The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
CASTp: computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues
Open accessAbstract
Cavities on a proteins surface as well as specific amino acid positioning within it create the physicochemical properties needed for a protein to perform its function. CASTp (http://cast.engr.uic.edu) is an online tool that locates and measures pockets and voids on 3D protein structures. This new version of CASTp includes annotated functional information of specific residues on the protein structure. The annotations are derived from the Protein Data Bank (PDB), Swiss-Prot, as well as Online Mendelian Inheritance in Man (OMIM), the latter contains information on the variant single nucleotide polymorphisms (SNPs) that are known to cause disease. These annotated residues are mapped to surface pockets, interior voids or other regions of the PDB structures. We use a semi-global pair-wise sequence alignment method to obtain sequence mapping between entries in Swiss-Prot, OMIM and entries in PDB. The updated CASTp web server can be used to study surface features, functional regions and specific roles of key residues of proteins.
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CASTp: Computed Atlas of Surface Topography of proteins
Binkowski, T. A. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg512 · Cited by 1,693
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Self-citationMendelian Inheritance in Man: A Catalog of Human Genes and Genetic Disorders
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CASTp 3.0: computed atlas of surface topography of proteins
Tian, W., Chen, C., Lei, X., Zhao, J., & Liang, J. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky473 · Cited by 2,389
Self-citationFpocket: An open source platform for ligand pocket detection
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Role of computer-aided drug design in modern drug discovery
Macalino, S. J. Y., Gosu, V., Hong, S., & Choi, S. (2015) · Archives of Pharmacal Research · doi:10.1007/s12272-015-0640-5 · Cited by 762
Directed Evolution: Methodologies and Applications
Wang, Y., Xue, P., Cao, M., Yu, T., Lane, S., & Zhao, H. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00260 · Cited by 745
Principles of Protein−Protein Interactions: What are the Preferred Ways For Proteins To Interact?
Keskin, O., Gursoy, A., Ma, B., & Nussinov, R. (2008) · Chemical Reviews · doi:10.1021/cr040409x · Cited by 697
Metadata
- Authors
- Dundas, J., Ouyang, Z., Tseng, J., Binkowski, A., Turpaz, Y., & Liang, J.
- Affiliations
- University of Illinois Chicago (US)
- Corresponding author
- Dundas, J.
- ORCID
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2006-07-01
- Volume
- 34
- Issue
- Web Server
- Pages
- W116-W118
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- PMC
- PMC1538779
- OpenAlex
- W2077776336
- Cited by
- 1,725
- References
- 8
- Citations by year
- 2026: 25 · 2025: 45 · 2024: 59 · 2023: 48 · 2022: 58 · 2021: 67 · 2020: 70 · 2019: 100 · 2018: 133 · 2017: 115 · 2016: 143 · 2015: 142 · 2014: 143 · 2013: 115 · 2012: 128
- FWCI
- 16.74
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- other-oa
- Locations
- Nucleic Acids Research (publishedVersion, other-oa)
- PubMed (publishedVersion)
- Funders
- National Science Foundation (CAREER, 0133856)
- Office of Naval Research (N00014-06-1-0100, N00014)
- National Institute of General Medical Sciences (R01GM068958, GM 68958)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Drug Discovery › Computational Drug Discovery Methods
- Keywords
- surface voids, protein cavities, OMIM, Swiss-Prot, sequence mapping, web server, protein structure
- MeSH terms
- Amino Acids, Computer Graphics, Protein Conformation, Proteins, Software, Sequence Alignment, Internet, Sequence Analysis, Protein, Polymorphism, Single Nucleotide, Databases, Protein
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