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Volumn 3, Issue 1, 2004, Pages 21-29

A probabilistic method to correlate ion pairs with protein thermostability

Author keywords

Bayesian; Ion pairs; Protein thermostability

Indexed keywords

PROTEIN;

EID: 23844544684     PISSN: 11755636     EISSN: 11755636     Source Type: Journal    
DOI: 10.2165/00822942-200403010-00004     Document Type: Article
Times cited : (6)

References (25)
  • 3
    • 0242559061 scopus 로고    scopus 로고
    • Oxidizing enzymes as biocatalysts
    • Burton SG. 2003. Oxidizing enzymes as biocatalysts. Trends Biotechnol, 21:543-9.
    • (2003) Trends Biotechnol , vol.21 , pp. 543-549
    • Burton, S.G.1
  • 4
    • 0024620503 scopus 로고
    • Current research directions in the development of expert systems based on belief networks
    • Cooper G. 1989. Current research directions in the development of expert systems based on belief networks. Appl Stochastic Model Data Anal, 5:39-52.
    • (1989) Appl Stochastic Model Data Anal , vol.5 , pp. 39-52
    • Cooper, G.1
  • 5
    • 0033563515 scopus 로고    scopus 로고
    • A Bayesian statistical algorithm for RNA secondary structure prediction
    • Ding Y, Lawrence CE. 1999. A Bayesian statistical algorithm for RNA secondary structure prediction. Comput Chem, 23:387-400.
    • (1999) Comput Chem , vol.23 , pp. 387-400
    • Ding, Y.1    Lawrence, C.E.2
  • 6
    • 0017483653 scopus 로고
    • Clinical biostatistics. XXXIX. The haze of Bayes, the aerial palaces of decision analysis, and the computerized Ouija board
    • Feinstein AR. 1977. Clinical biostatistics. XXXIX. The haze of Bayes, the aerial palaces of decision analysis, and the computerized Ouija board. Clin Pharmacol Ther, 21:482-96.
    • (1977) Clin Pharmacol Ther , vol.21 , pp. 482-496
    • Feinstein, A.R.1
  • 8
    • 0642371854 scopus 로고    scopus 로고
    • Heat processing of barley and enzyme supplementation of diets for broilers
    • Gracia MI, Latorre MA, Garcia M et al. 2003. Heat processing of barley and enzyme supplementation of diets for broilers. Poult Sci, 82:1281-91.
    • (2003) Poult Sci , vol.82 , pp. 1281-1291
    • Gracia, M.I.1    Latorre, M.A.2    Garcia, M.3
  • 9
    • 0032715527 scopus 로고    scopus 로고
    • Important amino acid properties for enhanced thermostability from mesophilic to thermophilic proteins
    • Gromiha MM, Oobatake M, Sarai A. 1999. Important amino acid properties for enhanced thermostability from mesophilic to thermophilic proteins. Biophys Chem, 82:51-67.
    • (1999) Biophys Chem , vol.82 , pp. 51-67
    • Gromiha, M.M.1    Oobatake, M.2    Sarai, A.3
  • 10
    • 0036084144 scopus 로고    scopus 로고
    • ProTherm, thermodynamic database for proteins and mutants: Developments in version 3.0
    • Gromiha MM, Uedaira H, An J et al. 2002. ProTherm, thermodynamic database for proteins and mutants: developments in version 3.0. Nucleic Acids Res, 30:301-2.
    • (2002) Nucleic Acids Res , vol.30 , pp. 301-302
    • Gromiha, M.M.1    Uedaira, H.2    An, J.3
  • 11
    • 0035224502 scopus 로고    scopus 로고
    • Disambiguating proteins, genes, and RNA in text: A machine learning approach
    • Hatzivassiloglou V, Duboue PA, Rzhetsky A. 2001. Disambiguating proteins, genes, and RNA in text: a machine learning approach. Bioinformatics, 17(Suppl 1):S97-106.
    • (2001) Bioinformatics , vol.17 , Issue.1 SUPPL.
    • Hatzivassiloglou, V.1    Duboue, P.A.2    Rzhetsky, A.3
  • 12
    • 0027580356 scopus 로고
