메뉴 건너뛰기




Volumn 819, Issue , 2012, Pages 199-220

AGGRESCAN: Method, application, and perspectives for drug design

Author keywords

AGGRESCAN; Amyloid; Biomaterials; Inclusion bodies; Protein aggregation; Protein misfolding; Protein production

Indexed keywords

AMYLOID BETA PROTEIN; PEPTIDE; PREALBUMIN; PROTEIN;

EID: 84855926368     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-61779-465-0_14     Document Type: Article
Times cited : (65)

References (56)
  • 1
    • 0141831834 scopus 로고    scopus 로고
    • Bioprocessing of therapeutic proteins from the inclusion bodies of Escherichia coli
    • Panda, A. K. (2003) Bioprocessing of therapeutic proteins from the inclusion bodies of Escherichia coli, Adv Biochem Eng Biotechnol 85, 43-93.
    • (2003) Adv Biochem Eng Biotechnol , vol.85 , pp. 43-93
    • Panda, A.K.1
  • 3
    • 33748041958 scopus 로고    scopus 로고
    • Effects of protein aggregates: An Immunologic perspective
    • DOI 10.1208/aapsj080359, 59
    • Rosenberg, A. S. (2006) Effects of protein aggregates: an immunologic perspective, AAPS J 8, E501-507. (Pubitemid 44294011)
    • (2006) AAPS Journal , vol.8 , Issue.3
    • Rosenberg, A.S.1
  • 4
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • DOI 10.1146/annurev.biochem.75.101304.123901
    • Chiti, F., and Dobson, C. M. (2006) Protein misfolding, functional amyloid, and human disease, Annu Rev Biochem 75, 333-366. (Pubitemid 44118036)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 5
    • 78650081316 scopus 로고    scopus 로고
    • Protein aggregation from inclusion bodies to amyloid and biomaterials
    • Mitraki, A. Protein aggregation from inclusion bodies to amyloid and biomaterials, Adv Protein Chem Struct Biol 79, 89-125.
    • Adv Protein Chem Struct Biol , vol.79 , pp. 89-125
    • Mitraki, A.1
  • 6
    • 0042467550 scopus 로고    scopus 로고
    • Rationalization of the effects of mutations on peptide and protein aggregation rates
    • DOI 10.1038/nature01891
    • Chiti, F., Stefani, M., Taddei, N., Ramponi, G., and Dobson, C. M. (2003) Rationalization of the effects of mutations on peptide and protein aggregation rates, Nature 424, 805-808. (Pubitemid 37021713)
    • (2003) Nature , vol.424 , Issue.6950 , pp. 805-808
    • Chiti, F.1    Stefani, M.2    Taddel, N.3    Ramponi, G.4    Dobson, C.M.5
  • 9
    • 29444444251 scopus 로고    scopus 로고
    • How evolutionary pressure against protein aggregation shaped chaperone specificity
    • DOI 10.1016/j.jmb.2005.11.035, PII S002228360501421X
    • Rousseau, F., Serrano, L., and Schymkowitz, J. W. (2006) How evolutionary pressure against protein aggregation shaped chaperone specificity, J Mol Biol 355, 1037-1047. (Pubitemid 43012146)
    • (2006) Journal of Molecular Biology , vol.355 , Issue.5 , pp. 1037-1047
    • Rousseau, F.1    Serrano, L.2    Schymkowitz, J.W.H.3
  • 10
  • 11
    • 0034730203 scopus 로고    scopus 로고
    • Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: A structural clue to amyloid assembly
    • Otzen, D. E., Kristensen, O., and Oliveberg, M. (2000) Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: a structural clue to amyloid assembly, Proc Natl Acad Sci U S A 97, 9907-9912.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 9907-9912
    • Otzen, D.E.1    Kristensen, O.2    Oliveberg, M.3
  • 13
    • 3242785264 scopus 로고    scopus 로고
    • Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains
    • DOI 10.1016/j.jmb.2004.06.043, PII S0022283604006837
    • DuBay, K. F., Pawar, A. P., Chiti, F., Zurdo, J., Dobson, C. M., and Vendruscolo, M. (2004) Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains, J Mol Biol 341, 1317-1326. (Pubitemid 39092317)
    • (2004) Journal of Molecular Biology , vol.341 , Issue.5 , pp. 1317-1326
    • DuBay, K.F.1    Pawar, A.P.2    Chiti, F.3    Zurdo, J.4    Dobson, C.M.5    Vendruscolo, M.6
  • 15
    • 5044235541 scopus 로고    scopus 로고
    • Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
    • DOI 10.1038/nbt1012
    • Fernandez-Escamilla, A. M., Rousseau, F., Schymkowitz, J., and Serrano, L. (2004) Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins, Nat Biotechnol 22, 1302-1306. (Pubitemid 39336784)
    • (2004) Nature Biotechnology , vol.22 , Issue.10 , pp. 1302-1306
    • Fernandez-Escamilla, A.-M.1    Rousseau, F.2    Schymkowitz, J.3    Serrano, L.4
  • 16
    • 68249083699 scopus 로고    scopus 로고
    • Effects of disulfide bond formation and protein helicity on the aggregation of activating transcription factor 5
    • Ciaccio, N. A., and Laurence, J. S. (2009) Effects of disulfide bond formation and protein helicity on the aggregation of activating transcription factor 5, Mol Pharm 6, 1205-1215.
