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Volumn 325, Issue 3, 2004, Pages 707-710

Trimethylamine-N-oxide modulates the reductive unfolding of onconase

Author keywords

Free energy; Onconase; Osmolyte; Reductive unfolding; TMAO

Indexed keywords

RANPIRNASE; TRIMETHYLAMINE OXIDE;

EID: 8444249624     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.10.088     Document Type: Article
Times cited : (12)

References (20)
  • 1
    • 0030762556 scopus 로고    scopus 로고
    • A naturally occurring protective system in urea-rich cells: Mechanism of osmolyte protection of proteins against urea denaturation
    • A. Wang, and D.W. Bolen A naturally occurring protective system in urea-rich cells: mechanism of osmolyte protection of proteins against urea denaturation Biochemistry 36 1997 9101 9108
    • (1997) Biochemistry , vol.36 , pp. 9101-9108
    • Wang, A.1    Bolen, D.W.2
  • 2
    • 0032570873 scopus 로고    scopus 로고
    • Forcing thermodynamically unfolded proteins to fold
    • I. Baskakov, and D.W. Bolen Forcing thermodynamically unfolded proteins to fold J. Biol. Chem. 273 1998 4831 4834
    • (1998) J. Biol. Chem. , vol.273 , pp. 4831-4834
    • Baskakov, I.1    Bolen, D.W.2
  • 3
    • 0032755251 scopus 로고    scopus 로고
    • Manipulating the amyloid-β aggregation pathway with chemical chaperones
    • D.S. Yang, C.M. Yip, T.H. Huang, A. Chakrabartty, and P.E. Fraser Manipulating the amyloid-β aggregation pathway with chemical chaperones J. Biol. Chem. 274 1999 32970 32974
    • (1999) J. Biol. Chem. , vol.274 , pp. 32970-32974
    • Yang, D.S.1    Yip, C.M.2    Huang, T.H.3    Chakrabartty, A.4    Fraser, P.E.5
  • 4
    • 0034622669 scopus 로고    scopus 로고
    • 1H NMR studies of the effect of the counteracting osmolyte trimethylamine-N-oxide on interactions of urea with ribonuclease a
    • 1H NMR studies of the effect of the counteracting osmolyte trimethylamine-N-oxide on interactions of urea with ribonuclease A J. Biol. Chem. 275 2000 27708 27711
    • (2000) J. Biol. Chem. , vol.275 , pp. 27708-27711
    • Palmer, H.R.1    Bedford, J.J.2    Leader, J.P.3    Smith, R.A.4
  • 5
    • 0035976814 scopus 로고    scopus 로고
    • Trimethylamine-N-oxide-induced folding of α-synuclein
    • V.N. Uversky, J. Li, and A.L. Fink Trimethylamine-N-oxide-induced folding of α-synuclein FEBS Lett. 509 2001 31 35
    • (2001) FEBS Lett. , vol.509 , pp. 31-35
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 6
    • 0035824871 scopus 로고    scopus 로고
    • Crowding and hydration effects on protein conformation: A study with sol-gel encapsulated proteins
    • D.K. Eggers, and J.S. Valentine Crowding and hydration effects on protein conformation: a study with sol-gel encapsulated proteins J. Mol. Biol. 314 2001 911 922
    • (2001) J. Mol. Biol. , vol.314 , pp. 911-922
    • Eggers, D.K.1    Valentine, J.S.2
  • 7
    • 0035800731 scopus 로고    scopus 로고
    • Osmolytes stabilize ribonuclease S by stabilizing its fragments S protein and S peptide to compact folding-competent states
    • G.S. Ratnaparkhi, and R. Varadarajan Osmolytes stabilize ribonuclease S by stabilizing its fragments S protein and S peptide to compact folding-competent states J. Biol. Chem. 276 2001 28789 28798
    • (2001) J. Biol. Chem. , vol.276 , pp. 28789-28798
    • Ratnaparkhi, G.S.1    Varadarajan, R.2
  • 8
    • 0036076894 scopus 로고    scopus 로고
    • Osmolyte effects on helix formation in peptides and the stability of coiled-coils
    • S.A. Celinski, and J.M. Scholtz Osmolyte effects on helix formation in peptides and the stability of coiled-coils Protein Sci. 11 2002 2048 2051
    • (2002) Protein Sci. , vol.11 , pp. 2048-2051
    • Celinski, S.A.1    Scholtz, J.M.2
  • 9
    • 0036848921 scopus 로고    scopus 로고
    • Unusual organic osmolytes in deep-sea animals: Adaptations to hydrostatic pressure and other perturbants
    • P.H. Yancey, W.R. Blake, and J. Conley Unusual organic osmolytes in deep-sea animals: adaptations to hydrostatic pressure and other perturbants J. Comp. Biochem. Physiol. Part A 133 2002 667 676
    • (2002) J. Comp. Biochem. Physiol. Part a , vol.133 , pp. 667-676
