메뉴 건너뛰기




Volumn 53, Issue 20, 2014, Pages 3267-3277

Structural characterization of semen coagulum-derived SEM1(86-107) amyloid fibrils that enhance HIV-1 infection

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANES; GLYCOPROTEINS; MASS SPECTROMETRY; PEPTIDES;

EID: 84901398996     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi500427r     Document Type: Article
Times cited : (15)

References (76)
  • 1
    • 0033016106 scopus 로고    scopus 로고
    • Semenogelin I: A coagulum forming, multifunctional seminal vesicle protein
    • Robert, M. and Gagnon, C. (1999) Semenogelin I: A coagulum forming, multifunctional seminal vesicle protein Cell. Mol. Life Sci. 55, 944-960
    • (1999) Cell. Mol. Life Sci. , vol.55 , pp. 944-960
    • Robert, M.1    Gagnon, C.2
  • 2
    • 33846582018 scopus 로고    scopus 로고
    • Semenogelin, the main protein of the human semen coagulum, regulates sperm function
    • de Lamirande, E. (2007) Semenogelin, the main protein of the human semen coagulum, regulates sperm function Semin. Thromb. Hemostasis 33, 60-68
    • (2007) Semin. Thromb. Hemostasis , vol.33 , pp. 60-68
    • De Lamirande, E.1
  • 3
    • 40949124276 scopus 로고    scopus 로고
    • Physiological roles of semenogelin i and zinc in sperm motility and semen coagulation on ejaculation in humans
    • Yoshida, K., Kawano, N., Yoshiike, M., Yoshida, M., Iwamoto, T., and Morisawa, M. (2008) Physiological roles of semenogelin I and zinc in sperm motility and semen coagulation on ejaculation in humans Mol. Hum. Reprod. 14, 151-156
    • (2008) Mol. Hum. Reprod. , vol.14 , pp. 151-156
    • Yoshida, K.1    Kawano, N.2    Yoshiike, M.3    Yoshida, M.4    Iwamoto, T.5    Morisawa, M.6
  • 4
    • 0242541030 scopus 로고    scopus 로고
    • Quantification of seminal plasma motility inhibitor/semenogelin in human seminal plasma
    • Yoshida, K., Yamasaki, T., Yoshiike, M., Takano, S., Sato, I., and Iwamoto, T. (2003) Quantification of seminal plasma motility inhibitor/semenogelin in human seminal plasma J. Androl. 24, 878-884
    • (2003) J. Androl. , vol.24 , pp. 878-884
    • Yoshida, K.1    Yamasaki, T.2    Yoshiike, M.3    Takano, S.4    Sato, I.5    Iwamoto, T.6
  • 5
    • 0023392052 scopus 로고
    • Seminal vesicle-secreted proteins and their reactions during gelation and liquefaction of human semen
    • Lilja, H., Oldbring, J., Rannevik, G., and Laurell, C. B. (1987) Seminal vesicle-secreted proteins and their reactions during gelation and liquefaction of human semen J. Clin. Invest. 80, 281-285
    • (1987) J. Clin. Invest. , vol.80 , pp. 281-285
    • Lilja, H.1    Oldbring, J.2    Rannevik, G.3    Laurell, C.B.4
  • 6
    • 0024562089 scopus 로고
    • Semenogelin, the predominant protein in human semen. Primary structure and identification of closely related proteins in the male accessory sex glands and on the spermatozoa
    • Lilja, H., Abrahamsson, P. A., and Lundwall, A. (1989) Semenogelin, the predominant protein in human semen. Primary structure and identification of closely related proteins in the male accessory sex glands and on the spermatozoa J. Biol. Chem. 264, 1894-1900
    • (1989) J. Biol. Chem. , vol.264 , pp. 1894-1900
