메뉴 건너뛰기




Volumn 3, Issue 2, 2009, Pages 255-259

Backbone and side-chain 1H, 13C and 15N resonance assignments of LEN, a human immunoglobulin κiV light-chain variable domain

Author keywords

Bence Jones protein; Immunoglobulin light chain; Light chain amyloidosis; NMR spectroscopy; Protein misfolding

Indexed keywords

IMMUNOGLOBULIN KAPPA CHAIN;

EID: 70449524329     PISSN: 18742718     EISSN: 1874270X     Source Type: Journal    
DOI: 10.1007/s12104-009-9188-y     Document Type: Article
Times cited : (3)

References (27)
  • 3
    • 0031627465 scopus 로고    scopus 로고
    • An efficient and cost-effective isotope labeling protocol for proteins expressed in Escherichia coli
    • 10.1023/A:1008222131470
    • ML Cai Y Huang K Sakaguchi GM Clore AM Gronenborn R Craigie 1998 An efficient and cost-effective isotope labeling protocol for proteins expressed in Escherichia coli J Biomol NMR 11 97 102 10.1023/A:1008222131470
    • (1998) J Biomol NMR , vol.11 , pp. 97-102
    • Cai, M.L.1    Huang, Y.2    Sakaguchi, K.3    Clore, G.M.4    Gronenborn, A.M.5    Craigie, R.6
  • 5
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • DOI 10.1146/annurev.biochem.75.101304.123901
    • F Chiti CM Dobson 2006 Protein misfolding, functional amyloid, and human disease Annu Rev Biochem 75 333 366 10.1146/annurev.biochem.75.101304.123901 (Pubitemid 44118036)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 6
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • 10.1007/BF00197809
    • F Delaglio S Grzesiek GW Vuister G Zhu J Pfeifer A Bax 1995 NMRPipe: a multidimensional spectral processing system based on UNIX pipes J Biomol NMR 6 277 293 10.1007/BF00197809
    • (1995) J Biomol NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 7
    • 0016804680 scopus 로고
    • The molecular structure of a dimer composed of the variable portions of the Bence-Jones protein REI refined at 2.0 Å resolution
    • O Epp EE Lattman M Schiffer R Huber R Palm 1975 The molecular structure of a dimer composed of the variable portions of the Bence-Jones protein REI refined at 2.0 Å resolution Biochemistry 14 494 3 4952
    • (1975) Biochemistry , vol.14 , Issue.494 , pp. 3-4952
    • Epp, O.1    Lattman, E.E.2    Schiffer, M.3    Huber, R.4    Palm, R.5
  • 10
    • 0004757060 scopus 로고
    • University of California, San Francisco
    • Goddard TD, Kneller DG (1993) SPARKY 3, University of California, San Francisco
    • (1993) SPARKY , vol.3
    • Goddard, T.D.1    Kneller, D.G.2
  • 12
    • 0028556362 scopus 로고
    • Comparison of two homologous proteins: Structural origin of altered domain interactions in immunoglobulin light-chain dimers
    • 10.1021/bi00253a024
    • DB Huang CH Chang C Ainsworth AT Brunger M Eulitz A Solomon FJ Stevens M Schiffer 1994 Comparison of two homologous proteins: structural origin of altered domain interactions in immunoglobulin light-chain dimers Biochemistry 33 14848 14857 10.1021/bi00253a024
    • (1994) Biochemistry , vol.33 , pp. 14848-14857
    • Huang, D.B.1    Chang, C.H.2    Ainsworth, C.3    Brunger, A.T.4    Eulitz, M.5    Solomon, A.6    Stevens, F.J.7    Schiffer, M.8
  • 13
    • 0031390641 scopus 로고    scopus 로고
    • Variable domain structure of κIV human light chain Len: High homology to the murine light chain McPC603
    • DOI 10.1016/S0161-5890(98)00002-9, PII S0161589098000029
