메뉴 건너뛰기




Volumn 151, Issue 2, 2012, Pages 304-319

A structural basis for the assembly and functions of a viral polymer that inactivates multiple tumor suppressors

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; MRE11 PROTEIN; NIBRIN; ONCOPROTEIN; POLYMER; PROMYELOCYTIC LEUKEMIA PROTEIN; PROTEIN P53; RAD50 PROTEIN; TRIM24 PROTEIN; TUMOR SUPPRESSOR PROTEIN; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 84867564497     PISSN: 00928674     EISSN: 10974172     Source Type: Journal    
DOI: 10.1016/j.cell.2012.08.035     Document Type: Article
Times cited : (67)

References (75)
  • 1
    • 0022924035 scopus 로고
    • The three-dimensional structure of the actin filament revisited
    • U. Aebi, R. Millonig, H. Salvo, and A. Engel The three-dimensional structure of the actin filament revisited Ann. N Y Acad. Sci. 483 1986 100 119
    • (1986) Ann. N y Acad. Sci. , vol.483 , pp. 100-119
    • Aebi, U.1    Millonig, R.2    Salvo, H.3    Engel, A.4
  • 2
    • 33646375442 scopus 로고    scopus 로고
    • Deposition diseases and 3D domain swapping
    • M.J. Bennett, M.R. Sawaya, and D. Eisenberg Deposition diseases and 3D domain swapping Structure 14 2006 811 824
    • (2006) Structure , vol.14 , pp. 811-824
    • Bennett, M.J.1    Sawaya, M.R.2    Eisenberg, D.3
  • 3
    • 34447539077 scopus 로고    scopus 로고
    • Adenoviridae: The viruses and their replication
    • D.M. Knipe, P.M. Howley, Lippincott Williams & Wilkins and Wolters Kluwer Philadelphia
    • A.J. Berk Adenoviridae: the viruses and their replication D.M. Knipe, P.M. Howley, Fields Virology 2007 Lippincott Williams & Wilkins and Wolters Kluwer Philadelphia 2355 2394
    • (2007) Fields Virology , pp. 2355-2394
    • Berk, A.J.1
  • 4
    • 36448975490 scopus 로고    scopus 로고
    • Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies
    • R. Bernardi, and P.P. Pandolfi Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies Nat. Rev. Mol. Cell Biol. 8 2007 1006 1016
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 1006-1016
    • Bernardi, R.1    Pandolfi, P.P.2
  • 5
    • 0028840956 scopus 로고
    • Crystal structure of the DNA-binding domain of the Epstein-Barr virus origin-binding protein EBNA 1
    • A. Bochkarev, J.A. Barwell, R.A. Pfuetzner, W. Furey Jr., A.M. Edwards, and L. Frappier Crystal structure of the DNA-binding domain of the Epstein-Barr virus origin-binding protein EBNA 1 Cell 83 1995 39 46
    • (1995) Cell , vol.83 , pp. 39-46
    • Bochkarev, A.1    Barwell, J.A.2    Pfuetzner, R.A.3    Furey, Jr.W.4    Edwards, A.M.5    Frappier, L.6
  • 6
    • 0005588343 scopus 로고
    • Association of charge clusters with functional domains of cellular transcription factors
    • V. Brendel, and S. Karlin Association of charge clusters with functional domains of cellular transcription factors Proc. Natl. Acad. Sci. USA 86 1989 5698 5702
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5698-5702
    • Brendel, V.1    Karlin, S.2
  • 9
    • 34848927902 scopus 로고    scopus 로고
    • The many faces of actin: Matching assembly factors with cellular structures
    • E.S. Chhabra, and H.N. Higgs The many faces of actin: matching assembly factors with cellular structures Nat. Cell Biol. 9 2007 1110 1121
    • (2007) Nat. Cell Biol. , vol.9 , pp. 1110-1121
    • Chhabra, E.S.1    Higgs, H.N.2
  • 10
    • 0036276388 scopus 로고    scopus 로고
