메뉴 건너뛰기




Volumn 15, Issue 1, 2008, Pages 29-39

Biochemical and aggregation analysis of Bence Jones proteins from different light chain diseases

Author keywords

Aggregates; Amyloid; Circular dichroism; Electron microscopy; Fibrils; Light chain amyloidosis; Light chain deposition disease; Multiple myeloma

Indexed keywords

BENCE JONES PROTEIN; IMMUNOGLOBULIN LIGHT CHAIN;

EID: 39049154947     PISSN: 13506129     EISSN: 17442818     Source Type: Journal    
DOI: 10.1080/13506120701815324     Document Type: Article
Times cited : (38)

References (29)
  • 1
    • 0033557435 scopus 로고    scopus 로고
    • The structure of an entire noncovalent immunoglobulin kappa light-chain dimer (Bence-Jones protein) reveals a weak and unusual constant domains association
    • Roussel A, Spinelli S, Deret S, Navaza J, Aucouturier P, Cambillau C. The structure of an entire noncovalent immunoglobulin kappa light-chain dimer (Bence-Jones protein) reveals a weak and unusual constant domains association. Eur J Biochem 1999;26:192-199.
    • (1999) Eur J Biochem , vol.26 , pp. 192-199
    • Roussel, A.1    Spinelli, S.2    Deret, S.3    Navaza, J.4    Aucouturier, P.5    Cambillau, C.6
  • 3
    • 0034059396 scopus 로고    scopus 로고
    • New therapeutic approaches in primary systemic AL amyloidosis
    • Sezer O, Eucker J, Schmid P, Possinger K. New therapeutic approaches in primary systemic AL amyloidosis. Ann Hematol 2000;79:1-6.
    • (2000) Ann Hematol , vol.79 , pp. 1-6
    • Sezer, O.1    Eucker, J.2    Schmid, P.3    Possinger, K.4
  • 5
    • 0030830020 scopus 로고    scopus 로고
    • Domain stability in immunoglobulin light chain deposition disorders
    • Wetzel R. Domain stability in immunoglobulin light chain deposition disorders. Adv Protein Chem 1997;50:183-242.
    • (1997) Adv Protein Chem , vol.50 , pp. 183-242
    • Wetzel, R.1
  • 6
    • 0038264427 scopus 로고    scopus 로고
    • Immunoglobulin light chain variable (V) region genes influence clinical presentation and outcome in light chain-associated amyloidosis (AL)
    • Abraham RS, Geyer SM, Price-Troska TL, Allmer C, Kyle RA, Gertz MA, Fonseca R. Immunoglobulin light chain variable (V) region genes influence clinical presentation and outcome in light chain-associated amyloidosis (AL). Blood 2003;101:3801-3803.
    • (2003) Blood , vol.101 , pp. 3801-3803
    • Abraham, R.S.1    Geyer, S.M.2    Price-Troska, T.L.3    Allmer, C.4    Kyle, R.A.5    Gertz, M.A.6    Fonseca, R.7
  • 7
    • 0000913572 scopus 로고    scopus 로고
    • Structural bases of light chain-related pathology
    • Zanetti M, Capra JD, editors, Harwood Academic Publishers;
    • Stevens FJ, Weiss DT, Solomon A. Structural bases of light chain-related pathology. In: Zanetti M, Capra JD, editors. The Antibodies, Vol. 5. Harwood Academic Publishers; 1999. pp 175-208.
    • (1999) The Antibodies , vol.5 , pp. 175-208
    • Stevens, F.J.1    Weiss, D.T.2    Solomon, A.3
  • 8
    • 0026585875 scopus 로고
    • Mechanisms of disease: Monoclonal immunoglobulin deposition. Amyloidosis, light chain deposition disease, and light and heavy chain deposition disease
    • Buxbaum J. Mechanisms of disease: monoclonal immunoglobulin deposition. Amyloidosis, light chain deposition disease, and light and heavy chain deposition disease. Hematol Oncol Clin North Am 1992;6:323-346.
    • (1992) Hematol Oncol Clin North Am , vol.6 , pp. 323-346
    • Buxbaum, J.1
  • 9
    • 0028305304 scopus 로고
