메뉴 건너뛰기




Volumn 95, Issue 2, 2006, Pages 237-247

Effect of pH and ionic strength on the physical stability of adenovirus type 5

Author keywords

Absorption spectroscopy; Adenoviral vector; Fluorescence spectroscopy; Gene vectors; Light scattering (dynamic); Physical stability; Spectroscopy; UV Vis spectroscopy; Vaccines; Viral vectors

Indexed keywords

ADENOVIRUS VECTOR; VIRUS DNA; VIRUS VACCINE;

EID: 32644437409     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.20496     Document Type: Article
Times cited : (78)

References (36)
  • 2
    • 0027184774 scopus 로고
    • Difference imaging of adenovirus: Bridging the resolution gap between X-ray crystallography and electron microscopy
    • Stewart PL, Fuller SD, Burnett RM. 1993. Difference imaging of adenovirus: Bridging the resolution gap between X-ray crystallography and electron microscopy. Embo J 12:2589-2599.
    • (1993) Embo J , vol.12 , pp. 2589-2599
    • Stewart, P.L.1    Fuller, S.D.2    Burnett, R.M.3
  • 3
  • 6
    • 0014139233 scopus 로고
    • The effect of heat on the anatomy of the adenovirus
    • Russell WC, Valentine RC, Pereira HG. 1967. The effect of heat on the anatomy of the adenovirus. J Gen Virol 1:509-522.
    • (1967) J Gen Virol , vol.1 , pp. 509-522
    • Russell, W.C.1    Valentine, R.C.2    Pereira, H.G.3
  • 7
    • 0018372398 scopus 로고
    • Adenovirus aggregation and preservation in extracellular environment
    • Galdiero F. 1979. Adenovirus aggregation and preservation in extracellular environment. Arch Virol 59:99-105.
    • (1979) Arch Virol , vol.59 , pp. 99-105
    • Galdiero, F.1
  • 9
    • 0027496645 scopus 로고
    • Stepwise dismantling of adenovirus 2 during entry into cells
    • Greber UF, Willetts M, Webster P, Helenius A. 1993. Stepwise dismantling of adenovirus 2 during entry into cells. Cell 75:477-486.
    • (1993) Cell , vol.75 , pp. 477-486
    • Greber, U.F.1    Willetts, M.2    Webster, P.3    Helenius, A.4
  • 11
    • 0035477074 scopus 로고    scopus 로고
    • Stabilization of recombinant adenovirus: Site-directed mutagenesis of key asparagine residues in the hexon protein
    • Blanche F, Cameron B, Somarriba S, Maton L, Barbot A, Guillemin T. 2001. Stabilization of recombinant adenovirus: Site-directed mutagenesis of key asparagine residues in the hexon protein. Anal Biochem 297:1-9.
    • (2001) Anal Biochem , vol.297 , pp. 1-9
    • Blanche, F.1    Cameron, B.2    Somarriba, S.3    Maton, L.4    Barbot, A.5    Guillemin, T.6
  • 12
    • 0034823799 scopus 로고    scopus 로고
    • Development of formulations that enhance physical stability of viral vectors for gene therapy
    • Croyle MA, Cheng X, Wilson JM. 2001. Development of formulations that enhance physical stability of viral vectors for gene therapy. Gene Ther 8:1281-1290.
    • (2001) Gene Ther , vol.8 , pp. 1281-1290
    • Croyle, M.A.1    Cheng, X.2    Wilson, J.M.3
  • 14
    • 0141455064 scopus 로고    scopus 로고
    • PEGylated adenoviruses for gene delivery to the intestinal epithelium by the oral route
    • Cheng X, Ming X, Croyle MA. 2003. PEGylated adenoviruses for gene delivery to the intestinal epithelium by the oral route. Pharm Res 20:1444-1451.
    • (2003) Pharm Res , vol.20 , pp. 1444-1451
    • Cheng, X.1    Ming, X.2    Croyle, M.A.3
  • 15
    • 0035812633 scopus 로고    scopus 로고
    • Rough energy landscapes in protein folding: Dimeric E. coli Trp repressor folds through three parallel channels
    • Gloss LM, Simler BR, Matthews CR. 2001. Rough energy landscapes in protein folding: Dimeric E. coli Trp repressor folds through three parallel channels. J Mol Biol 312:1121-1134.
    • (2001) J Mol Biol , vol.312 , pp. 1121-1134
