Using guanidine-hydrochloride for fast and efficient protein digestion and single-step affinity-purification mass spectrometry.
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Summary
Gnd-HCl allow the efficient elution and subsequent fast digestion of PPIs to provide a convenient high-throughput methodology for affinity-purification mass spectrometry (AP-MS) experiments, and the identification of known interaction partners demonstrates the utility of the optimized Gnd- HCl protocol that is also scalable to the 96 well-plate format.
- Type
- article
- Published
- 2013-02-01
- Cited by
- 48
- References
- 60
- Access
- Open access
- OpenAlex
- https://openalex.org/W2015793846
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:2740069
Keywords
Shotgun proteomics, Shotgun, Chemistry, Mass spectrometry, Chromatography
References
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- Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips
- Mass spectrometric approaches for the identification of gel‐separated proteins
- In-gel digestion for mass spectrometric characterization of proteins and proteomes
- The Rsp5 ubiquitin ligase is coupled to and antagonized by the Ubp2 deubiquitinating enzyme
- Global landscape of HIV–human protein complexes
- A quantitative analysis software tool for mass spectrometry–based proteomics
- A Quantitative Study of the Effects of Chaotropic Agents, Surfactants, and Solvents on the Digestion Efficiency of Human Plasma Proteins by Trypsin
- Toward a High-Resolution View of Nuclear Dynamics
- Global analysis of protein expression in yeast
- Quantitative proteomics reveals subset-specific viral recognition in dendritic cells.
- Comparison of digestion protocols for microgram quantities of enriched protein samples.
- An improved trypsin digestion method minimizes digestion-induced modifications on proteins.
Cited by
- Biotin starvation causes mitochondrial protein hyperacetylation and partial rescue by the SIRT3-like deacetylase Hst4p
- A Two-step Protein Quality Control Pathway for a Misfolded DJ-1 Variant in Fission Yeast*
- Minimal, encapsulated proteomic-sample processing applied to copy-number estimation in eukaryotic cells
- Absolute quantitative profiling of the key metabolic pathways in slow and fast skeletal muscle.
- Accurate Protein Complex Retrieval by Affinity Enrichment Mass Spectrometry (AE-MS) Rather than Affinity Purification Mass Spectrometry (AP-MS)
- Rapid and deep proteomes by faster sequencing on a benchtop quadrupole ultra-high-field Orbitrap mass spectrometer.
- Time-resolved dissection of early phosphoproteome and ensuing proteome changes in response to TGF-β
- A Double-Barrel Liquid Chromatography-Tandem Mass Spectrometry (LC-MS/MS) System to Quantify 96 Interactomes per Day
- Proteomics of Skeletal Muscle: Focus on Insulin Resistance and Exercise Biology
- Analysis of Conformational Stability of Abnormal Prion Protein Aggregates across the Spectrum of Creutzfeldt-Jakob Disease Prions
- Simple and Reproducible Sample Preparation for Single-Shot Phosphoproteomics with High Sensitivity.
- Integral membrane proteins in proteomics. How to break open the black box?
- Comparison between chaotropic and detergent‐based sample preparation workflow in tendon for mass spectrometry analysis
- Specifying RNA-Binding Regions in Proteins by Peptide Cross-Linking and Affinity Purification.
- Proteome-Wide Identification of In Vivo ADP-Ribose Acceptor Sites by Liquid Chromatography-Tandem Mass Spectrometry.
- Proteomic analyses identify ARH3 as a serine mono-ADP-ribosylhydrolase
- Large-Scale Phosphoproteomics Reveals Shp-2 Phosphatase-Dependent Regulators of Pdgf Receptor Signaling
- Identification of Phosphorylated Proteins on a Global Scale
- Site-specific characterization of endogenous SUMOylation across species and organs
- UbiSite approach for comprehensive mapping of lysine and N-terminal ubiquitination sites
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