    • Lilja, H.1    Abrahamsson, P.A.2    Lundwall, A.3
  • 9
    • 33746377894 scopus 로고    scopus 로고
    • Protein Misfolding, Functional Amyloid, and Human Disease
    • Chiti, F. and Dobson, C. M. (2006) Protein Misfolding, Functional Amyloid, and Human Disease Annu. Rev. Biochem. 75, 333-366
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 10
    • 84858374665 scopus 로고    scopus 로고
    • The Amyloid State of Proteins in Human Diseases
    • Eisenberg, D. and Jucker, M. (2012) The Amyloid State of Proteins in Human Diseases Cell 148, 1188-1203
    • (2012) Cell , vol.148 , pp. 1188-1203
    • Eisenberg, D.1    Jucker, M.2
  • 11
    • 84887201251 scopus 로고    scopus 로고
    • Seminal Plasma and Semen Amyloids Enhance Cytomegalovirus Infection in Cell Culture
    • Tang, Q., Roan, N. R., and Yamamura, Y. (2013) Seminal Plasma and Semen Amyloids Enhance Cytomegalovirus Infection in Cell Culture J. Virol. 87, 12583-12591
    • (2013) J. Virol. , vol.87 , pp. 12583-12591
    • Tang, Q.1    Roan, N.R.2    Yamamura, Y.3
  • 18
    • 78149248966 scopus 로고    scopus 로고
    • Amyloid-binding Small Molecules Efficiently Block SEVI (Semen-derived Enhancer of Virus Infection)- and Semen-mediated Enhancement of HIV-1 Infection
    • Olsen, J. S., Brown, C., Capule, C. C., Rubinshtein, M., Doran, T. M., Srivastava, R. K., Feng, C., Nilsson, B. L., Yang, J., and Dewhurst, S. (2010) Amyloid-binding Small Molecules Efficiently Block SEVI (Semen-derived Enhancer of Virus Infection)- and Semen-mediated Enhancement of HIV-1 Infection J. Biol. Chem. 285, 35488-35496
    • (2010) J. Biol. Chem. , vol.285 , pp. 35488-35496
    • Olsen, J.S.1    Brown, C.2    Capule, C.C.3    Rubinshtein, M.4    Doran, T.M.5    Srivastava, R.K.6    Feng, C.7    Nilsson, B.L.8    Yang, J.9    Dewhurst, S.10
  • 19
    • 67049115575 scopus 로고    scopus 로고
    • The main green tea polyphenol epigallocatechin-3-gallate counteracts semen-mediated enhancement of HIV infection
    • Hauber, I., Hohenberg, H., Holstermann, B., Hunstein, W., and Hauber, J. (2009) The main green tea polyphenol epigallocatechin-3-gallate counteracts semen-mediated enhancement of HIV infection Proc. Natl. Acad. Sci. U.S.A. 106, 9033-9038
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 9033-9038
    • Hauber, I.1    Hohenberg, H.2    Holstermann, B.3    Hunstein, W.4    Hauber, J.5
  • 20
    • 84871554404 scopus 로고    scopus 로고
    • Core Sequence of PAPf39 Amyloid Fibrils and Mechanism of pH-Dependent Fibril Formation: The Role of Monomer Conformation
    • French, K. C. and Makhatadze, G. I. (2012) Core Sequence of PAPf39 Amyloid Fibrils and Mechanism of pH-Dependent Fibril Formation: The Role of Monomer Conformation Biochemistry 51, 10127-10136
    • (2012) Biochemistry , vol.51 , pp. 10127-10136
    • French, K.C.1    Makhatadze, G.I.2
  • 22
    • 0016160429 scopus 로고
    • Measurement of Protein by Spectrophotometry at 205 nm
    • Scopes, R. K. (1974) Measurement of Protein by Spectrophotometry at 205 nm Anal. Biochem. 59, 277-282
    • (1974) Anal. Biochem. , vol.59 , pp. 277-282
    • Scopes, R.K.1
  • 23
    • 0020855355 scopus 로고
    • Hydrogen exchange and structural dynamics of proteins and nucleic acids