    • The Mre11 complex: At the crossroads of dna repair and checkpoint signalling
    • D. D'Amours, and S.P. Jackson The Mre11 complex: at the crossroads of dna repair and checkpoint signalling Nat. Rev. Mol. Cell Biol. 3 2002 317 327
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 317-327
    • D'Amours, D.1    Jackson, S.P.2
  • 12
    • 14044262855 scopus 로고    scopus 로고
    • Serial block-face scanning electron microscopy to reconstruct three-dimensional tissue nanostructure
    • W. Denk, and H. Horstmann Serial block-face scanning electron microscopy to reconstruct three-dimensional tissue nanostructure PLoS Biol. 2 2004 e329
    • (2004) PLoS Biol. , vol.2 , pp. 329
    • Denk, W.1    Horstmann, H.2
  • 13
  • 14
    • 27144464910 scopus 로고    scopus 로고
    • Flexible nets. The roles of intrinsic disorder in protein interaction networks
    • A.K. Dunker, M.S. Cortese, P. Romero, L.M. Iakoucheva, and V.N. Uversky Flexible nets. The roles of intrinsic disorder in protein interaction networks FEBS J. 272 2005 5129 5148
    • (2005) FEBS J. , vol.272 , pp. 5129-5148
    • Dunker, A.K.1    Cortese, M.S.2    Romero, P.3    Iakoucheva, L.M.4    Uversky, V.N.5
  • 15
    • 0037404513 scopus 로고    scopus 로고
    • Distinct roles of the Adenovirus E4 ORF3 protein in viral DNA replication and inhibition of genome concatenation
    • J.D. Evans, and P. Hearing Distinct roles of the Adenovirus E4 ORF3 protein in viral DNA replication and inhibition of genome concatenation J. Virol. 77 2003 5295 5304
    • (2003) J. Virol. , vol.77 , pp. 5295-5304
    • Evans, J.D.1    Hearing, P.2
  • 16
    • 69449101615 scopus 로고    scopus 로고
    • Structural basis for subversion of cellular control mechanisms by the adenoviral E1A oncoprotein
    • J.C. Ferreon, M.A. Martinez-Yamout, H.J. Dyson, and P.E. Wright Structural basis for subversion of cellular control mechanisms by the adenoviral E1A oncoprotein Proc. Natl. Acad. Sci. USA 106 2009 13260 13265
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 13260-13265
    • Ferreon, J.C.1    Martinez-Yamout, M.A.2    Dyson, H.J.3    Wright, P.E.4
  • 17
    • 0024076907 scopus 로고
    • Structural and mutational analysis of E2 trans-activating proteins of papillomaviruses reveals three distinct functional domains
    • I. Giri, and M. Yaniv Structural and mutational analysis of E2 trans-activating proteins of papillomaviruses reveals three distinct functional domains EMBO J. 7 1988 2823 2829
    • (1988) EMBO J. , vol.7 , pp. 2823-2829
    • Giri, I.1    Yaniv, M.2
  • 18
    • 0034028826 scopus 로고    scopus 로고
    • Surpassing the lateral resolution limit by a factor of two using structured illumination microscopy
    • M.G. Gustafsson Surpassing the lateral resolution limit by a factor of two using structured illumination microscopy J. Microsc. 198 2000 82 87
    • (2000) J. Microsc. , vol.198 , pp. 82-87
    • Gustafsson, M.G.1
  • 20
    • 0032545160 scopus 로고    scopus 로고
    • Crystal structure of the E2 DNA-binding domain from human papillomavirus type 16: Implications for its DNA binding-site selection mechanism
    • R.S. Hegde, and E.J. Androphy Crystal structure of the E2 DNA-binding domain from human papillomavirus type 16: implications for its DNA binding-site selection mechanism J. Mol. Biol. 284 1998 1479 1489
    • (1998) J. Mol. Biol. , vol.284 , pp. 1479-1489
