메뉴 건너뛰기




Volumn 5, Issue , 2014, Pages

Erratum: Dynamic SUMO modification regulates mitotic chromosome assembly and cell cycle progression in Caenorhabditis elegans (Nature Communications (2015) 5 (5485) DOI: 10.1038/ncomms6485);Dynamic SUMO modification regulates mitotic chromosome assembly and cell cycle progression in Caenorhabditis elegans

Author keywords

[No Author keywords available]

Indexed keywords

SUMO PROTEIN; CAENORHABDITIS ELEGANS PROTEIN; UBIQUITIN CONJUGATING ENZYME;

EID: 84923281715     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms7352     Document Type: Erratum
Times cited : (51)

References (68)
  • 1
    • 28444448039 scopus 로고    scopus 로고
    • The SUMO pathway is essential for nuclear integrity and chromosome segregation in mice
    • Nacerddine, K. et al. The SUMO pathway is essential for nuclear integrity and chromosome segregation in mice. Dev. Cell 9, 769-779 (2005).
    • (2005) Dev. Cell , vol.9 , pp. 769-779
    • Nacerddine, K.1
  • 2
    • 84905370032 scopus 로고    scopus 로고
    • 2 is essential while SUMO3 is dispensable for mouse embryonic development
    • 2 is essential while SUMO3 is dispensable for mouse embryonic development. EMBO Rep. 15, 878-885 (2014).
    • (2014) EMBO Rep. , vol.15 , pp. 878-885
    • Wang, L.1
  • 3
    • 20244369068 scopus 로고    scopus 로고
    • New genes with roles in the C elegans embryo revealed using RNAi of ovary-enriched ORFeome clones
    • Fernandez, A. G. et al. New genes with roles in the C. elegans embryo revealed using RNAi of ovary-enriched ORFeome clones. Genome Res. 15, 250-259 (2005).
    • (2005) Genome Res. , vol.15 , pp. 250-259
    • Fernandez, A.G.1
  • 4
    • 18844465487 scopus 로고    scopus 로고
    • Functional and phylogenetic analysis of the ubiquitylation system in Caenorhabditis elegans: Ubiquitin-conjugating enzymes, ubiquitin-activating enzymes, and ubiquitinlike proteins
    • Jones, D., Crowe, E., Stevens, T. A. & Candido, E. P. Functional and phylogenetic analysis of the ubiquitylation system in Caenorhabditis elegans: ubiquitin-conjugating enzymes, ubiquitin-activating enzymes, and ubiquitinlike proteins. Genome Biol. 3, RESEARCH0002 (2002).
    • (2002) Genome Biol. 3, RESEARCH0002
    • Jones, D.1    Crowe, E.2    Stevens, T.A.3    Candido, E.P.4
  • 5
    • 0037448540 scopus 로고    scopus 로고
    • Systematic functional analysis of the Caenorhabditis elegans genome using RNAi
    • Kamath, R. S. et al. Systematic functional analysis of the Caenorhabditis elegans genome using RNAi. Nature 421, 231-237 (2003).
    • (2003) Nature , vol.421 , pp. 231-237
    • Kamath, R.S.1
  • 6
    • 7444270371 scopus 로고    scopus 로고
    • Toward improving Caenorhabditis elegans phenome mapping with an ORFeome-based RNAi library
    • Rual, J. F. et al. Toward improving Caenorhabditis elegans phenome mapping with an ORFeome-based RNAi library. Genome Res. 14, 2162-2168 (2004).
    • (2004) Genome Res. , vol.14 , pp. 2162-2168
    • Rual, J.F.1
  • 7
    • 84878944582 scopus 로고    scopus 로고
    • Sumoylation: A regulatory protein modification in health and disease
    • Flotho, A. & Melchior, F. Sumoylation: a regulatory protein modification in health and disease. Annu. Rev. Biochem. 82, 357-385 (2013).
    • (2013) Annu. Rev. Biochem. , vol.82 , pp. 357-385
    • Flotho, A.1    Melchior, F.2
  • 8
    • 78649396592 scopus 로고    scopus 로고
    • The SUMO pathway: Emerging mechanisms that shape specificity, conjugation and recognition
    • Gareau, J. R. & Lima, C. D. The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition. Nat. Rev. Mol. Cell Biol. 11, 861-871 (2010).
