메뉴 건너뛰기




Volumn 6, Issue 9, 2011, Pages

No interaction of barrier-to-autointegration factor (BAF) with HIV-1 MA, cone-rod homeobox (CRX) or MAN1-C in absence of DNA

Author keywords

[No Author keywords available]

Indexed keywords

BARRIER TO AUTOINTEGRATION FACTOR; CONE ROD HOMEOBOX PROTEIN; PROTEIN MAN1 C; UNCLASSIFIED DRUG; VIRUS DNA; VIRUS PROTEIN; BANF1 PROTEIN, HUMAN; DNA BINDING PROTEIN; HOMEODOMAIN PROTEIN; MAN1 PROTEIN, HUMAN; MATRIX PROTEIN; MEMBRANE PROTEIN; NUCLEAR PROTEIN; TRANSACTIVATOR PROTEIN;

EID: 80053055387     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0025123     Document Type: Article
Times cited : (11)

References (22)
  • 1
    • 0032539631 scopus 로고    scopus 로고
    • A previously unidentified host protein protects retroviral DNA from autointegration
    • Lee MS, Craigie R, (1998) A previously unidentified host protein protects retroviral DNA from autointegration. Proc Natl Acad Sci USA 95: 1528-1533.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 1528-1533
    • Lee, M.S.1    Craigie, R.2
  • 2
    • 0034255236 scopus 로고    scopus 로고
    • Barrier-to-autointegration factor (BAF) bridges DNA in a discrete, higher-order nucleoprotein complex
    • Zheng RL, Ghirlando R, Lee MS, Mizuuchi K, Krause M, et al. (2000) Barrier-to-autointegration factor (BAF) bridges DNA in a discrete, higher-order nucleoprotein complex. Proc Natl Acad Sci USA 97: 8997-9002.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 8997-9002
    • Zheng, R.L.1    Ghirlando, R.2    Lee, M.S.3    Mizuuchi, K.4    Krause, M.5
  • 3
    • 12444289583 scopus 로고    scopus 로고
    • Barrier-to-autointegration factor plays crucial roles in cell cycle progression and nuclear organization in Drosophila
    • Furukawa K, Sugiyama S, Osouda S, Goto H, Inagaki M, et al. (2003) Barrier-to-autointegration factor plays crucial roles in cell cycle progression and nuclear organization in Drosophila. J Cell Sci 116: 3811-3823.
    • (2003) J Cell Sci , vol.116 , pp. 3811-3823
    • Furukawa, K.1    Sugiyama, S.2    Osouda, S.3    Goto, H.4    Inagaki, M.5
  • 4
    • 14744280620 scopus 로고    scopus 로고
    • Barrier-to-autointegration factor is required to segregate and enclose chromosomes within the nuclear envelope and assemble the nuclear lamina
    • Margalit A, Segura-Totten M, Gruenbaum Y, Wilson KL, (2005) Barrier-to-autointegration factor is required to segregate and enclose chromosomes within the nuclear envelope and assemble the nuclear lamina. Proc Natl Acad Sci USA 102: 3290-3295.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 3290-3295
    • Margalit, A.1    Segura-Totten, M.2    Gruenbaum, Y.3    Wilson, K.L.4
  • 5
    • 33846195879 scopus 로고    scopus 로고
    • Caenorhabditis elegans BAF-1 and its kinase VRK-1 participate directly in post-mitotic nuclear envelope assembly
    • Gorjanacz M, Klerkx EPF, Galy V, Santarella R, Lopez-Iglesias C, et al. (2007) Caenorhabditis elegans BAF-1 and its kinase VRK-1 participate directly in post-mitotic nuclear envelope assembly. EMBO J 26: 132-143.
    • (2007) EMBO J , vol.26 , pp. 132-143
    • Gorjanacz, M.1    Klerkx, E.P.F.2    Galy, V.3    Santarella, R.4    Lopez-Iglesias, C.5
  • 6
    • 0031720496 scopus 로고    scopus 로고
    • Solution structure of the cellular factor BAF responsible for protecting retroviral DNA from autointegration
    • Cai M, Huang Y, Zheng R, Wei SQ, Ghirlando R, et al. (1998) Solution structure of the cellular factor BAF responsible for protecting retroviral DNA from autointegration. Nat Struct Biol 5: 903-909.