    • DB Huang CH Chang C Ainsworth G Johnson A Solomon FJ Stevens M Schiffer 1997 Variable domain structure of κIV human light chain Len: high homology to the murine light chain McPC603 Mol Immunol 34 1291 1301 10.1016/S0161- 5890(98)00002-9 (Pubitemid 28293377)
    • (1997) Molecular Immunology , vol.34 , Issue.18 , pp. 1291-1301
    • Huang, D.-B.1    Chang, C.-H.2    Ainsworth, C.3    Johnson, G.4    Solomon, A.5    Stevens, F.J.6    Schiffer, M.7
  • 16
    • 0035957228 scopus 로고    scopus 로고
    • Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates
    • DOI 10.1021/bi001782b
    • R Khurana JR Gillespie A Talapatra LJ Minert C Ionescu-Zanetti I Millett AL Fink 2001 Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates Biochemistry 40 3525 3535 10.1021/bi001782b (Pubitemid 32242809)
    • (2001) Biochemistry , vol.40 , Issue.12 , pp. 3525-3535
    • Khurana, R.1    Gillespie, J.R.2    Talapatra, A.3    Minert, L.J.4    Ionescu-Zanetti, C.5    Millett, I.6    Fink, A.L.7
  • 18
    • 0028970456 scopus 로고
    • Primary systemic amyloidosis: Clinical and laboratory features in 474 cases
    • RA Kyle MA Gertz 1995 Primary systemic amyloidosis: clinical and laboratory features in 474 cases Semin Hematol 32 45 59
    • (1995) Semin Hematol , vol.32 , pp. 45-59
    • Kyle, R.A.1    Gertz, M.A.2
  • 19
  • 21
    • 0028818272 scopus 로고
    • Tertiary structure of an amyloid immunoglobulin light chain protein: A proposed model for amyloid fibril formation
    • 10.1073/pnas.92.21.9490 1995PNAS.92.9490S
    • N Schormann JR Murrell JJ Liepnieks MD Benson 1995 Tertiary structure of an amyloid immunoglobulin light chain protein: a proposed model for amyloid fibril formation Proc Natl Acad Sci USA 92 9490 9494 10.1073/pnas.92.21.9490 1995PNAS...92.9490S
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 9490-9494
    • Schormann, N.1    Murrell, J.R.2    Liepnieks, J.J.3    Benson, M.D.4
  • 22
    • 0000573604 scopus 로고
    • Protein and host factors implicated in the pathogenesis of light chain amyloidosis (AL amyloidosis)
    • 10.3109/13506129508999010
    • A Solomon DT Weiss 1995 Protein and host factors implicated in the pathogenesis of light chain amyloidosis (AL amyloidosis) Amyloid 2 269 279 10.3109/13506129508999010
    • (1995) Amyloid , vol.2 , pp. 269-279
    • Solomon, A.1    Weiss, D.T.2
  • 23
    • 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
    • DOI 10.1074/jbc.M109230200
    • PO Souillac VN Uversky IS Millett R Khurana S Doniach AL Fink 2002 Effect of association state and conformational stability on the kinetics of immunoglobulin light chain amyloid fibril formation at physiological pH J Biol Chem 277 12657 12665 10.1074/jbc.M109230200 (Pubitemid 34952625)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.15 , 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
  • 24
    • 0038047044 scopus 로고    scopus 로고
    • Structural transformations of oligomeric intermediates in the fibrillation of the immunoglobulin light chain LEN
    • DOI 10.1021/bi034652m
    • PO Souillac VN Uversky AL Fink 2003 Structural transformations of oligomeric intermediates in the fibrillation of the immunoglobulin light chain LEN Biochemistry 42 8094 8104 10.1021/bi034652m (Pubitemid 36807726)
    • (2003) Biochemistry , vol.42 , Issue.26 , pp. 8094-8104
    • Souillac, P.O.1    Uversky, V.N.2    Fink, A.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.