The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
The protein folding ‘speed limit’
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Citations
Cites
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 · cited 1×
“However, stability may come at the expense of increased transient trapping in local energy minima due to stronger non-native inter-residue interactions (landscape ‘roughness’ [26]; see also the review by Onuchic and Wolynes, this issue), with the result that the folding time may first decrease with increasing gradient…”
BackgroundFolding funnels and energy landscapes of larger proteins within the capillarity approximation
Wolynes, P. G. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.12.6170 · Cited by 218
Cited by
Molecular chaperones in protein folding and proteostasis
Hartl, F. U., Bracher, A., & Hayer-Hartl, M. (2011) · Nature · doi:10.1038/nature10317 · Cited by 3,381
How fast-folding proteins fold
Lindorff-Larsen, K., Piana, S., Dror, R. O., & Shaw, D. E. (2011) · Science · doi:10.1126/science.1208351 · Cited by 1,980
Atomic-level characterization of the structural dynamics of proteins
Shaw, D. E., Maragakis, P., Lindorff-Larsen, K., Piana, S., Dror, R. O., Eastwood, M. P., Bank, J. A., Jumper, J. M., Salmon, J. K., Shan, Y., et al. (2010) · Science · doi:10.1126/science.1187409 · Cited by 1,923
Codon bias and heterologous protein expression
Gustafsson, C., Govindarajan, S., & Minshull, J. (2004) · Trends in Biotechnology · doi:10.1016/j.tibtech.2004.04.006 · Cited by 1,330
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
A pause for thought along the co-translational folding pathway
Komar, A. A. (2009) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2008.10.002 · Cited by 349
Atomic-level description of ubiquitin folding
Piana, S., Lindorff-Larsen, K., & Shaw, D. E. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1218321110 · Cited by 326
Abyzov, A., Blackledge, M., & Zweckstetter, M. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00774 · Cited by 215
Lin, Y.-S., Bowman, G. R., Beauchamp, K. A., & Pande, V. S. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2011.12.002 · Cited by 111
Zhuang, W., Cui, R. Z., Silva, D.-A., & Huang, X. (2011) · The Journal of Physical Chemistry B · doi:10.1021/jp109592b · Cited by 70
Deng, N.-J., Dai, W., & Levy, R. M. (2013) · The Journal of Physical Chemistry B · doi:10.1021/jp401962k · Cited by 64
A Molecular Interpretation of 2D IR Protein Folding Experiments with Markov State Models
Baiz, C. R., Lin, Y.-S., Peng, C. S., Beauchamp, K. A., Voelz, V. A., Pande, V. S., & Tokmakoff, A. (2014) · Biophysical Journal · doi:10.1016/j.bpj.2014.02.008 · Cited by 51
Hierarchical Folding Free Energy Landscape of HP35 Revealed by Most Probable Path Clustering
Jain, A., & Stock, G. (2014) · The Journal of Physical Chemistry B · doi:10.1021/jp410398a · Cited by 48
Folding kinetics and unfolded state dynamics of the GB1 hairpin from molecular simulation
De Sancho, D., Mittal, J., & Best, R. B. (2013) · Journal of Chemical Theory and Computation · doi:10.1021/ct301033r · Cited by 35
Pulse labeling reveals the tail end of protein folding by proteome profiling
Zhu, M., Kuechler, E. R., Wong, R. W. K., Calabrese, G., Sitarik, I. M., Rana, V., Stoynov, N., O’Brien, E. P., Gsponer, J., & Mayor, T. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111096 · Cited by 13
Metadata
- Authors
- Kubelka, J., Hofrichter, J., & Eaton, W. A.
- Venue
- Current Opinion in Structural Biology
- Publisher
- Elsevier BV
- Published
- 2004-02
- Volume
- 14
- Issue
- 1
- Pages
- 76-88
- ISSN
- 0959-440X (ISSN-L)
- OpenAlex
- W2102074396
- Cited by
- 830
- References
- 2
- FWCI
- 3.22
- Type
- journal article
- Language
- en
- Open access
- closed
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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.
