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  • Microscopy
  • Immunofluorescence microscopy indicated that the IseA-3xFLAG fusion protein was specifically localized at cell separation sites and poles on the vegetative cell surface in a similar manner of the d,l-endopeptidases. (biomedsearch.com)
  • modifications
  • Post-translational protein modifications catalyzed by Ca(2+)-dependent peptidylargininedeiminases have been shown to trigger immune responses including autoantibody generation, a hallmark of immune complexes deposition in rheumatoid arthritis. (umassmed.edu)
  • Often, this causes steric interference of the interaction of the target protein with binding partners, e.g. toxin-catalyzed ADP-ribosylation of actin at R177 sterically blocks actin polymerization.In case of the nucleotide-gated P2X7 ion channel, ADP-ribosylation at R125 in the vicinity of the ligand-binding site causes channel gating.In some cases, ADP-ribosylarginine is processed into secondary posttranslational modifications, e.g. phosphoribosylarginine or ornithine. (nih.gov)
  • In some cases, ADP-ribosylarginine is processed into secondary posttranslational modifications, e.g. phosphoribosylarginine or ornithine. (nih.gov)
  • Chemical
  • Arginine ADP-ribosylation, thus, causes a notable change in size and chemical property at the ADP-ribosylation site of the target protein. (nih.gov)
  • Mechanisms
  • The 19 chapters are divided into four sectors: A) describes and explores the genome, its evolution, expression and the mechanisms that contribute to protein, and hence biological, diversity. (wiley.com)
  • interactions
  • To begin elucidating the functions of the protein in signaling and its potential role in developmental processes, we characterized mutant and overexpression SRm160 phenotypes in Drosophila and their interactions with the locus encoding the LAMMER protein kinase, Doa. (cnrs.fr)
  • MeSH
  • GeneReviews/NIH/NCBI/UW entry on Pulmonary Fibrosis, Familial Pulmonary Surfactant-Associated Protein B at the US National Library of Medicine Medical Subject Headings (MeSH) PĂ©rez-Gil J (2002). (wikipedia.org)
  • subunit
  • 40S Small Subunit w/ 34 Proteins. (brainscape.com)
  • In addition to tankyrase-2, peptides derived from tankyrase-1, GA-binding protein subunit beta-2 (GABPB2) and the transient receptor potential vanilloid-4 (TRPV4) ARD all displayed +16 Da mass shifts after reaction with FIH (Fig. 6B). (nih.gov)
  • Hydrolases
  • ADP-ribosylarginine specific hydrolases (ARHs) can restore target protein function by hydrolytic removal of the entire ADP-ribose moiety. (nih.gov)
  • assess
  • Therefore, the aim of the study was to assess if nanoparticles are able to promote protein citrullination. (umassmed.edu)
  • genetic analyses to assess the role of these processes in genomic stability, cellular transformation, and cancer prevention and therapy. (elsevier.com)
  • function
  • The propeptide of pulmonary surfactant C has an N-terminal alpha-helical segment whose suggested function was stabilization of the protein structure, since the latter can irreversibly transform from its native alpha-helical structure to beta-sheet aggregates and form amyloid fibrils. (wikipedia.org)
  • lung
  • RESULTS: The studied nanoparticles induced protein citrullination both in cultured human cells and mouse lung tissues. (umassmed.edu)
  • Structure and influence on stability and activity of the N-terminal propeptide part of lung surfactant protein C". FEBS J. 273 (5): 926-35. (wikipedia.org)
  • family
  • The protein encoded by this gene belongs to the MYST family of histone acetyl transferases (HATs) and was originally isolated as an HIV-1 TAT-interactive protein. (cancerindex.org)
  • mature
  • Our quantitative pulse-chase studies suggest that of the two populations of MuMTV env precursors that are present in MuMTV-producing cells, only Pr70env is processed intracellularly to give rise to the mature MuMTV envelope proteins gp52 and gp36. (biomedsearch.com)
  • domains
  • Factor-inhibiting hypoxia-inducible factor (FIH) catalyses the post-translational hydroxylation of histidinyl residues within ankyrin repeat domains. (nih.gov)