    • (2009) Mol Pharm , vol.6 , pp. 1205-1215
    • Ciaccio, N.A.1    Laurence, J.S.2
  • 17
    • 77949516611 scopus 로고    scopus 로고
    • Using simple artificial intelligence methods for predicting amyloidogenesis in antibodies
    • David, M. P., Concepcion, G. P., and Padlan, E. A. Using simple artificial intelligence methods for predicting amyloidogenesis in antibodies, BMC Bioinformatics 11, 79.
    • BMC Bioinformatics , vol.11 , pp. 79
    • David, M.P.1    Concepcion, G.P.2    Padlan, E.A.3
  • 19
    • 77949466236 scopus 로고    scopus 로고
    • Cytotoxic aggregation and amyloid formation by the myostatin precursor protein
    • Starck, C. S., and Sutherland-Smith, A. J. Cytotoxic aggregation and amyloid formation by the myostatin precursor protein, PLoS One 5, e9170.
    • PLoS One , vol.5
    • Starck, C.S.1    Sutherland-Smith, A.J.2
  • 20
    • 52049108928 scopus 로고    scopus 로고
    • Structural and functional properties of peptides based on the Nterminus of HIV-1 gp41 and the C-terminus of the amyloid-beta protein
    • Gordon, L. M., Nisthal, A., Lee, A. B., Eskandari, S., Ruchala, P., Jung, C. L., Waring, A. J., and Mobley, P.W. (2008) Structural and functional properties of peptides based on the Nterminus of HIV-1 gp41 and the C-terminus of the amyloid-beta protein, Biochim Biophys Acta 1778, 2127-2137.
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 2127-2137
    • Gordon, L.M.1    Nisthal, A.2    Lee, A.B.3    Eskandari, S.4    Ruchala, P.5    Jung, L.6    Waring, C.A.J.7    Mobley, P.W.8
  • 22
    • 56349130674 scopus 로고    scopus 로고
    • Towards quantitative predictions in cell biology using chemical properties of proteins
    • Vendruscolo, M., and Tartaglia, G. G. (2008) Towards quantitative predictions in cell biology using chemical properties of proteins, Mol Biosyst 4, 1170-1175.
    • (2008) Mol Biosyst , vol.4 , pp. 1170-1175
    • Vendruscolo, M.1    Tartaglia, G.G.2
  • 23
    • 77949692501 scopus 로고    scopus 로고
    • Protein aggregation profile of the bacterial cytosol
    • de Groot, N. S., and Ventura, S. Protein aggregation profile of the bacterial cytosol, PLoS One 5, e9383.
    • PLoS One , vol.5
    • De Groot, N.S.1    Ventura, S.2
  • 24
    • 33846565857 scopus 로고    scopus 로고
    • Early kinetics of amyloid fibril formation reveals conformational reorganisation of initial aggregates
    • DOI 10.1016/j.jmb.2006.12.007, PII S0022283606016664
    • Cerda-Costa, N., Esteras-Chopo, A., Aviles, F. X., Serrano, L., and Villegas, V. (2007) Early kinetics of amyloid fibril formation reveals conformational reorganisation of initial aggregates, J Mol Biol 366, 1351-1363. (Pubitemid 46186391)
    • (2007) Journal of Molecular Biology , vol.366 , Issue.4 , pp. 1351-1363
    • Cerda-Costa, N.1    Esteras-Chopo, A.2    Aviles, F.X.3    Serrano, L.4    Villegas, V.5
  • 26
    • 33644940173 scopus 로고    scopus 로고
    • Mutagenesis of the central hydrophobic cluster in Abeta42 Alzheimer's peptide. Side-chain properties correlate with aggregation propensities
    • de Groot, N. S., Aviles, F. X., Vendrell, J., and Ventura, S. (2006) Mutagenesis of the central hydrophobic cluster in Abeta42 Alzheimer's peptide. Side-chain properties correlate with aggregation propensities, FEBS J 273, 658-668.
