메뉴 건너뛰기




Volumn 11, Issue 4, 2004, Pages 232-244

Amyloid formation: An emulation of matrix protein assembly?

Author keywords

Beta helix; Beta roll; Evolution; Matrix protein; Sequence repeats

Indexed keywords

AMYLOID P COMPONENT; APOLIPOPROTEIN E; CONGO RED; GLYCOSAMINOGLYCAN; MONOCLONAL ANTIBODY; PROTEIN SUBUNIT; THIOFLAVINE;

EID: 12244288360     PISSN: 13506129     EISSN: None     Source Type: Journal    
DOI: 10.1080/13506120400016265     Document Type: Conference Paper
Times cited : (7)

References (89)
  • 1
    • 0038612852 scopus 로고    scopus 로고
    • Amyloid as a natural product
    • Kelly JW and Balch WE (2003). Amyloid as a natural product. J Cell Biol 161, 461-462
    • (2003) J Cell Biol , vol.161 , pp. 461-462
    • Kelly, J.W.1    Balch, W.E.2
  • 3
    • 0028256397 scopus 로고
    • The fungal hydrophobin Sc3p self-assembles at the surface of aerial hyphae as a protein membrane constituting the hydrophobic rodlet layer
    • Wosten HA, Asgeirsdottir SA, Krook JH, Drenth JH and Wessels JG (1994). The fungal hydrophobin Sc3p self-assembles at the surface of aerial hyphae as a protein membrane constituting the hydrophobic rodlet layer. Eur J Cell Biol 63, 122-129
    • (1994) Eur J Cell Biol , vol.63 , pp. 122-129
    • Wosten, H.A.1    Asgeirsdottir, S.A.2    Krook, J.H.3    Drenth, J.H.4    Wessels, J.G.5
  • 4
    • 0028597937 scopus 로고
    • Interfacial self-assembly of a hydrophobin into an amphipathic protein membrane mediates fungal attachment to hydrophobic surfaces
    • Wosten HA, Schuren FH and Wessels JG (1994). Interfacial self-assembly of a hydrophobin into an amphipathic protein membrane mediates fungal attachment to hydrophobic surfaces. Embo J 13, 5848-5854
    • (1994) Embo J , vol.13 , pp. 5848-5854
    • Wosten, H.A.1    Schuren, F.H.2    Wessels, J.G.3
  • 5
    • 0031060711 scopus 로고    scopus 로고
    • Hydrophobins: Proteins that change the nature of the fungal surface
    • Wessels JG (1997). Hydrophobins: proteins that change the nature of the fungal surface. Adv Microb Physiol 38, 1-45
    • (1997) Adv Microb Physiol , vol.38 , pp. 1-45
    • Wessels, J.G.1
  • 7
    • 0343664397 scopus 로고    scopus 로고
    • Hydrophobins, the fungal coat unravelled
    • Wosten HA and de Vocht ML (2000). Hydrophobins, the fungal coat unravelled. Biochim Biophys Acta 1469, 79-86
    • (2000) Biochim Biophys Acta , vol.1469 , pp. 79-86
    • Wosten, H.A.1    De Vocht, M.L.2
  • 8
    • 0034775004 scopus 로고    scopus 로고
    • Hydrophobins: Multipurpose proteins
    • Wosten HA (2001). Hydrophobins: multipurpose proteins. Annu Rev Microbiol 55, 625-646
    • (2001) Annu Rev Microbiol , vol.55 , pp. 625-646
    • Wosten, H.A.1
  • 9
    • 0043199394 scopus 로고    scopus 로고
    • Experimental Evidence for Multiple Assembled States of Sc3 from Schizophyllum commune
