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Volumn 72, Issue 3, 2008, Pages 811-821

Effect of an amyloidogenic sequence attached to yellow fluorescent protein

Author keywords

AFM; Amyloid fibril; Infrared spectroscopy; Protein misfolding; TEM

Indexed keywords

AMYLOID PROTEIN; HYBRID PROTEIN; MEDIN; YELLOW FLUORESCENT PROTEIN;

EID: 47349117210     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21971     Document Type: Article
Times cited : (15)

References (45)
  • 1
    • 16844364450 scopus 로고    scopus 로고
    • Protein amyloidose misfolding: Mechanisms, detection, and pathological implications
    • Jeyashekar NS, Sadana A, Vo-Dinh T. Protein amyloidose misfolding: mechanisms, detection, and pathological implications. Methods Mol Biol 2005;300:417-435.
    • (2005) Methods Mol Biol , vol.300 , pp. 417-435
    • Jeyashekar, N.S.1    Sadana, A.2    Vo-Dinh, T.3
  • 2
    • 10644225416 scopus 로고    scopus 로고
    • Protein misfolding and aggregation: New examples in medicine and biology of the dark side of the protein world
    • Stefani M. Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world. Biochim Biophys Acta 2004;1739:5-25.
    • (2004) Biochim Biophys Acta , vol.1739 , pp. 5-25
    • Stefani, M.1
  • 3
    • 9344226144 scopus 로고    scopus 로고
    • Misfolded proteins and human diseases
    • Nayeem MS, Khan RH. Misfolded proteins and human diseases. Protein Pept Lett 2004;11:593-600.
    • (2004) Protein Pept Lett , vol.11 , pp. 593-600
    • Nayeem, M.S.1    Khan, R.H.2
  • 4
    • 0035961329 scopus 로고    scopus 로고
    • The structural basis of protein folding and its links with human disease
    • Dobson CM. The structural basis of protein folding and its links with human disease. Philos Trans R Soc Lond B Biol Sci 2001;356:133-145.
    • (2001) Philos Trans R Soc Lond B Biol Sci , vol.356 , pp. 133-145
    • Dobson, C.M.1
  • 6
    • 0035187228 scopus 로고    scopus 로고
    • Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domain
    • Chiti F, Bucciantini M, Capanni C, Taddei N, Dobson CM, Stefani M. Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domain. Protein Sci 2001;10:2541-2547.
    • (2001) Protein Sci , vol.10 , pp. 2541-2547
    • Chiti, F.1    Bucciantini, M.2    Capanni, C.3    Taddei, N.4    Dobson, C.M.5    Stefani, M.6
  • 8
    • 0036784667 scopus 로고    scopus 로고
    • A kinetic study of β-lactoglobulin amyloid fibril formation promoted by urea
    • Hamada D, Dobson CM. A kinetic study of β-lactoglobulin amyloid fibril formation promoted by urea. Protein Sci 2002;11:2417-2426.
    • (2002) Protein Sci , vol.11 , pp. 2417-2426
    • Hamada, D.1    Dobson, C.M.2
  • 9
  • 10
    • 0035826234 scopus 로고    scopus 로고
    • Amyloid fibrils from muscle myoglobin
    • Fändrich M, Fletcher MA, Dobson CM. Amyloid fibrils from muscle myoglobin. Nature 2001;410:165-166.
    • (2001) Nature , vol.410 , pp. 165-166
    • Fändrich, M.1    Fletcher, M.A.2    Dobson, C.M.3
  • 11
    • 0042467550 scopus 로고    scopus 로고
    • Rationalization of the effects of mutations on peptide and protein aggregation rates
    • Chiti F, Stefani M, Taddei N, Ramponi G, Dobson CM. Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature 2003;424:805-808.
    • (2003) Nature , vol.424 , pp. 805-808
    • Chiti, F.1    Stefani, M.2    Taddei, N.3    Ramponi, G.4    Dobson, C.M.5
  • 12
  • 13
    • 2342569618 scopus 로고    scopus 로고
    • Conformational constraints for amyloid fibrillation: The importance of being unfolded
    • Uversky VN, Fink AL. Conformational constraints for amyloid fibrillation: the importance of being unfolded. Biochim Biophys Acta 2004;1698:131-153.