    • Englander, S. W. and Kallenbach, N. R. (1983) Hydrogen exchange and structural dynamics of proteins and nucleic acids Q. Rev. Biophys. 16, 521-655
    • (1983) Q. Rev. Biophys. , vol.16 , pp. 521-655
    • Englander, S.W.1    Kallenbach, N.R.2
  • 24
    • 84984086367 scopus 로고
    • Hydrogen-Tritium Exchange of the Random Chain Polypeptide
    • Englander, S. W. and Poulsen, A. (1969) Hydrogen-Tritium Exchange of the Random Chain Polypeptide Biopolymers 7, 379-393
    • (1969) Biopolymers , vol.7 , pp. 379-393
    • Englander, S.W.1    Poulsen, A.2
  • 27
    • 84885350132 scopus 로고    scopus 로고
    • Protein hydrogen exchange at residue resolution by proteolytic fragmentation mass spectrometry analysis
    • Kan, Z.-Y., Walters, B. T., Mayne, L., and Englander, S. W. (2013) Protein hydrogen exchange at residue resolution by proteolytic fragmentation mass spectrometry analysis Proc. Natl. Acad. Sci. U.S.A. 110, 16438-16443
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 16438-16443
    • Kan, Z.-Y.1    Walters, B.T.2    Mayne, L.3    Englander, S.W.4
  • 29
    • 34548710335 scopus 로고    scopus 로고
    • Probing the Cross-β Core Structure of Amyloid Fibrils by Hydrogen-Deuterium Exchange Deep Ultraviolet Resonance Raman Spectroscopy
    • Xu, M., Shashilov, V., and Lednev, I. K. (2007) Probing the Cross-β Core Structure of Amyloid Fibrils by Hydrogen-Deuterium Exchange Deep Ultraviolet Resonance Raman Spectroscopy J. Am. Chem. Soc. 129, 11002-11003
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 11002-11003
    • Xu, M.1    Shashilov, V.2    Lednev, I.K.3
  • 30
    • 33745041235 scopus 로고    scopus 로고
    • Radiolytic protein footprinting with mass spectrometry to probe the structure of macromolecular complexes
    • Takamoto, K. and Chance, M. R. (2006) Radiolytic protein footprinting with mass spectrometry to probe the structure of macromolecular complexes Annu. Rev. Biophys. Biomol. Struct. 35, 251-276
    • (2006) Annu. Rev. Biophys. Biomol. Struct. , vol.35 , pp. 251-276
    • Takamoto, K.1    Chance, M.R.2
  • 31
    • 84862833364 scopus 로고    scopus 로고
    • Structural Mass Spectrometry of Proteins Using Hydroxyl Radical Based Protein Footprinting
    • Wang, L. and Chance, M. R. (2011) Structural Mass Spectrometry of Proteins Using Hydroxyl Radical Based Protein Footprinting Anal. Chem. 83, 7234-7241
    • (2011) Anal. Chem. , vol.83 , pp. 7234-7241
    • Wang, L.1    Chance, M.R.2
  • 32
    • 24944566705 scopus 로고    scopus 로고
    • Nanosecond laser-induced photochemical oxidation method for protein surface mapping with mass spectrometry
    • Aye, T. T., Low, T. Y., and Sze, S. K. (2005) Nanosecond laser-induced photochemical oxidation method for protein surface mapping with mass spectrometry Anal. Chem. 77, 5814-5822
    • (2005) Anal. Chem. , vol.77 , pp. 5814-5822
    • Aye, T.T.1    Low, T.Y.2    Sze, S.K.3
  • 33
    • 55149093649 scopus 로고    scopus 로고
    • Quantifying protein interface footprinting by hydroxyl radical oxidation and molecular dynamics simulation: Application to galectin-1