    • Stroud PA, Goodwin JS, Butko P, Cannon GC and McCormick CL (2003). Experimental Evidence for Multiple Assembled States of Sc3 from Schizophyllum commune. Biomacromolecules 4, 956-967
    • (2003) Biomacromolecules , vol.4 , pp. 956-967
    • Stroud, P.A.1    Goodwin, J.S.2    Butko, P.3    Cannon, G.C.4    McCormick, C.L.5
  • 11
    • 1342310507 scopus 로고    scopus 로고
    • Oligomerization of hydrophobin SC3 in solution: From soluble state to self-assembly
    • Wang X, Graveland-Bikker JF, de Kruif CG and Robillard GT (2004). Oligomerization of hydrophobin SC3 in solution: from soluble state to self-assembly. Protein Sci 13, 810-821
    • (2004) Protein Sci , vol.13 , pp. 810-821
    • Wang, X.1    Graveland-Bikker, J.F.2    De Kruif, C.G.3    Robillard, G.T.4
  • 13
    • 0035933540 scopus 로고    scopus 로고
    • Amyloid-like fibrils from an 18-residue peptide analogue of a part of the central domain of the B-family of silkmoth chorion proteins
    • Iconomidou VA, Chryssikos GD, Gionis V, Vriend G, Hoenger A and Hamodrakas SJ (2001). Amyloid-like fibrils from an 18-residue peptide analogue of a part of the central domain of the B-family of silkmoth chorion proteins. FEBS Lett 499, 268-273
    • (2001) FEBS Lett , vol.499 , pp. 268-273
    • Iconomidou, V.A.1    Chryssikos, G.D.2    Gionis, V.3    Vriend, G.4    Hoenger, A.5    Hamodrakas, S.J.6
  • 14
    • 17144449510 scopus 로고    scopus 로고
    • Influence of water hardening of the chorion on cadmium accumulation in medaka (Oryzias latipes) eggs
    • Gonzalez-Doncel M, Larrea M, Sanchez-Fortun S and Hinton DE (2003). Influence of water hardening of the chorion on cadmium accumulation in medaka (Oryzias latipes) eggs. Chemosphere 52, 75-83
    • (2003) Chemosphere , vol.52 , pp. 75-83
    • Gonzalez-Doncel, M.1    Larrea, M.2    Sanchez-Fortun, S.3    Hinton, D.E.4
  • 15
    • 0035005523 scopus 로고    scopus 로고
    • Survival of water stress in annual fish embryos: Dehydration avoidance and egg envelope amyloid fibers
    • Podrabsky JE, Carpenter JF and Hand SC (2001). Survival of water stress in annual fish embryos: dehydration avoidance and egg envelope amyloid fibers. Am J Physiol Regul Integr Comp Physiol 280, R123-131
    • (2001) Am J Physiol Regul Integr Comp Physiol , vol.280
    • Podrabsky, J.E.1    Carpenter, J.F.2    Hand, S.C.3
  • 17
    • 0031875649 scopus 로고    scopus 로고
    • Prion proteins as memory molecules: An hypothesis
    • Tompa P and Friedrich P (1998). Prion proteins as memory molecules: an hypothesis. Neuroscience 86, 1037-1043
    • (1998) Neuroscience , vol.86 , pp. 1037-1043
    • Tompa, P.1    Friedrich, P.2
  • 18
    • 0347355571 scopus 로고    scopus 로고
    • Memory, synaptic translation, and . . . prions?
    • Darnell RB (2003). Memory, synaptic translation, and . . . prions? Cell 115, 767-768
    • (2003) Cell , vol.115 , pp. 767-768
    • Darnell, R.B.1
  • 19
    • 0346727550 scopus 로고    scopus 로고
    • Neuroscience. Long-term memory: A positive role for a prion?