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 861-871
    • Gareau, J.R.1    Lima, C.D.2
  • 9
    • 69749124557 scopus 로고    scopus 로고
    • Structure of the Siz/PIAS SUMO E3 ligase Siz1 and determinants required for SUMO modification of PCNA
    • Yunus, A. A. & Lima, C. D. Structure of the Siz/PIAS SUMO E3 ligase Siz1 and determinants required for SUMO modification of PCNA. Mol. Cell 35, 669-682 (2009).
    • (2009) Mol. Cell , vol.35 , pp. 669-682
    • Yunus, A.A.1    Lima, C.D.2
  • 10
    • 0035929279 scopus 로고    scopus 로고
    • An E3-like factor that promotes SUMO conjugation to the yeast septins
    • Johnson, E. S. & Gupta, A. A. An E3-like factor that promotes SUMO conjugation to the yeast septins. Cell 106, 735-744 (2001).
    • (2001) Cell , vol.106 , pp. 735-744
    • Johnson, E.S.1    Gupta, A.A.2
  • 11
    • 34548483908 scopus 로고    scopus 로고
    • SUMO-specific proteases: A twist in the tail
    • Hay, R. T. SUMO-specific proteases: a twist in the tail. Trends Cell Biol. 17, 370-376 (2007).
    • (2007) Trends Cell Biol. , vol.17 , pp. 370-376
    • Hay, R.T.1
  • 12
    • 34249880519 scopus 로고    scopus 로고
    • Modification in reverse: The SUMO proteases
    • Mukhopadhyay, D. & Dasso, M. Modification in reverse: the SUMO proteases. Trends Biochem. Sci. 32, 286-295 (2007).
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 286-295
    • Mukhopadhyay, D.1    Dasso, M.2
  • 13
    • 84865602944 scopus 로고    scopus 로고
    • Growing sphere of influence: Cdc48/p97 orchestrates ubiquitin-dependent extraction from chromatin
    • Dantuma, N. P. & Hoppe, T. Growing sphere of influence: Cdc48/p97 orchestrates ubiquitin-dependent extraction from chromatin. Trends Cell Biol. 22, 483-491 (2012).
    • (2012) Trends Cell Biol. , vol.22 , pp. 483-491
    • Dantuma, N.P.1    Hoppe, T.2
  • 14
    • 74049138620 scopus 로고    scopus 로고
    • The Cul3-KLHL21 E3 ubiquitin ligase targets aurora B to midzone microtubules in anaphase and is required for cytokinesis
    • Maerki, S. et al. The Cul3-KLHL21 E3 ubiquitin ligase targets aurora B to midzone microtubules in anaphase and is required for cytokinesis. J. Cell Biol. 187, 791-800 (2009).
    • (2009) J. Cell Biol. , vol.187 , pp. 791-800
    • Maerki, S.1
  • 15
    • 84863867994 scopus 로고    scopus 로고
    • Substrate targeting by the ubiquitin-proteasome system in mitosis
    • Min, M. & Lindon, C. Substrate targeting by the ubiquitin-proteasome system in mitosis. Semin. Cell Dev. Biol. 23, 482-491 (2012).
    • (2012) Semin. Cell Dev. Biol. , vol.23 , pp. 482-491
    • Min, M.1    Lindon, C.2
  • 16
    • 37549068963 scopus 로고    scopus 로고
    • Cdc48/p97 promotes reformation of the nucleus by extracting the kinase Aurora B from chromatin
    • Ramadan, K. et al. Cdc48/p97 promotes reformation of the nucleus by extracting the kinase Aurora B from chromatin. Nature 450, 1258-1262 (2007).
    • (2007) Nature , vol.450 , pp. 1258-1262
    • Ramadan, K.1
  • 17
    • 34249305132 scopus 로고    scopus 로고
    • A Cul3-based E3 ligase removes Aurora B from mitotic chromosomes, regulating mitotic progression and completion of cytokinesis in human cells
    • Sumara, I. et al. A Cul3-based E3 ligase removes Aurora B from mitotic chromosomes, regulating mitotic progression and completion of cytokinesis in human cells. Dev. Cell 12, 887-900 (2007).