    • Hegde, R.S.1    Androphy, E.J.2
  • 22
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Web Server Issue
    • L. Holm, and P. Rosenström Dali server: conservation mapping in 3D Nucleic Acids Res. 38 Web Server issue 2010 W545 W549
    • (2010) Nucleic Acids Res. , vol.38
    • Holm, L.1    Rosenström, P.2
  • 23
    • 33644768122 scopus 로고    scopus 로고
    • Interaction of the adenovirus type 5 E4 Orf3 protein with promyelocytic leukemia protein isoform II is required for ND10 disruption
    • A. Hoppe, S.J. Beech, J. Dimmock, and K.N. Leppard Interaction of the adenovirus type 5 E4 Orf3 protein with promyelocytic leukemia protein isoform II is required for ND10 disruption J. Virol. 80 2006 3042 3049
    • (2006) J. Virol. , vol.80 , pp. 3042-3049
    • Hoppe, A.1    Beech, S.J.2    Dimmock, J.3    Leppard, K.N.4
  • 24
    • 0037452096 scopus 로고    scopus 로고
    • Dynamics and mechanics of the microtubule plus end
    • J. Howard, and A.A. Hyman Dynamics and mechanics of the microtubule plus end Nature 422 2003 753 758
    • (2003) Nature , vol.422 , pp. 753-758
    • Howard, J.1    Hyman, A.A.2
  • 26
    • 0034613274 scopus 로고    scopus 로고
    • The structural basis of DNA target discrimination by papillomavirus E2 proteins
    • S.S. Kim, J.K. Tam, A.F. Wang, and R.S. Hegde The structural basis of DNA target discrimination by papillomavirus E2 proteins J. Biol. Chem. 275 2000 31245 31254
    • (2000) J. Biol. Chem. , vol.275 , pp. 31245-31254
    • Kim, S.S.1    Tam, J.K.2    Wang, A.F.3    Hegde, R.S.4
  • 27
    • 0029879295 scopus 로고    scopus 로고
    • Computer visualization of three-dimensional image data using IMOD
    • J.R. Kremer, D.N. Mastronarde, and J.R. McIntosh Computer visualization of three-dimensional image data using IMOD J. Struct. Biol. 116 1996 71 76
    • (1996) J. Struct. Biol. , vol.116 , pp. 71-76
    • Kremer, J.R.1    Mastronarde, D.N.2    McIntosh, J.R.3
  • 28
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • E. Krissinel, and K. Henrick Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions Acta Crystallogr. D Biol. Crystallogr. 60 2004 2256 2268
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 29
    • 78650982368 scopus 로고    scopus 로고
    • β-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkages
    • C. Liu, M.R. Sawaya, and D. Eisenberg β-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkages Nat. Struct. Mol. Biol. 18 2011 49 55
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 49-55
    • Liu, C.1    Sawaya, M.R.2    Eisenberg, D.3
  • 30
    • 0036108484 scopus 로고    scopus 로고
    • 3D domain swapping: As domains continue to swap
    • Y. Liu, and D. Eisenberg 3D domain swapping: as domains continue to swap Protein Sci. 11 2002 1285 1299
    • (2002) Protein Sci. , vol.11 , pp. 1285-1299
    • Liu, Y.1    Eisenberg, D.2
  • 31
    • 0032476812 scopus 로고    scopus 로고
    • Polyvalent interactions in biological systems: Implications for design and use of multivalent ligands and inhibitors
    • M. Mammen, S.-K. Choi, and G.M. Whitesides Polyvalent interactions in biological systems: implications for design and use of multivalent ligands and inhibitors Angew. Chem. Int. Ed. Engl. 37 1998 2754 2794
    • (1998) Angew. Chem. Int. Ed. Engl. , vol.37 , pp. 2754-2794
    • Mammen, M.1    Choi, S.-K.2    Whitesides, G.M.3
  • 33
    • 51649122268 scopus 로고