    • (2004) Biochim Biophys Acta , vol.1698 , pp. 131-153
    • Uversky, V.N.1    Fink, A.L.2
  • 14
    • 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;30:521-525.
    • (2002) Biochem Soc Trans , vol.30 , pp. 521-525
    • Makin, O.S.1    Serpell, L.C.2
  • 15
    • 0036052739 scopus 로고    scopus 로고
    • Ideas of order for amyloid fibril structure
    • Wetzel R. Ideas of order for amyloid fibril structure. Structure 2002;10:1031-1036.
    • (2002) Structure , vol.10 , pp. 1031-1036
    • Wetzel, R.1
  • 18
    • 4143097041 scopus 로고    scopus 로고
    • Amyloid fibril formation by a partially structured intermediate state of α-chymotrypsin
    • Pallares I, Vendrell J, Aviles FX, Ventura S. Amyloid fibril formation by a partially structured intermediate state of α-chymotrypsin. J Mol Biol 2004;342:321-331.
    • (2004) J Mol Biol , vol.342 , pp. 321-331
    • Pallares, I.1    Vendrell, J.2    Aviles, F.X.3    Ventura, S.4
  • 19
    • 4143148674 scopus 로고    scopus 로고
    • Guanidine hydrochloride can induce amyloid fibril formation from hen egg-white lysozyme
    • Vernaglia BA, Huang J, Clark ED. Guanidine hydrochloride can induce amyloid fibril formation from hen egg-white lysozyme. Biomacromolecules 2004;5:1362-1370.
    • (2004) Biomacromolecules , vol.5 , pp. 1362-1370
    • Vernaglia, B.A.1    Huang, J.2    Clark, E.D.3
  • 20
    • 0038532258 scopus 로고    scopus 로고
    • Congo red populates partially unfolded states of an amyloidogenic protein to enhance aggregation and amyloid fibril formation
    • Kim YS, Randolph TW, Manning MC, Stevens FJ, Carpenter JF. Congo red populates partially unfolded states of an amyloidogenic protein to enhance aggregation and amyloid fibril formation. J Biol Chem 2003;278:10842-10850.
    • (2003) J Biol Chem , vol.278 , pp. 10842-10850
    • Kim, Y.S.1    Randolph, T.W.2    Manning, M.C.3    Stevens, F.J.4    Carpenter, J.F.5
  • 21
    • 0035920156 scopus 로고    scopus 로고
    • Tetramer dissociation and monomer partial unfolding precedes protofibril formation in amyloidogenic transthyretin variants
    • Quintas A, Vaz DC, Carsoso I, Saraiva MJ, Brito RM. Tetramer dissociation and monomer partial unfolding precedes protofibril formation in amyloidogenic transthyretin variants. J Biol Chem 2001;276:27207-27213.
    • (2001) J Biol Chem , vol.276 , pp. 27207-27213
    • Quintas, A.1    Vaz, D.C.2    Carsoso, I.3    Saraiva, M.J.4    Brito, R.M.5
  • 23
    • 0032555738 scopus 로고    scopus 로고
    • Protein subunit interactions and structural integrity of amyloidogenic transthyretins: Evidence from electrospray mass spectrometry
    • Nettleton EJ, Sunde M, Lai Z, Kelly JW, Dobson CM, Robinson CV. Protein subunit interactions and structural integrity of amyloidogenic transthyretins: evidence from electrospray mass spectrometry. J Mol Biol 1998;281:553-564.
    • (1998) J Mol Biol , vol.281 , pp. 553-564
    • Nettleton, E.J.1    Sunde, M.2    Lai, Z.3    Kelly, J.W.4    Dobson, C.M.5    Robinson, C.V.6
  • 24
    • 0036228167 scopus 로고    scopus 로고
    • Exploring protein aggregation and self-propagation using lattice models: Phase diagram and kinetics
    • Dima RI, Thirumalai D. Exploring protein aggregation and self-propagation using lattice models: phase diagram and kinetics. Protein Sci 2002;11:1036-1049.
    • (2002) Protein Sci , vol.11 , pp. 1036-1049
    • Dima, R.I.1    Thirumalai, D.2
  • 25
    • 0346500469 scopus 로고    scopus 로고
    • Monti M, Leij Garolla di Bard B, Calloni G, Chiti F, Amoresano A, Ramponi G, Pucci P. The regions of the sequence most exposed to the solvent within the amyloidogenic state of a protein initiate the aggregation process. J Mol Biol 2004;336:253-262.