    • Gloss, L.M.1    Simler, B.R.2    Matthews, C.R.3
  • 17
    • 0035916258 scopus 로고    scopus 로고
    • Effect of salts on the stability and folding of staphylococcal nuclease
    • Nishimura C, Uversky VN, Fink AL. 2001. Effect of salts on the stability and folding of staphylococcal nuclease. Biochemistry 40(7):2113-2128.
    • (2001) Biochemistry , vol.40 , Issue.7 , pp. 2113-2128
    • Nishimura, C.1    Uversky, V.N.2    Fink, A.L.3
  • 18
    • 0024276805 scopus 로고
    • Ribonuclease T1 is stabilized by cation and anion binding
    • Pace CN, Grimsley GR. 1988. Ribonuclease T1 is stabilized by cation and anion binding. Biochemistry 27:3242-3246.
    • (1988) Biochemistry , vol.27 , pp. 3242-3246
    • Pace, C.N.1    Grimsley, G.R.2
  • 19
    • 0041336626 scopus 로고    scopus 로고
    • Derivative absorbance spectroscopy and protein phase diagrams as tools for comprehensive protein characterization: A bGCSF case study
    • Kueltzo LA, Ersoy B, Ralston JP, Middaugh CR. 2003. Derivative absorbance spectroscopy and protein phase diagrams as tools for comprehensive protein characterization: A bGCSF case study. J Pharm Sci 92:1805-1820.
    • (2003) J Pharm Sci , vol.92 , pp. 1805-1820
    • Kueltzo, L.A.1    Ersoy, B.2    Ralston, J.P.3    Middaugh, C.R.4
  • 20
    • 0036063663 scopus 로고    scopus 로고
    • Evaluation of accuracy and precision of adenovirus absorptivity at 260 nm under conditions of complete DNA disruption
    • Sweeney JA, Hennessey JP, Jr. 2002. Evaluation of accuracy and precision of adenovirus absorptivity at 260 nm under conditions of complete DNA disruption. Virology 295:284-288.
    • (2002) Virology , vol.295 , pp. 284-288
    • Sweeney, J.A.1    Hennessey Jr., J.P.2
  • 21
    • 0017087229 scopus 로고
    • Diffusion coefficient and molecular weight of type 5 adenovirus by photon-correlation spectroscopy
    • Oliver CJ, Shortridge KF, Belyavin G. 1976. Diffusion coefficient and molecular weight of type 5 adenovirus by photon-correlation spectroscopy. Biochim Biophys Acta 437:589-598.
    • (1976) Biochim Biophys Acta , vol.437 , pp. 589-598
    • Oliver, C.J.1    Shortridge, K.F.2    Belyavin, G.3
  • 22
    • 0036360325 scopus 로고    scopus 로고
    • Effects of conformation on the chemical stability of pharmaceutically relevant polypeptides
    • Meyer JD, Ho B, Manning MC. 2002. Effects of conformation on the chemical stability of pharmaceutically relevant polypeptides. Pharm Biotechnol 13:85-107.
    • (2002) Pharm Biotechnol , vol.13 , pp. 85-107
    • Meyer, J.D.1    Ho, B.2    Manning, M.C.3
  • 23
    • 0037379808 scopus 로고    scopus 로고
    • Penton release from P22 heat-expanded capsids suggests importance of stabilizing pentonhexon interactions during capsid maturation
    • Teschke CM, McGough A, Thuman-Commike PA. 2003. Penton release from P22 heat-expanded capsids suggests importance of stabilizing pentonhexon interactions during capsid maturation. Biophys J 84:2585-2592.
    • (2003) Biophys J , vol.84 , pp. 2585-2592
    • Teschke, C.M.1    McGough, A.2    Thuman-Commike, P.A.3
  • 25
    • 0030337835 scopus 로고    scopus 로고
    • Acidification of lysosomes and endosomes
    • Van Dyke RW. 1996. Acidification of lysosomes and endosomes. Subcell Biochem 27:331-360.
    • (1996) Subcell Biochem , vol.27 , pp. 331-360
    • Van Dyke, R.W.1
  • 26
    • 0014601539 scopus 로고
    • Removal of pentons from particles of adenovirus type 2
    • Laver WG, Wrigley NG, Pereira HG. 1969. Removal of pentons from particles of adenovirus type 2. Virology 39:599-604.
    • (1969) Virology , vol.39 , pp. 599-604
    • Laver, W.G.1    Wrigley, N.G.2    Pereira, H.G.3
  • 27
