메뉴 건너뛰기




Volumn 141, Issue 2, 1998, Pages 321-333

Human autoantibodies reveal titin as a chromosomal protein

Author keywords

[No Author keywords available]

Indexed keywords

AUTOANTIBODY; CHROMOSOME PROTEIN; CONNECTIN;

EID: 0032550178     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.141.2.321     Document Type: Article
Times cited : (112)

References (113)
  • 1
    • 0025146907 scopus 로고
    • Patients with myasthenia gravis and thymoma have in their sera IgG autoantibodies against titin
    • Aarli, J.A., K. Stefansson, L.S.G. Marton, and R.L. Wollmann. 1990. Patients with myasthenia gravis and thymoma have in their sera IgG autoantibodies against titin. Clin. Exp. Immunol. 82:284-288.
    • (1990) Clin. Exp. Immunol. , vol.82 , pp. 284-288
    • Aarli, J.A.1    Stefansson, K.2    Marton, L.S.G.3    Wollmann, R.L.4
  • 3
    • 0031022257 scopus 로고    scopus 로고
    • Chromosomes with two intact axial cores are induced by G2 checkpoint override: Evidence that DNA decatenation is not required to template the chromosome structure
    • Andreasson, P.R., F.B. Lacroix, and R.L. Margolis. 1997. Chromosomes with two intact axial cores are induced by G2 checkpoint override: evidence that DNA decatenation is not required to template the chromosome structure. J. Cell Biol. 136:29-43.
    • (1997) J. Cell Biol. , vol.136 , pp. 29-43
    • Andreasson, P.R.1    Lacroix, F.B.2    Margolis, R.L.3
  • 5
    • 0028897497 scopus 로고
    • Both synchronous and asynchronous muscle isoforms of projectin (the Drosophila bent locus product) contain functional kinase domains
    • Ayme-Southgate, A., R. Southgate, J. Saide, G.M. Benian, and M.L. Pardue. 1995. Both synchronous and asynchronous muscle isoforms of projectin (the Drosophila bent locus product) contain functional kinase domains. J. Cell Biol. 128:393-403.
    • (1995) J. Cell Biol. , vol.128 , pp. 393-403
    • Ayme-Southgate, A.1    Southgate, R.2    Saide, J.3    Benian, G.M.4    Pardue, M.L.5
  • 6
    • 0030011358 scopus 로고    scopus 로고
    • Molecular cloning of an intronless gene for the hamster centromere antigen CENP-B
    • Bejarano, L.A., and M.M. Valdivia. 1996. Molecular cloning of an intronless gene for the hamster centromere antigen CENP-B. Biochim. Biophys. Acta. 1307:21-25.
    • (1996) Biochim. Biophys. Acta , vol.1307 , pp. 21-25
    • Bejarano, L.A.1    Valdivia, M.M.2
  • 7
    • 0024422164 scopus 로고
    • Sequence of an unusually large protein implicated in regulation of myosin activity in C. elegans
    • Benian, G.M., J.E. Kiff, N. Neckelmann, D.G. Moerman, and R.H. Waterston. 1989. Sequence of an unusually large protein implicated in regulation of myosin activity in C. elegans. Nature. 342:45-50.
    • (1989) Nature , vol.342 , pp. 45-50
    • Benian, G.M.1    Kiff, J.E.2    Neckelmann, N.3    Moerman, D.G.4    Waterston, R.H.5
  • 8
    • 0029848345 scopus 로고    scopus 로고
    • Twitchin and related giant Ig super family members of C. elegans and other invertebrates
    • Benian, G.M., X. Tang, and T.L. Tilney. 1996. Twitchin and related giant Ig super family members of C. elegans and other invertebrates. Adv. Biophys. 33: 183-197.
    • (1996) Adv. Biophys. , vol.33 , pp. 183-197
    • Benian, G.M.1    Tang, X.2    Tilney, T.L.3
  • 9
    • 0017198560 scopus 로고
    • The effect of heat shock on RNA synthesis in Drosophila tissues
    • Bonner, J.J., and M.L. Pardue. 1976. The effect of heat shock on RNA synthesis in Drosophila tissues. Cell. 8:43-50.
    • (1976) Cell , vol.8 , pp. 43-50
    • Bonner, J.J.1    Pardue, M.L.2