    • Monti M, Leij Garolla di Bard B, Calloni G, Chiti F, Amoresano A, Ramponi G, Pucci P. The regions of the sequence most exposed to the solvent within the amyloidogenic state of a protein initiate the aggregation process. J Mol Biol 2004;336:253-262.
  • 26
    • 26844498710 scopus 로고    scopus 로고
    • Sequence determinants of protein aggregation: Tools to increase protein solubility
    • Ventura S. Sequence determinants of protein aggregation: tools to increase protein solubility. Microb Cell Fact 2005;4:11.
    • (2005) Microb Cell Fact , vol.4 , pp. 11
    • Ventura, S.1
  • 28
    • 0036308719 scopus 로고    scopus 로고
    • Mutations that reduce aggregation of the Alzheimer's Aβ42 peptide: An unbiased search for the sequence determinants of Aβ amyloidogenesis
    • Wurth C, Guimard NK, Hecht MH. Mutations that reduce aggregation of the Alzheimer's Aβ42 peptide: an unbiased search for the sequence determinants of Aβ amyloidogenesis. J Mol Biol 2002;319:1279-1290.
    • (2002) J Mol Biol , vol.319 , pp. 1279-1290
    • Wurth, C.1    Guimard, N.K.2    Hecht, M.H.3
  • 29
    • 0037117485 scopus 로고    scopus 로고
    • Mechanism of inactivation on prion coversion of the Saccharomyces cerevisiae Ure2 protein
    • Baxa U, Speransky V, Steven AC, Wickner RB. Mechanism of inactivation on prion coversion of the Saccharomyces cerevisiae Ure2 protein. Proc Natl Acad Sci USA 2002;99:5253-5260.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 5253-5260
    • Baxa, U.1    Speransky, V.2    Steven, A.C.3    Wickner, R.B.4
  • 30
    • 0030712145 scopus 로고    scopus 로고
    • Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae
    • Glover JR, Kowal AS, Schirmer EC, Patino MM, Liu JJ, Lindquist S. Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae. Cell 1997;89:811-819.
    • (1997) Cell , vol.89 , pp. 811-819
    • Glover, J.R.1    Kowal, A.S.2    Schirmer, E.C.3    Patino, M.M.4    Liu, J.J.5    Lindquist, S.6
  • 32
    • 0034723391 scopus 로고    scopus 로고
    • Creating a protein-based element of inheritance
    • Li L, Lindquist SL. Creating a protein-based element of inheritance. Science 2000;287:661-664.
    • (2000) Science , vol.287 , pp. 661-664
    • Li, L.1    Lindquist, S.L.2
  • 33
    • 34447649216 scopus 로고    scopus 로고
    • Crystal structure of the bovine lactadherin C2 domain, a membrane binding motif, shows similarity to the C2 domains of factor V and factor VIII
    • Lin H, Huai Q, Huang M, Furie B, Furie BC. Crystal structure of the bovine lactadherin C2 domain, a membrane binding motif, shows similarity to the C2 domains of factor V and factor VIII. J Mol Biol 2007;371:717-724.
    • (2007) J Mol Biol , vol.371 , pp. 717-724
    • Lin, H.1    Huai, Q.2    Huang, M.3    Furie, B.4    Furie, B.C.5
  • 34
    • 0029655338 scopus 로고    scopus 로고
    • Evidence for two prions in yeast: [URE3] and [PSI]
    • Wickner RB, Masison DC. Evidence for two prions in yeast: [URE3] and [PSI]. Curr Top Microbiol Immunol 1996;207:147-160.
    • (1996) Curr Top Microbiol Immunol , vol.207 , pp. 147-160
    • Wickner, R.B.1    Masison, D.C.2
  • 35
    • 0036366021 scopus 로고    scopus 로고
    • Prions of yeast as epigenetic phonomena: High protein "copy number" inducing protein "silencing
    • Wickner RB, Edskes HK, Roberts BT, Pierce M, Baxa U. Prions of yeast as epigenetic phonomena: high protein "copy number" inducing protein "silencing." Adv Genet 2002;46:485-525.
    • (2002) Adv Genet , vol.46 , pp. 485-525
    • Wickner, R.B.1    Edskes, H.K.2    Roberts, B.T.3    Pierce, M.4    Baxa, U.5
  • 36
    • 0034160086 scopus 로고    scopus 로고
    • Protein-only inheritance in yeast: Something to get [PSI+]-ched about