    • Wickelgren I (2004). Neuroscience. Long-term memory: a positive role for a prion? Science 303, 28-29
    • (2004) Science , vol.303 , pp. 28-29
    • Wickelgren, I.1
  • 20
    • 0037986392 scopus 로고    scopus 로고
    • Proprotein convertase cleavage liberates a fibrillogenic fragment of a resident glycoprotein to initiate melanosome biogenesis
    • Berson JF, Theos AC, Harper DC, Tenza D, Raposo G and Marks MS (2003). Proprotein convertase cleavage liberates a fibrillogenic fragment of a resident glycoprotein to initiate melanosome biogenesis. J Cell Biol 161, 521-533
    • (2003) J Cell Biol , vol.161 , pp. 521-533
    • Berson, J.F.1    Theos, A.C.2    Harper, D.C.3    Tenza, D.4    Raposo, G.5    Marks, M.S.6
  • 21
    • 0027988041 scopus 로고
    • Polar zippers: Their role in human disease
    • Perutz M (1994). Polar zippers: their role in human disease. Protein Sci 3, 1629-1637
    • (1994) Protein Sci , vol.3 , pp. 1629-1637
    • Perutz, M.1
  • 22
    • 0029032138 scopus 로고
    • Polar zippers: Their role in human disease
    • Perutz MF (1995). Polar zippers: their role in human disease. Pharm Acta Helv 69, 213-224
    • (1995) Pharm Acta Helv , vol.69 , pp. 213-224
    • Perutz, M.F.1
  • 23
    • 0029401042 scopus 로고
    • Glutamine repeats as polar zippers: Their role in inherited neurodegenerative disease
    • Perutz MF (1995). Glutamine repeats as polar zippers: their role in inherited neurodegenerative disease. Mol Med 1, 718-721
    • (1995) Mol Med , vol.1 , pp. 718-721
    • Perutz, M.F.1
  • 24
    • 0030470459 scopus 로고    scopus 로고
    • Glutamine repeats and inherited neurodegenerative diseases: Molecular aspects
    • Perutz MF (1996). Glutamine repeats and inherited neurodegenerative diseases: molecular aspects. Curr Opin Struct Biol 6, 848-858
    • (1996) Curr Opin Struct Biol , vol.6 , pp. 848-858
    • Perutz, M.F.1
  • 25
    • 0031055820 scopus 로고    scopus 로고
    • Amyloid fibrils. Mutations make enzyme polymerize
    • Perutz MF (1997). Amyloid fibrils. Mutations make enzyme polymerize. Nature 385, 773, 775
    • (1997) Nature , vol.385 , pp. 773
    • Perutz, M.F.1
  • 26
    • 0033080367 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegenerative diseases: Molecular aspects
    • Perutz MF (1999). Glutamine repeats and neurodegenerative diseases: molecular aspects. Trends Biochem Sci 24, 58-63
    • (1999) Trends Biochem Sci , vol.24 , pp. 58-63
    • Perutz, M.F.1
  • 27
    • 0345533961 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegenerative diseases
    • Perutz MF (1999). Glutamine repeats and neurodegenerative diseases. Brain Res Bull 50, 467
    • (1999) Brain Res Bull , vol.50 , pp. 467
    • Perutz, M.F.1
  • 29
    • 0037117499 scopus 로고    scopus 로고
    • Aggregation of proteins with expanded glutamine and alanine repeats of the glutamine-rich and asparagine-rich domains of Sup35 and of the amyloid beta-peptide of amyloid plaques
    • Perutz MF, Pope BJ, Owen D, Wanker EE and Scherzinger E (2002). Aggregation of proteins with expanded glutamine and alanine repeats of the glutamine-rich and asparagine-rich domains of Sup35 and of the amyloid beta-peptide of amyloid plaques. Proc Natl Acad Sci USA 99, 5596-5600
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 5596-5600
    • Perutz, M.F.1    Pope, B.J.2    Owen, D.3    Wanker, E.E.4    Scherzinger, E.5
  • 30
    • 0032539573 scopus 로고    scopus 로고
    • Amyloid fibrils may be assembled from beta-helical protofibrils
    • Lazo ND and Downing DT (1998). Amyloid fibrils may be assembled from beta-helical protofibrils. Biochemistry 37, 1731-1735
    • (1998) Biochemistry , vol.37 , pp. 1731-1735
    • Lazo, N.D.1    Downing, D.T.2
