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eScholarship
Open Access Publications from the University of California

Scholarly Works (3 results)

  • Peer Reviewed
Books and Book Chapters (2019)

Scholarly communication is undergoing an ever accelerating evolution in how research and scholarship are being conducted, how scholarship is being disseminated, and who is included in the creation and communication of new knowledge. At the forefront of this evolution are libraries and academics who recognize that students are not only creating new knowledge that is valuable beyond the walls of the classroom but that there is a dire need to support and educate students and institutions about the impact of information sharing on a global scale. Students share and receive information on the internet with very little context and support for their roles as knowledge producers and global digital citizens.

This chapter discusses how acting on these opportunities benefit the student well after graduation by inspiring citizens who are information-literate advocates for education, intellectual engagement, and science. The undergraduate who is trusted and supported as a public scholar can become a more empathetic and productive digital citizen. The authors; a scholarly communications librarian, a liberal arts professor, and an undergraduate alumna discuss and relate experiences of how addressing this educational opportunity through 1) classroom assignments, 2) instruction, and 3) publishing has created space for a deepened engagement with the affordances and challenges of being a public scholar and global citizen.

    Cover page: Beyond the Sandbox: Student Scholarship, Digital Citizenship, and the Production of KnowledgeCreative Commons 'BY-NC' version 4.0 license
    • Article
    • Peer Reviewed
    UC Merced Previously Published Works (2017)
    Oxidation of critical signaling protein cysteines regulated by H2O2 has been considered to involve sulfenic acid (RSOH) formation. RSOH may subsequently form either a sulfenyl amide (RSNHR') with a neighboring amide, or a mixed disulfide (RSSR') with another protein cysteine or glutathione. Previous studies have claimed that RSOH can be detected as an adduct (e.g., with 5,5-dimethylcyclohexane-1,3-dione; dimedone). Here, kinetic data are discussed which indicate that few proteins can form RSOH under physiological signaling conditions. We also present experimental evidence that indicates that (1) dimedone reacts rapidly with sulfenyl amides, and more rapidly than with sulfenic acids, and (2) that disulfides can react reversibly with amides to form sulfenyl amides. As some proteins are more stable as the sulfenyl amide than as a glutathionylated species, the former may account for some of the species previously identified as the "sulfenome" - the cellular complement of reversibly-oxidized thiol proteins generated via sulfenic acids.
      Cover page: Protein cysteine oxidation in redox signaling: Caveats on sulfenic acid detection and quantification
      • Article
      • Peer Reviewed
      UC Merced Previously Published Works (2017)
      Oxidation of critical signaling protein cysteines regulated by H2O2 has been considered to involve sulfenic acid (RSOH) formation. RSOH may subsequently form either a sulfenyl amide (RSNHR') with a neighboring amide, or a mixed disulfide (RSSR') with another protein cysteine or glutathione. Previous studies have claimed that RSOH can be detected as an adduct (e.g., with 5,5-dimethylcyclohexane-1,3-dione; dimedone). Here, kinetic data are discussed which indicate that few proteins can form RSOH under physiological signaling conditions. We also present experimental evidence that indicates that (1) dimedone reacts rapidly with sulfenyl amides, and more rapidly than with sulfenic acids, and (2) that disulfides can react reversibly with amides to form sulfenyl amides. As some proteins are more stable as the sulfenyl amide than as a glutathionylated species, the former may account for some of the species previously identified as the "sulfenome" - the cellular complement of reversibly-oxidized thiol proteins generated via sulfenic acids.
        Cover page: Protein cysteine oxidation in redox signaling: Caveats on sulfenic acid detection and quantification.
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