  • 10
    • 0023772113 scopus 로고
    • Functional cDNA libraries from Drosophila embryos
    • Brown, N.H., and F.C. Kafatos. 1988. Functional cDNA libraries from Drosophila embryos. J. Mol. Biol. 203:425-437.
    • (1988) J. Mol. Biol. , vol.203 , pp. 425-437
    • Brown, N.H.1    Kafatos, F.C.2
  • 11
    • 0027516129 scopus 로고
    • Comparison of the Drosophila melanogaster, human and murine SmB cDNAs: Evolutionary conservation
    • Brunet, C., T. Quan, and J. Craft. 1993. Comparison of the Drosophila melanogaster, human and murine SmB cDNAs: evolutionary conservation. Gene. 124:269-273.
    • (1993) Gene , vol.124 , pp. 269-273
    • Brunet, C.1    Quan, T.2    Craft, J.3
  • 13
    • 0028104856 scopus 로고
    • DPY-27: A chromosome condensation protein homolog that regulates C. elegans dosage compensation through association with the X chromosome
    • Wtang, P.-T., D.G Albertson, and B.J. Meyer. 1994. DPY-27: a chromosome condensation protein homolog that regulates C. elegans dosage compensation through association with the X chromosome. Cell. 79:459-474.
    • (1994) Cell , vol.79 , pp. 459-474
    • Wtang, P.-T.1    Albertson, D.G.2    Meyer, B.J.3
  • 14
    • 0025015322 scopus 로고
    • The early expression of myofibrillar proteins in round post mitotic myoblasts of embryonic skeletal muscle
    • Colley, N.J., K.T. Tokuyasu, and S.J. Singer. 1990. The early expression of myofibrillar proteins in round post mitotic myoblasts of embryonic skeletal muscle. J. Cell Sci. 95:11-22.
    • (1990) J. Cell Sci. , vol.95 , pp. 11-22
    • Colley, N.J.1    Tokuyasu, K.T.2    Singer, S.J.3
  • 15
    • 0020681351 scopus 로고
    • Architecture of metaphase chromosomes and chromosome scaffolds
    • Earnshaw, W.C., and U.K. Laemmli. 1983. Architecture of metaphase chromosomes and chromosome scaffolds. J. Cell Biol. 96:84-93.
    • (1983) J. Cell Biol. , vol.96 , pp. 84-93
    • Earnshaw, W.C.1    Laemmli, U.K.2
  • 16
    • 0026270240 scopus 로고
    • The use of autoantibodies in the study of nuclear and chromosomal organization
    • Earnshaw, W.C., and J.B. Rattner. 1991. The use of autoantibodies in the study of nuclear and chromosomal organization. Methods Cell Biol. 35:135-175.
    • (1991) Methods Cell Biol. , vol.35 , pp. 135-175
    • Earnshaw, W.C.1    Rattner, J.B.2
  • 17
    • 0028030935 scopus 로고
    • Role of nonhistone proteins in the chromosomal events of mitosis, FASEB Fed
    • Earnshaw, W.C., and A.M. Mackay. 1994. Role of nonhistone proteins in the chromosomal events of mitosis, FASEB (Fed. Am. Soc. Exp. Biol.) J. 8:947-956.
    • (1994) Am. Soc. Exp. Biol. J. , vol.8 , pp. 947-956
    • Earnshaw, W.C.1    Mackay, A.M.2
  • 18
    • 0027956823 scopus 로고
    • Cellular titin localization in stress fibers and interaction with myosin II filaments in vitro
    • Eilertsen, K.J., S.T. Kazmierski, and T.C.S. Keller III. 1994. Cellular titin localization in stress fibers and interaction with myosin II filaments in vitro. J. Cell Biol. 126:1201-1210.
    • (1994) J. Cell Biol. , vol.126 , pp. 1201-1210
    • Eilertsen, K.J.1    Kazmierski, S.T.2    Keller III, T.C.S.3
  • 19
    • 0016738812 scopus 로고
    • The proteins of polytene chromosomes of Drosophila hydei
    • Elgin, S.C.R., and J.B. Boyd. 1975. The proteins of polytene chromosomes of Drosophila hydei. Chromosoma. 51:135-145.
    • (1975) Chromosoma , vol.51 , pp. 135-145
    • Elgin, S.C.R.1    Boyd, J.B.2
  • 21
    • 0030052266 scopus 로고    scopus 로고
