The DOI matches its Crossref record; 68 of the 68 references it cites were found in a registry or an index.
Engineering proteins for thermostability through rigidifying flexible sites
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Citations
Cites
Scalable molecular dynamics with NAMD
Phillips, J. C., Braun, R., Wang, W., Gumbart, J., Tajkhorshid, E., Villa, E., Chipot, C., Skeel, R. D., Kalé, L., & Schulten, K. (2005) · Journal of Computational Chemistry · doi:10.1002/jcc.20289 · Cited by 16,914
The Amber biomolecular simulation programs
Case, D. A., Cheatham, T. E., Darden, T., Gohlke, H., Luo, R., Merz, K. M., Onufriev, A., Simmerling, C., Wang, B., & Woods, R. J. (2005) · Journal of Computational Chemistry · doi:10.1002/jcc.20290 · Cited by 9,535
CHARMM: The biomolecular simulation program
Brooks, B. R., Brooks, C. L., Mackerell, A. D., Nilsson, L., Petrella, R. J., Roux, B., Won, Y., Archontis, G., Bartels, C., Boresch, S., et al. (2009) · Journal of Computational Chemistry · doi:10.1002/jcc.21287 · Cited by 8,939
GROMACS 3.0: a package for molecular simulation and trajectory analysis
Lindahl, E., Hess, B., & van der Spoel, D. (2001) · Journal of Molecular Modeling · doi:10.1007/s008940100045 · Cited by 6,977
Iterative saturation mutagenesis (ISM) for rapid directed evolution of functional enzymes
Reetz, M. T., & Carballeira, J. D. (2007) · Nature Protocols · doi:10.1038/nprot.2007.72 · Cited by 860
Directed evolution drives the next generation of biocatalysts
Turner, N. J. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.203 · Cited by 785
Long-timescale molecular dynamics simulations of protein structure and function
Klepeis, J. L., Lindorff-Larsen, K., Dror, R. O., & Shaw, D. E. (2009) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2009.03.004 · Cited by 750
Electrostatic Effects in Proteins
Perutz, M. F. (1978) · Science · doi:10.1126/science.694508 · Cited by 743
Protein flexibility predictions using graph theory
Jacobs, D. J., Rader, A. J., Kuhn, L. A., & Thorpe, M. F. (2001) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.1081 · Cited by 727
Scalable Molecular Dynamics with NAMD
(2016) · Parallel Science and Engineering Applications · doi:10.1201/b16251-15 · Cited by 639
Cited by
Amino acid sequence encodes protein abundance shaped by protein stability at reduced synthesis cost
(2024) · doi:10.1002/pro.5239 · Cited by 12
Xu, R., Pan, Q., Zhu, G., Ye, Y., Xin, M., Wang, Z., Wang, S., Li, W., Wei, Y., Guo, J., et al. (2024) · Protein Science · doi:10.1002/pro.5097 · Cited by 12
Metadata
- Authors
- Yu, H., & Huang, H.
- Venue
- Biotechnology Advances
- Publisher
- Elsevier BV
- Published
- 2014-03
- Volume
- 32
- Issue
- 2
- Pages
- 308-315
- ISSN
- 0734-9750 (ISSN-L)
- OpenAlex
- W2036532473
- Cited by
- 255
- References
- 68
- FWCI
- 4.57
- Type
- journal article
- Language
- en
- Open access
- closed
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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.
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- CoChat. (2026). Citation check: Engineering proteins for thermostability through rigidifying flexible sites. https://app.cochat.ai/papers/10.1016/j.biotechadv.2013.10.012
- The paper
- Yu, H., & Huang, H. (2014). Engineering proteins for thermostability through rigidifying flexible sites. Biotechnology Advances. https://doi.org/10.1016/j.biotechadv.2013.10.012
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.
