Diss. (sammanfattning) Stockholm : Karol. inst., 2005. / Härtill 4 uppsatser.

Thesis (Ph. D.)--University of Missouri--Columbia, 1998. / Typescript. Vita. Includes bibliographical references (leaves: 139-147). Also available on the Internet.

Thesis (Ph. D.)--West Virginia University, 2000. / Title from document title page. Document formatted into pages; contains ix, 135 p. : ill. (some col.). Includes abstract. Includes bibliographical references (p. 127-135).

Thesis (doctoral)--Lund University, 1994. / Added t.p. with thesis statement inserted.

Thesis (Ph.D.)--Ohio University, November, 2008. / Title from PDF t.p. Release of full electronic text on OhioLINK has been delayed until December 1, 2010. Includes bibliographical references (leaves 140-162)

Thesis (doctoral)--Lund University, 1994. / Added t.p. with thesis statement inserted.

Thesis (M.S.)--The University of North Carolina at Greensboro, 2009. / Directed by Mark Hens; submitted to the Dept. of Biology. Title from PDF t.p. (viewed May 17, 2010). Includes bibliographical references (p. 60-65).

Thesis (Ph. D.)--University of Lund, 1998. / Originally issued as the author's doctoral thesis. Includes bibliographical references.

Thesis (Ph.D.)--Ohio University, November, 2008. / Release of full electronic text on OhioLINK has been delayed until December 1, 2010. Includes bibliographical references (leaves 140-162)

<p>S-nitrosylation, the prototypic mechanism of redox-based signal transduction, involves the covalent attachment of a nitrogen monoxide group to a Cys-thiol side chain. S-nitrosylation of proteins has been demonstrated to affect a broad range of functional parameters including enzymatic activity, subcellular localization, protein-protein interactions and protein stability. The primary focus of my dissertation was to solve a problem of great importance in the field of S-nitrosylation, which is, to identify denitrosylase(s) i.e., enzymes that remove NO groups from S-nitrosothiols. Recent progress in elucidating the cellular regulation of S-nitrosylation has led to the identification of two physiologically relevant denitrosylating activities that remove the NO group from S-nitrosylated substrates. Thioredoxin/thioredoxin reductase (Trx system) functions as an NADPH-dependent denitrosylase across a broad range of S-nitrosylated proteins (SNO-proteins). S-nitroso-glutathione reductase (GSNOR), which is highly conserved across phylogeny, metabolizes GSNO utilizing NADH as a reducing coenzyme, thereby shifting equilibria between GSNO and SNO-proteins. This dissertation describes the discovery of two novel denitrosylases: one from yeast and the other from mammals. Using technique of column chromatography we have purified these novel denitrosylases to homogeneity and have demonstrated a principal contribution of these enzymes towards S-nitrosothiol metabolism.</p> / Dissertation