Non-cross-linking advanced glycation end products affect prohormone processing

Keyphrases

• Advanced Glycation End Products 100%
• Prohormone Processing 100%
• Non-cross-linked 100%
• Protease 75%
• Methylglyoxal 37%
• Modified Substrate 37%
• Proinsulin 37%
• Proprotein Convertase 25%
• N-carboxymethyllysine 25%
• Insulin 25%
• Pathomechanism 25%
• Prohormone 25%
• Product Modification 25%
• Carboxypeptidase E 25%
• Hydroimidazolone 25%
• Incubation 12%
• Lysine 12%
• Diabetes 12%
• Amino Acids 12%
• Post-translational Modification 12%
• Concentration-dependent 12%
• Obesity 12%
• Etiopathogenesis 12%
• Arginine 12%
• Substrate Effect 12%
• Trypsin 12%
• Inhibitory Effect 12%
• Peptide Substrate 12%
• Cleavage Site 12%
• Substrate Modification 12%
• Modified Proteins 12%
• Solid-phase Peptide Synthesis 12%
• Physiological Concentrations 12%
• Protease Substrate 12%
• Diabetes Complications 12%
• C-terminal Cleavage 12%
• Cysteine Cathepsins 12%
• Modified Protease 12%
• Modified Peptide 12%

Biochemistry, Genetics and Molecular Biology

• Cross-Link 100%
• Advanced Glycation End-Product 100%
• Protease 75%
• Methylglyoxal 37%
• Proinsulin 37%
• Serine Protease 25%
• Carboxypeptidase E 25%
• Amino Acids 12%
• Posttranslational Modification 12%
• Peptide Synthesis 12%
• C-Terminus 12%
• Cathepsin 12%
• Lysine 12%
• Cysteine 12%
• Protease 12%
• Arginine 12%

Pharmacology, Toxicology and Pharmaceutical Science

• Advanced Glycation End Product 100%
• Hormone Precursor 100%
• Methylglyoxal 37%
• Proinsulin 37%
• 6 N Carboxymethyllysine 25%
• Serine Proteinase 25%
• Carboxypeptidase H 25%
• Cathepsin 12%
• Cysteine 12%
• Amino Acid 12%
• Proteinase 12%
• Diabetic Complication 12%
• Lysine 12%
• Arginine 12%