Compounds > asparagine

asparagine and cathepsin g

asparagine has been researched along with cathepsin g in 3 studies

Research

Studies (3)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's1 (33.33)18.2507
2000's1 (33.33)29.6817
2010's1 (33.33)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Cantell, K; Julkunen, I; Pirhonen, J; Sareneva, T1
Beck, A; Brandenburg, J; Burster, T; Driessen, C; Falk, K; Kalbacher, H; Lautwein, A; Lehmann, R; Marin-Esteban, V; Melms, A; Reich, M; Rötzschke, O; Schwarz, G; Stevanovic, S; Tolosa, E; Wiendl, H1
Loke, I; Packer, NH; Thaysen-Andersen, M1

Other Studies

3 other study(ies) available for asparagine and cathepsin g

ArticleYear
N-glycosylation of human interferon-gamma: glycans at Asn-25 are critical for protease resistance.
    The Biochemical journal, 1995, May-15, Volume: 308 ( Pt 1)

    Topics: Animals; Asparagine; Cathepsin G; Cathepsins; Endopeptidases; Fibrinolysin; Glycosylation; Hot Temperature; Humans; Interferon-gamma; Mutagenesis, Site-Directed; Pancreatic Elastase; Protein Processing, Post-Translational; Protein Structure, Tertiary; Recombinant Proteins; Serine Endopeptidases; Spodoptera; Structure-Activity Relationship

1995
Cathepsin G, and not the asparagine-specific endoprotease, controls the processing of myelin basic protein in lysosomes from human B lymphocytes.
    Journal of immunology (Baltimore, Md. : 1950), 2004, May-01, Volume: 172, Issue:9

    Topics: Adult; Amino Acid Sequence; Animals; Antigen-Presenting Cells; Asparagine; B-Lymphocyte Subsets; Cathepsin G; Cathepsins; Cell Line; Cell Line, Transformed; Cell Separation; Cysteine Endopeptidases; Humans; Hydrolysis; Lymphocyte Activation; Lysine; Lysosomes; Mice; Molecular Sequence Data; Myelin Basic Protein; Phenylalanine; Protein Processing, Post-Translational; Serine; Serine Endopeptidases

2004
Complementary LC-MS/MS-Based N-Glycan, N-Glycopeptide, and Intact N-Glycoprotein Profiling Reveals Unconventional Asn71-Glycosylation of Human Neutrophil Cathepsin G.
    Biomolecules, 2015, Aug-12, Volume: 5, Issue:3

    Topics: Amino Acid Sequence; Asparagine; Catalytic Domain; Cathepsin G; Chromatography, Liquid; Glycopeptides; Glycoproteins; Glycosylation; Humans; Hydrophobic and Hydrophilic Interactions; Intracellular Space; Models, Molecular; Neutrophils; Polysaccharides; Protein Processing, Post-Translational; Solid Phase Extraction; Tandem Mass Spectrometry

2015