    • (2006) FEBS J , vol.273 , pp. 658-668
    • De Groot, N.S.1    Aviles, F.X.2    Vendrell, J.3    Ventura, S.4
  • 28
    • 42649110014 scopus 로고    scopus 로고
    • The in vivo and in vitro aggregation properties of globular proteins correlate with their conformational stability: The SH3 case
    • Espargaro, A., Castillo, V., de Groot, N. S., and Ventura, S. (2008) The in vivo and in vitro aggregation properties of globular proteins correlate with their conformational stability: the SH3 case, J Mol Biol 378, 1116-1131.
    • (2008) J Mol Biol , vol.378 , pp. 1116-1131
    • Espargaro, A.1    Castillo, V.2    De Groot, N.S.3    Ventura, S.4
  • 29
    • 70049090962 scopus 로고    scopus 로고
    • Amyloidogenic regions and interaction surfaces overlap in globular proteins related to conformational diseases
    • Castillo, V., and Ventura, S. (2009) Amyloidogenic regions and interaction surfaces overlap in globular proteins related to conformational diseases, PLoS Comput Biol 5, e1000476.
    • (2009) PLoS Comput Biol , vol.5
    • Castillo, V.1    Ventura, S.2
  • 30
    • 67649274356 scopus 로고    scopus 로고
    • Binding of amphipathic alpha-helical antimicrobial peptides to lipid membranes: Lessons from temporins B and L
    • Mahalka, A. K., and Kinnunen, P. K. (2009) Binding of amphipathic alpha-helical antimicrobial peptides to lipid membranes: lessons from temporins B and L, Biochim Biophys Acta 1788, 1600-1609.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 1600-1609
    • Mahalka, A.K.1    Kinnunen, P.K.2
  • 33
    • 58849147963 scopus 로고    scopus 로고
    • Thermal aggregation of a model allosteric protein in different conformational states
    • Sabbaghian, M., Ebrahim-Habibi, A., and Nemat-Gorgani, M. (2009) Thermal aggregation of a model allosteric protein in different conformational states, Int J Biol Macromol 44, 156-162.
    • (2009) Int J Biol Macromol , vol.44 , pp. 156-162
    • Sabbaghian, M.1    Ebrahim-Habibi, A.2    Nemat-Gorgani, M.3
  • 34
    • 39049165852 scopus 로고    scopus 로고
    • Characterization of Apin, a secreted protein highly expressed in tooth-associated epithelia
    • DOI 10.1002/jcb.21465
    • Moffatt, P., Smith, C. E., St-Arnaud, R., and Nanci, A. (2008) Characterization of Apin, a secreted protein highly expressed in toothassociated epithelia, J Cell Biochem 103, 941-956. (Pubitemid 351240629)
    • (2008) Journal of Cellular Biochemistry , vol.103 , Issue.3 , pp. 941-956
    • Moffatt, P.1    Smith, C.E.2    St-Arnaud, R.3    Nanci, A.4
  • 35
    • 77949586101 scopus 로고    scopus 로고
    • Comparison of human RNase 3 and RNase 7 bactericidal action at the Gram-negative and Gram-positive bacterial cell wall
    • Torrent, M., Badia, M., Moussaoui, M., Sanchez, D., Nogues, M. V., and Boix, E. Comparison of human RNase 3 and RNase 7 bactericidal action at the Gram-negative and Gram-positive bacterial cell wall, FEBS J 277, 1713-1725.