    • (2007) Dev. Cell , vol.12 , pp. 887-900
    • Sumara, I.1
  • 18
    • 0031104910 scopus 로고    scopus 로고
    • A human homologue of the S cerevisiae SMT3 gene, maps to chromosome 21qter and defines a novel gene family
    • Lapenta, V. et al. a human homologue of the S. cerevisiae SMT3 gene, maps to chromosome 21qter and defines a novel gene family. Genomics 40, 362-366 (1997).
    • (1997) Genomics , vol.40 , pp. 362-366
    • Lapenta, V.1
  • 19
    • 0029044625 scopus 로고
    • Evidence that the MIF2 gene of Saccharomyces cerevisiae encodes a centromere protein with homology to the mammalian centromere protein CENP-C
    • Meluh, P. B. & Koshland, D. Evidence that the MIF2 gene of Saccharomyces cerevisiae encodes a centromere protein with homology to the mammalian centromere protein CENP-C. Mol. Biol. Cell 6, 793-807 (1995).
    • (1995) Mol. Biol. Cell , vol.6 , pp. 793-807
    • Meluh, P.B.1    Koshland, D.2
  • 20
    • 0033580444 scopus 로고    scopus 로고
    • A new protease required for cell-cycle progression in yeast
    • Li, S. J. & Hochstrasser, M. A new protease required for cell-cycle progression in yeast. Nature 398, 246-251 (1999).
    • (1999) Nature , vol.398 , pp. 246-251
    • Li, S.J.1    Hochstrasser, M.2
  • 21
    • 0028967267 scopus 로고
    • Role of a ubiquitin-conjugating enzyme in degradation of S-and M-phase cyclins
    • Seufert, W., Futcher, B. & Jentsch, S. Role of a ubiquitin-conjugating enzyme in degradation of S-and M-phase cyclins. Nature 373, 78-81 (1995).
    • (1995) Nature , vol.373 , pp. 78-81
    • Seufert, W.1    Futcher, B.2    Jentsch, S.3
  • 22
    • 21844437072 scopus 로고    scopus 로고
    • PIASy mediates SUMO-2 conjugation of Topoisomerase-II on mitotic chromosomes
    • Azuma, Y., Arnaoutov, A., Anan, T. & Dasso, M. PIASy mediates SUMO-2 conjugation of Topoisomerase-II on mitotic chromosomes. EMBO J. 24, 2172-2182 (2005).
    • (2005) EMBO J. , vol.24 , pp. 2172-2182
    • Azuma, Y.1    Arnaoutov, A.2    Anan, T.3    Dasso, M.4
  • 23
    • 0036291014 scopus 로고    scopus 로고
    • The SUMO-1 isopeptidase Smt4 is linked to centromeric cohesion through SUMO-1 modification of DNA topoisomerase II
    • Bachant, J., Alcasabas, A., Blat, Y., Kleckner, N. & Elledge, S. J. The SUMO-1 isopeptidase Smt4 is linked to centromeric cohesion through SUMO-1 modification of DNA topoisomerase II. Mol. Cell 9, 1169-1182 (2002).
    • (2002) Mol. Cell , vol.9 , pp. 1169-1182
    • Bachant, J.1    Alcasabas, A.2    Blat, Y.3    Kleckner, N.4    Elledge, S.J.5
  • 24
    • 0034754698 scopus 로고    scopus 로고
    • Genes involved in sister chromatid separation and segregation in the budding yeast Saccharomyces cerevisiae
    • Biggins, S., Bhalla, N., Chang, A., Smith, D. L. & Murray, A. W. Genes involved in sister chromatid separation and segregation in the budding yeast Saccharomyces cerevisiae. Genetics 159, 453-470 (2001).
    • (2001) Genetics , vol.159 , pp. 453-470
    • Biggins, S.1    Bhalla, N.2    Chang, A.3    Smith, D.L.4    Murray, A.W.5
  • 25
    • 0242414786 scopus 로고    scopus 로고
    • The SUMO isopeptidase Ulp2 prevents accumulation of SUMO chains in yeast
    • Bylebyl, G. R., Belichenko, I. & Johnson, E. S. The SUMO isopeptidase Ulp2 prevents accumulation of SUMO chains in yeast. J. Biol. Chem. 278, 44113-44120 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 44113-44120
    • Bylebyl, G.R.1    Belichenko, I.2    Johnson, E.S.3
  • 26
    • 84888241658 scopus 로고    scopus 로고
    • SENP1 and SENP2 affect spatial and temporal control of sumoylation in mitosis
    • Cubenas-Potts, C., Goeres, J. D. & Matunis, M. J. SENP1 and SENP2 affect spatial and temporal control of sumoylation in mitosis. Mol. Biol. Cell 24, 3483-3495 (2013).
