Importance of extended protease substrate recognition motifs in steering BNIP-2 cleavage by human and mouse granzymes B

• Main Authors: Van Damme, P, Plasman, K, Vandemoortele, G, Jonckheere, V, Maurer-Stroh, S, Gevaert, K
• Other Authors: BIOLOGICAL SCIENCES
• Format: Article
• Published: 2020
• Subjects: bnip2 protein; granzyme B; protein; protein bcl 2; signal peptide; unclassified drug; BNIPL protein, human; granzyme; peptide hydrolase; signal transducing adaptor protein; amino acid sequence; animal cell; apoptosis; Article; cell death; cell lysate; controlled study; enzyme specificity; freeze thawing; human; human cell; in vitro study; jurkat cell line; liquid chromatography; mouse; nonhuman; nucleotide sequence; protein expression; protein function; protein motif; protein processing; protein protein interaction; signal transduction; site directed mutagenesis; tandem mass spectrometry; translation initiation; animal; chemistry; metabolism; molecular genetics; sequence homology; Adaptor Proteins, Signal Transducing; Amino Acid Sequence; Animals; Chromatography, Liquid; Granzymes; Humans; Mice; Molecular Sequence Data; Peptide Hydrolases; Sequence Homology, Amino Acid; Substrate Specificity; Tandem Mass Spectrometry
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/181486
• Institution: National University of Singapore

10.1186/1471-2091-15-21