메뉴 건너뛰기




Volumn 41, Issue 9, 2012, Pages 695-704

Inhibition of semen-derived enhancer of virus infection (SEVI) fibrillogenesis by zinc and copper

Author keywords

Amyloidogenic protein; Fibrillization inhibitor; Histidine ionization; Human immunodeficiency virus; Intrinsically unfolded peptide; Sexual transmission

Indexed keywords

AMYLOID; COPPER; HISTIDINE; PEPTIDE FRAGMENT; PROSTATIC ACID PHOSPHATASE (248 286), HUMAN; PROSTATIC ACID PHOSPHATASE (248-286), HUMAN; PROTEIN TYROSINE PHOSPHATASE; ZINC;

EID: 84866528327     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-012-0846-0     Document Type: Article
Times cited : (15)

References (43)
  • 1
    • 0141747176 scopus 로고    scopus 로고
    • Structure and disorder in the ribonuclease s-eptide probed by nmr residual dipolar couplings
    • Alexandrescu AT, Kammerer RA (2003) Structure and disorder in the ribonuclease S-eptide probed by NMR residual dipolar couplings Protein Sci 12:2132-2140
    • (2003) Protein Sci , vol.12 , pp. 2132-2140
    • Alexandrescu, A.T.1    Kammerer, R.A.2
  • 2
    • 0022456807 scopus 로고
    • The measurement of cooperative protein self-assembly by turbidity and other techniques
    • Andreu JM, Timasheff SN (1986) The measurement of cooperative protein self-assembly by turbidity and other techniques Methods Enzymol 130:47-59
    • (1986) Methods Enzymol , vol.130 , pp. 47-59
    • Andreu, J.M.1    Timasheff, S.N.2
  • 3
    • 0036557830 scopus 로고    scopus 로고
    • Preparation of metal ion buffers for biological experimentation: A methods approach with emphasis on iron and zinc
    • Aslamkhan AG, Aslamkhan A, Ahearn GA (2002) Preparation of metal ion buffers for biological experimentation: a methods approach with emphasis on iron and zinc J Exp Zool 292:507-522
    • (2002) J Exp Zool , vol.292 , pp. 507-522
    • Aslamkhan, A.G.1    Aslamkhan, A.2    Ahearn, G.A.3
  • 4
    • 0027250665 scopus 로고
    • Primary structure effects on peptide group hydrogen exchange
    • Bai Y, Milne JS, Mayne L, Englander SW (1993) Primary structure effects on peptide group hydrogen exchange Proteins 17:75-86
    • (1993) Proteins , vol.17 , pp. 75-86
    • Bai, Y.1    Milne, J.S.2    Mayne, L.3    Englander, S.W.4
  • 5
    • 0027999194 scopus 로고
    • Zinc, copper and selenium in reproduction
    • Bedwal RS, Bahuguna A (1994) Zinc, copper and selenium in reproduction Experientia 50:626-640
    • (1994) Experientia , vol.50 , pp. 626-640
    • Bedwal, R.S.1    Bahuguna, A.2
  • 6
    • 0027973029 scopus 로고
    • Zinc levels of serum and cervicovaginal secretion in recurrent vulvovaginal candidiasis
    • Bohler K, Meisinger V, Klade H, Reinthaller A (1994) Zinc levels of serum and cervicovaginal secretion in recurrent vulvovaginal candidiasis Genitourin Med 70:308-310
    • (1994) Genitourin Med , vol.70 , pp. 308-310
    • Bohler, K.1    Meisinger, V.2    Klade, H.3    Reinthaller, A.4
  • 8
    • 79751537254 scopus 로고    scopus 로고
    • The amyloidogenic sevi precursor, pap248-286, is highly unfolded in solution despite an underlying helical tendency
    • Brender JR, Nanga RP, Popovych N, Soong R, Macdonald PM, Ramamoorthy A (2011) The amyloidogenic SEVI precursor, PAP248-286, is highly unfolded in solution despite an underlying helical tendency Biochim Biophys Acta 1808:1161-1169
    • (2011) Biochim Biophys Acta , vol.1808 , pp. 1161-1169
    • Brender, J.R.1    Nanga, R.P.2    Popovych, N.3    Soong, R.4    Macdonald, P.M.5    Ramamoorthy, A.6
  • 9
    • 82455192383 scopus 로고    scopus 로고