  • 31
    • 0032980443 scopus 로고    scopus 로고
    • Fibril formation by amyloid-beta proteins may involve beta-helical protofibrils
    • Lazo ND and Downing DT (1999). Fibril formation by amyloid-beta proteins may involve beta-helical protofibrils. J Pept Res 53, 633-640
    • (1999) J Pept Res , vol.53 , pp. 633-640
    • Lazo, N.D.1    Downing, D.T.2
  • 32
    • 0033569687 scopus 로고    scopus 로고
    • Molecular modelling indicates that the pathological conformations of prion proteins might be beta-helical
    • Downing DT and Lazo ND (1999). Molecular modelling indicates that the pathological conformations of prion proteins might be beta-helical. Biochem J 343 Pt 2, 453-460
    • (1999) Biochem J , vol.343 , Issue.2 PART , pp. 453-460
    • Downing, D.T.1    Lazo, N.D.2
  • 33
    • 0035543109 scopus 로고    scopus 로고
    • The architecture of parallel beta-helices and related folds
    • Jenkins J and Pickersgill R (2001). The architecture of parallel beta-helices and related folds. Prog Biophys Mol Biol 77, 111-175
    • (2001) Prog Biophys Mol Biol , vol.77 , pp. 111-175
    • Jenkins, J.1    Pickersgill, R.2
  • 34
    • 0036052739 scopus 로고    scopus 로고
    • Ideas of order for amyloid fibril structure
    • Wetzel R (2002). Ideas of order for amyloid fibril structure. Structure 10, 1031-1036
    • (2002) Structure , vol.10 , pp. 1031-1036
    • Wetzel, R.1
  • 35
    • 0037313696 scopus 로고    scopus 로고
    • A primordial structure underlying amyloid
    • Pickersgill RW (2003). A primordial structure underlying amyloid. Structure (Camb) 11, 137-138
    • (2003) Structure (Camb) , vol.11 , pp. 137-138
    • Pickersgill, R.W.1
  • 37
    • 0031793928 scopus 로고    scopus 로고
    • Iterated profile searches with PSI-BLAST-a tool for discovery in protein databases
    • Altschul SF and Koonin EV (1998). Iterated profile searches with PSI-BLAST-a tool for discovery in protein databases. Trends Biochem Sci 23, 444-447
    • (1998) Trends Biochem Sci , vol.23 , pp. 444-447
    • Altschul, S.F.1    Koonin, E.V.2
  • 40
    • 14744304631 scopus 로고    scopus 로고
    • Efficient recognition of protein fold in the twilight and midnight zones by conservative application of Psi-BLAST
    • in press
    • Stevens FJ (2004). Efficient recognition of protein fold in the twilight and midnight zones by conservative application of Psi-BLAST. J Molec Recogn in press
    • (2004) J Molec Recogn
    • Stevens, F.J.1
  • 41
    • 14744304631 scopus 로고    scopus 로고
    • Efficient recognition of protein fold in the twilight and midnight zones: Application
    • in press
    • Stevens FJ, Kuemmel C, Babnigg G and Collart F (2004). Efficient recognition of protein fold in the twilight and midnight zones: Application. J Molec Recogn in press
    • (2004) J Molec Recogn
    • Stevens, F.J.1    Kuemmel, C.2    Babnigg, G.3    Collart, F.4
  • 42
    • 0025830469 scopus 로고
    • A method to identify protein sequences that fold into a known three-dimensional structure
    • Bowie JU, Luthy R and Eisenberg D (1991). A method to identify protein sequences that fold into a known three-dimensional structure. Science 253, 164-170
    • (1991) Science , vol.253 , pp. 164-170
    • Bowie, J.U.1    Luthy, R.2    Eisenberg, D.3
  • 43
    • 0037271276 scopus 로고    scopus 로고
    • Fold recognition methods
    • Godzik A (2003). Fold recognition methods. Methods Biochem Anal 44, 525-546
    • (2003) Methods Biochem Anal , vol.44 , pp. 525-546
    • Godzik, A.1
  • 44
    • 0034595501 scopus 로고    scopus 로고
    • Enhanced genome annotation using structural profiles in the program 3D-PSSM
    • Kelley LA, MacCallum RM and Sternberg MJ (2000). Enhanced genome annotation using structural profiles in the program 3D-PSSM. J Mol Biol 299, 499-520
