The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
Three-dimensional structure of human monoamine oxidase A (MAO A): Relation to the structures of rat MAO A and human MAO B
Open accessAbstract
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 ≈550 Å 3, which is smaller than that determined from the structure of deprenyl-inhibited hMAO B (≈700 Å 3) but larger than that of rat MAO A (≈450 Å 3). 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.
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PROCHECK: a program to check the stereochemical quality of protein structures
Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581
The CCP4 suite: programs for protein crystallography
Collaborative Computational Project, N. 4. (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,270
Refinement of Macromolecular Structures by the Maximum-Likelihood Method
Murshudov, G. N., Vagin, A. A., & Dodson, E. J. (1997) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444996012255 · Cited by 14,742
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
Kraulis, P. J. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891004399 · Cited by 14,085
Jones, T. A., Zou, J. Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,648
Role of genotype in the cycle of violence in maltreated children
Caspi, A., McClay, J., Moffitt, T. E., Mill, J., Martin, J., Craig, I. W., Taylor, A., & Poulton, R. (2002) · Science · doi:10.1126/science.1072290 · Cited by 4,842
[26] Raster3D: Photorealistic molecular graphics
Merritt, E. A., & Bacon, D. J. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)77028-9 · Cited by 3,739
The integration of macromolecular diffraction data
Leslie, A. G. W. (2006) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444905039107 · Cited by 1,341
A Perspective on Enzyme Catalysis
Benkovic, S. J., & Hammes-Schiffer, S. (2003) · Science · doi:10.1126/science.1085515 · Cited by 1,262
Detection, delineation, measurement and display of cavities in macromolecular structures
Kleywegt, G. J., & Jones, T. A. (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444993011333 · Cited by 969
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Ramírez, D., & Caballero, J. (2018) · Molecules · doi:10.3390/molecules23051038 · Cited by 624
Son, S.-Y., Ma, J., Kondou, Y., Yoshimura, M., Yamashita, E., & Tsukihara, T. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0710626105 · Cited by 623
Inhibitors of MAO-A and MAO-B in Psychiatry and Neurology
Finberg, J. P. M., & Rabey, J. M. (2016) · Frontiers in Pharmacology · doi:10.3389/fphar.2016.00340 · Cited by 432
Sharma, P., Srivastava, P., Seth, A., Tripathi, P. N., Banerjee, A. G., & Shrivastava, S. K. (2019) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.12.006 · Cited by 331
Structures and mechanism of the monoamine oxidase family
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Metadata
- Authors
- De Colibus, L., Li, M., Binda, C., Lustig, A., Edmondson, D. E., & Mattevi, A.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2005-08-29
- Volume
- 102
- Issue
- 36
- Pages
- 12684-12689
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2108364115
- Cited by
- 527
- References
- 31
- FWCI
- 10.28
- Type
- journal article
- Language
- en
- Open access
- green
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- De Colibus, L., Li, M., Binda, C., Lustig, A., Edmondson, D. E., & Mattevi, A. (2005). Three-dimensional structure of human monoamine oxidase A (MAO A): Relation to the structures of rat MAO A and human MAO B. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0505975102
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