The DOI matches its Crossref record; 28 of the 28 references it cites were found in a registry or an index.
Protein folding: The stepwise assembly of foldon units
Open accessAbstract
Equilibrium and kinetic hydrogen exchange experiments show that cytochrome c is composed of five foldon units that continually unfold and refold even under native conditions. Folding proceeds by the stepwise assembly of the foldon units rather than one amino acid at a time. The folding pathway is determined by a sequential stabilization process; previously formed foldons guide and stabilize subsequent foldons to progressively build the native protein. Four other proteins have been found to show similar behavior. These results support stepwise protein folding pathways through discrete intermediates.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Principles that Govern the Folding of Protein Chains
Anfinsen, C. B. (1973) · Science · doi:10.1126/science.181.4096.223 · Cited by 7,096
Funnels, pathways, and the energy landscape of protein folding: A synthesis
Bryngelson, J. D., Onuchic, J. N., Socci, N. D., & Wolynes, P. G. (1995) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340210302 · Cited by 2,648
From Levinthal to pathways to funnels
Dill, K. A., & Chan, H. S. (1997) · Nature Structural & Molecular Biology · doi:10.1038/nsb0197-10 · Cited by 2,293
Primary structure effects on peptide group hydrogen exchange
Bai, Y., Milne, J. S., Mayne, L., & Englander, S. W. (1993) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340170110 · Cited by 1,902
Self-citationTheory of the Phase Transition between Helix and Random Coil in Polypeptide Chains
Zimm, B. H., & Bragg, J. K. (1959) · The Journal of Chemical Physics · doi:10.1063/1.1730390 · Cited by 1,785
Myers, J. K., Nick Pace, C., & Martin Scholtz, J. (1995) · Protein Science · doi:10.1002/pro.5560041020 · Cited by 1,720
Plaxco, K. W., Simons, K. T., & Baker, D. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1645 · Cited by 1,518
Onuchic, J. N., & Wolynes, P. G. (2004) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2004.01.009 · Cited by 1,301
Protein Folding Intermediates: Native-State Hydrogen Exchange
Bai, Y., Sosnick, T. R., Mayne, L., & Englander, S. W. (1995) · Science · doi:10.1126/science.7618079 · Cited by 990
Self-citationIsotope effects in peptide group hydrogen exchange
Connelly, G. P., Bai, Y., Jeng, M., & Englander, S. W. (1993) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340170111 · Cited by 376
Self-citation
Cited by
Dill, K. A., Ozkan, S. B., Shell, M. S., & Weikl, T. R. (2008) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.37.092707.153558 · Cited by 1,163
Cytochrome c/cardiolipin relations in mitochondria: a kiss of death
Kagan, V. E., Bayır, H. A., Belikova, N. A., Kapralov, O., Tyurina, Y. Y., Tyurin, V. A., Jiang, J., Stoyanovsky, D. A., Wipf, P., Kochanek, P. M., et al. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.03.004 · Cited by 444
Belikova, N. A., Vladimirov, Y. A., Osipov, A. N., Kapralov, A. A., Tyurin, V. A., Potapovich, M. V., Basova, L. V., Peterson, J., Kurnikov, I. V., & Kagan, V. E. (2006) · Biochemistry · doi:10.1021/bi0525573 · Cited by 398
Single-molecule fluorescence spectroscopy maps the folding landscape of a large protein
Pirchi, M., Ziv, G., Riven, I., Cohen, S. S., Zohar, N., Barak, Y., & Haran, G. (2011) · Nature Communications · doi:10.1038/ncomms1504 · Cited by 179
Structural transformations of cytochrome c upon interaction with cardiolipin
Muenzner, J., & Pletneva, E. V. (2014) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2013.11.002 · Cited by 74
Metadata
- Authors
- Maity, H., Maity, M., Krishna, M. M. G., Mayne, L., & Englander, S. W.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2005-03-17
- Volume
- 102
- Issue
- 13
- Pages
- 4741-4746
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2112444949
- Cited by
- 300
- References
- 28
- FWCI
- 7.38
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Protein folding: The stepwise assembly of foldon units. https://app.cochat.ai/papers/10.1073/pnas.0501043102
- The paper
- Maity, H., Maity, M., Krishna, M. M. G., Mayne, L., & Englander, S. W. (2005). Protein folding: The stepwise assembly of foldon units. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0501043102
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.