    • (2000) J Mol Biol , vol.299 , pp. 499-520
    • Kelley, L.A.1    MacCallum, R.M.2    Sternberg, M.J.3
  • 46
    • 0037031949 scopus 로고    scopus 로고
    • A beta-helical antifreeze protein isoform with increased activity. Structural and functional insights
    • Leinala EK, Davies PL, Doucet D, Tyshenko MG, Walker VK and Jia Z (2002). A beta-helical antifreeze protein isoform with increased activity. Structural and functional insights. J Biol Chem 277, 33349-33352
    • (2002) J Biol Chem , vol.277 , pp. 33349-33352
    • Leinala, E.K.1    Davies, P.L.2    Doucet, D.3    Tyshenko, M.G.4    Walker, V.K.5    Jia, Z.6
  • 47
  • 50
  • 53
    • 0029151238 scopus 로고
    • Apolipoprotein E carboxyl-terminal fragments are complexed to amyloids A and L. Implications for amyloidogenesis and Alzheimer's disease
    • Castano EM, Prelli F, Pras M and Frangione B (1995). Apolipoprotein E carboxyl-terminal fragments are complexed to amyloids A and L. Implications for amyloidogenesis and Alzheimer's disease. J Biol Chem 270, 17610-17615
    • (1995) J Biol Chem , vol.270 , pp. 17610-17615
    • Castano, E.M.1    Prelli, F.2    Pras, M.3    Frangione, B.4
  • 54
    • 0037022297 scopus 로고    scopus 로고
    • Conformational Abs recognizing a generic amyloid fibril epitope
    • O'Nuallain B and Wetzel R (2002). Conformational Abs recognizing a generic amyloid fibril epitope. Proc Natl Acad Sci USA 99, 1485-1490
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 1485-1490
    • O'Nuallain, B.1    Wetzel, R.2
  • 56
    • 0347569588 scopus 로고    scopus 로고
    • Immunotherapy in systemic primary (AL) amyloidosis using amyloid-reactive monoclonal antibodies
    • Solomon A, Weiss DT and Wall JS (2003). Immunotherapy in systemic primary (AL) amyloidosis using amyloid-reactive monoclonal antibodies. Cancer Biother Radiopharm 18, 853-860
    • (2003) Cancer Biother Radiopharm , vol.18 , pp. 853-860
    • Solomon, A.1    Weiss, D.T.2    Wall, J.S.3
  • 57
    • 0141791455 scopus 로고    scopus 로고
    • Therapeutic potential of chimeric amyloid-reactive monoclonal antibody 11-1F4
    • Solomon A, Weiss DT and Wall JS (2003). Therapeutic potential of chimeric amyloid-reactive monoclonal antibody 11-1F4. Clin Cancer Res 9, 3831S-3838S
    • (2003) Clin Cancer Res , vol.9
    • Solomon, A.1    Weiss, D.T.2    Wall, J.S.3
  • 59
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson CM (1999). Protein misfolding, evolution and disease. Trends Biochem Sci 24, 329-332
    • (1999) Trends Biochem Sci , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 60
    • 34548200331 scopus 로고    scopus 로고
    • Protein folding and misfolding inside and outside the cell
    • Dobson CM and Ellis RJ (1998). Protein folding and misfolding inside and outside the cell. EMBO 17, 5251-5254
    • (1998) EMBO , vol.17 , pp. 5251-5254
    • Dobson, C.M.1    Ellis, R.J.2
  • 63
    • 0035826234 scopus 로고    scopus 로고
    • Amyloid fibrils from muscle myoglobin
    • Fandrich M, Fletcher MA and Dobson CM (2001). Amyloid fibrils from muscle myoglobin. Nature 410, 165-166
    • (2001) Nature , vol.410 , pp. 165-166
    • Fandrich, M.1    Fletcher, M.A.2    Dobson, C.M.3
  • 65
    • 0037457810 scopus 로고    scopus 로고
    • In vitro characterization of lactoferrin aggregation and amyloid formation
    • Nilsson MR and Dobson CM (2003). In vitro characterization of lactoferrin aggregation and amyloid formation. Biochemistry 42, 375-382
    • (2003) Biochemistry , vol.42 , pp. 375-382
    • Nilsson, M.R.1    Dobson, C.M.2
  • 66
    • 0942276377 scopus 로고    scopus 로고
    • Amyloid fibril formation by lens crystallin proteins and its implications for cataract formation