    • Charvátová, O., Foley, B. L., Bern, M. W., Sharp, J. S., Orlando, R., and Woods, R. J. (2008) Quantifying protein interface footprinting by hydroxyl radical oxidation and molecular dynamics simulation: Application to galectin-1 J. Am. Soc. Mass Spectrom. 19, 1692-1705
    • (2008) J. Am. Soc. Mass Spectrom. , vol.19 , pp. 1692-1705
    • Charvátová, O.1    Foley, B.L.2    Bern, M.W.3    Sharp, J.S.4    Orlando, R.5    Woods, R.J.6
  • 34
    • 84869451240 scopus 로고    scopus 로고
    • Fast Photochemical Oxidation of Proteins and Mass Spectrometry Follow Submillisecond Protein Folding at the Amino-Acid Level
    • Chen, J. W., Rempel, D. L., Gau, B. C., and Gross, M. L. (2012) Fast Photochemical Oxidation of Proteins and Mass Spectrometry Follow Submillisecond Protein Folding at the Amino-Acid Level J. Am. Chem. Soc. 134, 18724-18731
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 18724-18731
    • Chen, J.W.1    Rempel, D.L.2    Gau, B.C.3    Gross, M.L.4
  • 35
    • 68849107091 scopus 로고    scopus 로고
    • Fast Photochemical Oxidation of Protein Footprints Faster than Protein Unfolding
    • Gau, B. C., Sharp, J. S., Rempel, D. L., and Gross, M. L. (2009) Fast Photochemical Oxidation of Protein Footprints Faster than Protein Unfolding Anal. Chem. 81, 6563-6571
    • (2009) Anal. Chem. , vol.81 , pp. 6563-6571
    • Gau, B.C.1    Sharp, J.S.2    Rempel, D.L.3    Gross, M.L.4
  • 36
    • 65549111220 scopus 로고    scopus 로고
    • Aliphatic Peptidyl Hydroperoxides as a Source of Secondary Oxidation in Hydroxyl Radical Protein Footprinting
    • Saladino, J., Liu, M., Live, D., and Sharp, J. S. (2009) Aliphatic Peptidyl Hydroperoxides as a Source of Secondary Oxidation in Hydroxyl Radical Protein Footprinting J. Am. Soc. Mass Spectrom. 20, 1123-1126
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , pp. 1123-1126
    • Saladino, J.1    Liu, M.2    Live, D.3    Sharp, J.S.4
  • 37
    • 84860758736 scopus 로고    scopus 로고
    • Conformational Analysis of Therapeutic Proteins by Hydroxyl Radical Protein Footprinting
    • Watson, C. and Sharp, J. S. (2012) Conformational Analysis of Therapeutic Proteins by Hydroxyl Radical Protein Footprinting AAPS J. 14, 206-217
    • (2012) AAPS J. , vol.14 , pp. 206-217
    • Watson, C.1    Sharp, J.S.2
  • 38
    • 34548337296 scopus 로고    scopus 로고
    • Hydroxyl radical-mediated modification of proteins as probes for structural proteomics
    • Xu, G. and Chance, M. R. (2007) Hydroxyl radical-mediated modification of proteins as probes for structural proteomics Chem. Rev. 107, 3514-3543
    • (2007) Chem. Rev. , vol.107 , pp. 3514-3543
    • Xu, G.1    Chance, M.R.2
  • 39
    • 0031543338 scopus 로고    scopus 로고
    • A Set of Constructed Type Spectra for the Practical Estimation of Peptide Secondary Structure from Circular Dichroism
    • Reed, J. and Reed, T. A. (1997) A Set of Constructed Type Spectra for the Practical Estimation of Peptide Secondary Structure from Circular Dichroism Anal. Biochem. 254, 36-40
    • (1997) Anal. Biochem. , vol.254 , pp. 36-40
    • Reed, J.1    Reed, T.A.2
  • 40
    • 0022503457 scopus 로고
    • Calculation of protein conformation from circular dichroism