    • Serio TR, Lindquist SL. Protein-only inheritance in yeast: something to get [PSI+]-ched about. Trends Cell Biol 2001;10:98-105.
    • (2001) Trends Cell Biol , vol.10 , pp. 98-105
    • Serio, T.R.1    Lindquist, S.L.2
  • 37
    • 0034943645 scopus 로고    scopus 로고
    • The yeast prion [PSI+]: Molecule insights and functional consequences
    • Serio TR, Lindquist SL. The yeast prion [PSI+]: molecule insights and functional consequences. Adv Protein Chem 2001;57:335-366.
    • (2001) Adv Protein Chem , vol.57 , pp. 335-366
    • Serio, T.R.1    Lindquist, S.L.2
  • 38
    • 9644287905 scopus 로고    scopus 로고
    • The yeast prion protein Ure2 shows glutathione peroxidase activity in both native and fibrillar forms
    • Bai M, Zhou J-M, Perrett S. The yeast prion protein Ure2 shows glutathione peroxidase activity in both native and fibrillar forms. J Biol Chem 2004;279:50025-50030.
    • (2004) J Biol Chem , vol.279 , pp. 50025-50030
    • Bai, M.1    Zhou, J.-M.2    Perrett, S.3
  • 39
    • 0037124337 scopus 로고    scopus 로고
    • The yeast prion Ure2p retains its native α-helical conformation upon assembly into protein fibrils in vitro
    • Bousset L, Thomson NH, Radford SE, Melki R. The yeast prion Ure2p retains its native α-helical conformation upon assembly into protein fibrils in vitro. EMBO J 2002;21:2903-2911.
    • (2002) EMBO J , vol.21 , pp. 2903-2911
    • Bousset, L.1    Thomson, N.H.2    Radford, S.E.3    Melki, R.4
  • 41
    • 0026551594 scopus 로고
    • Senile aortic amyloid. Evidence for two distinct forms of localized deposits
    • Mucchiano G, Cornwell GG, III, Westermark P. Senile aortic amyloid. Evidence for two distinct forms of localized deposits. Am J Pathol 1992;140:871-877.
    • (1992) Am J Pathol , vol.140 , pp. 871-877
    • Mucchiano, G.1    Cornwell III, G.G.2    Westermark, P.3
  • 42
    • 0037592927 scopus 로고    scopus 로고
    • Direct observation of amyloid fibril growth monitored by thioflavin T fluorescence
    • Ban T, Hamada D, Hasegawa K, Naiki H, Goto Y. Direct observation of amyloid fibril growth monitored by thioflavin T fluorescence. J Biol Chem 2003;278:16462-16465.
    • (2003) J Biol Chem , vol.278 , pp. 16462-16465
    • Ban, T.1    Hamada, D.2    Hasegawa, K.3    Naiki, H.4    Goto, Y.5
  • 43
    • 0025005940 scopus 로고
    • Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier-transform infrared spectroscopy on hydrated films
    • Goormaghtigh E, Cabiaux V, Ruysschaert JM. Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier-transform infrared spectroscopy on hydrated films. Eur J Biochem 1990;193:409-420.
    • (1990) Eur J Biochem , vol.193 , pp. 409-420
    • Goormaghtigh, E.1    Cabiaux, V.2    Ruysschaert, J.M.3
  • 44
    • 0029586689 scopus 로고
    • Localization, trafficking, and temperature-dependence of the Aequorea green fluorescent protein in cultured vertebrate cells
    • Ogawa H, Inouye S, Tsuji FI, Yasuda K, Umesono K. Localization, trafficking, and temperature-dependence of the Aequorea green fluorescent protein in cultured vertebrate cells. Proc Natl Acad Sci USA 1995;92:11899-11903.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 11899-11903
    • Ogawa, H.1    Inouye, S.2    Tsuji, F.I.3    Yasuda, K.4    Umesono, K.5
  • 45
    • 1642563960 scopus 로고    scopus 로고
    • Engineering amyloidogenicity towards the development of nanofibrillar materials
    • Hamada D, Yanagihara I, Tsumoto K. Engineering amyloidogenicity towards the development of nanofibrillar materials. Trends Biotechnol 2004;22:93-97.
    • (2004) Trends Biotechnol , vol.22 , pp. 93-97
    • Hamada, D.1    Yanagihara, I.2    Tsumoto, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.