메뉴 건너뛰기




Volumn 587, Issue 11, 2013, Pages 1605-1609

NMR characterization of the interaction of GroEL with amyloid β as a model ligand

Author keywords

Amyloid ; Chaperonin; GroEL; NMR; NOE

Indexed keywords

ALANINE; AMYLOID BETA PROTEIN[1-40]; CHAPERONIN 60; LEUCINE; VALINE;

EID: 84878237719     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2013.04.007     Document Type: Article
Times cited : (20)

References (28)
  • 1
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • F.U. Hartl Molecular chaperones in cellular protein folding Nature 381 1996 571 579
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 2
    • 0027933369 scopus 로고
    • GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms
    • J.S. Weissman, Y. Kashi, W.A. Fenton, and A.L. Horwich GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms Cell 78 1994 693 702
    • (1994) Cell , vol.78 , pp. 693-702
    • Weissman, J.S.1    Kashi, Y.2    Fenton, W.A.3    Horwich, A.L.4
  • 5
    • 0033543736 scopus 로고    scopus 로고
    • NMR analysis of the binding of a rhodanese peptide to a minichaperone in solution
    • N. Kobayashi, S.M. Freund, J. Chatellier, R. Zahn, and A.R. Fersht NMR analysis of the binding of a rhodanese peptide to a minichaperone in solution J. Mol. Biol. 292 1999 181 190
    • (1999) J. Mol. Biol. , vol.292 , pp. 181-190
    • Kobayashi, N.1    Freund, S.M.2    Chatellier, J.3    Zahn, R.4    Fersht, A.R.5
  • 6
    • 0033598941 scopus 로고    scopus 로고
    • The crystal structure of a GroEL/peptide complex: Plasticity as a basis for substrate diversity
    • L. Chen, and P.B. Sigler The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity Cell 99 1999 757 768
    • (1999) Cell , vol.99 , pp. 757-768
    • Chen, L.1    Sigler, P.B.2
  • 7
    • 0031554905 scopus 로고    scopus 로고
    • Multiple cycles of global unfolding of GroEL-bound cyclophilin A evidenced by NMR
    • S.E. Nieba-Axmann, M. Ottiger, K. Wüthrich, and A. Plückthun Multiple cycles of global unfolding of GroEL-bound cyclophilin A evidenced by NMR J. Mol. Biol. 271 1997 803 818
    • (1997) J. Mol. Biol. , vol.271 , pp. 803-818
    • Nieba-Axmann, S.E.1    Ottiger, M.2    Wüthrich, K.3    Plückthun, A.4
  • 8
    • 0028260023 scopus 로고
    • Destabilization of the complete protein secondary structure on binding to the chaperone GroEL
    • R. Zahn, C. Spitzfaden, M. Ottiger, K. Wüthrich, and A. Plückthun Destabilization of the complete protein secondary structure on binding to the chaperone GroEL Nature 368 1994 261 265
    • (1994) Nature , vol.368 , pp. 261-265
    • Zahn, R.1    Spitzfaden, C.2    Ottiger, M.3    Wüthrich, K.4    Plückthun, A.5
  • 10
    • 0034880923 scopus 로고    scopus 로고
    • Folding of malate dehydrogenase inside the GroEL-GroES cavity
    • J. Chen, S. Walter, A.L. Horwich, and D.L. Smith Folding of malate dehydrogenase inside the GroEL-GroES cavity Nat. Struct. Biol. 8 2001 721 728
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 721-728
    • Chen, J.1    Walter, S.2    Horwich, A.L.3    Smith, D.L.4
  • 12
    • 79960684196 scopus 로고    scopus 로고
    • Nuclear magnetic resonance spectroscopy with the stringent substrate rhodanese bound to the single-ring variant SR1 of the E. coli chaperonin GroEL
    • E. Koculi, R. Horst, A.L. Horwich, and K. Wüthrich Nuclear magnetic resonance spectroscopy with the stringent substrate rhodanese bound to the single-ring variant SR1 of the E. coli chaperonin GroEL Protein Sci. 20 2011 1380 1386
    • (2011) Protein Sci. , vol.20 , pp. 1380-1386
    • Koculi, E.1    Horst, R.2    Horwich, A.L.3    Wüthrich, K.4
  • 13
    • 84866872549 scopus 로고    scopus 로고
    • Revisiting the contribution of negative charges on the chaperonin cage wall to the acceleration of protein folding
    • F. Motojima, Y. Motojima-Miyazaki, and M. Yoshida Revisiting the contribution of negative charges on the chaperonin cage wall to the acceleration of protein folding Proc. Natl. Acad. Sci. USA 109 2012 15740 15745
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 15740-15745
    • Motojima, F.1    Motojima-Miyazaki, Y.2    Yoshida, M.3
  • 14
    • 0035783169 scopus 로고    scopus 로고
    • Review: Mechanisms of disaggregation and refolding of stable protein aggregates by molecular chaperones
    • A.P. Ben-Zvi, and P. Goloubinoff Review: mechanisms of disaggregation and refolding of stable protein aggregates by molecular chaperones J. Struct. Biol. 135 2001 84 93
    • (2001) J. Struct. Biol. , vol.135 , pp. 84-93
