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Volumn 49, Issue 34, 2010, Pages 7239-7241

Do prokaryotes have more kinetically stable proteins than eukaryotic organisms?

Author keywords

[No Author keywords available]

Indexed keywords

EUKARYOTIC ORGANISMS; KINETIC STABILITY; SODIUM DODECYL SULFATE-POLYACRYLAMIDE GEL ELECTROPHORESIS;

EID: 77956013449     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi1010877     Document Type: Article
Times cited : (11)

References (9)
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    • Baker, D. and Agard, D. A. (1994) Kinetics versus thermodynamics in protein folding Biochemistry 33, 7505-7509
    • (1994) Biochemistry , vol.33 , pp. 7505-7509
    • Baker, D.1    Agard, D.A.2
  • 2
    • 77951977004 scopus 로고    scopus 로고
    • Protein kinetic stability
    • Sanchez-Ruiz, J. M. (2010) Protein kinetic stability Biophys. Chem. 148, 1-15
    • (2010) Biophys. Chem. , vol.148 , pp. 1-15
    • Sanchez-Ruiz, J.M.1
  • 4
    • 0034237295 scopus 로고    scopus 로고
    • Lower kinetic limit to protein thermal stability: A proposal regarding protein stability in vivo and its relation with misfolding diseases
    • Plaza del Pino, I. M., Ibarra-Molero, B., and Sanchez-Ruiz, J. M. (2000) Lower kinetic limit to protein thermal stability: A proposal regarding protein stability in vivo and its relation with misfolding diseases Proteins 40, 58-70
    • (2000) Proteins , vol.40 , pp. 58-70
    • Plaza Del Pino, I.M.1    Ibarra-Molero, B.2    Sanchez-Ruiz, J.M.3
  • 5
    • 0037058942 scopus 로고    scopus 로고
    • Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity
    • Hammarstrom, P., Jiang, X., Hurshman, A. R., Powers, E. T., and Kelly, J. W. (2002) Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity Proc. Natl. Acad. Sci. U.S.A. 99, 16427-16432
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 16427-16432
    • Hammarstrom, P.1    Jiang, X.2    Hurshman, A.R.3    Powers, E.T.4    Kelly, J.W.5
  • 6
    • 4444330121 scopus 로고    scopus 로고
    • Structural basis of protein kinetic stability: Resistance to sodium dodecyl sulfate suggests a central role for rigidity and a bias toward α-sheet structure
    • Manning, M. and Colon, W. (2004) Structural basis of protein kinetic stability: Resistance to sodium dodecyl sulfate suggests a central role for rigidity and a bias toward α-sheet structure Biochemistry 43, 11248-11254
    • (2004) Biochemistry , vol.43 , pp. 11248-11254
    • Manning, M.1    Colon, W.2
  • 7
    • 36849036714 scopus 로고    scopus 로고
    • Identifying the subproteome of kinetically stable proteins via diagonal 2D SDS/PAGE
    • Xia, K., Manning, M., Hesham, H., Lin, Q., Bystroff, C., and Colon, W. (2007) Identifying the subproteome of kinetically stable proteins via diagonal 2D SDS/PAGE Proc. Natl. Acad. Sci. U.S.A. 104, 17329-17334
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 17329-17334
    • Xia, K.1    Manning, M.2    Hesham, H.3    Lin, Q.4    Bystroff, C.5    Colon, W.6
  • 8
    • 11144256229 scopus 로고    scopus 로고
    • Kinetic stability of Cu/Zn superoxide dismutase is dependent on its metal ligands: Implications for ALS
    • Lynch, S. M., Boswell, S. A., and Colon, W. (2004) Kinetic stability of Cu/Zn superoxide dismutase is dependent on its metal ligands: Implications for ALS Biochemistry 43, 16525-16531
    • (2004) Biochemistry , vol.43 , pp. 16525-16531
    • Lynch, S.M.1    Boswell, S.A.2    Colon, W.3
  • 9
    • 58749085415 scopus 로고    scopus 로고
    • Rescuing proteins of low kinetic stability by chaperones and natural ligands phenylketonuria, a case study
    • Martinez, A., Calvo, A. C., Teigen, K., and Pey, A. L. (2008) Rescuing proteins of low kinetic stability by chaperones and natural ligands phenylketonuria, a case study Prog. Mol. Biol. Transl. Sci. 83, 89-134
    • (2008) Prog. Mol. Biol. Transl. Sci. , vol.83 , pp. 89-134
    • Martinez, A.1    Calvo, A.C.2    Teigen, K.3    Pey, A.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.