| http://purl.uniprot.org/citations/16129825 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16129825 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16129825 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/16129825 | http://www.w3.org/2000/01/rdf-schema#comment | "The three-dimensional structure of recombinant human monoamine oxidase A (hMAO A) as its clorgyline-inhibited adduct is described. Although the chain-fold of hMAO A is similar to that of rat MAO A and human MAO B (hMAO B), hMAO A is unique in that it crystallizes as a monomer and exhibits the solution hydrodynamic behavior of a monomeric form rather than the dimeric form of hMAO B and rat MAO A. hMAO A's active site consists of a single hydrophobic cavity of approximately 550 A3, which is smaller than that determined from the structure of deprenyl-inhibited hMAO B (approximately 700 A3) but larger than that of rat MAO A (approximately 450 A3). An important component of the active site structure of hMAO A is the loop conformation of residues 210-216, which differs from that of hMAO B and rat MAO A. The origin of this structural alteration is suggested to result from long-range interactions in the monomeric form of the enzyme. In addition to serving as a basis for the development of hMAO A specific inhibitors, these data support the proposal that hMAO A involves a change from the dimeric to the monomeric form through a Glu-151 --> Lys mutation that is specific of hMAO A [Andrès, A. M., Soldevila, M., Navarro, A., Kidd, K. K., Oliva, B. & Bertranpetit, J. (2004) Hum. Genet. 115, 377-386]. These considerations put into question the use of MAO A from nonhuman sources in drug development for use in humans."xsd:string |
| http://purl.uniprot.org/citations/16129825 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.0505975102"xsd:string |
| http://purl.uniprot.org/citations/16129825 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.0505975102"xsd:string |
| http://purl.uniprot.org/citations/16129825 | http://purl.uniprot.org/core/author | "Li M."xsd:string |
| http://purl.uniprot.org/citations/16129825 | http://purl.uniprot.org/core/author | "Li M."xsd:string |
| http://purl.uniprot.org/citations/16129825 | http://purl.uniprot.org/core/author | "Mattevi A."xsd:string |
| http://purl.uniprot.org/citations/16129825 | http://purl.uniprot.org/core/author | "Mattevi A."xsd:string |
| http://purl.uniprot.org/citations/16129825 | http://purl.uniprot.org/core/author | "Binda C."xsd:string |
| http://purl.uniprot.org/citations/16129825 | http://purl.uniprot.org/core/author | "Binda C."xsd:string |
| http://purl.uniprot.org/citations/16129825 | http://purl.uniprot.org/core/author | "Edmondson D.E."xsd:string |
| http://purl.uniprot.org/citations/16129825 | http://purl.uniprot.org/core/author | "Edmondson D.E."xsd:string |
| http://purl.uniprot.org/citations/16129825 | http://purl.uniprot.org/core/author | "Lustig A."xsd:string |
| http://purl.uniprot.org/citations/16129825 | http://purl.uniprot.org/core/author | "Lustig A."xsd:string |
| http://purl.uniprot.org/citations/16129825 | http://purl.uniprot.org/core/author | "De Colibus L."xsd:string |
| http://purl.uniprot.org/citations/16129825 | http://purl.uniprot.org/core/author | "De Colibus L."xsd:string |
| http://purl.uniprot.org/citations/16129825 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/16129825 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/16129825 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/16129825 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/16129825 | http://purl.uniprot.org/core/pages | "12684-12689"xsd:string |
| http://purl.uniprot.org/citations/16129825 | http://purl.uniprot.org/core/pages | "12684-12689"xsd:string |
| http://purl.uniprot.org/citations/16129825 | http://purl.uniprot.org/core/title | "Three-dimensional structure of human monoamine oxidase A (MAO A): relation to the structures of rat MAO A and human MAO B."xsd:string |