    • FEBS J , vol.277 , pp. 1713-1725
    • Torrent, M.1    Badia, M.2    Moussaoui, M.3    Sanchez, D.4    Nogues, M.V.5    Boix, E.6
  • 36
    • 65249140613 scopus 로고    scopus 로고
    • Comparison of the membrane interaction mechanism of two antimicrobial RNases: RNase 3/ ECP and RNase 7
    • Torrent, M., Sanchez, D., Buzon, V., Nogues, M. V., Cladera, J., and Boix, E. (2009) Comparison of the membrane interaction mechanism of two antimicrobial RNases: RNase 3/ ECP and RNase 7, Biochim Biophys Acta 1788, 1116-1125.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 1116-1125
    • Torrent, M.1    Sanchez, D.2    Buzon, V.3    Nogues, M.V.4    Cladera, J.5    Boix, E.6
  • 39
    • 0036669897 scopus 로고    scopus 로고
    • Inhibition of toxicity and protofibril formation in the amyloid-β peptide β(25-35) using N-methylated derivatives
    • DOI 10.1042/BST0300537
    • Doig, A. J., Hughes, E., Burke, R. M., Su, T. J., Heenan, R. K., and Lu, J. (2002) Inhibition of toxicity and protofibril formation in the amyloid-beta peptide beta(25-35) using Nmethylated derivatives, Biochem Soc Trans 30, 537-542. (Pubitemid 35001594)
    • (2002) Biochemical Society Transactions , vol.30 , Issue.4 , pp. 537-542
    • Doig, A.J.1    Hughes, E.2    Burke, R.M.3    Su, T.J.4    Heenan, R.K.5    Lu, J.6
  • 40
    • 18244365849 scopus 로고    scopus 로고
    • Protein drug stability: A formulation challenge
    • DOI 10.1038/nrd1695
    • Frokjaer, S., and Otzen, D. E. (2005) Protein drug stability: a formulation challenge, Nat Rev Drug Discov 4, 298-306. (Pubitemid 41130943)
    • (2005) Nature Reviews Drug Discovery , vol.4 , Issue.4 , pp. 298-306
    • Frokjaer, S.1    Otzen, D.E.2
  • 41
    • 77954502545 scopus 로고    scopus 로고
    • A more precise characterization of chaperonin substrates
    • Raineri, E., Ribeca, P., Serrano, L., and Maier, T. A more precise characterization of chaperonin substrates, Bioinformatics 26, 1685-1689.
    • Bioinformatics , vol.26 , pp. 1685-1689
    • Raineri, E.1    Ribeca, P.2    Serrano, L.3    Maier, T.4
  • 42
    • 76849089849 scopus 로고
    • Chemical modification of lysine residues in lysozyme may dramatically influence its amyloid fibrillation
    • Morshedi, D., Ebrahim-Habibi, A., Moosavi-Movahedi, A. A., and Nemat-Gorgani, M. Chemical modification of lysine residues in lysozyme may dramatically influence its amyloid fibrillation, Biochim Biophys Acta 1804, 714-722.
    • (1804) Biochim Biophys Acta , pp. 714-722
    • Morshedi, D.1    Ebrahim-Habibi, A.2    Moosavi-Movahedi, A.A.3    Nemat-Gorgani, M.4
  • 43
    • 77955578891 scopus 로고    scopus 로고
    • Eosinophil cationic protein aggregation: Identification of an N-terminus amyloid prone region
    • Torrent, M., Odorizzi, F., Nogués, M., and Boix, E. (2010) Eosinophil Cationic Protein Aggregation: Identification of an N-Terminus Amyloid Prone Region, Biomacromolecules 11, 1983-1990.
    • (2010) Biomacromolecules , vol.11 , pp. 1983-1990
    • Torrent, M.1    Odorizzi, F.2    Nogués, M.3    Boix, E.4
  • 46
    • 67651236366 scopus 로고    scopus 로고
    • Common key-signals in learning and neurodegeneration: Focus on excito-amino acids, betaamyloid peptides and alpha-synuclein
    • Agnati, L. F., Leo, G., Genedani, S., Piron, L., Rivera, A., Guidolin, D., and Fuxe, K. (2009) Common key-signals in learning and neurodegeneration: focus on excito-amino acids, betaamyloid peptides and alpha-synuclein, J Neural Transm 116, 953-974.
    • (2009) J Neural Transm , vol.116 , pp. 953-974
    • Agnati, L.F.1    Leo, G.2    Genedani, S.3    Piron, L.4    Rivera, A.5    Guidolin, D.6    Fuxe, K.7
  • 47
    • 34547646436 scopus 로고    scopus 로고
    • The distribution of residues in a polypeptide sequence is a determinant of aggregation optimized by evolution
    • DOI 10.1529/biophysj.107.111336
    • Monsellier, E., Ramazzotti, M., de Laureto, P. P., Tartaglia, G. G., Taddei, N., Fontana, A., Vendruscolo, M., and Chiti, F. (2007) The distribution of residues in a polypeptide sequence is a determinant of aggregation optimized by evolution, Biophys J 93, 4382-4391. (Pubitemid 350294484)
    • (2007) Biophysical Journal , vol.93 , Issue.12 , pp. 4382-4391
    • Monsellier, E.1    Ramazzotti, M.2    De Laureto, P.P.3    Tartaglia, G.-G.4    Taddei, N.5    Fontana, A.6    Vendruscolo, M.7    Chiti, F.8
  • 48
    • 65849165676 scopus 로고    scopus 로고
    • Competition between intramolecular and intermolecular interactions in an amyloidforming protein
    • Routledge, K. E., Tartaglia, G. G., Platt, G.W., Vendruscolo, M., and Radford, S. E. (2009) Competition between intramolecular and intermolecular interactions in an amyloidforming protein, J Mol Biol 389, 776-786.
