Endoplasmic reticulum-associated N-glycan degradation of cold-upregulated glycoproteins in response to chilling stress in Arabidopsis

Keyphrases

• Glycoprotein 100%
• Endoplasmic Reticulum 100%
• Arabidopsis 100%
• Chilling Stress 100%
• N-glycan Degradation 100%
• Glycopeptides 40%
• N-glycan 40%
• Complex Mixtures 20%
• Stress Conditions 20%
• Low Temperature 20%
• Data Dependency 20%
• LC-MS Analysis 20%
• Enzyme Activity 20%
• Selective Enrichment 20%
• Structure-activity 20%
• Stress-related 20%
• Proteomics Methods 20%
• Database Search 20%
• Plant Stress 20%
• Glycoproteomics 20%
• Protein Folding 20%
• Quantitative Measurement 20%
• Structural Characterization 20%
• Highly Sensitive 20%
• Public Database 20%
• Immunogenicity 20%
• In-house Database 20%
• High-mannose-type 20%
• Rapid Analysis 20%
• Misfolding 20%
• Comprehensive Identification 20%
• Metabolic Labeling 20%
• Cellular Mechanisms 20%
• Molecular Signature 20%
• Database Size 20%
• N-glycoproteome 20%
• Cold Treatment 20%
• Stress-responsive 20%
• Structure Conformation 20%
• Folding Topology 20%
• Conformation Stability 20%
• Surface Topology 20%
• Large-scale Identification 20%
• Protein Surface 20%
• Structural Nitrogen 20%
• N-glycosylation 20%
• Proteome-wide Analysis 20%
• Glycoprotein Structure 20%
• N-glycoproteins 20%

Immunology and Microbiology

• Arabidopsis 100%
• Glycan 100%
• Endoplasmic Reticulum 100%
• Glycoprotein 100%
• Glycopeptide 28%
• Proteomics 14%
• Tandem Mass Spectrometry 14%
• Protein Folding 14%
• Immunogenicity 14%
• Enzyme Activity 14%
• Glycosylation 14%
• Conformation 14%
• Cold Treatment 14%

Biochemistry, Genetics and Molecular Biology

• Arabidopsis 100%
• Glycoprotein 100%
• Polysaccharide 100%
• Glycopeptide 28%
• Proteomics 14%
• Tandem Mass Spectrometry 14%
• Proteome 14%
• Enzyme Activity 14%
• Quantitative Technique 14%
• Glycosylation 14%
• Glycoproteomics 14%
• Protein Folding 14%
• Conformation 14%
• Immunogenicity 14%
• Mannose 14%
• Cold Treatment 14%