    • Meehan S, Berry Y, Luisi B, Dobson CM, Carver JA and MacPhee CE (2004). Amyloid fibril formation by lens crystallin proteins and its implications for cataract formation. J Biol Chem 279, 3413-3419
    • (2004) J Biol Chem , vol.279 , pp. 3413-3419
    • Meehan, S.1    Berry, Y.2    Luisi, B.3    Dobson, C.M.4    Carver, J.A.5    MacPhee, C.E.6
  • 67
    • 0033059275 scopus 로고    scopus 로고
    • Amyloid-like aggregates of a plant protein: A case of a sweet-tasting protein, monellin
    • Konno T, Murata K and Nagayama K (1999). Amyloid-like aggregates of a plant protein: a case of a sweet-tasting protein, monellin. FEBS Lett 454, 122-126
    • (1999) FEBS Lett , vol.454 , pp. 122-126
    • Konno, T.1    Murata, K.2    Nagayama, K.3
  • 69
    • 0023052247 scopus 로고
    • Human prion protein cDNA: Molecular cloning, chromosomal mapping, and biological implications
    • Liao YC, Lebo RV, Clawson GA and Smuckler EA (1986). Human prion protein cDNA: molecular cloning, chromosomal mapping, and biological implications. Science 233, 364-367
    • (1986) Science , vol.233 , pp. 364-367
    • Liao, Y.C.1    Lebo, R.V.2    Clawson, G.A.3    Smuckler, E.A.4
  • 70
    • 0023001210 scopus 로고
    • Molecular cloning and complete sequence of prion protein cDNA from mouse brain infected with the scrapie agent
    • Locht C, Chesebro B, Race R and Keith JM (1986). Molecular cloning and complete sequence of prion protein cDNA from mouse brain infected with the scrapie agent. Proc Natl Acad Sci USA 83, 6372-6376
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 6372-6376
    • Locht, C.1    Chesebro, B.2    Race, R.3    Keith, J.M.4
  • 71
    • 0037470178 scopus 로고    scopus 로고
    • Copper binding to the octarepeats of the prion protein. Affinity, specificity, folding, and cooperativity: Insights from circular dichroism
    • Garnett AP and Viles JH (2003). Copper binding to the octarepeats of the prion protein. Affinity, specificity, folding, and cooperativity: insights from circular dichroism. J Biol Chem 278, 6795-6802
    • (2003) J Biol Chem , vol.278 , pp. 6795-6802
    • Garnett, A.P.1    Viles, J.H.2
  • 72
    • 0033430342 scopus 로고    scopus 로고
    • Internal repeats of prion protein and A beta PP, and reciprocal similarity with the amyloid-related proteins
    • Benvenga S, Campenni A and Facchiano A (1999). Internal repeats of prion protein and A beta PP, and reciprocal similarity with the amyloid-related proteins. Amyloid Internat J Clin Exp Invest 6, 250-255
    • (1999) Amyloid Internat J Clin Exp Invest , vol.6 , pp. 250-255
    • Benvenga, S.1    Campenni, A.2    Facchiano, A.3
  • 75
    • 0035799312 scopus 로고    scopus 로고
    • Ablation of the metal ion-induced endocytosis of the prion protein by disease-associated mutation of the octarepeat region
    • Perera WS and Hooper NM (2001). Ablation of the metal ion-induced endocytosis of the prion protein by disease-associated mutation of the octarepeat region. Curr Biol 11, 519-523
    • (2001) Curr Biol , vol.11 , pp. 519-523
    • Perera, W.S.1    Hooper, N.M.2
  • 76
    • 0032509499 scopus 로고    scopus 로고
    • Copper stimulates endocytosis of the prion protein
    • Pauly PC and Harris DA (1998). Copper stimulates endocytosis of the prion protein. J Biol Chem 273, 33107-33110
    • (1998) J Biol Chem , vol.273 , pp. 33107-33110
    • Pauly, P.C.1    Harris, D.A.2
  • 78
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • Caughey B and Lansbury PT (2003). Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu Rev Neurosci 26, 267-298
    • (2003) Annu Rev Neurosci , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 81
    • 0036774262 scopus 로고    scopus 로고
