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Showing 1 to 3 of 3 for “"protein lipidation"”.

  1. REDEFINING THE SCOPE OF PRENYLATION: DISCOVERY OF “FORBIDDEN” SUBSTRATE RECOGNITION AND DEVELOPMENT OF METHODS UTILIZING PRENYLATED PROTEINS

    … function and cell behavior through changes in protein structure, activity, and localization. Prenylation is one such modification wherein a 15- or 20-carbon isoprenoid group is attached to a cysteine residue near the C-terminus of a substrate protein by one of three enzymes: protein

    syracuse-diss Repository record for REDEFINING THE SCOPE OF PRENYLATION: DISCOVERY OF “FORBIDDEN” SUBSTRATE RECOGNITION AND DEVELOPMENT OF METHODS UTILIZING PRENYLATED PROTEINS (opens in a new tab)

  2. Chemical Reporters for Investigating Lipidated Proteins at the Host-Pathogen Interface

    <p>Lipidation of proteins regulates many cellular processes such as signaling transduction and membrane sorting by modulating protein localization and proteinprotein interactions. As such, defects in protein lipidation can render host cells more susceptible to microbial infection and are also …

    rockefeller Repository record for Chemical Reporters for Investigating Lipidated Proteins at the Host-Pathogen Interface (opens in a new tab)

  3. UNDERSTANDING THE RAL GTPASES: THE REGULATION BY PROTEIN LYSINE FATTY ACYLATION, SIRT2, AND INTERACTING PROTEINS

    … regulated by lysine fatty acylation. Lipidation, such as cysteine palmitoylation and prenylation, is a key regulatory mechanism for small GTPases. Recently it has been reported that lysine fatty acylation also regulates several small GTPases. My graduate work shows that RalB, but not …

    cornell Repository record for UNDERSTANDING THE RAL GTPASES: THE REGULATION BY PROTEIN LYSINE FATTY ACYLATION, SIRT2, AND INTERACTING PROTEINS (opens in a new tab)