References
Arican, P., Gencpinar, P., Kirbiyik, O., Bozkaya Yilmaz, S., Ersen, A., Oztekin, O., & Olgac Dundar, N. (2019). The Clinical and Molecular Characteristics of Molybdenum Cofactor Deficiency Due to MOCS2 Mutations. Pediatric neurology99 , 55–59. https://doi.org/10.1016/j.pediatrneurol.2019.04.021
Bendl, J., Stourac, J., Salanda, O., Pavelka, A., Wieben, E. D., Zendulka, J., Brezovsky, J., & Damborsky, J. (2014). PredictSNP: robust and accurate consensus classifier for prediction of disease-related mutations. PLoS computational biology10 (1), e1003440. https://doi.org/10.1371/journal.pcbi.1003440
Daniels, J. N., Wuebbens, M. M., Rajagopalan, K. V., & Schindelin, H. (2008). Crystal structure of a molybdopterin synthase-precursor Z complex: insight into its sulfur transfer mechanism and its role in molybdenum cofactor deficiency. Biochemistry47 (2), 615–626. https://doi.org/10.1021/bi701734g
Johnson, J. L., Waud, W. R., Rajagopalan, K. V., Duran, M., Beemer, F. A., & Wadman, S. K. (1980). Inborn errors of molybdenum metabolism: combined deficiencies of sulfite oxidase and xanthine dehydrogenase in a patient lacking the molybdenum cofactor. Proceedings of the National Academy of Sciences of the United States of America77 (6), 3715–3719. https://doi.org/10.1073/pnas.77.6.3715
Kopec, J., Bailey, H., Fitzpatrick, F., Strain-Damerell, C., Oberholzer, A.E., Williams, E., Burgess-Brown, N., von Delft, F., Arrowsmith, C., Edwards, A., Bountra, C., & Yue, W.W. (2016). Crystal structure of human molybdopterin synthase complex DOI: 10.2210/pdb5mpo/pdb
Leimkuhler, S., Freuer, A., Araujo, J. A., Rajagopalan, K. V., & Mendel, R. R. (2003). Mechanistic studies of human molybdopterin synthase reaction and characterization of mutants identified in group B patients of molybdenum cofactor deficiency. The Journal of biological chemistry278 (28), 26127–26134. https://doi.org/10.1074/jbc.M303092200
Reiss, J., Dorche, C., Stallmeyer, B., Mendel, R. R., Cohen, N., & Zabot, M. T. (1999). Human molybdopterin synthase gene: genomic structure and mutations in molybdenum cofactor deficiency type B. American journal of human genetics64 (3), 706–711. https://doi.org/10.1086/302296
Reiss, J., & Hahnewald, R. (2011). Molybdenum cofactor deficiency: Mutations in GPHN, MOCS1, and MOCS2. Human mutation, 32(1), 10–18. https://doi.org/10.1002/humu.21390
Rose, P. W., Prlić, A., Altunkaya, A., Bi, C., Bradley, A. R., Christie, C. H., Costanzo, L. D., Duarte, J. M., Dutta, S., Feng, Z., Green, R. K., Goodsell, D. S., Hudson, B., Kalro, T., Lowe, R., Peisach, E., Randle, C., Rose, A. S., Shao, C., Tao, Y. P., … Burley, S. K. (2017). The RCSB protein data bank: integrative view of protein, gene and 3D structural information. Nucleic acids research45 (D1), D271–D281. https://doi.org/10.1093/nar/gkw1000
Seo, G.H., Taeho, K., Park, J., et al. Pilot study of EVIDENCE: High diagnostic yield and clinical utility of whole exome sequencing using an automated interpretation system for patients with suspected genetic disorders. doi: https://doi.org/10.1101/628438
Subramanian, K., Góra, A., Spruijt, R., Mitusińska, K., Suarez-Diez, M., Martins Dos Santos, V., & Schaap, P. J. (2018). Modulating D-amino acid oxidase (DAAO) substrate specificity through facilitated solvent access. PloS one13 (6), e0198990. https://doi.org/10.1371/journal.pone.0198990