    • (2013) Mol. Biol. Cell , vol.24 , pp. 3483-3495
    • Cubenas-Potts, C.1    Goeres, J.D.2    Matunis, M.J.3
  • 27
    • 1542407105 scopus 로고    scopus 로고
    • Smt3/SUMO and Ubc9 are required for efficient APC/C-mediated proteolysis in budding yeast
    • Dieckhoff, P., Bolte, M., Sancak, Y., Braus, G. H. & Irniger, S. Smt3/SUMO and Ubc9 are required for efficient APC/C-mediated proteolysis in budding yeast. Mol. Microbiol. 51, 1375-1387 (2004).
    • (2004) Mol. Microbiol. , vol.51 , pp. 1375-1387
    • Dieckhoff, P.1    Bolte, M.2    Sancak, Y.3    Braus, G.H.4    Irniger, S.5
  • 28
    • 0035883939 scopus 로고    scopus 로고
    • Creation and characterization of temperature-sensitive CENP-C mutants in vertebrate cells
    • Fukagawa, T., Regnier, V. & Ikemura, T. Creation and characterization of temperature-sensitive CENP-C mutants in vertebrate cells. Nucleic Acids Res. 29, 3796-3803 (2001).
    • (2001) Nucleic Acids Res. , vol.29 , pp. 3796-3803
    • Fukagawa, T.1    Regnier, V.2    Ikemura, T.3
  • 30
    • 77949378117 scopus 로고    scopus 로고
    • The SUMO protease SENP6 is essential for inner kinetochore assembly
    • Mukhopadhyay, D., Arnaoutov, A. & Dasso, M. The SUMO protease SENP6 is essential for inner kinetochore assembly. J. Cell Biol. 188, 681-692 (2010).
    • (2010) J. Cell Biol. , vol.188 , pp. 681-692
    • Mukhopadhyay, D.1    Arnaoutov, A.2    Dasso, M.3
  • 31
    • 0344736804 scopus 로고    scopus 로고
    • Pds5p regulates the maintenance of sister chromatid cohesion and is sumoylated to promote the dissolution of cohesion
    • Stead, K. et al. Pds5p regulates the maintenance of sister chromatid cohesion and is sumoylated to promote the dissolution of cohesion. J. Cell Biol. 163, 729-741 (2003).
    • (2003) J. Cell Biol. , vol.163 , pp. 729-741
    • Stead, K.1
  • 32
    • 0035004370 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae SMT4 encodes an evolutionarily conserved protease with a role in chromosome condensation regulation
    • Strunnikov, A. V., Aravind, L. & Koonin, E. V. Saccharomyces cerevisiae SMT4 encodes an evolutionarily conserved protease with a role in chromosome condensation regulation. Genetics 158, 95-107 (2001).
    • (2001) Genetics , vol.158 , pp. 95-107
    • Strunnikov, A.V.1    Aravind, L.2    Koonin, E.V.3
  • 33
    • 40849115019 scopus 로고    scopus 로고
    • SUMO-2/3 modification and binding regulate the association of CENP-E with kinetochores and progression through mitosis
    • Zhang, X. D. et al. SUMO-2/3 modification and binding regulate the association of CENP-E with kinetochores and progression through mitosis. Mol. Cell 29, 729-741 (2008).
    • (2008) Mol. Cell , vol.29 , pp. 729-741
    • Zhang, X.D.1
  • 34
    • 37549071893 scopus 로고    scopus 로고
    • Molecular architecture of the kinetochoremicrotubule interface
    • Cheeseman, I. M. & Desai, A. Molecular architecture of the kinetochoremicrotubule interface. Nat. Rev. Mol. Cell Biol. 9, 33-46 (2008).
