The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Nucleoside triphosphate-binding proteins: different scaffolds to achieve phosphoryl transfer
Abstract
Nucleoside triphosphates are crucial mediators of life. The high energy phosphoanhydride bond of (usually) ATP is used to drive unfavorable chemical reactions, to fuel biological machines, and to regulate a vast number of processes via phosphorylation of proteins. GTP, in turn, is used almost exclusively for the regulation of signal transduction and transport processes, whereas the other nucleotides play a less important role, except in synthesis pathways involving sugars (UTP) and phospholipids (CTP) and as building blocks of polynucleotides such as RNA and DNA. Proteins that bind and use these nucleotides for enzymatic reaction and regulation are very diverse. Although some of them constitute the largest protein superfamilies known (e.g. protein kinases), others seem to be far less conserved in evolution.
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Cites
Crystal structure at 3.5 A resolution of HIV-1 reverse transcriptase complexed with an inhibitor
Kohlstaedt, L. A., Wang, J., Friedman, J. M., Rice, P. A., & Steitz, T. A. (1992) · Science · doi:10.1126/science.1377403 · Cited by 1,914 · cited 7×
“Crystal structure at 3.5 A/ resolution of HIV-1 reverse transcriptase complexed with an inhibitor.”
MethodInfluentialAtomic structure of the MAP kinase ERK2 at 2.3 A resolution
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A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone
Prodromou, C., Roe, S. M., Piper, P. W., & Pearl, L. H. (1997) · Nature Structural Biology · doi:10.1038/nsb0697-477 · Cited by 239
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Freymann, D. M., Keenan, R. J., Stroud, R. M., & Walter, P. (1997) · Nature · doi:10.1038/385361a0 · Cited by 228
Crystal structure of the NG domain from the signal-recognition particle receptor FtsY.
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Cited by
Classification and evolution of P-loop GTPases and related ATPases
Leipe, D. D., Wolf, Y. I., Koonin, E. V., & Aravind, L. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5378 · Cited by 1,148
Evolutionary history and higher order classification of AAA+ ATPases
Iyer, L. M., Leipe, D. D., Koonin, E. V., & Aravind, L. (2004) · Journal of Structural Biology · doi:10.1016/j.jsb.2003.10.010 · Cited by 787
Development of polyphosphate parameters for use with the AMBER force field
Meagher, K. L., Redman, L. T., & Carlson, H. A. (2003) · Journal of Computational Chemistry · doi:10.1002/jcc.10262 · Cited by 708
Burroughs, A. M., Allen, K. N., Dunaway-Mariano, D., & Aravind, L. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.06.049 · Cited by 438
Structural diversity of ABC transporters
ter Beek, J., Guskov, A., & Slotboom, D. J. (2014) · Journal of General Physiology · doi:10.1085/jgp.201411164 · Cited by 384
Metadata
- Authors
- Vetter, I. R., & Wittinghofer, A.
- Venue
- Quarterly Reviews of Biophysics
- Publisher
- Cambridge University Press (CUP)
- Published
- 1999-02
- Volume
- 32
- Issue
- 1
- Pages
- 1-56
- ISSN
- 0033-5835 (ISSN-L)
- 1469-8994
- OpenAlex
- W2085784933
- Cited by
- 184
- References
- 5
- FWCI
- 1.52
- Type
- journal article
- Language
- en
- Open access
- closed
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- Vetter, I. R., & Wittinghofer, A. (1999). Nucleoside triphosphate-binding proteins: different scaffolds to achieve phosphoryl transfer. Quarterly Reviews of Biophysics. https://doi.org/10.1017/s0033583599003480
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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.
