The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index.
ProTherm, version 4.0: thermodynamic database for proteins and mutants
Open accessAbstract
Release 4.0 of ProTherm, thermodynamic database for proteins and mutants, contains approximately 14,500 numerical data (approximately 450% of the first version) of several thermodynamic parameters along with experimental methods and conditions, and structural, functional and literature information. The sequence and structural information of proteins is connected with thermodynamic data through links between entries in Protein Data Bank, Protein Information Resource and SWISS-PROT and the data in ProTherm. We have separated the Gibbs free energy change obtained at extrapolated temperature from the data on denaturation temperature measured by the thermal denaturation method. We have added the statistics of amino acid replacements and links to homologous structures to each protein. Further, we have improved the search and display options to enhance search capability through the web interface. ProTherm is freely available at http://gibk26. bse.kyutech.ac.jp/jouhou/Protherm/protherm.html.
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Cites
Berman, H. M. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.1.235 · Cited by 40,196
The SWISS-PROT protein knowledgebase and its supplement TrEMBL in 2003
Boeckmann, B. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg095 · Cited by 3,890
The SWISS-PROT protein sequence data bank and its supplement TrEMBL
Bairoch, A., & Apweiler, R. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.1.31 · Cited by 3,587
The SWISS-PROT protein sequence data bank and its supplement TrEMBL in 1998
Bairoch, A. (1998) · Nucleic Acids Research · doi:10.1093/nar/26.1.38 · Cited by 3,280
Guerois, R., Nielsen, J. E., & Serrano, L. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00442-4 · Cited by 1,728
A simple physical model for binding energy hot spots in protein–protein complexes
Kortemme, T., & Baker, D. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.202485799 · Cited by 804
The Protein Information Resource
Wu, C. H. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg040 · Cited by 454
The Protein Information Resource (PIR)
Barker, W. C. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.1.41 · Cited by 208
ProTherm: Thermodynamic Database for Proteins and Mutants
Gromiha, M. M., An, J., Kono, H., Oobatake, M., Uedaira, H., & Sarai, A. (1999) · Nucleic Acids Research · doi:10.1093/nar/27.1.286 · Cited by 150
Relationship Between Amino Acid Properties and Protein Stability: Buried Mutations
Gromiha, M. M., Oobatake, M., Kono, H., Uedaira, H., & Sarai, A. (1999) · Journal of Protein Chemistry · doi:10.1023/a:1020603401001 · Cited by 78
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Bornscheuer, U. T., Huisman, G. W., Kazlauskas, R. J., Lutz, S., Moore, J. C., & Robins, K. (2012) · Nature · doi:10.1038/nature11117 · Cited by 2,628
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Capriotti, E., Fariselli, P., & Casadio, R. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki375 · Cited by 2,052
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Kumar, M. D. S. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkj103 · Cited by 411
Cell-wide analysis of protein thermal unfolding reveals determinants of thermostability
Leuenberger, P., Ganscha, S., Kahraman, A., Cappelletti, V., Boersema, P. J., von Mering, C., Claassen, M., & Picotti, P. (2017) · Science · doi:10.1126/science.aai7825 · Cited by 411
Metadata
- Authors
- Bava, K. A.
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2004-01-01
- Volume
- 32
- Issue
- 90001
- Pages
- 120D-121
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- OpenAlex
- W2916078022
- Cited by
- 367
- References
- 14
- FWCI
- 8.12
- Type
- journal article
- Language
- en
- Open access
- bronze
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