    • Yang, J. T., Wu, C. S., and Martinez, H. M. (1986) Calculation of protein conformation from circular dichroism Methods Enzymol. 130, 208-269
    • (1986) Methods Enzymol. , vol.130 , pp. 208-269
    • Yang, J.T.1    Wu, C.S.2    Martinez, H.M.3
  • 41
    • 3042774002 scopus 로고    scopus 로고
    • The sequences appended to the amyloid core region of the HET-s prion protein determine higher-order aggregate organization in vivo
    • Balguerie, A., Dos Reis, S., Coulary-Salin, B., Chaignepain, S., Sabourin, M., Schmitter, J. M., and Saupe, S. J. (2004) The sequences appended to the amyloid core region of the HET-s prion protein determine higher-order aggregate organization in vivo J. Cell Sci. 117, 2599-2610
    • (2004) J. Cell Sci. , vol.117 , pp. 2599-2610
    • Balguerie, A.1    Dos Reis, S.2    Coulary-Salin, B.3    Chaignepain, S.4    Sabourin, M.5    Schmitter, J.M.6    Saupe, S.J.7
  • 43
    • 24644447303 scopus 로고    scopus 로고
    • Seeding-dependent propagation and maturation of amyloid fibril conformation
    • Yamaguchi, K., Takahashi, S., Kawai, T., Naiki, H., and Goto, Y. (2005) Seeding-dependent propagation and maturation of amyloid fibril conformation J. Mol. Biol. 352, 952-960
    • (2005) J. Mol. Biol. , vol.352 , pp. 952-960
    • Yamaguchi, K.1    Takahashi, S.2    Kawai, T.3    Naiki, H.4    Goto, Y.5
  • 44
    • 66449136918 scopus 로고    scopus 로고
    • Disulfide bond formation significantly accelerates the assembly of Ure2p fibrils because of the proximity of a potential amyloid stretch
    • Fei, L. and Perrett, S. (2009) Disulfide bond formation significantly accelerates the assembly of Ure2p fibrils because of the proximity of a potential amyloid stretch J. Biol. Chem. 284, 11134-11141
    • (2009) J. Biol. Chem. , vol.284 , pp. 11134-11141
    • Fei, L.1    Perrett, S.2
  • 45
    • 0024509805 scopus 로고
    • Fluorometric Determination of Amyloid Fibrils in Vitro Using the Fluorescent Dye, Thioflavin T
    • Naiki, H., Higuchi, K., Hosokawa, M., and Takeda, T. (1989) Fluorometric Determination of Amyloid Fibrils in Vitro Using the Fluorescent Dye, Thioflavin T Anal. Biochem. 177, 244-249
    • (1989) Anal. Biochem. , vol.177 , pp. 244-249
    • Naiki, H.1    Higuchi, K.2    Hosokawa, M.3    Takeda, T.4
  • 46
    • 20544446960 scopus 로고    scopus 로고
    • A Review of the Physical and Chemical Properties of Human Semen and the Formulation of a Semen Simulant
    • Owen, D. H. and Katz, D. F. (2005) A Review of the Physical and Chemical Properties of Human Semen and the Formulation of a Semen Simulant J. Androl. 26, 459-469
    • (2005) J. Androl. , vol.26 , pp. 459-469
    • Owen, D.H.1    Katz, D.F.2
  • 48
    • 77957756752 scopus 로고    scopus 로고
    • Probing the Conformation of a Prion Protein Fibril with Hydrogen Exchange
    • Damo, S. M., Phillips, A. H., Young, A. L., Li, S., Woods, V. L., and Wemmer, D. E. (2010) Probing the Conformation of a Prion Protein Fibril with Hydrogen Exchange J. Biol. Chem. 285, 32303-32311
    • (2010) J. Biol. Chem. , vol.285 , pp. 32303-32311
    • Damo, S.M.1    Phillips, A.H.2    Young, A.L.3    Li, S.4    Woods, V.L.5    Wemmer, D.E.6
  • 49
    • 27344436619 scopus 로고    scopus 로고
