메뉴 건너뛰기




Volumn 107, Issue 2, 2004, Pages 197-211

A fast and accurate procedure to collect and analyze unfolding fluorescence signal: The case of dystroglycan domains

Author keywords

Dystroglycan; Fluorescence; Immunoglobulins; Protein unfolding; Proteins

Indexed keywords

CELL ADHESION MOLECULE; DYSTROGLYCAN; IMMUNOGLOBULIN;

EID: 1242293695     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2003.09.005     Document Type: Article
Times cited : (30)

References (33)
  • 1
    • 0023643422 scopus 로고
    • Genetic and structural analysis of the protein stability problem
    • Matthews B. Genetic and structural analysis of the protein stability problem. Biochemistry. 26:1987;6885-6888.
    • (1987) Biochemistry , vol.26 , pp. 6885-6888
    • Matthews, B.1
  • 2
    • 0037686252 scopus 로고    scopus 로고
    • The present view of the mechanism of protein folding
    • Daggett V., Fersht A. The present view of the mechanism of protein folding. Nat. Rev. Mol. Cell Biol. 4:(6):2003;497-502.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , Issue.6 , pp. 497-502
    • Daggett, V.1    Fersht, A.2
  • 5
    • 0027275643 scopus 로고
    • A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
    • Ervasti J.M., Campbell K.P. A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin. J. Cell Biol. 122:1993;809-823.
    • (1993) J. Cell Biol. , vol.122 , pp. 809-823
    • Ervasti, J.M.1    Campbell, K.P.2
  • 6
    • 0038182574 scopus 로고    scopus 로고
    • Dystrophin-glycoprotein complex: Post-translational processing and dystroglycan function
    • Michele D.E., Campbell K.P. Dystrophin-glycoprotein complex: post-translational processing and dystroglycan function. J. Biol. Chem. 278:2003;15457-15460.
    • (2003) J. Biol. Chem. , vol.278 , pp. 15457-15460
    • Michele, D.E.1    Campbell, K.P.2
  • 7
    • 0036166823 scopus 로고    scopus 로고
    • Domain structure and organisation in extracellular matrix proteins
    • Hohenester E., Engel J. Domain structure and organisation in extracellular matrix proteins. Matrix Biol. 21:2002;115-128.
    • (2002) Matrix Biol. , vol.21 , pp. 115-128
    • Hohenester, E.1    Engel, J.2
  • 8
    • 0042734819 scopus 로고    scopus 로고
    • An adhesion molecule involved in muscular dystrophies: Structural and functional analysis of dystroglycan domains
    • Brancaccio A. An adhesion molecule involved in muscular dystrophies: structural and functional analysis of dystroglycan domains. Ital. J. Biochem. 52:2003;51-54.
    • (2003) Ital. J. Biochem. , vol.52 , pp. 51-54
    • Brancaccio, A.1
  • 9
    • 0033539929 scopus 로고    scopus 로고
    • Structural and functional analysis of the N-terminal extracellular region of β-dystroglycan
    • Di Stasio E., Sciandra F., Maras B., et al. Structural and functional analysis of the N-terminal extracellular region of β-dystroglycan. Biochem. Biophys. Res. Commun. 266:1999;274-278.
    • (1999) Biochem. Biophys. Res. Commun. , vol.266 , pp. 274-278
    • Di Stasio, E.1    Sciandra, F.2    Maras, B.3
  • 10
    • 0030916837 scopus 로고    scopus 로고
    • The N-terminal region of α-dystroglycan is an autonomous globular domain
    • Brancaccio A., Schulthess T., Gesemann M., Engel J. The N-terminal region of α-dystroglycan is an autonomous globular domain. Eur. J. Biochem. 246:1997;166-172.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 166-172
    • Brancaccio, A.1    Schulthess, T.2    Gesemann, M.3    Engel, J.4
  • 12
    • 0034624995 scopus 로고    scopus 로고
    • Identification of a binding site for quaternary amines in factor Xa