    • (1998) Nat Struct Biol , vol.5 , pp. 903-909
    • Cai, M.1    Huang, Y.2    Zheng, R.3    Wei, S.Q.4    Ghirlando, R.5
  • 7
    • 0034622513 scopus 로고    scopus 로고
    • Structural basis of DNA bridging by barrier-to-autointegration factor
    • Umland TC, Wei SQ, Craigie R, Davies DR, (2000) Structural basis of DNA bridging by barrier-to-autointegration factor. Biochemistry 39: 9130-9138.
    • (2000) Biochemistry , vol.39 , pp. 9130-9138
    • Umland, T.C.1    Wei, S.Q.2    Craigie, R.3    Davies, D.R.4
  • 9
    • 70349748587 scopus 로고    scopus 로고
    • Barrier-to-autointegration factor (BAF) condenses DNA by looping
    • Skoko D, Li M, Huang Y, Mizuuchi M, Cai ML, et al. (2009) Barrier-to-autointegration factor (BAF) condenses DNA by looping. Proc Natl Acad Sci USA 106: 16610-16615.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 16610-16615
    • Skoko, D.1    Li, M.2    Huang, Y.3    Mizuuchi, M.4    Cai, M.L.5
  • 10
    • 0032778974 scopus 로고    scopus 로고
    • LAP2 binding protein 1 (L2BP1/BAF) is a candidate mediator of LAP2-chromatin interaction
    • Furukawa K, (1999) LAP2 binding protein 1 (L2BP1/BAF) is a candidate mediator of LAP2-chromatin interaction. J Cell Sci 112: 2485-2492.
    • (1999) J Cell Sci , vol.112 , pp. 2485-2492
    • Furukawa, K.1
  • 11
    • 34249777825 scopus 로고    scopus 로고
    • LEM-domain proteins: New insights into lamin-interacting proteins
    • Wagner N, Krohne G, (2007) LEM-domain proteins: New insights into lamin-interacting proteins. Int Rev Cytol 261: 1-46.
    • (2007) Int Rev Cytol , vol.261 , pp. 1-46
    • Wagner, N.1    Krohne, G.2
  • 12
    • 34347226730 scopus 로고    scopus 로고
    • Solution NMR structure of the barrier-to-autointegration factor-emerin complex
    • Cai ML, Huang Y, Suh JY, Louis JM, Ghirlando R, et al. (2007) Solution NMR structure of the barrier-to-autointegration factor-emerin complex. J Biol Chem 282: 14525-14535.
    • (2007) J Biol Chem , vol.282 , pp. 14525-14535
    • Cai, M.L.1    Huang, Y.2    Suh, J.Y.3    Louis, J.M.4    Ghirlando, R.5
  • 13
    • 33745450085 scopus 로고    scopus 로고
    • The vaccinia-related kinases phosphorylate the N ′ terminus of BAF, regulating its interaction with DNA and its retention in the nucleus
    • Nichols RJ, Wiebe MS, Traktman P, (2006) The vaccinia-related kinases phosphorylate the N ′ terminus of BAF, regulating its interaction with DNA and its retention in the nucleus. Mol Biol Cell 17: 2451-2464.
    • (2006) Mol Biol Cell , vol.17 , pp. 2451-2464
    • Nichols, R.J.1    Wiebe, M.S.2    Traktman, P.3
  • 14
    • 33644864100 scopus 로고    scopus 로고
    • Barrier-to-autointegration factor phosphorylation on Ser-4 regulates emerin binding to lamin A in vitro and emerin localization in vivo
    • Bengtsson L, Wilson KL, (2006) Barrier-to-autointegration factor phosphorylation on Ser-4 regulates emerin binding to lamin A in vitro and emerin localization in vivo. Mol Biol Cell 17: 1154-1163.
    • (2006) Mol Biol Cell , vol.17 , pp. 1154-1163
    • Bengtsson, L.1    Wilson, K.L.2
  • 15
    • 0344736902 scopus 로고    scopus 로고
    • Barrier-to-autointegration factor BAF binds p55 Gag and matrix and is a host component of human immunodeficiency virus type 1 virions
    • Mansharamani M, Graham DRM, Monie D, Lee KK, Hildreth JEK, et al. (2003) Barrier-to-autointegration factor BAF binds p55 Gag and matrix and is a host component of human immunodeficiency virus type 1 virions. J Virol 77: 13084-13092.
    • (2003) J Virol , vol.77 , pp. 13084-13092
