Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprint

Profile analysis: detection of distantly related proteins.

Gribskov, M., McLachlan, A. D., & Eisenberg, D. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.13.4355 · Cited by 1,325

Inositol Trisphosphate Receptor Ca2+Release Channels

Foskett, J. K., White, C., Cheung, K.-H., & Mak, D.-O. D. (2007) · Physiological Reviews · doi:10.1152/physrev.00035.2006 · Cited by 1,188

Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts

van Berkel, W. J. H., Kamerbeek, N. M., & Fraaije, M. W. (2006) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2006.03.044 · Cited by 671

Glyceraldehyde-3-phosphate Dehydrogenase Selectively Binds AU-rich RNA in the NAD+-binding Region (Rossmann Fold)

Nagy, E., & Rigby, W. F. C. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.6.2755 · Cited by 361

Missense mutation in flavin-containing mono-oxygenase 3 gene, FMO3, underlies fish-odour syndrome

Dolphin, C. T., Janmohamed, A., Smith, R. L., Shephard, E. A., & Phillips, L. R. (1997) · Nature Genetics · doi:10.1038/ng1297-491 · Cited by 284

The Human Homologue of the Yeast Proteins Skb1 and Hsl7p Interacts with Jak Kinases and Contains Protein Methyltransferase Activity

Pollack, B. P., Kotenko, S. V., He, W., Izotova, L. S., Barnoski, B. L., & Pestka, S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.44.31531 · Cited by 290

NAD-binding domains of dehydrogenases

Lesk, A. M. (1995) · Current Opinion in Structural Biology · doi:10.1016/0959-440x(95)80010-7 · Cited by 239

A novel membrane-bound respiratory complex from Desulfovibrio desulfuricans ATCC 27774

Pires, R. H., Lourenço, A. I., Morais, F., Teixeira, M., Xavier, A. V., Saraiva, L. M., & Pereira, I. A. C. (2003) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(03)00065-3 · Cited by 115

Metabolic enzymes that bind RNA: yet another level of cellular regulatory network?

Cieśla, J. (2006) · Acta Biochimica Polonica · doi:10.18388/abp.2006_3360 · Cited by 106

Identification of All-trans-Retinol:All-trans-13,14-dihydroretinol Saturase

Moise, A. R., Kuksa, V., Imanishi, Y., & Palczewski, K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409130200 · Cited by 103

Identification of the NAD+-Binding Fold of Glyceraldehyde-3-Phosphate Dehydrogenase as a Novel RNA-Binding Domain

Nagy, E., Henics, T., Eckert, M., Miseta, A., Lightowlers, R. N., & Kellermayer, M. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3246 · Cited by 99

Crystal structure of the NADP+-dependent aldehyde dehydrogenase from Vibrio harveyi: structural implications for cofactor specificity and affinity

AHVAZI, B., COULOMBE, R., DELARGE, M., VEDADI, M., ZHANG, L., MEIGHEN, E., & VRIELINK, A. (2000) · Biochemical Journal · doi:10.1042/bj3490853 · Cited by 82

Cloning and sequence of the human adrenodoxin reductase gene

Lin, D., Shi, Y. F., & Miller, W. L. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.21.8516 · Cited by 61

Retinol Dehydrogenases Regulate Vitamin A Metabolism for Visual Function

Sahu, B., & Maeda, A. (2016) · Nutrients · doi:10.3390/nu8110746 · Cited by 61

The Effect of Relational Background Knowledge on Learning of Protein Three-Dimensional Fold Signatures

Turcotte, M., Muggleton, S. H., & Sternberg, M. J. E. (2001) · Machine Learning · doi:10.1023/a:1007672817406 · Cited by 30

Isolated Bacillus subtilis HemY has coproporphyrinogenIII to coproporphyrinIII oxidase activity

Hansson, M., Gustafsson, M. C. U., Kannangara, C. G., & Hederstedt, L. (1997) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(97)00030-7 · Cited by 28

Structural and Functional Characterization of a Gene Cluster Responsible for Deglycosylation of C-glucosyl Flavonoids and Xanthonoids by Deinococcus aerius

Furlanetto, V., Kalyani, D. C., Kostelac, A., Puc, J., Haltrich, D., Hällberg, B. M., & Divne, C. (2024) · Journal of Molecular Biology · doi:10.1016/j.jmb.2024.168547 · Cited by 9