    • Monnaie D., Arosio D., Griffon N., Rose T., Rezaie A.R., Di Cera E. Identification of a binding site for quaternary amines in factor Xa. Biochemistry. 39:(18):2000;5349-5354.
    • (2000) Biochemistry , vol.39 , Issue.18 , pp. 5349-5354
    • Monnaie, D.1    Arosio, D.2    Griffon, N.3    Rose, T.4    Rezaie, A.R.5    Di Cera, E.6
  • 13
  • 14
    • 0032011350 scopus 로고    scopus 로고
    • The use of fluorescence methods to monitor unfolding transitions in proteins
    • Eftink M.R. The use of fluorescence methods to monitor unfolding transitions in proteins. Biochemistry (Mosc.). 63:(3):1998;276-284.
    • (1998) Biochemistry (Mosc.) , vol.63 , Issue.3 , pp. 276-284
    • Eftink, M.R.1
  • 15
    • 0025929570 scopus 로고
    • Fluorescence techniques for studying protein structure
    • Eftink M.R. Fluorescence techniques for studying protein structure. Method. Biochem. Anal. 35:1991;127-205.
    • (1991) Method. Biochem. Anal. , vol.35 , pp. 127-205
    • Eftink, M.R.1
  • 17
    • 0030971246 scopus 로고    scopus 로고
    • Fluorescence methods for studying kinetics of protein-folding reactions
    • Eftink M.R., Shastry M.C. Fluorescence methods for studying kinetics of protein-folding reactions. Method. Enzymol. 278:1997;258-286.
    • (1997) Method. Enzymol. , vol.278 , pp. 258-286
    • Eftink, M.R.1    Shastry, M.C.2
  • 18
    • 0030956737 scopus 로고    scopus 로고
    • Fluorescence methods for studying equilibrium macromolecule-ligand interactions
    • Eftink M.R. Fluorescence methods for studying equilibrium macromolecule-ligand interactions. Method. Enzymol. 278:1997;221-257.
    • (1997) Method. Enzymol. , vol.278 , pp. 221-257
    • Eftink, M.R.1
  • 19
    • 0017616818 scopus 로고
    • Fluorescence of proteins in aqueous neutral salt solutions. I. Influence of anions
    • Altekar W. Fluorescence of proteins in aqueous neutral salt solutions. I. Influence of anions. Biopolymers. 16:1977;341-368.
    • (1977) Biopolymers , vol.16 , pp. 341-368
    • Altekar, W.1
  • 20
    • 0027958069 scopus 로고
    • The use of fluorescence methods to monitor unfolding transitions in proteins
    • Eftink M.R. The use of fluorescence methods to monitor unfolding transitions in proteins. Biophys. J. 66:1994;482-501.
    • (1994) Biophys. J. , vol.66 , pp. 482-501
    • Eftink, M.R.1
  • 21
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace C.N. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Method. Enzymol. 131:1986;266-280.
    • (1986) Method. Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 22
    • 0023068366 scopus 로고
    • The thermodynamic stability of proteins
    • Schellman J.A. The thermodynamic stability of proteins. Annu. Rev. Biophys. Chem. 16:1987;115-137.
    • (1987) Annu. Rev. Biophys. Chem. , vol.16 , pp. 115-137
    • Schellman, J.A.1
  • 24
    • 0035831251 scopus 로고    scopus 로고
    • Plasticity of secondary structure in the N-terminal region of beta-dystroglycan
    • Boffi A., Bozzi M., Sciandra F., et al. Plasticity of secondary structure in the N-terminal region of beta-dystroglycan. Biochim. Biophys. Acta. 1546:(1):2001;114-121.
    • (2001) Biochim. Biophys. Acta , vol.1546 , Issue.1 , pp. 114-121
    • Boffi, A.1    Bozzi, M.2    Sciandra, F.3
  • 25
    • 0027141463 scopus 로고
    • A model for multiexponential tryptophan fluorescence intensity decay in proteins
    • Bajzer Z., Prendergast F.G. A model for multiexponential tryptophan fluorescence intensity decay in proteins. Biophys. J. 65:(6):1993;2313-2323.
    • (1993) Biophys. J. , vol.65 , Issue.6 , pp. 2313-2323