    • Selenium copper and zinc in seminal plasma of men with varicocele, relationship with seminal parameters
    • doi 101007/s12011-011-8957-8965
    • Camejo MI, Abdala L, Vivas-Acevedo G, Lozano-Hernandez R, Angeli-Greaves M, Greaves ED (2011) Selenium, Copper and Zinc in seminal plasma of men with varicocele, relationship with seminal parameters Biol Trace Elem Res 143:1247-1254 doi: 10.1007/s12011-011-8957-5
    • (2011) Biol Trace Elem Res , vol.143 , pp. 1247-1254
    • Camejo, M.I.1    Abdala, L.2    Vivas-Acevedo, G.3    Lozano-Hernandez, R.4    Angeli-Greaves, M.5    Greaves, E.D.6
  • 10
    • 0037022186 scopus 로고    scopus 로고
    • Heparin and other glycosaminoglycans stimulate the formation of amyloid fibrils from alpha-synuclein in vitro
    • Cohlberg JA, Li J, Uversky VN, Fink AL (2002) Heparin and other glycosaminoglycans stimulate the formation of amyloid fibrils from alpha-synuclein in vitro Biochemistry 41:1502-1511
    • (2002) Biochemistry , vol.41 , pp. 1502-1511
    • Cohlberg, J.A.1    Li, J.2    Uversky, V.N.3    Fink, A.L.4
  • 11
    • 0018331959 scopus 로고
    • Binding of zn2? By buffers
    • Collier HB (1979) Binding of Zn2? by buffers Clin Chem 25:495-496
    • (1979) Clin Chem , vol.25 , pp. 495-496
    • Collier, H.B.1
  • 13
    • 79953855831 scopus 로고    scopus 로고
    • Enhancement of hiv-1 infectivity by simple, self-assembling modular peptides
    • Easterhoff D, DiMaio JT, Doran TM, Dewhurst S, Nilsson BL (2011) Enhancement of HIV-1 infectivity by simple, self-assembling modular peptides Biophys J 100:1325-1334
    • (2011) Biophys J , vol.100 , pp. 1325-1334
    • Easterhoff, D.1    DiMaio, J.T.2    Doran, T.M.3    Dewhurst, S.4    Nilsson, B.L.5
  • 14
    • 77950689601 scopus 로고    scopus 로고
    • Strategies to increase the reproducibility of protein fibrillization in plate reader assays
    • Giehm L, Otzen DE (2010) Strategies to increase the reproducibility of protein fibrillization in plate reader assays Anal Biochem 400:270-281
    • (2010) Anal Biochem , vol.400 , pp. 270-281
    • Giehm, L.1    Otzen, D.E.2
  • 16
    • 0015391286 scopus 로고
    • Intrauterine contraception with the copper-t device 4 Influence on protein and copper concentrations and enzyme activities in uterine washings
    • Hagenfeldt K (1972) Intrauterine contraception with the copper-T device 4 Influence on protein and copper concentrations and enzyme activities in uterine washings Contraception 6:219-230
    • (1972) Contraception , vol.6 , pp. 219-230
    • Hagenfeldt, K.1
  • 17
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • Harper JD, Lansbury PT Jr. (1997) Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins Annu Rev Biochem 66:385-407
    • (1997) Annu Rev Biochem , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury Jr., P.T.2
  • 18
    • 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, Hauber J (2009) The main green tea polyphenol epigallocatechin-3-gallate counteracts semen-mediated enhancement of HIV infection Proc Natl Acad Sci USA 106:9033-9038
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 9033-9038
    • Hauber, I.1    Hohenberg, H.2    Holstermann, B.3    Hunstein, W.4    Hauber, J.5
  • 19
    • 67650427451 scopus 로고    scopus 로고
    • Fibrils of prostatic acid phosphatase fragments boost infections with xmrv (xenotropic murine leukemia virus-related virus), a human retrovirus associated with prostate cancer