    • A role for destabilizing amino acid replacements in light-chain amyloidosis
    • Hurle MR, Helms LR, Li L, Chan W, Wetzel R. A role for destabilizing amino acid replacements in light-chain amyloidosis. Proc Natl Acad Sci USA 1994;91:5446-5450.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 5446-5450
    • Hurle, M.R.1    Helms, L.R.2    Li, L.3    Chan, W.4    Wetzel, R.5
  • 11
    • 0002846347 scopus 로고    scopus 로고
    • Measuring the conformational stability of a protein
    • Creighton TE, editor, 2nd ed. New York: Oxford University Press;
    • Pace CN, Scholtz M. Measuring the conformational stability of a protein. In: Creighton TE, editor. Protein Structure A Practical Approach. 2nd ed. New York: Oxford University Press; 1997. pp 299-321.
    • (1997) Protein Structure A Practical Approach , pp. 299-321
    • Pace, C.N.1    Scholtz, M.2
  • 13
    • 0037369167 scopus 로고    scopus 로고
    • Mutations in the B1 domain of protein G that delay the onset of amyloid fibril formation in vitro
    • Ramirez-Alvarado M, Cocco MJ, Regan L. Mutations in the B1 domain of protein G that delay the onset of amyloid fibril formation in vitro. Protein Sci 2003;12:567-576.
    • (2003) Protein Sci , vol.12 , pp. 567-576
    • Ramirez-Alvarado, M.1    Cocco, M.J.2    Regan, L.3
  • 14
    • 0034255027 scopus 로고    scopus 로고
    • A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro
    • Ramirez-Alvarado M, Merkel JS, Regan L. A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro. Proc Natl Acad Sci USA 2000;97:8979-8984.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 8979-8984
    • Ramirez-Alvarado, M.1    Merkel, J.S.2    Regan, L.3
  • 15
    • 0030590876 scopus 로고    scopus 로고
    • Structural and functional characterization of three human immunoglobulin k light chains with different pathological implications
    • Bellotti V, Stoppini M, Mangione PP, Fornasieri A, Min AL, Merlini G, Ferri G. Structural and functional characterization of three human immunoglobulin k light chains with different pathological implications. Biochim Biophys Acta 1996;1317:161-167.
    • (1996) Biochim Biophys Acta , vol.1317 , pp. 161-167
    • Bellotti, V.1    Stoppini, M.2    Mangione, P.P.3    Fornasieri, A.4    Min, A.L.5    Merlini, G.6    Ferri, G.7
  • 16
    • 0345426278 scopus 로고    scopus 로고
    • Thermodynamic instability of human lambda 6 light chains: Correlation with fibrillogenicity
    • Wall J, Schell M, Murphy C, Hrncic R, Stevens FJ, Solomon A. Thermodynamic instability of human lambda 6 light chains: correlation with fibrillogenicity. Biochemistry 1999;38:14101-14108.
    • (1999) Biochemistry , vol.38 , pp. 14101-14108
    • Wall, J.1    Schell, M.2    Murphy, C.3    Hrncic, R.4    Stevens, F.J.5    Solomon, A.6
  • 18
    • 0024963570 scopus 로고
    • Conformational states of beta-lactamase: Molten-globule states at acidic and alkaline pH with high salt
    • Goto Y, Fink AL. Conformational states of beta-lactamase: molten-globule states at acidic and alkaline pH with high salt. Biochemistry 1989;28:945-952.
    • (1989) Biochemistry , vol.28 , pp. 945-952
    • Goto, Y.1    Fink, A.L.2
  • 20
    • 0001951590 scopus 로고    scopus 로고
    • 8-Anilinonaphthalene-1-Sulfonic Acid
    • Creighton TE, editor, New York: John Wiley and Sons;
    • Fink AL. 8-Anilinonaphthalene-1-Sulfonic Acid. In: Creighton TE, editor. The Encyclopedia of Molecular Biology. New York: John Wiley and Sons; 1999. pp 140-142.
    • (1999) The Encyclopedia of Molecular Biology , pp. 140-142