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 33-46
    • Cheeseman, I.M.1    Desai, A.2
  • 35
    • 84892702467 scopus 로고    scopus 로고
    • Sumoylated NHR-25/NR5A regulates cell fate during C elegans vulval development
    • Ward, J. D. et al. Sumoylated NHR-25/NR5A regulates cell fate during C. elegans vulval development. PLoS Genet. 9, e1003992 (2013).
    • (2013) PLoS Genet. , vol.9
    • Ward, J.D.1
  • 36
    • 4644228886 scopus 로고    scopus 로고
    • The small ubiquitin-like modifier (SUMO) is required for gonadal and uterine-vulval morphogenesis in Caenorhabditis elegans
    • Broday, L. et al. The small ubiquitin-like modifier (SUMO) is required for gonadal and uterine-vulval morphogenesis in Caenorhabditis elegans. Genes Dev. 18, 2380-2391 (2004).
    • (2004) Genes Dev. , vol.18 , pp. 2380-2391
    • Broday, L.1
  • 37
    • 57749101303 scopus 로고    scopus 로고
    • Regulated proteolysis of DNA polymerase eta during the DNA-damage response in C elegans
    • Kim, S. H. & Michael, W. M. Regulated proteolysis of DNA polymerase eta during the DNA-damage response in C. elegans. Mol. Cell 32, 757-766 (2008).
    • (2008) Mol. Cell , vol.32 , pp. 757-766
    • Kim, S.H.1    Michael, W.M.2
  • 38
    • 71549169907 scopus 로고    scopus 로고
    • SUMO regulates the assembly and function of a cytoplasmic intermediate filament protein in C elegans
    • Kaminsky, R. et al. SUMO regulates the assembly and function of a cytoplasmic intermediate filament protein in C. elegans. Dev. Cell 17, 724-735 (2009).
    • (2009) Dev. Cell , vol.17 , pp. 724-735
    • Kaminsky, R.1
  • 39
    • 2442439113 scopus 로고    scopus 로고
    • SUMO modification is required for in vivo Hox gene regulation by the Caenorhabditis elegans Polycomb group protein SOP-2
    • Zhang, H. et al. SUMO modification is required for in vivo Hox gene regulation by the Caenorhabditis elegans Polycomb group protein SOP-2. Nat. Genet. 36, 507-511 (2004).
    • (2004) Nat. Genet. , vol.36 , pp. 507-511
    • Zhang, H.1
  • 40
    • 16344370926 scopus 로고    scopus 로고
    • A SUMO ligase is part of a nuclear multiprotein complex that affects DNA repair and chromosomal organization
    • Zhao, X. & Blobel, G. A SUMO ligase is part of a nuclear multiprotein complex that affects DNA repair and chromosomal organization. Proc. Natl Acad. Sci. USA 102, 4777-4782 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 4777-4782
    • Zhao, X.1    Blobel, G.2
  • 41
    • 33645293158 scopus 로고    scopus 로고
    • Checkpoint silencing during the DNA damage response in Caenorhabditis elegans embryos
    • Holway, A. H., Kim, S. H., La Volpe, A. & Michael, W. M. Checkpoint silencing during the DNA damage response in Caenorhabditis elegans embryos. J. Cell Biol. 172, 999-1008 (2006).
    • (2006) J. Cell Biol. , vol.172 , pp. 999-1008
    • Holway, A.H.1    Kim, S.H.2    La Volpe, A.3    Michael, W.M.4
  • 43
    • 4444223267 scopus 로고    scopus 로고
    • Holo er than thou: Chromosome segregation and kinetochore function in C elegans
    • Maddox, P. S., Oegema, K., Desai, A. & Cheeseman, I. M. "Holo"er than thou: chromosome segregation and kinetochore function in C. elegans. Chromosome Res. 12, 641-653 (2004).
    • (2004) Chromosome Res. , vol.12 , pp. 641-653
    • Maddox, P.S.1    Oegema, K.2    Desai, A.3    Cheeseman, I.M.4
  • 44
    • 33947239252 scopus 로고    scopus 로고
    • Functional genomics identifies a Myb domain-containing protein family required for assembly of CENP-A chromatin
    • Maddox, P. S., Hyndman, F., Monen, J., Oegema, K. & Desai, A. Functional genomics identifies a Myb domain-containing protein family required for assembly of CENP-A chromatin. J. Cell Biol. 176, 757-763 (2007).