    • Structure and properties of α-synuclein and other amyloids determined at the amino acid level
    • Del Mar, C., Greenbaum, E. A., Mayne, L., Englander, S. W., and Woods, V. L. (2005) Structure and properties of α-synuclein and other amyloids determined at the amino acid level Proc. Natl. Acad. Sci. U.S.A. 102, 15477-15482
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 15477-15482
    • Del Mar, C.1    Greenbaum, E.A.2    Mayne, L.3    Englander, S.W.4    Woods, V.L.5
  • 50
    • 33749838193 scopus 로고    scopus 로고
    • Hydrogen/Deuterium Exchange Mass Spectrometry Window into Amyloid Structure
    • Kheterpal, I. and Wetzel, R. (2006) Hydrogen/Deuterium Exchange Mass Spectrometry Window into Amyloid Structure Acc. Chem. Res. 39, 584-593
    • (2006) Acc. Chem. Res. , vol.39 , pp. 584-593
    • Kheterpal, I.1    Wetzel, R.2
  • 51
    • 33846811599 scopus 로고    scopus 로고
    • β-Sheet core of human prion protein amyloid fibrils as determined by hydrogen/deuterium exchange
    • Lu, X., Wintrode, P. L., and Surewicz, W. K. (2007) β-Sheet core of human prion protein amyloid fibrils as determined by hydrogen/deuterium exchange Proc. Natl. Acad. Sci. U.S.A. 104, 1510-1515
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 1510-1515
    • Lu, X.1    Wintrode, P.L.2    Surewicz, W.K.3
  • 52
    • 84868575176 scopus 로고    scopus 로고
    • Minimizing Back Exchange in the Hydrogen Exchange-Mass Spectrometry Experiment
    • Walters, B. T., Ricciuti, A., Mayne, L., and Englander, S. W. (2012) Minimizing Back Exchange in the Hydrogen Exchange-Mass Spectrometry Experiment J. Am. Soc. Mass Spectrom. 23, 2132-2139
    • (2012) J. Am. Soc. Mass Spectrom. , vol.23 , pp. 2132-2139
    • Walters, B.T.1    Ricciuti, A.2    Mayne, L.3    Englander, S.W.4
  • 54
    • 0842283944 scopus 로고    scopus 로고
    • Analysis of Protein Solvent Accessible Surfaces by Photochemical Oxidation and Mass Spectrometry
    • Sharp, J. S., Becker, J. M., and Hettich, R. L. (2004) Analysis of Protein Solvent Accessible Surfaces by Photochemical Oxidation and Mass Spectrometry Anal. Chem. 76, 672-683
    • (2004) Anal. Chem. , vol.76 , pp. 672-683
    • Sharp, J.S.1    Becker, J.M.2    Hettich, R.L.3
  • 55
    • 27844593258 scopus 로고    scopus 로고
    • Laser flash photolysis of hydrogen peroxide to oxidize protein solvent-accessible residues on the microsecond timescale
    • Hambly, D. M. and Gross, M. L. (2005) Laser flash photolysis of hydrogen peroxide to oxidize protein solvent-accessible residues on the microsecond timescale J. Am. Soc. Mass Spectrom. 16, 2057-2063
    • (2005) J. Am. Soc. Mass Spectrom. , vol.16 , pp. 2057-2063
    • Hambly, D.M.1    Gross, M.L.2
  • 56
    • 33947517558 scopus 로고    scopus 로고
    • AGGRESCAN: A server for the prediction and evaluation of "hot spots" of aggregation in polypeptides
    • Conchillo-Sole, O., de Groot, N., Aviles, F., Vendrell, J., Daura, X., and Ventura, S. (2007) AGGRESCAN: A server for the prediction and evaluation of "hot spots" of aggregation in polypeptides BMC Bioinf. 8, 65
    • (2007) BMC Bioinf. , vol.8 , pp. 65
    • Conchillo-Sole, O.1    De Groot, N.2    Aviles, F.3    Vendrell, J.4    Daura, X.5    Ventura, S.6
  • 57
