The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
NMR characterization of the full‐length recombinant murine prion protein, m PrP(23–231)
Open accessAbstract
The recombinant murine prion protein, m PrP(23–231), was expressed in E. coli with uniform 15 N‐labeling. NMR experiments showed that the previously determined globular three‐dimensional structure of the C‐terminal domain m PrP(121–231) is preserved in the intact protein, and that the N‐terminal polypeptide segment 23–120 is flexibly disordered. This structural information is based on nearly complete sequence‐specific assignments for the backbone amide nitrogens, amide protons and α‐protons of the polypeptide segment of residues 121–231 in m PrP(23–231). Coincidence of corresponding sequential and medium‐range nuclear Overhauser effects (NOE) showed that the helical secondary structures previously identified in m PrP(121–231) are also present in m PrP(23–231), and near‐identity of corresponding amide nitrogen and amide proton chemical shifts indicates that the three‐dimensional fold of m PrP(121–231) is also preserved in the intact protein. The linewidths in heteronuclear 1 H–15 N correlation spectra and 15 N{1 H}‐NOEs showed that the well structured residues 126–230 have correlation times of several nanoseconds, as is typical for small globular proteins, whereas correlation times shorter than 1 nanosecond were observed for all residues of m PrP(23–231) outside of this domain.
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Citations
Cites
Novel Proteinaceous Infectious Particles Cause Scrapie
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Mice devoid of PrP are resistant to scrapie
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The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
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Self-citationNMR structure of the mouse prion protein domain PrP(121–231)
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Cited by
Prusiner, S. B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13363 · Cited by 5,373
Physiology of the prion protein
Linden, R., Martins, V. R., Prado, M. A. M., Cammarota, M., Izquierdo, I., & Brentani, R. R. (2008) · Physiological Reviews · doi:10.1152/physrev.00007.2007 · Cited by 617
PATHOLOGIC CONFORMATIONS OF PRION PROTEINS
Cohen, F. E., & Prusiner, S. B. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.793 · Cited by 533
Neurological Illness in Transgenic Mice Expressing a Prion Protein with an Insertional Mutation
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Metadata
- Authors
- Riek, R., Hornemann, S., Wider, G., Glockshuber, R., & Wüthrich, K.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1997-08-18
- Volume
- 413
- Issue
- 2
- Pages
- 282-288
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2109401365
- Cited by
- 722
- References
- 20
- FWCI
- 15.30
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Riek, R., Hornemann, S., Wider, G., Glockshuber, R., & Wüthrich, K. (1997). NMR characterization of the full‐length recombinant murine prion protein, m PrP(23–231). FEBS Letters. https://doi.org/10.1016/s0014-5793(97)00920-4
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