    • Yancey, P.H.1    Blake, W.R.2    Conley, J.3
  • 10
    • 0037138672 scopus 로고    scopus 로고
    • The molecular mechanism of stabilization of proteins by TMAO and its ability to counteract the effects of urea
    • Q. Zou, B.J. Bennion, V. Daggett, and K.P. Murphy The molecular mechanism of stabilization of proteins by TMAO and its ability to counteract the effects of urea J. Am. Chem. Soc. 124 2002 1192 1202
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 1192-1202
    • Zou, Q.1    Bennion, B.J.2    Daggett, V.3    Murphy, K.P.4
  • 11
    • 0038290339 scopus 로고    scopus 로고
    • Hydrogen exchange kinetics of RNase a and the urea: TMAO paradigm
    • Y. Qu, and D.W. Bolen Hydrogen exchange kinetics of RNase A and the urea: TMAO paradigm Biochemistry 42 2003 5837 5849
    • (2003) Biochemistry , vol.42 , pp. 5837-5849
    • Qu, Y.1    Bolen, D.W.2
  • 12
    • 2342614722 scopus 로고    scopus 로고
    • Counteraction of urea-induced protein denaturation by trimethylamine-N-oxide: A chemical chaperone at atomic resolution
    • B.J. Bennion, and V. Daggett Counteraction of urea-induced protein denaturation by trimethylamine-N-oxide: a chemical chaperone at atomic resolution Proc. Natl. Acad. Sci. USA 101 2004 6433 6438
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 6433-6438
    • Bennion, B.J.1    Daggett, V.2
  • 13
    • 0842304735 scopus 로고    scopus 로고
    • Additive transfer free energies of the peptide backbone unit that are independent of the model compound and the choice of concentration scale
    • M. Auton, and D.W. Bolen Additive transfer free energies of the peptide backbone unit that are independent of the model compound and the choice of concentration scale Biochemistry 43 2004 1329 1342
    • (2004) Biochemistry , vol.43 , pp. 1329-1342
    • Auton, M.1    Bolen, D.W.2
  • 14
    • 4644261149 scopus 로고    scopus 로고
    • Osmolytes induce structure in an early intermediate on the folding pathway of barstar
    • L. Pradeep, and J.B. Udgaonkar Osmolytes induce structure in an early intermediate on the folding pathway of barstar J. Biol. Chem. 279 2004 40303 40313
    • (2004) J. Biol. Chem. , vol.279 , pp. 40303-40313
    • Pradeep, L.1    Udgaonkar, J.B.2
  • 15
    • 0028266432 scopus 로고
    • Refined 1.7 Å X-ray crystallographic structure of P-30 protein, an amphibian ribonuclease with anti-tumor activity
    • S.C. Mosimann, W. Ardelt, and M.N. James Refined 1.7 Å X-ray crystallographic structure of P-30 protein, an amphibian ribonuclease with anti-tumor activity J. Mol. Biol. 236 1994 1141 1153
    • (1994) J. Mol. Biol. , vol.236 , pp. 1141-1153
    • Mosimann, S.C.1    Ardelt, W.2    James, M.N.3
  • 17
    • 1542428864 scopus 로고    scopus 로고
    • Characterization of the fast-forming intermediate, des [30-75], in the reductive unfolding of onconase
    • G. Xu, M. Narayan, E. Welker, and H.A. Scheraga Characterization of the fast-forming intermediate, des [30-75], in the reductive unfolding of onconase Biochemistry 43 2004 3246 3254
    • (2004) Biochemistry , vol.43 , pp. 3246-3254
    • Xu, G.1    Narayan, M.2    Welker, E.3    Scheraga, H.A.4
  • 19
    • 0026781216 scopus 로고
    • Equilibrium and kinetic constants for the thiol-disulfide interchange reaction between glutathione and dithiothreitol
    • D.M. Rothwarf, and H.A. Scheraga Equilibrium and kinetic constants for the thiol-disulfide interchange reaction between glutathione and dithiothreitol Proc. Natl. Acad. Sci. USA 89 1992 7944 7948
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7944-7948
    • Rothwarf, D.M.1    Scheraga, H.A.2
  • 20
    • 14044270712 scopus 로고    scopus 로고
    • Impact of an easily reducible disulfide bond on the oxidative folding rate of multi-disulfide-containing proteins
    • (in press)
    • H.J. Leung, G. Xu, M. Narayan, H.A. Scheraga, Impact of an easily reducible disulfide bond on the oxidative folding rate of multi-disulfide- containing proteins, J. Pep. Res. (in press)
    • J. Pep. Res.
    • Leung, H.J.1    Xu, G.2    Narayan, M.3    Scheraga, H.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.