    • 36248964819 scopus 로고    scopus 로고
    • The PASTA server for protein aggregation prediction
    • Trovato, A., Seno, F., and Tosatto, S. C. E. (2007) The PASTA server for protein aggregation prediction Protein Eng., Des. Sel. 20, 521-523
    • (2007) Protein Eng., Des. Sel. , vol.20 , pp. 521-523
    • Trovato, A.1    Seno, F.2    Tosatto, S.C.E.3
  • 59
    • 77649240855 scopus 로고    scopus 로고
    • Identifying the amylome, proteins capable of forming amyloid-like fibrils
    • Goldschmidt, L., Teng, P. K., Riek, R., and Eisenberg, D. (2010) Identifying the amylome, proteins capable of forming amyloid-like fibrils Proc. Natl. Acad. Sci. U.S.A. 107, 3487-3492
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 3487-3492
    • Goldschmidt, L.1    Teng, P.K.2    Riek, R.3    Eisenberg, D.4
  • 61
    • 60849089613 scopus 로고    scopus 로고
    • Prediction of amyloid fibril-forming segments based on a support vector machine
    • Tian, J., Wu, N., Guo, J., and Fan, Y. (2009) Prediction of amyloid fibril-forming segments based on a support vector machine BMC Bioinf. 10, S45
    • (2009) BMC Bioinf. , vol.10 , pp. 45
    • Tian, J.1    Wu, N.2    Guo, J.3    Fan, Y.4
  • 62
    • 73149094532 scopus 로고    scopus 로고
    • Mechanism of Fibril Formation by a 39-Residue Peptide (PAPf39) from Human Prostatic Acidic Phosphatase
    • Ye, Z., French, K. C., Popova, L. A., Lednev, I. K., Lopez, M. M., and Makhatadze, G. I. (2009) Mechanism of Fibril Formation by a 39-Residue Peptide (PAPf39) from Human Prostatic Acidic Phosphatase Biochemistry 48, 11582-11591
    • (2009) Biochemistry , vol.48 , pp. 11582-11591
    • Ye, Z.1    French, K.C.2    Popova, L.A.3    Lednev, I.K.4    Lopez, M.M.5    Makhatadze, G.I.6
  • 64
    • 0030897784 scopus 로고    scopus 로고
    • Vaginal pH neutralization by semen as a cofactor of HIV transmission
    • Bouvet, J.-P., Grésenguet, G., and Bélec, L. (1997) Vaginal pH neutralization by semen as a cofactor of HIV transmission Clin. Microbiol. Infect. 3, 19-23
    • (1997) Clin. Microbiol. Infect. , vol.3 , pp. 19-23
    • Bouvet, J.-P.1    Grésenguet, G.2    Bélec, L.3
  • 65
    • 49849099241 scopus 로고    scopus 로고
    • Bacterial vaginosis and HIV acquisition: A meta-analysis of published studies
    • Atashili, J., Poole, C., Ndumbe, P. M., Adimora, A. A., and Smith, J. S. (2008) Bacterial vaginosis and HIV acquisition: A meta-analysis of published studies AIDS 22, 1493-1501
    • (2008) AIDS , vol.22 , pp. 1493-1501
    • Atashili, J.1    Poole, C.2    Ndumbe, P.M.3    Adimora, A.A.4    Smith, J.S.5
  • 66
    • 3142699791 scopus 로고    scopus 로고
    • Template-assisted filament growth by parallel stacking of tau
    • Margittai, M. and Langen, R. (2004) Template-assisted filament growth by parallel stacking of tau Proc. Natl. Acad. Sci. U.S.A. 101, 10278-10283
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 10278-10283
    • Margittai, M.1    Langen, R.2
  • 67
    • 40849120669 scopus 로고    scopus 로고
    • Amyloid Fibrils of the HET-s(218-289) Prion Form a β Solenoid with a Triangular Hydrophobic Core