    • Hong S, Klein EA, Das Gupta J, Hanke K, Weight CJ, Nguyen C, Gaughan C, Kim KA, Bannert N, Kirchhoff F, Munch J, Silverman RH (2009) Fibrils of prostatic acid phosphatase fragments boost infections with XMRV (xenotropic murine leukemia virus-related virus), a human retrovirus associated with prostate cancer J Virol 83:6995-7003
    • (2009) J Virol , vol.83 , pp. 6995-7003
    • Hong, S.1    Klein, E.A.2    Das Gupta, J.3    Hanke, K.4    Weight, C.J.5    Nguyen, C.6    Gaughan, C.7    Kim, K.A.8    Bannert, N.9    Kirchhoff, F.10    Munch, J.11    Silverman, R.H.12
  • 20
  • 22
    • 0027502784 scopus 로고
    • Thioflavine t interaction with synthetic alzheimer's disease beta-amyloid peptides: Detection of amyloid aggregation in solution
    • LeVine H 3rd (1993) Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution Protein Sci 2:404-410
    • (1993) Protein Sci , vol.2 , pp. 404-410
    • LeVine III, H.1
  • 24
    • 0035367287 scopus 로고    scopus 로고
    • Kidney dialysis-associated amyloidosis: A molecular role for copper in fiber formation
    • Morgan CJ, Gelfand M, Atreya C, Miranker AD (2001) Kidney dialysis-associated amyloidosis: a molecular role for copper in fiber formation J Mol Biol 309:339-345
    • (2001) J Mol Biol , vol.309 , pp. 339-345
    • Morgan, C.J.1    Gelfand, M.2    Atreya, C.3    Miranker, A.D.4
  • 25
    • 59349083966 scopus 로고    scopus 로고
    • Protein aggregation kinetics, mechanism, and curve-fitting: A review of the literature
    • Morris AM, Watzky MA, Finke RG (2009) Protein aggregation kinetics, mechanism, and curve-fitting: a review of the literature Biochim Biophys Acta 1794:375-397
    • (2009) Biochim Biophys Acta , vol.1794 , pp. 375-397
    • Morris, A.M.1    Watzky, M.A.2    Finke, R.G.3
  • 27
    • 77956654475 scopus 로고    scopus 로고
    • Zn(ii) ions co-secreted with insulin suppress inherent amyloidogenic properties of monomeric insulin
    • Noormagi A, Gavrilova J, Smirnova J, Tougu V, Palumaa P (2010) Zn(II) ions co-secreted with insulin suppress inherent amyloidogenic properties of monomeric insulin Biochem J 430: 511-518
    • (2010) Biochem J , vol.430 , pp. 511-518
    • Noormagi, A.1    Gavrilova, J.2    Smirnova, J.3    Tougu, V.4    Palumaa, P.5
  • 28
    • 78149248966 scopus 로고    scopus 로고
    • Amyloid-binding small molecules efficiently block sevi (semen-derived enhancer of virus infection)-and semenmediated enhancement of hiv-1 infection
    • Olsen JS, Brown C, Capule CC, Rubinshtein M, Doran TM, Srivastava RK, Feng C, Nilsson BL, Yang J, Dewhurst S (2010) Amyloid-binding small molecules efficiently block SEVI (semen-derived enhancer of virus infection)-and semenmediated enhancement of HIV-1 infection J Biol Chem 285:3 5488-35496
    • (2010) J Biol Chem , vol.285 , Issue.3 , pp. 5488-35496
    • 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
  • 29
    • 84859492320 scopus 로고    scopus 로고
    • Seminal plasma accelerates semen-derived enhancer of viral infection (sevi) fibril formation by the prostatic acid phosphatase (pap248-286) peptide
    • Olsen JS, Dimaio JT, Doran TM, Brown C, Nilsson BL, Dewhurst S (2012) Seminal plasma accelerates semen-derived enhancer of viral infection (SEVI) fibril formation by the prostatic acid phosphatase (PAP248-286) peptide J Biol Chem 287:11842-11849
    • (2012) J Biol Chem , vol.287 , pp. 11842-11849
    • Olsen, J.S.1    Dimaio, J.T.2    Doran, T.M.3    Brown, C.4    Nilsson, B.L.5    Dewhurst, S.6
  • 30
    • 20544446960 scopus 로고    scopus 로고
    • A review of the physical and chemical properties of human semen and the formulation of a semen simulant
