The DOI matches its Crossref record; 41 of the 41 references it cites were found in a registry or an index.
Structure, mechanism and catalytic duality of thiamine-dependent enzymes
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Citations
Cites
Sequential Proton Transfer Through Water Bridges in Acid-Base Reactions
Mohammed, O. F., Pines, D., Dreyer, J., Pines, E., & Nibbering, E. T. J. (2005) · Science · doi:10.1126/science.1117756 · Cited by 526
POLARITY AND IONIZATION FROM THE STANDPOINT OF THE LEWIS THEORY OF VALENCE.
Latimer, W. M., & Rodebush, W. H. (1920) · Journal of the American Chemical Society · doi:10.1021/ja01452a015 · Cited by 526
Structural basis for gene regulation by a thiamine pyrophosphate-sensing riboswitch
Serganov, A., Polonskaia, A., Phan, A. T., Breaker, R. R., & Patel, D. J. (2006) · Nature · doi:10.1038/nature04740 · Cited by 441
Metabolite-binding RNA domains are present in the genes of eukaryotes
SUDARSAN, N., BARRICK, J. E., & BREAKER, R. R. (2003) · RNA · doi:10.1261/rna.5090103 · Cited by 420
Structure, evolution and action of vitamin B6-dependent enzymes
Jansonius, J. N. (1998) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(98)80096-1 · Cited by 390
Cusack, S. (1997) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(97)80161-3 · Cited by 378
Lindqvist, Y., Schneider, G., Ermler, U., & Sundström, M. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05301.x · Cited by 366
Structure of the Eukaryotic Thiamine Pyrophosphate Riboswitch with Its Regulatory Ligand
Thore, S., Leibundgut, M., & Ban, N. (2006) · Science · doi:10.1126/science.1128451 · Cited by 345
RAPID DEUTERIUM EXCHANGE IN THIAZOLIUM SALTS1
Breslow, R. (1957) · Journal of the American Chemical Society · doi:10.1021/ja01564a064 · Cited by 319
A common structural motif in thiamin pyrophosphate‐binding enzymes
Hawkins, C. F., Borges, A., & Perham, R. N. (1989) · FEBS Letters · doi:10.1016/0014-5793(89)81064-6 · Cited by 317
Cited by
Donnino, M. W., Andersen, L. W., Chase, M., Berg, K. M., Tidswell, M., Giberson, T., Wolfe, R., Moskowitz, A., Smithline, H., Ngo, L., et al. (2016) · Critical Care Medicine · doi:10.1097/ccm.0000000000001572 · Cited by 293
Thiamin Diphosphate Catalysis: Enzymic and Nonenzymic Covalent Intermediates
Kluger, R., & Tittmann, K. (2008) · Chemical Reviews · doi:10.1021/cr068444m · Cited by 281
Cheah, Y. E., Xu, Y., Sacco, S. A., Babele, P. K., Zheng, A. O., Johnson, C. H., & Young, J. D. (2020) · Metabolic Engineering · doi:10.1016/j.ymben.2020.03.007 · Cited by 52
Metadata
- Authors
- Frank, R. A. W., Leeper, F. J., & Luisi, B. F.
- Venue
- Cellular and Molecular Life Sciences
- Published
- 2007-02-13
- Volume
- 64
- Issue
- 7-8
- Pages
- 892-905
- ISSN
- 1420-682X (ISSN-L)
- 1420-9071
- OpenAlex
- W2015324008
- Cited by
- 259
- References
- 41
- FWCI
- 3.66
- Type
- journal article
- Language
- en
- Open access
- green
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- Frank, R. A. W., Leeper, F. J., & Luisi, B. F. (2007). Structure, mechanism and catalytic duality of thiamine-dependent enzymes. Cellular and Molecular Life Sciences. https://doi.org/10.1007/s00018-007-6423-5
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