    • A correlative study by electron and light microscopy of the development of type 5 adenovirus. I. Electron microscopy
    • C. Morgan, G.C. Godman, P.M. Breitenfeld, and H.M. Rose A correlative study by electron and light microscopy of the development of type 5 adenovirus. I. Electron microscopy J. Exp. Med. 112 1960 373 382
    • (1960) J. Exp. Med. , vol.112 , pp. 373-382
    • Morgan, C.1    Godman, G.C.2    Breitenfeld, P.M.3    Rose, H.M.4
  • 34
    • 0028137826 scopus 로고
    • Human adenovirus encodes two proteins which have opposite effects on accumulation of alternatively spliced mRNAs
    • K. Nordqvist, K. Ohman, and G. Akusjärvi Human adenovirus encodes two proteins which have opposite effects on accumulation of alternatively spliced mRNAs Mol. Cell. Biol. 14 1994 437 445
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 437-445
    • Nordqvist, K.1    Ohman, K.2    Akusjärvi, G.3
  • 35
    • 27944502157 scopus 로고    scopus 로고
    • Viruses - Seeking and destroying the tumor program
    • C.C. O'Shea Viruses - seeking and destroying the tumor program Oncogene 24 2005 7640 7655
    • (2005) Oncogene , vol.24 , pp. 7640-7655
    • O'Shea, C.C.1
  • 36
    • 79953248134 scopus 로고    scopus 로고
    • The critical protein interactions and structures that elicit growth deregulation in cancer and viral replication
    • H.D. Ou, A.P. May, and C.C. O'Shea The critical protein interactions and structures that elicit growth deregulation in cancer and viral replication Wiley Interdiscip. Rev. Syst. Biol. Med. 3 2011 48 73
    • (2011) Wiley Interdiscip. Rev. Syst. Biol. Med. , vol.3 , pp. 48-73
    • Ou, H.D.1    May, A.P.2    O'Shea, C.C.3
  • 37
    • 77955121836 scopus 로고    scopus 로고
    • Domain distribution and intrinsic disorder in hubs in the human protein-protein interaction network
    • A. Patil, K. Kinoshita, and H. Nakamura Domain distribution and intrinsic disorder in hubs in the human protein-protein interaction network Protein Sci. 19 2010 1461 1468
    • (2010) Protein Sci. , vol.19 , pp. 1461-1468
    • Patil, A.1    Kinoshita, K.2    Nakamura, H.3
  • 38
    • 47749130885 scopus 로고    scopus 로고
    • Intrinsic structural disorder in adenovirus E1A: A viral molecular hub linking multiple diverse processes
    • P. Pelka, J.N. Ablack, G.J. Fonseca, A.F. Yousef, and J.S. Mymryk Intrinsic structural disorder in adenovirus E1A: a viral molecular hub linking multiple diverse processes J. Virol. 82 2008 7252 7263
    • (2008) J. Virol. , vol.82 , pp. 7252-7263
    • Pelka, P.1    Ablack, J.N.2    Fonseca, G.J.3    Yousef, A.F.4    Mymryk, J.S.5
  • 39
    • 0034308172 scopus 로고    scopus 로고
    • Discriminating between homodimeric and monomeric proteins in the crystalline state
    • H. Ponstingl, K. Henrick, and J.M. Thornton Discriminating between homodimeric and monomeric proteins in the crystalline state Proteins 41 2000 47 57
    • (2000) Proteins , vol.41 , pp. 47-57
    • Ponstingl, H.1    Henrick, K.2    Thornton, J.M.3
  • 40
    • 0029032354 scopus 로고
    • Adenovirus infection induces rearrangements in the intranuclear distribution of the nuclear body-associated PML protein
    • F. Puvion-Dutilleul, M.K. Chelbi-Alix, M. Koken, F. Quignon, E. Puvion, and H. de Thé Adenovirus infection induces rearrangements in the intranuclear distribution of the nuclear body-associated PML protein Exp. Cell Res. 218 1995 9 16