    • Owen DH, Katz DF (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.Z.2
  • 31
    • 18144374793 scopus 로고    scopus 로고
    • Metal ion-dependent effects of clioquinol on the fibril growth of an amyloid beta peptide
    • Raman B, Ban T, Yamaguchi K, Sakai M, Kawai T, Naiki H, Goto Y (2005) Metal ion-dependent effects of clioquinol on the fibril growth of an amyloid beta peptide J Biol Chem 280:16157-16162
    • (2005) J Biol Chem , vol.280 , pp. 16157-16162
    • Raman, B.1    Ban, T.2    Yamaguchi, K.3    Sakai, M.4    Kawai, T.5    Naiki, H.6    Goto, Y.7
  • 33
    • 0036527699 scopus 로고    scopus 로고
    • Therapeutic strategies for human amyloid diseases
    • Sacchettini JC, Kelly JW (2002) Therapeutic strategies for human amyloid diseases Nat Rev Drug Discov 1:267-275
    • (2002) Nat Rev Drug Discov , vol.1 , pp. 267-275
    • Sacchettini, J.C.1    Kelly, J.W.2
  • 35
    • 77956072590 scopus 로고    scopus 로고
    • Metalloproteomics and metal toxicology of alpha-synuclein
    • Santner A, Uversky VN (2010) Metalloproteomics and metal toxicology of alpha-synuclein Metallomics 2:378-392
    • (2010) Metallomics , vol.2 , pp. 378-392
    • Santner, A.1    Uversky, V.N.2
  • 36
    • 79251588504 scopus 로고    scopus 로고
    • Electrostatic contributions to the stabilities of native proteins and amyloid complexes
    • Sheftic SR, Croke RL, LaRochelle JR, Alexandrescu AT (2009) Electrostatic contributions to the stabilities of native proteins and amyloid complexes Methods Enzymol 466:233-258
    • (2009) Methods Enzymol , vol.466 , pp. 233-258
    • Sheftic, S.R.1    Croke, R.L.2    LaRochelle, J.R.3    Alexandrescu, A.T.4
  • 37
    • 69249236973 scopus 로고    scopus 로고
    • The polyketide cyclase remf from streptomyces resistomycificus contains an unusual octahedral zinc binding site
    • Silvennoinen L, Sandalova T, Schneider G (2009) The polyketide cyclase RemF from Streptomyces resistomycificus contains an unusual octahedral zinc binding site FEBS Lett 583:2917-2921
    • (2009) FEBS Lett , vol.583 , pp. 2917-2921
    • Silvennoinen, L.1    Sandalova, T.2    Schneider, G.3
  • 38
    • 74749091456 scopus 로고    scopus 로고
    • Prion protein and metal interaction: Physiological and pathological implications
    • Singh N, Das D, Singh A, Mohan ML (2010) Prion protein and metal interaction: physiological and pathological implications Curr Issues Mol Biol 12:99-107
    • (2010) Curr Issues Mol Biol , vol.12 , pp. 99-107
    • Singh, N.1    Das, D.2    Singh, A.3    Mohan, M.L.4
  • 40
    • 79952513228 scopus 로고    scopus 로고
    • Interactions of zn(ii) and cu(ii) ions with alzheimer's amyloid-beta peptide Metal ion binding, contribution to fibrillization and toxicity
    • Tougu V, Tiiman A, Palumaa P (2011) Interactions of Zn(II) and Cu(II) ions with Alzheimer's amyloid-beta peptide Metal ion binding, contribution to fibrillization and toxicity Metallomics 3:250-261
    • (2011) Metallomics , vol.3 , pp. 250-261
    • Tougu, V.1    Tiiman, A.2    Palumaa, P.3
  • 41
    • 33846817163 scopus 로고    scopus 로고
    • Relationships between the sequence of alpha-synuclein and its membrane affinity, fibrillization propensity, and yeast toxicity
    • Volles MJ, Lansbury PT Jr. (2007) Relationships between the sequence of alpha-synuclein and its membrane affinity, fibrillization propensity, and yeast toxicity J Mol Biol 366:1510-1522
    • (2007) J Mol Biol , vol.366 , pp. 1510-1522
    • Volles, M.J.1    Lansbury Jr., P.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.