    • 0022348579 scopus 로고
    • Molecular composition of the adenovirus type 2 virion
    • van Oostrum J, Burnett RM. 1985. Molecular composition of the adenovirus type 2 virion. J Virol 56:439-448.
    • (1985) J Virol , vol.56 , pp. 439-448
    • Van Oostrum, J.1    Burnett, R.M.2
  • 28
    • 13444311651 scopus 로고    scopus 로고
    • Adenovirus protein VI mediates membrane disruption following capsid disassembly
    • Wiethoff CM, Wodrich H, Gerace L, Nemerow GR. 2005. Adenovirus protein VI mediates membrane disruption following capsid disassembly. J Virol 79:1992-2000.
    • (2005) J Virol , vol.79 , pp. 1992-2000
    • Wiethoff, C.M.1    Wodrich, H.2    Gerace, L.3    Nemerow, G.R.4
  • 29
    • 0344888156 scopus 로고
    • Effect of cations on thermal inactivation of vaccinia, herpes simplex, and adenoviruses
    • Wallis C, Yang CS, Melnick JL. 1962. Effect of cations on thermal inactivation of vaccinia, herpes simplex, and adenoviruses. J Immunol 89:41-46.
    • (1962) J Immunol , vol.89 , pp. 41-46
    • Wallis, C.1    Yang, C.S.2    Melnick, J.L.3
  • 30
    • 32644442860 scopus 로고
    • Adenovirus vaccine prepared by thermal inactivation of the infective moiety of the virus in magnesium ions
    • Yang CS, Tai FH, Wallis C, Melnick JL. 1963. Adenovirus Vaccine Prepared By Thermal Inactivation Of The Infective Moiety Of The Virus In Magnesium Ions. J Immunol 91:283-286.
    • (1963) J Immunol , vol.91 , pp. 283-286
    • Yang, C.S.1    Tai, F.H.2    Wallis, C.3    Melnick, J.L.4
  • 32
    • 0020477047 scopus 로고
    • Preferential interactions of proteins with salts in concentrated solutions
    • Arakawa T, Timasheff SN. 1982. Preferential interactions of proteins with salts in concentrated solutions. Biochemistry 21:6545-6552.
    • (1982) Biochemistry , vol.21 , pp. 6545-6552
    • Arakawa, T.1    Timasheff, S.N.2
  • 33
    • 0036063663 scopus 로고    scopus 로고
    • Evaluation of accuracy and precision of adenovirus absorptivity at 260 nm under conditions of complete DNA disruption
    • Sweeney JA, Hennessey JP, Jr. 2002. Evaluation of accuracy and precision of adenovirus absorptivity at 260 nm under conditions of complete DNA disruption. Virology 295:284-288.
    • (2002) Virology , vol.295 , pp. 284-288
    • Sweeney, J.A.1    Hennessey Jr., J.P.2
  • 34
    • 0022097612 scopus 로고
    • Interpretation of photon correlation spectroscopy data: A comparison of analysis methods
    • Stock RS, Ray WH. 1985. Interpretation of photon correlation spectroscopy data: A comparison of analysis methods. J Poly Sci: Poly Phys Ed 23:1393-1447.
    • (1985) J Poly Sci: Poly Phys Ed , vol.23 , pp. 1393-1447
    • Stock, R.S.1    Ray, W.H.2
  • 35
    • 0027996853 scopus 로고
    • Simultaneous monitoring of the environment of tryptophan, tyrosine, and phenylalanine residues in proteins by near-ultraviolet second-derivative spectroscopy
    • Mach H, Middaugh CR. 1994. Simultaneous monitoring of the environment of tryptophan, tyrosine, and phenylalanine residues in proteins by near-ultraviolet second-derivative spectroscopy. Anal Biochem 222:323-331.
    • (1994) Anal Biochem , vol.222 , pp. 323-331
    • Mach, H.1    Middaugh, C.R.2
  • 36
    • 0029186565 scopus 로고
    • Ultraviolet absorption spectroscopy
    • Shirley BA, editor. Totowa, NJ: Humana Press
    • Mach H, Volkin DB, Burke CJ, Middaugh CR. 1995. Ultraviolet absorption spectroscopy. In: Shirley BA, editor. Methods in molecular biology. Vol 40: Totowa, NJ: Humana Press, pp 91-113.
    • (1995) Methods in Molecular Biology , vol.40 , pp. 91-113
    • Mach, H.1    Volkin, D.B.2    Burke, C.J.3    Middaugh, C.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.