    • Wasmer, C., Lange, A., Van Melckebeke, H., Siemer, A. B., Riek, R., and Meier, B. H. (2008) Amyloid Fibrils of the HET-s(218-289) Prion Form a β Solenoid with a Triangular Hydrophobic Core Science 319, 1523-1526
    • (2008) Science , vol.319 , pp. 1523-1526
    • Wasmer, C.1    Lange, A.2    Van Melckebeke, H.3    Siemer, A.B.4    Riek, R.5    Meier, B.H.6
  • 68
    • 2542542833 scopus 로고    scopus 로고
    • A model for Ure2p prion filaments and other amyloids: The parallel superpleated β-structure
    • Kajava, A. V., Baxa, U., Wickner, R. B., and Steven, A. C. (2004) A model for Ure2p prion filaments and other amyloids: The parallel superpleated β-structure Proc. Natl. Acad. Sci. U.S.A. 101, 7885-7890
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 7885-7890
    • Kajava, A.V.1    Baxa, U.2    Wickner, R.B.3    Steven, A.C.4
  • 69
    • 77952305367 scopus 로고    scopus 로고
    • β arcades: Recurring motifs in naturally occurring and disease-related amyloid fibrils
    • Kajava, A. V., Baxa, U., and Steven, A. C. (2010) β arcades: Recurring motifs in naturally occurring and disease-related amyloid fibrils FASEB J. 24, 1311-1319
    • (2010) FASEB J. , vol.24 , pp. 1311-1319
    • Kajava, A.V.1    Baxa, U.2    Steven, A.C.3
  • 70
    • 79952772833 scopus 로고    scopus 로고
    • Structural dependence of HET-s amyloid fibril infectivity assessed by cryoelectron microscopy
    • Mizuno, N., Baxa, U., and Steven, A. C. (2011) Structural dependence of HET-s amyloid fibril infectivity assessed by cryoelectron microscopy Proc. Natl. Acad. Sci. U.S.A. 108, 3252-3257
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 3252-3257
    • Mizuno, N.1    Baxa, U.2    Steven, A.C.3
  • 71
    • 0141733169 scopus 로고    scopus 로고
    • Structural Organization of α-Synuclein Fibrils Studied by Site-directed Spin Labeling
    • Der-Sarkissian, A., Jao, C. C., Chen, J., and Langen, R. (2003) Structural Organization of α-Synuclein Fibrils Studied by Site-directed Spin Labeling J. Biol. Chem. 278, 37530-37535
    • (2003) J. Biol. Chem. , vol.278 , pp. 37530-37535
    • Der-Sarkissian, A.1    Jao, C.C.2    Chen, J.3    Langen, R.4
  • 72
    • 16244376187 scopus 로고    scopus 로고
    • The Parallel Superpleated β-structure as a Model for Amyloid Fibrils of Human Amylin
    • Kajava, A. V., Aebi, U., and Steven, A. C. (2005) The Parallel Superpleated β-structure as a Model for Amyloid Fibrils of Human Amylin J. Mol. Biol. 348, 247-252
    • (2005) J. Mol. Biol. , vol.348 , pp. 247-252
    • Kajava, A.V.1    Aebi, U.2    Steven, A.C.3
  • 74
    • 33646076466 scopus 로고    scopus 로고
    • Standard Conformations of β-Arches in β-Solenoid Proteins
    • Hennetin, J., Jullian, B., Steven, A. C., and Kajava, A. V. (2006) Standard Conformations of β-Arches in β-Solenoid Proteins J. Mol. Biol. 358, 1094-1105
    • (2006) J. Mol. Biol. , vol.358 , pp. 1094-1105
    • Hennetin, J.1    Jullian, B.2    Steven, A.C.3    Kajava, A.V.4
  • 75
    • 0034327349 scopus 로고    scopus 로고
    • Prediction of Tight Turns and Their Types in Proteins
    • Chou, K.-C. (2000) Prediction of Tight Turns and Their Types in Proteins Anal. Biochem. 286, 1-16
    • (2000) Anal. Biochem. , vol.286 , pp. 1-16
    • Chou, K.-C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.