The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index.
Evidence for a molten globule state as a general intermediate in protein folding
Abstract
We propose that the formation of the transient molten globule state occurs early on the pathway of folding of all globular proteins.
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Citations
Cites
Kim, P. S., & Baldwin, R. L. (1982) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.51.070182.002331 · Cited by 1,035
Roder, H., Elöve, G. A., & Englander, S. W. (1988) · Nature · doi:10.1038/335700a0 · Cited by 813
α‐lactalbumin: compact state with fluctuating tertiary structure?
Dolgikh, D. A., Gilmanshin, R. I., Brazhnikov, E. V., Bychkova, V. E., Semisotnov, G. V., Venyaminov, S. Y., & Ptitsyn, O. B. (1981) · FEBS Letters · doi:10.1016/0014-5793(81)80642-4 · Cited by 616
Self-citationNMR evidence for an early framework intermediate on the folding pathway of ribonuclease A
Udgaonkar, J. B., & Baldwin, R. L. (1988) · Nature · doi:10.1038/335694a0 · Cited by 575
Protein folding: Hypotheses and experiments
Ptitsyn, O. B. (1987) · Journal of Protein Chemistry · doi:10.1007/bf00248050 · Cited by 543
Self-citationBaum, J., Dobson, C. M., Evans, P. A., & Hanley, C. (1989) · Biochemistry · doi:10.1021/bi00427a002 · Cited by 470
Comparison of the transient folding intermediates in lysozyme and .alpha.-lactalbumin
Kuwajima, K., Hiraoka, Y., Ikeguchi, M., & Sugai, S. (1985) · Biochemistry · doi:10.1021/bi00325a010 · Cited by 280
Compact state of a protein molecule with pronounced small-scale mobility: bovine ?-lactalbumin
Dolgikh, D. A., Abaturov, L. V., Bolotina, I. A., Brazhnikov, E. V., Bychkova, V. E., Gilmanshin, R. I., Lebedev, Y. O., Semisotnov, G. V., Tiktopulo, E. I., & Ptitsyn, O. B. (1985) · European Biophysics Journal · doi:10.1007/bf00256531 · Cited by 258
Self-citationIkeguchi, M., Kuwajima, K., Mitani, M., & Sugai, S. (1986) · Biochemistry · doi:10.1021/bi00370a034 · Cited by 255
Three-state denaturation of α-lactalbumin by guanidine hydrochloride
Kuwajima, K., Nitta, K., Yoneyama, M., & Sugai, S. (1976) · Journal of Molecular Biology · doi:10.1016/0022-2836(76)90091-7 · Cited by 248
Cited by
Martin, J., Langer, T., Boteva, R., Schramel, A., Horwich, A. L., & Hartl, F.-U. (1991) · Nature · doi:10.1038/352036a0 · Cited by 854
Protein Design: Toward Functional Metalloenzymes
Yu, F., Cangelosi, V. M., Zastrow, M. L., Tegoni, M., Plegaria, J. S., Tebo, A. G., Mocny, C. S., Ruckthong, L., Qayyum, H., & Pecoraro, V. L. (2014) · Chemical Reviews · doi:10.1021/cr400458x · Cited by 441
Protein folding: local structures, domains, subunits, and assemblies
Jaenicke, R. (1991) · Biochemistry · doi:10.1021/bi00227a001 · Cited by 438
De novo and inverse folding predictions of protein structure and dynamics
Godzik, A., Kolinski, A., & Skolnick, J. (1993) · Journal of Computer-Aided Molecular Design · doi:10.1007/bf02337559 · Cited by 91
Thomas, D. J. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)80892-k · Cited by 15
Metadata
- Authors
- Ptitsyn, O. B., Pain, R. H., Semisotnov, G. V., Zerovnik, E., & Razgulyaev, O. I.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1990-03-12
- Volume
- 262
- Issue
- 1
- Pages
- 20-24
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2044328480
- Cited by
- 678
- References
- 14
- FWCI
- 15.94
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Evidence for a molten globule state as a general intermediate in protein folding. https://app.cochat.ai/papers/10.1016/0014-5793(90)80143-7
- The paper
- Ptitsyn, O. B., Pain, R. H., Semisotnov, G. V., Zerovnik, E., & Razgulyaev, O. I. (1990). Evidence for a molten globule state as a general intermediate in protein folding. FEBS Letters. https://doi.org/10.1016/0014-5793(90)80143-7
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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.