    • Fink, A.L.1
  • 21
    • 0036396520 scopus 로고    scopus 로고
    • Does the location of a mutation determine the ability to form amyloid fibrils?
    • Ramirez-Alvarado M, Regan L. Does the location of a mutation determine the ability to form amyloid fibrils? J Mol Biol 2002;323:17-22.
    • (2002) J Mol Biol , vol.323 , pp. 17-22
    • Ramirez-Alvarado, M.1    Regan, L.2
  • 22
    • 0003320620 scopus 로고    scopus 로고
    • Protein Fluorescence
    • 2nd ed. New York: Plenum Publishing Corporation;
    • Lakowicz JR. Protein Fluorescence. Principles of Fluorescence Spectroscopy, 2nd ed. New York: Plenum Publishing Corporation; 1999. pp 445-486.
    • (1999) Principles of Fluorescence Spectroscopy , pp. 445-486
    • Lakowicz, J.R.1
  • 23
    • 0036669903 scopus 로고    scopus 로고
    • Examining the structure of the mature amyloid fibril
    • Makin OS, Serpell LC. Examining the structure of the mature amyloid fibril. Biochem Soc Trans 2002;20:521-525.
    • (2002) Biochem Soc Trans , vol.20 , pp. 521-525
    • Makin, O.S.1    Serpell, L.C.2
  • 24
    • 0037066786 scopus 로고    scopus 로고
    • Effect of association state and conformational stability on the kinetics of immunoglobulin light chain amyloid fibril formation at physiological pH
    • Souillac PO, Uversky VN, Millett IS, Khurana R, Doniach S, Fink AL. Effect of association state and conformational stability on the kinetics of immunoglobulin light chain amyloid fibril formation at physiological pH. J Biol Chem 2002;277:12657-12665.
    • (2002) J Biol Chem , vol.277 , pp. 12657-12665
    • Souillac, P.O.1    Uversky, V.N.2    Millett, I.S.3    Khurana, R.4    Doniach, S.5    Fink, A.L.6
  • 25
    • 0037066715 scopus 로고    scopus 로고
    • Elucidation of the molecular mechanism during the early events in immunoglobulin light chain amyloid fibrillation. Evidence for an off- pathway oligomer at acidic pH
    • Souillac PO, Uversky VN, Millett IS, Khurana R, Doniach S, Fink AL. Elucidation of the molecular mechanism during the early events in immunoglobulin light chain amyloid fibrillation. Evidence for an off- pathway oligomer at acidic pH. J Biol Chem 2002;277:12666-12679.
    • (2002) J Biol Chem , vol.277 , pp. 12666-12679
    • Souillac, P.O.1    Uversky, V.N.2    Millett, I.S.3    Khurana, R.4    Doniach, S.5    Fink, A.L.6
  • 26
    • 0038047044 scopus 로고    scopus 로고
    • Structural transformations of oligomeric intermediates in the fibrillation of immunoglobulin light chain LEN
    • Souillac PO, Uversky VN, Fink AL. Structural transformations of oligomeric intermediates in the fibrillation of immunoglobulin light chain LEN. Biochemistry 2003;42:8094-8104.
    • (2003) Biochemistry , vol.42 , pp. 8094-8104
    • Souillac, P.O.1    Uversky, V.N.2    Fink, A.L.3
  • 27
    • 0344146434 scopus 로고    scopus 로고
    • Somatic mutations of the L12a Gene in V-k1 light chain deposition disease potential effects on aberrant protein conformation and deposition
    • Vidal R, Goni F, Stevens F, Aucouturier P, Kumar A, Frangione B, Ghiso J, Gallo G. Somatic mutations of the L12a Gene in V-k1 light chain deposition disease potential effects on aberrant protein conformation and deposition. Am J Pathol 1999;155:2009-2017.
    • (1999) Am J Pathol , vol.155 , pp. 2009-2017
    • Vidal, R.1    Goni, F.2    Stevens, F.3    Aucouturier, P.4    Kumar, A.5    Frangione, B.6    Ghiso, J.7    Gallo, G.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.