The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 Å
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Citations
Cites
Kabsch, W., & Sander, C. (1983) · Biopolymers · doi:10.1002/bip.360221211 · Cited by 15,320
The Leucine Zipper: A Hypothetical Structure Common to a New Class of DNA Binding Proteins
Landschulz, W. H., Johnson, P. F., & McKnight, S. L. (1988) · Science · doi:10.1126/science.3289117 · Cited by 3,443
Cited by
Predicting coiled coils from protein sequences.
Lupas, A., Van Dyke, M., & Stock, J. (1991) · Science · doi:10.1126/science.252.5009.1162 · Cited by 3,953
Molecular Physiology of P2X Receptors
North, R. A. (2002) · Physiological Reviews · doi:10.1152/physrev.00015.2002 · Cited by 2,919
Wolf, Y. I., Aravind, L., Grishin, N. V., & Koonin, E. V. (1999) · Genome Research · doi:10.1101/gr.9.8.689 · Cited by 410
Predicting oligomerization states of coiled coils
Woolfson, D. N., & Alber, T. (1995) · Protein Science · doi:10.1002/pro.5560040818 · Cited by 214
Controlled formation of model homo- and heterodimer coiled coil polypeptides
Graddis, T. J., Myszka, D. G., & Chaiken, I. M. (1993) · Biochemistry · doi:10.1021/bi00210a015 · Cited by 153
Metadata
- Authors
- Cusack, S., Berthet-Colominas, C., Härtlein, M., Nassar, N., & Leberman, R.
- Venue
- Nature
- Published
- 1990-09
- Volume
- 347
- Issue
- 6290
- Pages
- 249-255
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2057481603
- Cited by
- 619
- References
- 2
- FWCI
- 18.10
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 Å. https://app.cochat.ai/papers/10.1038/347249a0
- The paper
- Cusack, S., Berthet-Colominas, C., Härtlein, M., Nassar, N., & Leberman, R. (1990). A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 Å. Nature. https://doi.org/10.1038/347249a0
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.