    • Archacal surface layer proteins contain beta propeller, PKD, and beta helix domains and are related to metazoan cell surface proteins
    • Jing H, Takagi J, Liu JH, Lindgren S, Zhang RG. Joachimiak A, Wang JH and Springer TA (2002). Archacal surface layer proteins contain beta propeller, PKD, and beta helix domains and are related to metazoan cell surface proteins. Structure (Camb) 10, 1453-1464
    • (2002) Structure (Camb) , vol.10 , pp. 1453-1464
    • Jing, H.1    Takagi, J.2    Liu, J.H.3    Lindgren, S.4    Zhang, R.G.5    Joachimiak, A.6    Wang, J.H.7    Springer, T.A.8
  • 82
    • 1842562406 scopus 로고    scopus 로고
    • The Yersinia adhesin YadA collagen-binding domain structure is a novel left-handed parallel beta-roll
    • Nummelin H, Merckel MC, Leo JC, Lankinen H, Skurnik M and Goldman A (2004). The Yersinia adhesin YadA collagen-binding domain structure is a novel left-handed parallel beta-roll. Embo J 23, 701-711
    • (2004) Embo J , vol.23 , pp. 701-711
    • Nummelin, H.1    Merckel, M.C.2    Leo, J.C.3    Lankinen, H.4    Skurnik, M.5    Goldman, A.6
  • 83
    • 0037022563 scopus 로고    scopus 로고
    • Natural β-sheet proteins use negative design to avoid edge-to-edge aggregation
    • Richardson JS and Richardson DC (2002). Natural β-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc Natl Acad Sci USA 99, 2754-2759
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 2754-2759
    • Richardson, J.S.1    Richardson, D.C.2
  • 84
    • 0034691568 scopus 로고    scopus 로고
    • Mimicry of ice structure by surface hydroxyls and water of a beta-helix antifreeze protein
    • Liou YC, Tocilj A, Davies PL and Jia Z (2000). Mimicry of ice structure by surface hydroxyls and water of a beta-helix antifreeze protein. Nature 406, 322-324
    • (2000) Nature , vol.406 , pp. 322-324
    • Liou, Y.C.1    Tocilj, A.2    Davies, P.L.3    Jia, Z.4
  • 85
    • 0030732162 scopus 로고    scopus 로고
    • Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation
    • Borhani DW, Rogers DP, Engler JA and Brouillette CG (1997). Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation. Proc Natl Acad Sci USA 94, 12291-12296
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12291-12296
    • Borhani, D.W.1    Rogers, D.P.2    Engler, J.A.3    Brouillette, C.G.4
  • 86
    • 0037342768 scopus 로고    scopus 로고
    • Crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by cold-adapted proteases
    • Aghajari N, Van Petegem F, Villeret V, Chessa JP, Gerday C, Haser R and Van Beeumen J (2003). Crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by cold-adapted proteases. Proteins 50, 636-647
    • (2003) Proteins , vol.50 , pp. 636-647
    • Aghajari, N.1    Van Petegem, F.2    Villeret, V.3    Chessa, J.P.4    Gerday, C.5    Haser, R.6    Van Beeumen, J.7
  • 88
    • 0029645872 scopus 로고
    • The three domains of a bacterial sialidase: A beta-propeller, an immunoglobulin module and a galactose-binding jelly-roll
    • Gaskell A, Crennell S and Taylor G (1995). The three domains of a bacterial sialidase: a beta-propeller, an immunoglobulin module and a galactose-binding jelly-roll. Structure 3, 1197-1205
    • (1995) Structure , vol.3 , pp. 1197-1205
    • Gaskell, A.1    Crennell, S.2    Taylor, G.3
  • 89
    • 0029988488 scopus 로고    scopus 로고
    • Structure of Bordetella pertussis virulence factor P.69 pertactin
    • Emsley P, Charles IG, Fairweather NF and Isaacs NW (1996). Structure of Bordetella pertussis virulence factor P.69 pertactin. Nature 381, 90-92
    • (1996) Nature , vol.381 , pp. 90-92
    • Emsley, P.1    Charles, I.G.2    Fairweather, N.F.3    Isaacs, N.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.