    • (2007) J. Cell Biol. , vol.176 , pp. 757-763
    • Maddox, P.S.1    Hyndman, F.2    Monen, J.3    Oegema, K.4    Desai, A.5
  • 45
    • 26944490411 scopus 로고    scopus 로고
    • A combined approach for the localization and tandem affinity purification of protein complexes from metazoans
    • Cheeseman, I. M. & Desai, A. A combined approach for the localization and tandem affinity purification of protein complexes from metazoans. Science's STKE 2005, pl1 (2005).
    • (2005) Science's STKE 2005 , pp. l1
    • Cheeseman, I.M.1    Desai, A.2
  • 46
    • 0034687807 scopus 로고    scopus 로고
    • Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1)
    • Poukka, H., Karvonen, U., Janne, O. A. & Palvimo, J. J. Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1). Proc. Natl. Acad. Sci. USA 97, 14145-14150 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 14145-14150
    • Poukka, H.1    Karvonen, U.2    Janne, O.A.3    Palvimo, J.J.4
  • 47
    • 81355147328 scopus 로고    scopus 로고
    • Different roles for Aurora B in condensin targeting during mitosis and meiosis
    • Collette, K. S., Petty, E. L., Golenberg, N., Bembenek, J. N. & Csankovszki, G. Different roles for Aurora B in condensin targeting during mitosis and meiosis. J. Cell Sci. 124, 3684-3694 (2011).
    • (2011) J. Cell Sci. , vol.124 , pp. 3684-3694
    • Collette, K.S.1    Petty, E.L.2    Golenberg, N.3    Bembenek, J.N.4    Csankovszki, G.5
  • 48
    • 0037087623 scopus 로고    scopus 로고
    • Elegans condensin promotes mitotic chromosome architecture, centromere organization, and sister chromatid segregation during mitosis and meiosis
    • Hagstrom, K. A., Holmes, V. F., Cozzarelli, N. R. & Meyer, B. J. C. elegans condensin promotes mitotic chromosome architecture, centromere organization, and sister chromatid segregation during mitosis and meiosis. Genes Dev. 16, 729-742 (2002).
    • (2002) Genes Dev. , vol.16 , pp. 729-742
    • Hagstrom, K.A.1    Holmes, V.F.2    Cozzarelli, N.R.3    Meyer, B.J.C.4
  • 49
    • 0037076212 scopus 로고    scopus 로고
    • The aurora B kinase AIR-2 regulates kinetochores during mitosis and is required for separation of homologous Chromosomes during meiosis
    • Kaitna, S., Pasierbek, P., Jantsch, M., Loidl, J. & Glotzer, M. The aurora B kinase AIR-2 regulates kinetochores during mitosis and is required for separation of homologous Chromosomes during meiosis. Curr. Biol. 12, 798-812 (2002).
    • (2002) Curr. Biol. , vol.12 , pp. 798-812
    • Kaitna, S.1    Pasierbek, P.2    Jantsch, M.3    Loidl, J.4    Glotzer, M.5
  • 50
    • 0032517860 scopus 로고    scopus 로고
    • AIR-2: An Aurora/Ipl1-related protein kinase associated with chromosomes and midbody microtubules is required for polar body extrusion and cytokinesis in Caenorhabditis elegans embryos
    • Schumacher, J. M., Golden, A. & Donovan, P. J. AIR-2: An Aurora/Ipl1-related protein kinase associated with chromosomes and midbody microtubules is required for polar body extrusion and cytokinesis in Caenorhabditis elegans embryos. J. Cell Biol. 143, 1635-1646 (1998).
    • (1998) J. Cell Biol. , vol.143 , pp. 1635-1646
    • Schumacher, J.M.1    Golden, A.2    Donovan, P.J.3
  • 51
    • 33751252292 scopus 로고    scopus 로고
    • Direct observation of individual endogenous protein complexes in situ by proximity ligation
    • Soderberg, O. et al. Direct observation of individual endogenous protein complexes in situ by proximity ligation. Nat. Methods 3, 995-1000 (2006).