    • Very simple classification rules perform well on most commonly used dataset
    • Holte RC. 1993. Very simple classification rules perform well on most commonly used dataset. Machine Learn, 3:63-91.
    • (1993) Machine Learn , vol.3 , pp. 63-91
    • Holte, R.C.1
  • 13
    • 1042263811 scopus 로고    scopus 로고
    • PGTdb: A database providing growth temperatures of prokaryotes
    • Huang SL, Wu LC, Liang HK et al. 2004. PGTdb: a database providing growth temperatures of prokaryotes. Bioinfomatics, 20:276-8.
    • (2004) Bioinfomatics , vol.20 , pp. 276-278
    • Huang, S.L.1    Wu, L.C.2    Liang, H.K.3
  • 14
    • 0142052944 scopus 로고    scopus 로고
    • A Bayesian networks approach for predicting protein-protein interactions from genomic data
    • Jansen R, Yu H, Greenbaum D et al. 2003. A Bayesian networks approach for predicting protein-protein interactions from genomic data. Science, 302:449-53.
    • (2003) Science , vol.302 , pp. 449-453
    • Jansen, R.1    Yu, H.2    Greenbaum, D.3
  • 16
    • 0033550299 scopus 로고    scopus 로고
    • Salt bridge stability in monomeric proteins
    • Kumar S, Nussinov R. 1999. Salt bridge stability in monomeric proteins. J Mol Biol, 293:1241-55.
    • (1999) J Mol Biol , vol.293 , pp. 1241-1255
    • Kumar, S.1    Nussinov, R.2
  • 17
    • 0033523004 scopus 로고    scopus 로고
    • Engineering activity and stability of Thermotoga maritima glutamate dehydrogenase. II: Construction of a 16-residue ion-pair network at the subunit interface
    • Lebbink JH, Knapp S, van der Oost J et al. 1999. Engineering activity and stability of Thermotoga maritima glutamate dehydrogenase. II: Construction of a 16-residue ion-pair network at the subunit interface. J Mol Biol, 289:357-69.
    • (1999) J Mol Biol , vol.289 , pp. 357-369
    • Lebbink, J.H.1    Knapp, S.2    Van Der Oost, J.3
  • 18
    • 0004155427 scopus 로고
    • New York: WH Freeman Pr.
    • Lubert S. 1995. Biochemistry. New York: WH Freeman Pr.
    • (1995) Biochemistry
    • Lubert, S.1
  • 22
    • 0039116206 scopus 로고    scopus 로고
    • Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: Results of a comprehensive survey
    • Szilagyi A, Zavodszky P. 2000. Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: results of a comprehensive survey. Struct Fold Des, 8:493-504.
    • (2000) Struct Fold des , vol.8 , pp. 493-504
    • Szilagyi, A.1    Zavodszky, P.2
  • 23
    • 0031580199 scopus 로고    scopus 로고
    • Protein thermal stability, hydrogen bonds, and ion pairs
    • Vogt G, Woell S, Argos P. 1997. Protein thermal stability, hydrogen bonds, and ion pairs. J Mol Biol, 269:631-43.
    • (1997) J Mol Biol , vol.269 , pp. 631-643
    • Vogt, G.1    Woell, S.2    Argos, P.3
  • 24
    • 0037014664 scopus 로고    scopus 로고
    • Temperature-induced selective death of the C-domain within angiotensin-converting enzyme molecule
    • Voronov S, Zueva N, Orlov V et al. 2002. Temperature-induced selective death of the C-domain within angiotensin-converting enzyme molecule. FEBS Lett, 522:77-82.
    • (2002) FEBS Lett , vol.522 , pp. 77-82
    • Voronov, S.1    Zueva, N.2    Orlov, V.3
  • 25
    • 0031874740 scopus 로고    scopus 로고
    • Bayesian adaptive sequence alignment algorithms
    • Zhu J, Liu JS, Lawrence CE. 1998. Bayesian adaptive sequence alignment algorithms. Bioinformatics, 14:25-39.
    • (1998) Bioinformatics , vol.14 , pp. 25-39
    • Zhu, J.1    Liu, J.S.2    Lawrence, C.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.