Development of Spin-Labeled Pargyline Analogues as Specific Inhibitors of Human Monoamine Oxidases A and B
Author:
Affiliation:
1. Departments of Biochemistry and Chemistry, Emory University, Atlanta, Georgia 30322
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi9002106
Reference29 articles.
1. Comparison of the Structural Properties of the Active Site Cavities of Human and Rat Monoamine Oxidase A and B in Their Soluble and Membrane-Bound Forms
2. Determination of the Oligomeric States of Human and Rat Monoamine Oxidases in the Outer Mitochondrial Membrane and Octyl β-d-Glucopyranoside Micelles Using Pulsed Dipolar Electron Spin Resonance Spectroscopy
3. Three-dimensional structure of human monoamine oxidase A (MAO A): Relation to the structures of rat MAO A and human MAO B
4. Structure of human monoamine oxidase A at 2.2-A resolution: The control of opening the entry for substrates/inhibitors
5. Structure of human monoamine oxidase B, a drug target for the treatment of neurological disorders
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