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Showing 1 to 9 of 9 for “"AMPylation"”.

  1. Genetic Analysis of Fic-Mediated BiP AMPylation in Photoreceptors

    … levels, the ER-resident Fic protein catalyzes AMPylation or deAMPylation of BiP, the major ER chaperone. This work elucidates a critical role of the reversible AMPylation of BiP in maintaining the Drosophila visual system in response to constant light-induced stress. In response to extended …

    utswmed Repository record for Genetic Analysis of Fic-Mediated BiP AMPylation in Photoreceptors (opens in a new tab)

  2. Fic-Mediated AMPylation in Bacterial Infection and Endoplasmic Reticulum Stress

    The post-translational modification AMPylation is emerging as a significant regulatory mechanism in both prokaryotic and eukaryotic biology. This process involves the covalent addition of an adenosine monophosphate to a protein resulting in a modified protein with altered activity. Proteins capable …

    utswmed Repository record for Fic-Mediated AMPylation in Bacterial Infection and Endoplasmic Reticulum Stress (opens in a new tab)

  3. Uncovering Reversible AMPylation of BiP Mediated by dFic During ER Homeostasis

    AMPylation is a posttranslational modification involving a covalent attachment of an AMP moiety from ATP to hydroxyl side chains of target substrates. Fic domain which mediates AMPylation is highly conserved across species, including higher eukaryotes, implicating an essential role of this …

    tdl Repository record for Uncovering Reversible AMPylation of BiP Mediated by dFic During ER Homeostasis (opens in a new tab)

  4. Structural and Kinetic Characterization of Protein Ampylation by VopS Fic Domain

    … on the functions of conserved residues for the AMPylation activity. Further mechanistic analysis of VopS with its two substrates, ATP and Cdc42, demonstrates that VopS utilizes a sequential mechanism to AMPylate Rho GTPases. The structure of VopS and its ternary reaction mechanism provide …

    utswmed Repository record for Structural and Kinetic Characterization of Protein Ampylation by VopS Fic Domain (opens in a new tab)

  5. Uncovering Reversible AMPylation of BiP Mediated by dFic During ER Homeostasis

    AMPylation is a posttranslational modification involving a covalent attachment of an AMP moiety from ATP to hydroxyl side chains of target substrates. Fic domain which mediates AMPylation is highly conserved across species, including higher eukaryotes, implicating an essential role of this …

    utswmed Repository record for Uncovering Reversible AMPylation of BiP Mediated by dFic During ER Homeostasis (opens in a new tab)

  6. Post-translational regulation of BiP by FICD-mediated AMPylation and deAMPylation

    … to dynamically adjust BiP’s activity through AMPylation and deAMPylation. These two mutually antagonistic reactions, catalysed by the single active site of FICD, are reciprocally regulated by an oligomeric state-dependent switch. Under conditions of low unfolded protein load this bifunctional …

    cambridge Repository record for Post-translational regulation of BiP by FICD-mediated AMPylation and deAMPylation (opens in a new tab)

  7. Chemical Reporters for Bacterial Pathogenesis and Beyond

    … a chemical reporter for the study of protein AMPylation, a key posttranslational modification used by various bacterial pathogens to rewire host-signaling pathways. This reporter is used by all of the known AMPylation enzyme classes and allows the proteomic identification of enzyme-specific …

    rockefeller Repository record for Chemical Reporters for Bacterial Pathogenesis and Beyond (opens in a new tab)

  8. Characterization of Vibrio VopS, an AMPylator of Rho GTPases

    … Our preliminary studies indicated that AMPylation is utilized by eukaryotes. We have shown that a Fic protein from humans, HYPE, possesses auto-AMPylation activity, confirming our hypothesis that these domains are involved in AMPylation. Ongoing and future studies seek to identify the …

    utswmed Repository record for Characterization of Vibrio VopS, an AMPylator of Rho GTPases (opens in a new tab)

  9. Bacterial defense islands: CRISPR-Cas and toxin-antitoxin systems /

    … activity is neutralized by covalent di AMPylation performed by MNT antitoxin. In addition, the data reveals that the unmodified active HEPN toxin cleaves 4 nt from 3′-stem of a range of tRNA, showing a new mechanism of toxin action on tRNA.

    vilnius Repository record for Bacterial defense islands: CRISPR-Cas and toxin-antitoxin systems / (opens in a new tab)