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ProteomicsAnion-Exchange Chromatography of Tryptic and Phosphopeptides: WAX vs. SAX and AEX vs. ERLIC
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
ProteomicsAnion-Exchange Chromatography of Tryptic and Phosphopeptides: WAX vs. SAX and AEX vs. ERLIC
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 (Human) 
2015-04-23 | PXD001333 | Pride
Chromatography erlic sax wax aex 
ProteomicsAnalysis of Pancreatic Extracellular Matrix Protein Post-Translational Modifications via Electrostatic Repulsion-Hydrophilic Interaction Chromatography Coupled with Mass Spectrometry
The pancreas is a vital organ with digestive and endocrine roles, and diseases of the pancreas affect millions of people yearly. A better understanding of the pancreas proteome and its dynamic post-translational modifications (PTMs) is necessary to engineer higher fidelity tissue analogues for use ...
ORGANISM(S): Homo sapiens (Human) 
2021-08-06 | PXD025048 | Pride
Pancreas Mass spectrometry Glycopeptide Post-translational modifications (ptm) Electrostatic repulsion-hydrophilic interaction chromatography (erlic) Phosphopeptide Extracellular matrix 
ProteomicsCounterion Optimization Dramatically Improves Selectivity for Phosphopeptides and Glycopeptides in Electrostatic Repulsion-Hydrophilic Interaction Chromatography (ERLIC)
A well-hydrated counterion can selectively and dramatically increase retention of a charged analyte in hydrophilic interaction chromatography (HILIC). The effect is enhanced if the column is charged, as in electrostatic repulsion-hydrophilic interaction chromatography (ERLIC). This combination was...
ORGANISM(S): Mus musculus (Mouse) 
2021-06-01 | PXD022988 | Pride
Peptide Fraction Ptm Glyco Phosphate Erlic 
ProteomicsPeptide Retention Time Prediction for Electrostatic Repulsion-Hydrophilic Interaction Chromatography
Electrostatic Repulsion-Hydrophilic Interaction Chromatography (ERLIC) is a legacy separation tools developed by Dr. Andrew Alpert and has been used for developing unique separation methods of hydrophilic compounds, including peptides. We employed a proteomics-derived ~170,000 peptide retention data...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
MSV000095965 | MassIVE
ProteomicsHighly sensitive phosphoproteomics by tailoring solid-phase extraction to electrostatic repulsion-hydrophilic interaction chromatography
The dataset contains the data of key experiments for developing a novel and highly sensitive bottom-up phosphoproteomics strategy termed ERLIC-SCX/RP-LC-MS. We compared two SPE types (RP, SCX) for an ERLIC run with 7 fractions. The results were used to design a workflow for highly sensitive bottom-u...
ORGANISM(S): Homo sapiens (Human) 
2014-12-02 | PXD001381 | Pride
Phosphoproteomics Phosphopeptide enrichment Lc-ms Solid-phase extraction Scx Protein phosphorylation Rp 
UnknownAnion-exchange chromatography of phosphopeptides: weak anion exchange versus strong anion exchange and anion-exchange chromatography versus electrostatic repulsion-hydrophilic interaction chromatography.
Not available
S-EPMC4423237 | biostudies-literature
OtherHighly sensitive phosphoproteomics by tailoring solid-phase extraction to electrostatic repulsion-hydrophilic interaction chromatography.
Data from ProteomeXchange, PXD ID: PXD001381. Experiment: ERLIC2, file: Velos02_06349 ERLIC2 F14.mzml. Published as part of Anal Chem. 2014 Nov 18 . From the Abstract: {{i}} ... Here we introduce a highly sensitive and easy-to-establish 2D bottom-up strategy for -g-scale phosphoproteomics, based on...
ORGANISM(S): Homo_sapiens_viruses, Human_female 
GPM32320005256 | GPMDB
Resource Reanalysis 
UnknownCounterion Optimization Dramatically Improves Selectivity for Phosphopeptides and Glycopeptides in Electrostatic Repulsion-Hydrophilic Interaction Chromatography.
Not available
S-EPMC8237654 | biostudies-literature
UnknownSimultaneous Enrichment of Plasma Soluble and Extracellular Vesicular Glycoproteins Using Prolonged Ultracentrifugation-Electrostatic Repulsion-hydrophilic Interaction Chromatography (PUC-ERLIC) Approach.
Not available
S-EPMC4458727 | biostudies-literature
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