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Cited by 312

The DOI matches its Crossref record; 762 of the 762 references it cites were found in a registry or an index.

Protein Design: From the Aspect of Water Solubility and Stability

Open access
Qing, Rui, Hao, Shilei, Smorodina, Eva, Jin, David, Zalevsky, Arthur, Zhang, Shuguang·2022·Chemical Reviews

Abstract

transmembrane protein design. Traditional strategies to enhance protein solubility and structural stability are introduced. The designs of stable protein complexes and high-order assemblies are covered. Computational methodologies behind these endeavors, including structure prediction programs, machine learning algorithms, and specialty software dedicated to the evaluation of protein solubility and aggregation, are discussed. The findings and opportunities for Cryo-EM are presented. This review provides an overview of significant progress and prospects in accurate protein design for solubility and stability.

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Crossref · 10.1021/acs.chemrev.1c00757

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Metadata

Authors
Qing, R., Hao, S., Smorodina, E., Jin, D., Zalevsky, A., & Zhang, S.
Venue
Chemical Reviews
Published
2022-08-03
Volume
122
Issue
18
Pages
14085-14179
ISSN
  • 0009-2665 (ISSN-L)
  • 1520-6890
OpenAlex
W4289653737
Cited by
312
References
762
FWCI
4.66
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Protein Design: From the Aspect of Water Solubility and Stability. https://app.cochat.ai/papers/10.1021/acs.chemrev.1c00757
The paper
Qing, R., Hao, S., Smorodina, E., Jin, D., Zalevsky, A., & Zhang, S. (2022). Protein Design: From the Aspect of Water Solubility and Stability. Chemical Reviews. https://doi.org/10.1021/acs.chemrev.1c00757

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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.