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Volumn 4, Issue , 2008, Pages 29-32

Pressure acceleration of proteolysis: A general mechanism

Author keywords

chymotrypsin; Pressure enhanced proteolysis; Shift of conformational equilibrium; Ubiquitin; Unfolded conformer

Indexed keywords


EID: 70350054629     PISSN: None     EISSN: 13492942     Source Type: Journal    
DOI: 10.2142/biophysics.4.29     Document Type: Article
Times cited : (22)

References (16)
  • 1
    • 0342325481 scopus 로고
    • Pressure inactivation of alphachymotrypsin
    • Taniguchi, Y. & Suzuki, K. Pressure inactivation of alphachymotrypsin. J. Phys. Chem. 87, 5185-5193 (1983).
    • (1983) J. Phys. Chem. , vol.87 , pp. 5185-5193
    • Taniguchi, Y.1    Suzuki, K.2
  • 2
    • 10144249599 scopus 로고    scopus 로고
    • Application of high hydrostatic pressure for increasing activity and stability of enzymes
    • Mozhaev, V. V., Lange, R., Kudryashova, E. V. & Balny, C. Application of high hydrostatic pressure for increasing activity and stability of enzymes. Biotechnol. Bioeng. 52, 320-331 (1996).
    • (1996) Biotechnol. Bioeng. , Issue.52 , pp. 320-331
    • Mozhaev, V.V.1    Lange, R.2    Kudryashova, E.V.3    Balny, C.4
  • 3
    • 0019484519 scopus 로고
    • The theory of pressure effects on enzymes
    • Morild, E. The theory of pressure effects on enzymes. Adv. Prot. Chem. 34, 93-166 (1981).
    • (1981) Adv. Prot. Chem. , vol.34 , pp. 93-166
    • Morild, E.1
  • 4
    • 0023644679 scopus 로고
    • Structure of ubiquitin refined at 1.8 Å resolution
    • Vijay-Kumar, S., Bugg, C. E. & Cook, W. J. Structure of ubiquitin refined at 1.8 Å resolution. J. Mol. Biol. 194, 531-544 (1987).
    • (1987) J. Mol. Biol. , vol.194 , pp. 531-544
    • Vijay-Kumar, S.1    Bugg, C.E.2    Cook, W.J.3
  • 5
    • 0023522385 scopus 로고
    • 1H NMR assignments and secondary structure identification of human ubiquitin
    • H NMR assignments and secondary structure identification of human ubiquitin. Biochemistry 26, 7282-7290 (1987).
    • (1987) Biochemistry , vol.26 , pp. 7282-7290
    • Weber, P.L.1    Brown, S.C.2    Mueller, L.3
  • 6
    • 0032528033 scopus 로고    scopus 로고
    • Validation of protein structure from anisotoropic carbonyl chemical shifts in dilute liquid crystalline phase
    • Cornilescu, G., Marquardt, J. L., Ottiger, M. & Bax, A. Validation of protein structure from anisotoropic carbonyl chemical shifts in dilute liquid crystalline phase. J. Am. Chem. Soc. 120, 6836-6837 (1998).
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 6836-6837
    • Cornilescu, G.1    Marquardt, J.L.2    Ottiger, M.3    Bax, A.4
  • 8
    • 37849000182 scopus 로고    scopus 로고
    • Basic folded and low-populated locally disordered conformers of SUMO-2 characterized by NMR spectroscopy at varying pressures
    • Kitahara, R., Zhao, C., Saito, K., Koshiba, S., Ioune, M., Kigawa, T., Yokoyama, S. & Akasaka, K. Basic folded and low-populated locally disordered conformers of SUMO-2 characterized by NMR spectroscopy at varying pressures. Biochemistry 47, 30-39 (2008).
    • (2008) Biochemistry , vol.47 , pp. 30-39
    • Kitahara, R.1    Zhao, C.2    Saito, K.3    Koshiba, S.4    Ioune, M.5    Kigawa, T.6    Yokoyama, S.7    Akasaka, K.8
  • 10
    • 0025784725 scopus 로고
    • Mechanisms of temporary inhibition in Streptomyces subtilisin inhibitor induced by an amino acid substitution, tryptophan 86 replaced by histidine
    • Tamura, A., Kanaori, K., Kojima, S., Kumagai, I., Miura, K. & Akasaka, K. Mechanisms of temporary inhibition in Streptomyces subtilisin inhibitor induced by an amino acid substitution, tryptophan 86 replaced by histidine. Biochemistry 30, 5275-5286 (1991).
    • (1991) Biochemistry , vol.30 , pp. 5275-5286
    • Tamura, A.1    Kanaori, K.2    Kojima, S.3    Kumagai, I.4    Miura, K.5    Akasaka, K.6
  • 11
    • 0037452877 scopus 로고    scopus 로고
    • Close identity of a pressurestabilized intermediate with a kinetic intermediate in protein folding
    • Kitahara, R. & Akasaka, K. Close identity of a pressurestabilized intermediate with a kinetic intermediate in protein folding. Proc. Nat. Acad. Sci. USA 100, 3167-3172 (2003).
    • (2003) Proc. Nat. Acad. Sci. USA , vol.100 , pp. 3167-3172
    • Kitahara, R.1    Akasaka, K.2
  • 12
    • 14644424521 scopus 로고    scopus 로고
    • NMR snapshots of a fluctuating protein structure. Ubiquitin at 30 bar-3 kbar
    • Kitahara, R., Yokoyama, S. & Akasaka, K. NMR snapshots of a fluctuating protein structure. Ubiquitin at 30 bar-3 kbar. J. Mol. Biol. 347, 277-285 (2005).
    • (2005) J. Mol. Biol. , vol.347 , pp. 277-285
    • Kitahara, R.1    Yokoyama, S.2    Akasaka, K.3
  • 14
    • 33646900712 scopus 로고    scopus 로고
    • Probing conformational fluctuation of proteins by pressure perturbation
    • Akasaka, K. Probing conformational fluctuation of proteins by pressure perturbation. Chem. Rev. 106, 1814-1835 (2006).
    • (2006) Chem. Rev. , vol.106 , pp. 1814-1835
    • Akasaka, K.1
  • 15
    • 3342936435 scopus 로고    scopus 로고
    • High-pressure NMR spectroscopy for characterizing folding intermediates and denatured states of proteins
    • Kamatari, Y. O., Kitahara, R., Yamada, H., Yokoyama, S. & Akasaka, K. High-pressure NMR spectroscopy for characterizing folding intermediates and denatured states of proteins. Methods 34, 133-143 (2004).
    • (2004) Methods , vol.34 , pp. 133-143
    • Kamatari, Y.O.1    Kitahara, R.2    Yamada, H.3    Yokoyama, S.4    Akasaka, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.