메뉴 건너뛰기




Volumn 281, Issue 3, 1998, Pages 553-564

Protein subunit interactions and structural integrity of amyloidogenic transthyretins: Evidence from electrospray mass spectrometry

Author keywords

Amyloid; Hydrogen exchange; Mass spectrometry; Thyroxine; Transthyretin

Indexed keywords

AMYLOID; PREALBUMIN; PROTEIN SUBUNIT; THYROXINE; WATER;

EID: 0032555738     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1937     Document Type: Article
Times cited : (157)

References (36)
  • 1
    • 77957180065 scopus 로고
    • A peculiar form of peripheral neurophaphy. Familial atypical generalised amyloidosis with special involvement of the peripheral nerves
    • Andrade C. A peculiar form of peripheral neurophaphy. Familial atypical generalised amyloidosis with special involvement of the peripheral nerves. Brain. 75:1952;408-427
    • (1952) Brain , vol.75 , pp. 408-427
    • Andrade, C.1
  • 3
    • 0029120465 scopus 로고
    • Thermodynamic parameters from hydrogen exchange measurements
    • Bai Y.W., Milne J.S., Mayne L., Englander S.W. Thermodynamic parameters from hydrogen exchange measurements. Methods Enzymol. 259:1995;344-356
    • (1995) Methods Enzymol. , vol.259 , pp. 344-356
    • Bai, Y.W.1    Milne, J.S.2    Mayne, L.3    Englander, S.W.4
  • 4
    • 0024503518 scopus 로고
    • Familial amyloidotic polyneuropaphy
    • Benson M.D. Familial amyloidotic polyneuropaphy. Trends Neurosci. 12:1989;88-92
    • (1989) Trends Neurosci. , vol.12 , pp. 88-92
    • Benson, M.D.1
  • 5
    • 0017824077 scopus 로고
    • Structure of prealbumin: Secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 Å
    • Blake C.C.F., Geisow M.J., Oatley S.J., Rerat B., Rerat C. Structure of prealbumin secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 Å J. Mol. Biol. 121:1978;339-356
    • (1978) J. Mol. Biol. , vol.121 , pp. 339-356
    • Blake, C.C.F.1    Geisow, M.J.2    Oatley, S.J.3    Rerat, B.4    Rerat, C.5
  • 8
    • 0031202280 scopus 로고    scopus 로고
    • Hydrogen exchange at equilibrium: A short cut for analysing protein-folding pathways?
    • Clarke J., Itzhaki L.S., Fersht A.R. Hydrogen exchange at equilibrium a short cut for analysing protein-folding pathways? Trends Biochem. Sci. 22:1997;284-287
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 284-287
    • Clarke, J.1    Itzhaki, L.S.2    Fersht, A.R.3
  • 9
    • 0026675307 scopus 로고
    • Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro
    • Colon W., Kelly J.W. Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro. Biochemistry. 31:1992;8654-8660
    • (1992) Biochemistry , vol.31 , pp. 8654-8660
    • Colon, W.1    Kelly, J.W.2
  • 10
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced colouring capabilities
    • Esnouf R.M. An extensively modified version of MolScript that includes greatly enhanced colouring capabilities. J. Mol. Graph. Model. 15:1997;132
    • (1997) J. Mol. Graph. Model. , vol.15 , pp. 132
    • Esnouf, R.M.1
  • 11
    • 0001413545 scopus 로고
    • Detection of non-covalent receptor-ligand complexes by mass spectrometry
    • Ganem B., Li Y.T., Henion J.D. Detection of non-covalent receptor-ligand complexes by mass spectrometry. J. Am. Chem. Soc. 113:1991;6294-6296
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 6294-6296
    • Ganem, B.1    Li, Y.T.2    Henion, J.D.3
  • 13
    • 0026612659 scopus 로고
    • Transthyretin Pro55, a variant associated with early-onset, aggressive, diffuse amyloidosis with cardiac and neurologic involvement
    • Jacobsen D.R., McFarlin D.E., Kane I., Buxbaum J.N. Transthyretin Pro55, a variant associated with early-onset, aggressive, diffuse amyloidosis with cardiac and neurologic involvement. Human Genet. 89:1992;353-356
    • (1992) Human Genet. , vol.89 , pp. 353-356
    • Jacobsen, D.R.1    McFarlin, D.E.2    Kane, I.3    Buxbaum, J.N.4
  • 14
    • 0014336534 scopus 로고