    • (1995) Exp. Cell Res. , vol.218 , pp. 9-16
    • Puvion-Dutilleul, F.1    Chelbi-Alix, M.K.2    Koken, M.3    Quignon, F.4    Puvion, E.5    De Thé, H.6
  • 43
    • 70849112486 scopus 로고    scopus 로고
    • Cell signaling in space and time: Where proteins come together and when they're apart
    • J.D. Scott, and T. Pawson Cell signaling in space and time: where proteins come together and when they're apart Science 326 2009 1220 1224
    • (2009) Science , vol.326 , pp. 1220-1224
    • Scott, J.D.1    Pawson, T.2
  • 46
    • 0033849738 scopus 로고    scopus 로고
    • Review: History of the amyloid fibril
    • J.D. Sipe, and A.S. Cohen Review: history of the amyloid fibril J. Struct. Biol. 130 2000 88 98
    • (2000) J. Struct. Biol. , vol.130 , pp. 88-98
    • Sipe, J.D.1    Cohen, A.S.2
  • 47
    • 77956167119 scopus 로고    scopus 로고
    • Heterochromatin silencing of p53 target genes by a small viral protein
    • C. Soria, F.E. Estermann, K.C. Espantman, and C.C. O'Shea Heterochromatin silencing of p53 target genes by a small viral protein Nature 466 2010 1076 1081
    • (2010) Nature , vol.466 , pp. 1076-1081
    • Soria, C.1    Estermann, F.E.2    Espantman, K.C.3    O'Shea, C.C.4
  • 48
    • 34248653184 scopus 로고    scopus 로고
    • Rapid, transient expression of fluorescent fusion proteins in tobacco plants and generation of stably transformed plants
    • I.A. Sparkes, J. Runions, A. Kearns, and C. Hawes Rapid, transient expression of fluorescent fusion proteins in tobacco plants and generation of stably transformed plants Nat. Protoc. 1 2006 2019 2025
    • (2006) Nat. Protoc. , vol.1 , pp. 2019-2025
    • Sparkes, I.A.1    Runions, J.2    Kearns, A.3    Hawes, C.4
  • 49
    • 0037130170 scopus 로고    scopus 로고
    • Adenovirus oncoproteins inactivate the Mre11-Rad50-NBS1 DNA repair complex
    • T.H. Stracker, C.T. Carson, and M.D. Weitzman Adenovirus oncoproteins inactivate the Mre11-Rad50-NBS1 DNA repair complex Nature 418 2002 348 352
    • (2002) Nature , vol.418 , pp. 348-352
    • Stracker, T.H.1    Carson, C.T.2    Weitzman, M.D.3
  • 51
    • 34247562651 scopus 로고    scopus 로고
    • Adenovirus E4 ORF3 protein inhibits the interferon-mediated antiviral response
    • A.J. Ullman, N.C. Reich, and P. Hearing Adenovirus E4 ORF3 protein inhibits the interferon-mediated antiviral response J. Virol. 81 2007 4744 4752
    • (2007) J. Virol. , vol.81 , pp. 4744-4752
    • Ullman, A.J.1    Reich, N.C.2    Hearing, P.3
  • 52
    • 79952674000 scopus 로고    scopus 로고
    • Interactome networks and human disease
    • M. Vidal, M.E. Cusick, and A.L. Barabási Interactome networks and human disease Cell 144 2011 986 998
    • (2011) Cell , vol.144 , pp. 986-998
    • Vidal, M.1    Cusick, M.E.2    Barabási, A.L.3
  • 53
    • 27944462290 scopus 로고    scopus 로고
    • Inactivating intracellular antiviral responses during adenovirus infection
    • M.D. Weitzman, and D.A. Ornelles Inactivating intracellular antiviral responses during adenovirus infection Oncogene 24 2005 7686 7696
    • (2005) Oncogene , vol.24 , pp. 7686-7696
    • Weitzman, M.D.1    Ornelles, D.A.2
  • 54
    • 37249004920 scopus 로고    scopus 로고
    • Reaching for high-hanging fruit in drug discovery at protein-protein interfaces
    • J.A. Wells, and C.L. McClendon Reaching for high-hanging fruit in drug discovery at protein-protein interfaces Nature 450 2007 1001 1009
