Influence of S-nitrosylation on muscarinic acetylcholine receptors
Keywords and Phrases
"Muscarinic acetylcholine receptors possess a conserved pair of extracellular cysteines which form a disulfide bond between the 1st and the 2nd extracellular loop. Previous work has shown that the disulfide bond forming cysteines influence ligand binding and receptor interaction with transducer proteins. Nitric oxide (NO) has multiple roles in cellular signaling. One mechanism for NO activity is the nitrosylation of protein sulfhydryl groups. Accordingly, in the present studies the role of the nitric oxide generating compound sodium nitroprusside on ligand binding to muscarinic receptors of rat brainstem was studied"--Abstract, leaf iii.
M.S. in Applied and Environmental Biology
University of Missouri--Rolla
x, 57 leaves
© 2007 Pradnya Pandurang Patil, All rights reserved.
Thesis - Citation
Library of Congress Subject Headings
Cellular signal transduction
Print OCLC #
Link to Catalog Record
Full-text not available: Request this publication directly from Missouri S&T Library or contact your local library.http://laurel.lso.missouri.edu/record=b5973583~S5
Patil, Pradnya Pandurang, "Influence of S-nitrosylation on muscarinic acetylcholine receptors" (2007). Masters Theses. 26.
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