three putative BMPR2 N-glycosylation sites (N29, N84, and N100) were observed. Glycopeptide analyses revealed N-glycan compositions consistent with hybrid and complex glycoforms with abundant fucosylation and sialylation.
ORGANISM(S): Homo sapiens (Human) 
2026-07-06 | PXD066494 | Pride
N-glycopeptide Scehcd Bmpr2 Ethcd N-glycosylation Hek293 
UnknownLaminin γ1 C-terminal Glu to Gln mutation induces early postimplantation lethality.
Not available
S-EPMC6238537 | biostudies-literature
UnknownMildly acidic conditions eliminate deamidation artifact during proteolysis: digestion with endoprotease Glu-C at pH 4.5.
Not available
S-EPMC4795971 | biostudies-literature
ProteomicsOne-step Isolation of Protein C-terminal Peptides from Protease-digested Proteins by Metal Oxide-based Ligand Exchange Chromatography
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) 
2021-12-28 | PXD027960 | JPOST Repository
ProteomicsGeLC-FAIMS-MS Workflow for In-Depth Middle-Down Proteomics
Middle-down proteomics is an analytical approach whereby protein samples are digested with proteases such as Glu-C to generate large peptides (>3 kDa) that are then analyzed by mass spectrometry. This method is useful for characterizing high-molecular-weight proteins that are difficult to detect by ...
ORGANISM(S): Homo sapiens (Human) 
2024-11-20 | PXD041358 | Pride
Glu-c digestion Proteoform Middle-down proteomics Lc-faims orbitrap mass spectrometry Peppi-ms Anexsp 
UnknownRole of the C-terminal lysine residues of streptococcal surface enolase in Glu- and Lys-plasminogen-binding activities of group A streptococci.
Not available
S-EPMC343989 | biostudies-literature
UnknownGlu-286 rotation and water wire reorientation are unlikely the gating elements for proton pumping in cytochrome C oxidase.
Not available
S-EPMC3127198 | biostudies-literature
ProteomicsSequential Digestion with Different Proteases
We examined three combinations of different proteases for digestion of proteins from TurboID-STING-expressing cells: trypsin alone, Lys-C followed by trypsin, and Glu-C followed by trypsin. First, we tested whether PTS buffer used to solubilize precipitated proteins is compatible with digestion with...
ORGANISM(S): Mus Musculus (mouse) 
2022-08-25 | PXD035242 | JPOST Repository
TranscriptomicsSch9 Is a Major Target of TORC1 in Saccharomyces cerevisiae
The Target Of Rapamycin (TOR) protein is a Ser/Thr kinase that functions in two distinct multiprotein complexes: TORC1 and TORC2. These conserved complexes regulate many different aspects of cell growth in response to intra- and extracellular cues. Here we report the first bona fide substrate of yea...
ORGANISM(S): Saccharomyces cerevisiae 
2010-09-15 | E-GEOD-7660 | biostudies-arrayexpress
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