    • (2006) Nat. Methods , vol.3 , pp. 995-1000
    • Soderberg, O.1
  • 52
    • 48049110299 scopus 로고    scopus 로고
    • Characterizing proteins and their interactions in cells and tissues using the in situ proximity ligation assay
    • Soderberg, O. et al. Characterizing proteins and their interactions in cells and tissues using the in situ proximity ligation assay. Methods 45, 227-232 (2008).
    • (2008) Methods , vol.45 , pp. 227-232
    • Soderberg, O.1
  • 53
    • 79956311920 scopus 로고    scopus 로고
    • Mitotic kinase Aurora-B is regulated by SUMO-2/3 conjugation/deconjugation during mitosis
    • Ban, R., Nishida, T. & Urano, T. Mitotic kinase Aurora-B is regulated by SUMO-2/3 conjugation/deconjugation during mitosis. GenesCells 16, 652-669 (2011).
    • (2011) GenesCells , vol.16 , pp. 652-669
    • Ban, R.1    Nishida, T.2    Urano, T.3
  • 54
    • 77956009377 scopus 로고    scopus 로고
    • SUMOylation modulates the function of Aurora-B kinase
    • Fernandez-Miranda, G. et al. SUMOylation modulates the function of Aurora-B kinase. J. Cell. Sci. 123, 2823-2833 (2010).
    • (2010) J. Cell. Sci. , vol.123 , pp. 2823-2833
    • Fernandez-Miranda, G.1
  • 55
    • 84899759007 scopus 로고    scopus 로고
    • 2 modification sites
    • 2 modification sites. Sci. Signal. 7, rs2 (2014).
    • (2014) Sci. Signal. , vol.7 , pp. rs2
    • Tammsalu, T.1
  • 56
    • 53249109785 scopus 로고    scopus 로고
    • An Afg2/Spaf-related Cdc48-like AAA ATPase regulates the stability and activity of the C elegans Aurora B kinase AIR-2
    • Heallen, T. R., Adams, H. P., Furuta, T., Verbrugghe, K. J. & Schumacher, J. M. An Afg2/Spaf-related Cdc48-like AAA ATPase regulates the stability and activity of the C. elegans Aurora B kinase AIR-2. Dev. Cell 15, 603-616 (2008).
    • (2008) Dev. Cell , vol.15 , pp. 603-616
    • Heallen, T.R.1    Adams, H.P.2    Furuta, T.3    Verbrugghe, K.J.4    Schumacher, J.M.5
  • 57
    • 84865475874 scopus 로고    scopus 로고
    • Dual recruitment of Cdc48 (p97)-Ufd1-Npl4 ubiquitin-selective segregase by small ubiquitin-like modifier protein (SUMO) and ubiquitin in SUMO-targeted ubiquitin ligase-mediated genome stability functions
    • Nie, M. et al. Dual recruitment of Cdc48 (p97)-Ufd1-Npl4 ubiquitin-selective segregase by small ubiquitin-like modifier protein (SUMO) and ubiquitin in SUMO-targeted ubiquitin ligase-mediated genome stability functions. J. Biol. Chem. 287, 29610-29619 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 29610-29619
    • Nie, M.1
  • 58
    • 84877585813 scopus 로고    scopus 로고
    • Role of Cdc48/p97 as a SUMO-targeted segregase curbing Rad51-Rad52 interaction
    • Bergink, S. et al. Role of Cdc48/p97 as a SUMO-targeted segregase curbing Rad51-Rad52 interaction. Nat. Cell Biol. 15, 526-532 (2013).
    • (2013) Nat. Cell Biol. , vol.15 , pp. 526-532
    • Bergink, S.1
  • 59
    • 84884966441 scopus 로고    scopus 로고
    • SUMOylation is essential for sex-specific assembly and function of the Caenorhabditis elegans dosage compensation complex on X chromosomes
    • Pferdehirt, R. R. & Meyer, B. J. SUMOylation is essential for sex-specific assembly and function of the Caenorhabditis elegans dosage compensation complex on X chromosomes. Proc. Natl Acad. Sci. USA 110, E3810-E3819 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. E3810-E3819
    • Pferdehirt, R.R.1    Meyer, B.J.2
  • 60
    • 18044376285 scopus 로고    scopus 로고
    • The CENP-F-like proteins HCP-1 and HCP-2 target CLASP to kinetochores to mediate chromosome segregation
    • Cheeseman, I. M., MacLeod, I., Yates, 3rd J. R., Oegema, K. & Desai, A. The CENP-F-like proteins HCP-1 and HCP-2 target CLASP to kinetochores to mediate chromosome segregation. Curr. Biol. 15, 771-777 (2005).