    • Mansharamani, M.1    Graham, D.R.M.2    Monie, D.3    Lee, K.K.4    Hildreth, J.E.K.5
  • 16
    • 18644386771 scopus 로고    scopus 로고
    • Barrier to autointegration factor interacts with the cone-rod homeobox and represses its Transactivation function
    • Wang XJ, Xu SQ, Rivolta C, Li LY, Peng GH, et al. (2002) Barrier to autointegration factor interacts with the cone-rod homeobox and represses its Transactivation function. J Biol Chem 277: 43288-43300.
    • (2002) J Biol Chem , vol.277 , pp. 43288-43300
    • Wang, X.J.1    Xu, S.Q.2    Rivolta, C.3    Li, L.Y.4    Peng, G.H.5
  • 17
    • 17144380019 scopus 로고    scopus 로고
    • Direct binding of nuclear membrane protein MAN1 to emerin in vitro and two modes of binding to barrier-to-autointegration factor
    • Mansharamani M, Wilson KL, (2005) Direct binding of nuclear membrane protein MAN1 to emerin in vitro and two modes of binding to barrier-to-autointegration factor. J Biol Chem 280: 13863-13870.
    • (2005) J Biol Chem , vol.280 , pp. 13863-13870
    • Mansharamani, M.1    Wilson, K.L.2
  • 18
    • 39649106576 scopus 로고    scopus 로고
    • The N-terminal basic domain of the HIV-1 matrix protein does not contain a conventional nuclear localization sequence but is required for DNA binding and protein self-association
    • Hearps AC, Wagstaff KM, Piller SC, Jans DA, (2008) The N-terminal basic domain of the HIV-1 matrix protein does not contain a conventional nuclear localization sequence but is required for DNA binding and protein self-association. Biochemistry 47: 2199-2210.
    • (2008) Biochemistry , vol.47 , pp. 2199-2210
    • Hearps, A.C.1    Wagstaff, K.M.2    Piller, S.C.3    Jans, D.A.4
  • 19
    • 78650831349 scopus 로고    scopus 로고
    • Structural Basis of the Association of HIV-1 Matrix Protein with DNA
    • Cai ML, Huang Y, Craigie R, Clore GM, (2010) Structural Basis of the Association of HIV-1 Matrix Protein with DNA. Plos One 5: e15675.
    • (2010) Plos One , vol.5
    • Cai, M.L.1    Huang, Y.2    Craigie, R.3    Clore, G.M.4
  • 20
    • 79955833841 scopus 로고    scopus 로고
    • Exome Sequencing and Functional Analysis Identifies BANF1 Mutation as the Cause of a Hereditary Progeroid Syndrome
    • Puente XS, Quesada V, Osorio FG, Cabanillas R, Cadinanos J, et al. (2011) Exome Sequencing and Functional Analysis Identifies BANF1 Mutation as the Cause of a Hereditary Progeroid Syndrome. American Journal of Human Genetics 88: 650-656.
    • (2011) American Journal of Human Genetics , vol.88 , pp. 650-656
    • Puente, X.S.1    Quesada, V.2    Osorio, F.G.3    Cabanillas, R.4    Cadinanos, J.5
  • 21
    • 0029400480 scopus 로고
    • NMRPIPE - A multidimensional spectral processing system based on UNIX pipes
    • Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, et al. (1995) NMRPIPE- A multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6: 277-293.
    • (1995) J Biomol NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5
  • 22
    • 0000041361 scopus 로고
    • A common-sense approach to peak picking in 2-dimensional, 3-dimensional, and 4-dimensional spectra using automatic computer-analysis of contour diagrams
    • Garrett DS, Powers R, Gronenborn AM, Clore GM, (1991) A common-sense approach to peak picking in 2-dimensional, 3-dimensional, and 4-dimensional spectra using automatic computer-analysis of contour diagrams. J Magn Reson 95: 214-220.
    • (1991) J Magn Reson , vol.95 , pp. 214-220
    • Garrett, D.S.1    Powers, R.2    Gronenborn, A.M.3    Clore, G.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.