    • (2007) Nature , vol.450 , pp. 1001-1009
    • Wells, J.A.1    McClendon, C.L.2
  • 55
    • 34247147729 scopus 로고    scopus 로고
    • The adenovirus E4 ORF3 protein binds and reorganizes the TRIM family member transcriptional intermediary factor 1 alpha
    • M.A. Yondola, and P. Hearing The adenovirus E4 ORF3 protein binds and reorganizes the TRIM family member transcriptional intermediary factor 1 alpha J. Virol. 81 2007 4264 4271
    • (2007) J. Virol. , vol.81 , pp. 4264-4271
    • Yondola, M.A.1    Hearing, P.2
  • 56
    • 0030038464 scopus 로고    scopus 로고
    • Methods used in the structure determination of bovine mitochondrial F1 ATPase
    • Abrahams, J.P., and Leslie, A.G. (1996). Methods used in the structure determination of bovine mitochondrial F1 ATPase. Acta Crystallogr. D Biol. Crystallogr. 52, 30-42.
    • (1996) Acta Crystallogr. D Biol. Crystallogr. , vol.52 , pp. 30-42
    • Abrahams, J.P.1    Leslie, A.G.2
  • 57
    • 0035964342 scopus 로고    scopus 로고
    • Electrostatics of nanosystems: Application to microtubules and the ribosome
    • Baker, N.A., Sept, D., Joseph, S., Holst, M.J., and McCammon, J.A. (2001). Electrostatics of nanosystems: application to microtubules and the ribosome. Proc. Natl. Acad. Sci. USA 98, 10037-10041.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10037-10041
    • Baker, N.A.1    Sept, D.2    Joseph, S.3    Holst, M.J.4    McCammon, J.A.5
  • 58
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 (1994). The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763.
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 59
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • de la Fortelle, E., and Bricogne, G. (1997). Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276, 472-494.
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 60
  • 61
    • 0032639282 scopus 로고    scopus 로고
    • Laterally modulated excitation microscopy: Improvement of resolution by using a diffraction grating
    • Heintzmann, R., and Cremer, C. (1998). Laterally modulated excitation microscopy: improvement of resolution by using a diffraction grating. Proc. SPIE 3568, 185-195.
    • (1998) Proc. SPIE , vol.3568 , pp. 185-195
    • Heintzmann, R.1    Cremer, C.2
  • 62
    • 33845400134 scopus 로고    scopus 로고
    • The nucleolus: A model for the organization of nuclear functions
    • Hernandez-Verdun, D. (2006). The nucleolus: a model for the organization of nuclear functions. Histochem. Cell Biol. 126, 135-148.
    • (2006) Histochem. Cell Biol. , vol.126 , pp. 135-148
    • Hernandez-Verdun, D.1
  • 63
    • 50249136103 scopus 로고    scopus 로고
    • Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7
    • Langer, G., Cohen, S.X., Lamzin, V.S., and Perrakis, A. (2008). Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7. Nat. Protoc. 3, 1171-1179.
    • (2008) Nat. Protoc. , vol.3 , pp. 1171-1179
    • Langer, G.1    Cohen, S.X.2    Lamzin, V.S.3    Perrakis, A.4
  • 64
    • 33646070293 scopus 로고    scopus 로고
    • Transform-based backprojection for volume reconstruction of large format electron microscope tilt series
    • Lawrence, A., Bouwer, J.C., Perkins, G., and Ellisman, M.H. (2006). Transform-based backprojection for volume reconstruction of large format electron microscope tilt series. J. Struct. Biol. 154, 144-167.