    • (2009) J Mol Biol , vol.389 , pp. 776-786
    • Routledge, K.E.1    Tartaglia, G.G.2    Platt, G.W.3    Vendruscolo, M.4    Radford, S.E.5
  • 49
    • 73649102728 scopus 로고    scopus 로고
    • Analysis of a new crystal form of procarboxypeptidase B: Further insights into the catalytic mechanism
    • Fernandez, D., Boix, E., Pallares, I., Aviles, F. X., and Vendrell, J. Analysis of a new crystal form of procarboxypeptidase B: further insights into the catalytic mechanism, Biopolymers 93, 178-185.
    • Biopolymers , vol.93 , pp. 178-185
    • Fernandez, D.1    Boix, E.2    Pallares, I.3    Aviles, F.X.4    Vendrell, J.5
  • 50
    • 84855923610 scopus 로고    scopus 로고
    • FASTA format description
    • FASTA format description: http://www.ncbi. nlm.nih.gov/BLAST/ blastcgihelp.shtml.
  • 51
    • 56349116391 scopus 로고    scopus 로고
    • Molecular genetics of Alzheimer's disease: An update
    • Brouwers, N., Sleegers, K., and Van Broeckhoven, C. (2008) Molecular genetics of Alzheimer's disease: an update, Ann Med 40, 562-583.
    • (2008) Ann Med , vol.40 , pp. 562-583
    • Brouwers, N.1    Sleegers, K.2    Van Broeckhoven, C.3
  • 53
    • 0033526553 scopus 로고    scopus 로고
    • β-Sheet breaker peptide inhibitor of Alzheimer's amyloidogenesis with increased blood-brain barrier permeability and resistance to proteolytic degradation in plasma
    • DOI 10.1002/(SICI)1097-4695(19990605)39:3<371::AID-NEU4>3.0.CO;2-E
    • Poduslo, J. F., Curran, G. L., Kumar, A., Frangione, B., and Soto, C. (1999) Beta-sheet breaker peptide inhibitor of Alzheimer's amyloidogenesis with increased blood-brain barrier permeability and resistance to proteolytic degradation in plasma, J Neurobiol 39, 371-382. (Pubitemid 29239200)
    • (1999) Journal of Neurobiology , vol.39 , Issue.3 , pp. 371-382
    • Poduslo, J.F.1    Curran, G.L.2    Kumar, A.3    Frangione, B.4    Soto, C.5
  • 54
    • 78349308081 scopus 로고    scopus 로고
    • The role of protein sequence and amino acid composition in amyloid formation: Scrambling and reading backwards IAPP amyloid fibrils
    • Sabate, R., Espargaro, A., de Groot, N. S., Valle-Delgado, J. J., Fernandez-Busquets, X., and Ventura, S. (2010) The Role of Protein Sequence and Amino Acid Composition in Amyloid Formation: Scrambling and Reading Backwards IAPP Amyloid Fibrils, J Mol Biol 404, 337-352.
    • (2010) J Mol Biol , vol.404 , pp. 337-352
    • Sabate, R.1    Espargaro, A.2    De Groot, N.S.3    Valle-Delgado, J.J.4    Fernandez-Busquets, X.5    Ventura, S.6
  • 55
    • 32344448608 scopus 로고    scopus 로고
    • Protein aggregation and amyloidosis: Confusion of the kinds?
    • DOI 10.1016/j.sbi.2006.01.011, PII S0959440X06000121
    • Rousseau, F., Schymkowitz, J., and Serrano, L. (2006) Protein aggregation and amyloidosis: confusion of the kinds?, Curr Opin Struct Biol 16, 118-126. (Pubitemid 43221880)
    • (2006) Current Opinion in Structural Biology , vol.16 , Issue.1 , pp. 118-126
    • Rousseau, F.1    Schymkowitz, J.2    Serrano, L.3
  • 56
    • 57749098600 scopus 로고    scopus 로고
    • Amyloid formation by globular proteins under native conditions
    • Chiti, F., and Dobson, C. M. (2009) Amyloid formation by globular proteins under native conditions, Nat Chem Biol 5, 15-22.
    • (2009) Nat Chem Biol , vol.5 , pp. 15-22
    • Chiti, F.1    Dobson, C.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.