    • Bajzer, Z.1    Prendergast, F.G.2
  • 26
    • 0030999858 scopus 로고    scopus 로고
    • Molecular mechanics analysis of Tet repressor TRP-43 fluorescence
    • Silvi Antonini P., Hillen W., Ettner N., et al. Molecular mechanics analysis of Tet repressor TRP-43 fluorescence. Biophys. J. 72:(4):1997;1800- 1811.
    • (1997) Biophys. J. , vol.72 , Issue.4 , pp. 1800-1811
    • Silvi Antonini, P.1    Hillen, W.2    Ettner, N.3
  • 27
    • 0020187001 scopus 로고
    • Denaturation by guanidine hydrochloride of the Fc(t) and pFc' fragments of human immunoglobulin G
    • Sumi A., Hamaguchi K. Denaturation by guanidine hydrochloride of the Fc(t) and pFc' fragments of human immunoglobulin G. J. Biochem. (Tokyo). 92:(3):1982;823-833.
    • (1982) J. Biochem. (Tokyo) , vol.92 , Issue.3 , pp. 823-833
    • Sumi, A.1    Hamaguchi, K.2
  • 28
    • 0035252649 scopus 로고    scopus 로고
    • The complexities of dystroglycan
    • Winder S.J. The complexities of dystroglycan. Trends Biochem. Sci. 26:2001;118-124.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 118-124
    • Winder, S.J.1
  • 29
    • 0035933537 scopus 로고    scopus 로고
    • A synthetic peptide corresponding to the 550-585 region of α-dystroglycan binds β-dystroglycan as revealed by NMR spectroscopy
    • Bozzi M., Veglia G., Paci M., Sciandra F., Giardina B., Brancaccio A. A synthetic peptide corresponding to the 550-585 region of α-dystroglycan binds β-dystroglycan as revealed by NMR spectroscopy. FEBS Lett. 499:2001;210-214.
    • (2001) FEBS Lett. , vol.499 , pp. 210-214
    • Bozzi, M.1    Veglia, G.2    Paci, M.3    Sciandra, F.4    Giardina, B.5    Brancaccio, A.6
  • 30
    • 0035889080 scopus 로고    scopus 로고
    • Molecular analysis of the interaction of LCMV with its cellular receptor α-dystroglycan
    • Kunz S., Sevilla N., McGavern D.B., Campbell K.P., Oldstone M.B. Molecular analysis of the interaction of LCMV with its cellular receptor α-dystroglycan. J. Cell Biol. 155:2001;301-310.
    • (2001) J. Cell Biol. , vol.155 , pp. 301-310
    • Kunz, S.1    Sevilla, N.2    McGavern, D.B.3    Campbell, K.P.4    Oldstone, M.B.5
  • 31
    • 0031697295 scopus 로고    scopus 로고
    • Sequence analysis suggests the presence of an IG-like domain in the N-terminal region of α-dystroglycan which was crystallized after mutation of a protease susceptible site (Arg168(His)
    • Bozic D., Engel J., Brancaccio A. Sequence analysis suggests the presence of an IG-like domain in the N-terminal region of α-dystroglycan which was crystallized after mutation of a protease susceptible site (Arg168(His). Matrix Biol. 17:1998;495-500.
    • (1998) Matrix Biol. , vol.17 , pp. 495-500
    • Bozic, D.1    Engel, J.2    Brancaccio, A.3
  • 32
    • 0028172534 scopus 로고
    • The immunoglobulin fold. Structural classification sequence patterns and common core
    • Bork P., Holm L., Sander C. The immunoglobulin fold. Structural classification sequence patterns and common core. J. Mol. Biol. 242:1994;309-320.
    • (1994) J. Mol. Biol. , vol.242 , pp. 309-320
    • Bork, P.1    Holm, L.2    Sander, C.3
  • 33
    • 0036126711 scopus 로고    scopus 로고
    • Cadherin-like domains in α-dystroglycan, α/ ε-sarcoglycan and yeast and bacterial proteins
    • Dickens N.J., Beatson S., Ponting C.P. Cadherin-like domains in α-dystroglycan, α/ε-sarcoglycan and yeast and bacterial proteins. Curr. Biol. 12:2002;197-199.
    • (2002) Curr. Biol. , vol.12 , pp. 197-199
    • Dickens, N.J.1    Beatson, S.2    Ponting, C.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.