    • (2005) Curr. Biol. , vol.15 , pp. 771-777
    • Cheeseman, I.M.1    Macleod, I.2    Yates, J.R.3    Oegema, K.4    Desai, A.5
  • 61
    • 14844304695 scopus 로고    scopus 로고
    • A spindle checkpoint functions during mitosis in the early Caenorhabditis elegans embryo
    • Encalada, S. E., Willis, J., Lyczak, R. & Bowerman, B. A spindle checkpoint functions during mitosis in the early Caenorhabditis elegans embryo. Mol. Biol. Cell 16, 1056-1070 (2005).
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1056-1070
    • Encalada, S.E.1    Willis, J.2    Lyczak, R.3    Bowerman, B.4
  • 62
    • 0016063911 scopus 로고
    • The genetics of Caenorhabditis elegans
    • Brenner, S. The genetics of Caenorhabditis elegans. Genetics 77, 71-94 (1974).
    • (1974) Genetics , vol.77 , pp. 71-94
    • Brenner, S.1
  • 63
    • 0035099902 scopus 로고    scopus 로고
    • Creation of low-copy integrated transgenic lines in Caenorhabditis elegans
    • Praitis, V., Casey, E., Collar, D. & Austin, J. Creation of low-copy integrated transgenic lines in Caenorhabditis elegans. Genetics 157, 1217-1226 (2001).
    • (2001) Genetics , vol.157 , pp. 1217-1226
    • Praitis, V.1    Casey, E.2    Collar, D.3    Austin, J.4
  • 64
    • 33845713718 scopus 로고    scopus 로고
    • Katanin controls mitotic and meiotic spindle length
    • McNally, K., Audhya, A., Oegema, K. & McNally, F. J. Katanin controls mitotic and meiotic spindle length. J. Cell Biol. 175, 881-891 (2006).
    • (2006) J. Cell Biol. , vol.175 , pp. 881-891
    • McNally, K.1    Audhya, A.2    Oegema, K.3    McNally, F.J.4
  • 65
    • 37249024245 scopus 로고    scopus 로고
    • Expression and imaging of fluorescent proteins in the C elegans gonad and early embryo
    • Green, R. A. et al. Expression and imaging of fluorescent proteins in the C. elegans gonad and early embryo. Methods Cell Biol. 85, 179-218 (2008).
    • (2008) Methods Cell Biol. , vol.85 , pp. 179-218
    • Green, R.A.1
  • 66
    • 0038725897 scopus 로고    scopus 로고
    • Genome-wide RNAi screening in Caenorhabditis elegans
    • Kamath, R. S. & Ahringer, J. Genome-wide RNAi screening in Caenorhabditis elegans. Methods 30, 313-321 (2003).
    • (2003) Methods , vol.30 , pp. 313-321
    • Kamath, R.S.1    Ahringer, J.2
  • 67
    • 84856735748 scopus 로고    scopus 로고
    • The dynamics of replication licensing in live Caenorhabditis elegans embryos
    • Sonneville, R., Querenet, M., Craig, A., Gartner, A. & Blow, J. J. The dynamics of replication licensing in live Caenorhabditis elegans embryos. J. Cell Biol. 196, 233-246 (2012).
    • (2012) J. Cell Biol. , vol.196 , pp. 233-246
    • Sonneville, R.1    Querenet, M.2    Craig, A.3    Gartner, A.4    Blow, J.J.5
  • 68
    • 20144384755 scopus 로고    scopus 로고
    • An automated method to quantify and visualize colocalized fluorescent signals
    • Jaskolski, F., Mulle, C. & Manzoni, O. J. An automated method to quantify and visualize colocalized fluorescent signals. J. Neurosci. Methods 146, 42-49 (2005).
    • (2005) J. Neurosci. Methods , vol.146 , pp. 42-49
    • Jaskolski, F.1    Mulle, C.2    Manzoni, O.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.