    • Retinol binding protein - The transport protein for vitamin a in human plasma
    • Kanai M., Raz A., Goodman D.S. Retinol binding protein - the transport protein for vitamin A in human plasma. J. Clin. Invest. 47:1968;2025-2044
    • (1968) J. Clin. Invest. , vol.47 , pp. 2025-2044
    • Kanai, M.1    Raz, A.2    Goodman, D.S.3
  • 15
    • 0027949973 scopus 로고
    • A chemical approach to elucidate the mechanism of transthyretin and B protein amyloid fibril formation
    • Kelly J.W., Lansbury P.T. A chemical approach to elucidate the mechanism of transthyretin and B protein amyloid fibril formation. Amyloid: Int. J. Exp. Clin. Invest. 1:1994;186-205
    • (1994) Amyloid: Int. J. Exp. Clin. Invest. , vol.1 , pp. 186-205
    • Kelly, J.W.1    Lansbury, P.T.2
  • 16
    • 0030004644 scopus 로고    scopus 로고
    • The acid mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid
    • Lai Z., Colon W., Kelly J.W. The acid mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid. Biochemistry. 35:1996;6470-6482
    • (1996) Biochemistry , vol.35 , pp. 6470-6482
    • Lai, Z.1    Colon, W.2    Kelly, J.W.3
  • 17
    • 0030874395 scopus 로고    scopus 로고
    • Guanidine hydrochloride induced denaturation and refolding of transthyretin exhibits a marked hysteresis: Equilibria with high kinetic barriers
    • Lai Z., McCulloch J., Lahuel A., Kelly J.W. Guanidine hydrochloride induced denaturation and refolding of transthyretin exhibits a marked hysteresis: equilibria with high kinetic barriers. Biochemistry. 36:1997;10230-10239
    • (1997) Biochemistry , vol.36 , pp. 10230-10239
    • Lai, Z.1    McCulloch, J.2    Lahuel, A.3    Kelly, J.W.4
  • 18
    • 0032558978 scopus 로고    scopus 로고
    • Characterisation of the transthyretin acid denaturation pathway by analytical ultracentrifugation: Implications for amyloid fibril formation
    • in the press
    • Lai Z., Lashuel H.A., Kelly J.W. Characterisation of the transthyretin acid denaturation pathway by analytical ultracentrifugation: implications for amyloid fibril formation. Biochemistry. 1998;. in the press
    • (1998) Biochemistry
    • Lai, Z.1    Lashuel, H.A.2    Kelly, J.W.3
  • 19
    • 0028447420 scopus 로고
    • Observation of non-covalent quaternary associations of proteins by electrospray ionization mass spectrometry
    • Light-Wahl K.J., Schwartz B.L., Smith R.D. Observation of non-covalent quaternary associations of proteins by electrospray ionization mass spectrometry. J. Am. Chem. Soc. 116:1994;5271-5278
    • (1994) J. Am. Chem. Soc , vol.116 , pp. 5271-5278
    • Light-Wahl, K.J.1    Schwartz, B.L.2    Smith, R.D.3
  • 20
    • 0027461675 scopus 로고
    • Tandem mass spectrometry of very large molecules 2. Dissociation of multiply charged proline-containing proteins from electrospray ionization
    • Loo J.A., Edmonds C.G., Smith R.D. Tandem mass spectrometry of very large molecules 2. Dissociation of multiply charged proline-containing proteins from electrospray ionization. Anal. Chem. 65:1993;425-438
    • (1993) Anal. Chem. , vol.65 , pp. 425-438
    • Loo, J.A.1    Edmonds, C.G.2    Smith, R.D.3
  • 21
    • 0027363264 scopus 로고
    • Transthyretin mutation Leu-55-Pro significantly alters tetramer stability and increases amyloidogenicity
    • McCutchen S.L., Colon W., Kelly J.W. Transthyretin mutation Leu-55-Pro significantly alters tetramer stability and increases amyloidogenicity. Biochemistry. 32:1993;12119-12127
    • (1993) Biochemistry , vol.32 , pp. 12119-12127
    • McCutchen, S.L.1    Colon, W.2    Kelly, J.W.3
  • 22
    • 0028057108 scopus 로고
    • Raster 3D version 2.0: A program for photorealistic molecular graphics
    • Merritt E., Murphy M. Raster 3D version 2.0: a program for photorealistic molecular graphics. Acta Crystallog. sect. D. 50:1994;869-873
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 869-873
    • Merritt, E.1    Murphy, M.2
  • 24
    • 13144271417 scopus 로고