    • (2006) J. Struct. Biol. , vol.154 , pp. 144-167
    • Lawrence, A.1    Bouwer, J.C.2    Perkins, G.3    Ellisman, M.H.4
  • 66
    • 0025666490 scopus 로고
    • Localization of adenovirus-encoded DNA replication proteins in the nucleus by immunogold electron microscopy
    • Murti, K.G., Davis, D.S., and Kitchingman, G.R. (1990). Localization of adenovirus-encoded DNA replication proteins in the nucleus by immunogold electron microscopy. J. Gen. Virol. 71, 2847-2857.
    • (1990) J. Gen. Virol. , vol.71 , pp. 2847-2857
    • Murti, K.G.1    Davis, D.S.2    Kitchingman, G.R.3
  • 67
    • 40649109074 scopus 로고    scopus 로고
    • Expedited approaches to whole cell electron tomography and organelle mark-up in situ in high-pressure frozen pancreatic islets
    • Noske, A.B., Costin, A.J., Morgan, G.P., and Marsh, B.J. (2008). Expedited approaches to whole cell electron tomography and organelle mark-up in situ in high-pressure frozen pancreatic islets. J. Struct. Biol. 161, 298-313.
    • (2008) J. Struct. Biol. , vol.161 , pp. 298-313
    • Noske, A.B.1    Costin, A.J.2    Morgan, G.P.3    Marsh, B.J.4
  • 69
    • 22244479672 scopus 로고    scopus 로고
    • Heat shock phenocopies E1B-55K late functions and selectively sensitizes refractory tumor cells to ONYX-015 oncolytic viral therapy
    • O'Shea, C.C., Soria, C., Bagus, B., and McCormick, F. (2005). Heat shock phenocopies E1B-55K late functions and selectively sensitizes refractory tumor cells to ONYX-015 oncolytic viral therapy. Cancer Cell 8, 61-74.
    • (2005) Cancer Cell , vol.8 , pp. 61-74
    • O'Shea, C.C.1    Soria, C.2    Bagus, B.3    McCormick, F.4
  • 70
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997). Processing of X-ray Diffraction Data Collected in Oscillation Mode. Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 71
    • 77950793231 scopus 로고    scopus 로고
    • Experimental phasing with SHELXC/D/E: Combining chain tracing with density modification
    • Sheldrick, G.M. (2010). Experimental phasing with SHELXC/D/E: combining chain tracing with density modification. Acta Crystallogr. D Biol. Crystallogr. 66, 479-485.
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 479-485
    • Sheldrick, G.M.1
  • 72
    • 0030452512 scopus 로고    scopus 로고
    • Mutations that suppress the thermosensitivity of green fluorescent protein
    • Siemering, K.R., Golbik, R., Sever, R., and Haseloff, J. (1996). Mutations that suppress the thermosensitivity of green fluorescent protein. Curr. Biol. 6, 1653-1663.
    • (1996) Curr. Biol. , vol.6 , pp. 1653-1663
    • Siemering, K.R.1    Golbik, R.2    Sever, R.3    Haseloff, J.4
  • 74
  • 75
    • 0036134273 scopus 로고    scopus 로고
    • Two-stage polymerase chain reaction protocol allowing introduction of multiple mutations, deletions, and insertions, using QuikChange site-directed mutagenesis
    • Wang, W., and Malcolm, B.A. (2002). Two-stage polymerase chain reaction protocol allowing introduction of multiple mutations, deletions, and insertions, using QuikChange site-directed mutagenesis. Methods Mol. Biol. 182, 37-43.
    • (2002) Methods Mol. Biol. , vol.182 , pp. 37-43
    • Wang, W.1    Malcolm, B.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.