    • Ben-Zvi, A.P.1    Goloubinoff, P.2
  • 16
    • 84879125630 scopus 로고    scopus 로고
    • NMR approaches for characterizing interactions between the bacterial chaperonin GroEL and unstructured proteins
    • (in press) doi: 10.1016/j.jbiosc.2013.02.012
    • Nishida, N., Yagi-Utsumi, M., Motojima, F., Yoshida, M., Shimada, I. and Kato, K. (in press). NMR approaches for characterizing interactions between the bacterial chaperonin GroEL and unstructured proteins. J. Biosci. Bioeng.,doi: 10.1016/j.jbiosc.2013.02.012.
    • J. Biosci. Bioeng.
    • Nishida, N.1    Yagi-Utsumi, M.2    Motojima, F.3    Yoshida, M.4    Shimada, I.5    Kato, K.6
  • 17
    • 0023105114 scopus 로고
    • The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
    • J. Kang The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor Nature 325 1987 733 736
    • (1987) Nature , vol.325 , pp. 733-736
    • Kang, J.1
  • 18
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • J. Hardy, and D.J. Selkoe The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics Science 297 2002 353 356
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 19
    • 0033569635 scopus 로고    scopus 로고
    • Chaperonin-affected refolding of alpha-lactalbumin: Effects of nucleotides and the co-chaperonin GroES
    • T. Makio, M. Arai, and K. Kuwajima Chaperonin-affected refolding of alpha-lactalbumin: effects of nucleotides and the co-chaperonin GroES J. Mol. Biol. 293 1999 125 137
    • (1999) J. Mol. Biol. , vol.293 , pp. 125-137
    • Makio, T.1    Arai, M.2    Kuwajima, K.3
  • 20
    • 79952141716 scopus 로고    scopus 로고
    • Spectroscopic characterization of intermolecular interaction of amyloid β promoted on GM1 micelles
    • M. Yagi-Utsumi, K. Matsuo, K. Yanagisawa, K. Gekko, and K. Kato Spectroscopic characterization of intermolecular interaction of amyloid β promoted on GM1 micelles Int. J. Alzheimer's Dis. 2011 2010 925073
    • (2010) Int. J. Alzheimer's Dis. , vol.2011 , pp. 925073
    • Yagi-Utsumi, M.1    Matsuo, K.2    Yanagisawa, K.3    Gekko, K.4    Kato, K.5
  • 23
    • 1342324027 scopus 로고    scopus 로고
    • Progress towards a molecular-level structural understanding of amyloid fibrils
    • R. Tycko Progress towards a molecular-level structural understanding of amyloid fibrils Curr. Opin. Struct. Biol. 14 2004 96 103
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 96-103
    • Tycko, R.1
  • 24
    • 72649096531 scopus 로고    scopus 로고
    • Up-and-down topological mode of amyloid β-peptide lying on hydrophilic/hydrophobic interface of ganglioside clusters
    • M. Utsumi, Y. Yamaguchi, H. Sasakawa, N. Yamamoto, K. Yanagisawa, and K. Kato Up-and-down topological mode of amyloid β-peptide lying on hydrophilic/hydrophobic interface of ganglioside clusters Glycoconj. J. 26 2009 999 1006
    • (2009) Glycoconj. J. , vol.26 , pp. 999-1006
    • Utsumi, M.1    Yamaguchi, Y.2    Sasakawa, H.3    Yamamoto, N.4    Yanagisawa, K.5    Kato, K.6
  • 25
    • 77649270452 scopus 로고    scopus 로고
    • NMR characterization of the interactions between lyso-GM1 aqueous micelles and amyloid β
    • M. Yagi-Utsumi, T. Kameda, Y. Yamaguchi, and K. Kato NMR characterization of the interactions between lyso-GM1 aqueous micelles and amyloid β FEBS Lett. 584 2010 831 836
    • (2010) FEBS Lett. , vol.584 , pp. 831-836
    • Yagi-Utsumi, M.1    Kameda, T.2    Yamaguchi, Y.3    Kato, K.4
  • 26
    • 33644818046 scopus 로고    scopus 로고
    • Alanine scanning mutagenesis of Aβ(1-40) amyloid fibril stability
    • A.D. Williams, S. Shivaprasad, and R. Wetzel Alanine scanning mutagenesis of Aβ(1-40) amyloid fibril stability J. Mol. Biol. 357 2006 1283 1294
    • (2006) J. Mol. Biol. , vol.357 , pp. 1283-1294
    • Williams, A.D.1    Shivaprasad, S.2    Wetzel, R.3
  • 27
    • 63249121483 scopus 로고    scopus 로고
    • GroEL recognizes an amphipathic helix and binds to the hydrophobic side
    • Y. Li, X. Gao, and L. Chen GroEL recognizes an amphipathic helix and binds to the hydrophobic side J. Biol. Chem. 284 2009 4324 4331
    • (2009) J. Biol. Chem. , vol.284 , pp. 4324-4331
    • Li, Y.1    Gao, X.2    Chen, L.3
  • 28
    • 0030870719 scopus 로고    scopus 로고
    • The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
    • Z. Xu, A.L. Horwich, and P.B. Sigler The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex Nature 388 1997 741 750
    • (1997) Nature , vol.388 , pp. 741-750
    • Xu, Z.1    Horwich, A.L.2    Sigler, P.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.