    • Interactions of retinol with binding proteins: Studies with retinol-binding protein and with transthyretin
    • Noy N., Slosberg E., Scarlata S. Interactions of retinol with binding proteins studies with retinol-binding protein and with transthyretin. Biochemistry. 14:1992;282-289
    • (1992) Biochemistry , vol.14 , pp. 282-289
    • Noy, N.1    Slosberg, E.2    Scarlata, S.3
  • 25
    • 0015831649 scopus 로고
    • Binding of thyroxine and thyroxine analogs to human serum prealbumin
    • Pages R.A., Robbins J., Endelhock H. Binding of thyroxine and thyroxine analogs to human serum prealbumin. Biochemistry. 12:1973;2773-2779
    • (1973) Biochemistry , vol.12 , pp. 2773-2779
    • Pages, R.A.1    Robbins, J.2    Endelhock, H.3
  • 26
    • 0002699669 scopus 로고
    • Multiple modes of binding of thyroid hormones and iodothyronines to human plasma transthyretin
    • C. Beddell. New York: John Wiley & Sons Ltd
    • Paz P.d.l., Burridge J., Oatley S., Blake C.C.F. Multiple modes of binding of thyroid hormones and iodothyronines to human plasma transthyretin. Beddell C. The Design of Drugs to Macromolecular Targets. 1992;120-172 John Wiley & Sons Ltd, New York
    • (1992) The Design of Drugs to Macromolecular Targets , pp. 120-172
    • D, P.P.L.1    Burridge, J.2    Oatley, S.3    Blake, C.C.F.4
  • 27
    • 0014690587 scopus 로고
    • The interaction of thyroxine with human plasma prealbumin and with the prealbumin retinol binding protein complex
    • Raz A., Goodman D. The interaction of thyroxine with human plasma prealbumin and with the prealbumin retinol binding protein complex. J. Biol. Chem. 244:1969;3230-3237
    • (1969) J. Biol. Chem. , vol.244 , pp. 3230-3237
    • Raz, A.1    Goodman, D.2
  • 29
    • 0029794153 scopus 로고    scopus 로고
    • Probing the nature of non-covalent interactions by mass spectrometry. a study of protein-CoA ligand binding and assembly
    • Robinson C.V., Chung E.W., Kragelund B.B., Knudsen J., Aplin R.T., Poulsen F.M., Dobson C.M. Probing the nature of non-covalent interactions by mass spectrometry. A study of protein-CoA ligand binding and assembly. J. Am. Chem. Soc. 118:1996;8646-8653
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 8646-8653
    • Robinson, C.V.1    Chung, E.W.2    Kragelund, B.B.3    Knudsen, J.4    Aplin, R.T.5    Poulsen, F.M.6    Dobson, C.M.7
  • 30
    • 0028969996 scopus 로고
    • Transthyretin mutation in health and disease
    • Savaiva M. Transthyretin mutation in health and disease. Human Mutat. 5:1995;191-196
    • (1995) Human Mutat. , vol.5 , pp. 191-196
    • Savaiva, M.1
  • 31
    • 0141715644 scopus 로고
    • Frequency analysis and structural correlation of FAP mutations in transthyretin
    • New York: Parthenon Publishing Group Inc
    • Serpell L., Blake C.C.F. Frequency analysis and structural correlation of FAP mutations in transthyretin. Amyloid and Amyloidoses. 1994;447-450 Parthenon Publishing Group Inc, New York
    • (1994) Amyloid and Amyloidoses , pp. 447-450
    • Serpell, L.1    Blake, C.C.F.2
  • 32
    • 1842589542 scopus 로고    scopus 로고
    • The "edge strand" hypothesis: Prediction and test of a mutational "hot spot" on the transthyretin molecule associated with FAP amyloidogenesis
    • Serpell L., Goldstein G., Dacklin I., Lundgren E., Blake C.C.F. The "edge strand" hypothesis prediction and test of a mutational "hot spot" on the transthyretin molecule associated with FAP amyloidogenesis. Amyloid: Int. J. Exp. Clin. Invest. 3:1996;75-85
    • (1996) Amyloid: Int. J. Exp. Clin. Invest. , vol.3 , pp. 75-85
    • Serpell, L.1    Goldstein, G.2    Dacklin, I.3    Lundgren, E.4    Blake, C.C.F.5
  • 35
    • 0030572683 scopus 로고    scopus 로고
    • For protein misassembly its the I decade
    • Wetzel R. For protein misassembly its the I decade. Cell. 86:1996;699-702
    • (1996) Cell , vol.86 , pp. 699-702
    • Wetzel, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.