    • A molecular map of the interaction between titin and myosin-binding protein C. Implications for sarcomeric assembly in familial hypertrophic cardiomyopathy
    • Freiburg, A., and M. Gautel. 1996. A molecular map of the interaction between titin and myosin-binding protein C. Implications for sarcomeric assembly in familial hypertrophic cardiomyopathy. Eur. J. Biochem. 235:317-323.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 317-323
    • Freiburg, A.1    Gautel, M.2
  • 22
    • 0031050603 scopus 로고    scopus 로고
    • Autoantibodies: Diagnostic fingerprints and etiological perplexities
    • Fritzler, M.J. 1997. Autoantibodies: diagnostic fingerprints and etiological perplexities. Clin. Invest. Med. 20:103-115.
    • (1997) Clin. Invest. Med. , vol.20 , pp. 103-115
    • Fritzler, M.J.1
  • 23
    • 0030989899 scopus 로고    scopus 로고
    • Organization of protein and mRNA for titin and other myofibril components during myofibrillogenesis in cultured chicken skeletal muscle
    • Fulton, A.B., and C. Alftine. 1997. Organization of protein and mRNA for titin and other myofibril components during myofibrillogenesis in cultured chicken skeletal muscle. Cell Struct. Funct. 22:51-58.
    • (1997) Cell Struct. Funct. , vol.22 , pp. 51-58
    • Fulton, A.B.1    Alftine, C.2
  • 24
    • 0023924769 scopus 로고
    • The organization of titin filaments in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy: A map of ten nonrepetitive epitopes starting at the Z-line extends close to the M-line
    • Fürst, D.O., M. Osborn, R. Nave, and K. Weber. 1988. The organization of titin filaments in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy: a map of ten nonrepetitive epitopes starting at the Z-line extends close to the M-line. J. Cell Biol. 106:1563-1572.
    • (1988) J. Cell Biol. , vol.106 , pp. 1563-1572
    • Fürst, D.O.1    Osborn, M.2    Nave, R.3    Weber, K.4
  • 25
    • 0024727278 scopus 로고
    • Repetitive titin epitopes with a 42 nm spacing coincide in relative position with known a band striations also identified by major myosin-associated proteins. An immunoelectron-microscopical study on myofibrils
    • Fürst. D.O., R. Nave, M. Osborn, and K. Weber. 1989. Repetitive titin epitopes with a 42 nm spacing coincide in relative position with known A band striations also identified by major myosin-associated proteins. An immunoelectron-microscopical study on myofibrils. J. Cell Sci, 94:119-125.
    • (1989) J. Cell Sci , vol.94 , pp. 119-125
    • Fürst, D.O.1    Nave, R.2    Osborn, M.3    Weber, K.4
  • 26
    • 0025325694 scopus 로고
    • Molecular genetics of Drosophila α-actinin: Mutant alleles disrupt Z disk integrity and muscle insertions
    • Fyrberg, E., M. Kelly, E. Ball, C. Fyrberg, and M.C. Reedy. 1990. Molecular genetics of Drosophila α-actinin: mutant alleles disrupt Z disk integrity and muscle insertions. J. Cell Biol. 110:1999-2011.
    • (1990) J. Cell Biol. , vol.110 , pp. 1999-2011
    • Fyrberg, E.1    Kelly, M.2    Ball, E.3    Fyrberg, C.4    Reedy, M.C.5
  • 27
    • 0026768103 scopus 로고
    • Drosophila projectin: Relatedness to titin and twitchin and correlation with lethal(4)102 CDa and bent-dominant mutants
    • Fyrberg, C.C., S. Labeit, B. Bullard, B. Leonard, and E. Fyrberg. 1992. Drosophila projectin: relatedness to titin and twitchin and correlation with lethal(4)102 CDa and bent-dominant mutants. Proc. R. Lond. B. Biol. Sci. 249: 33-40.
    • (1992) Proc. R. Lond. B. Biol. Sci. , vol.249 , pp. 33-40
    • Fyrberg, C.C.1    Labeit, S.2    Bullard, B.3    Leonard, B.4    Fyrberg, E.5
  • 28
    • 0029882110 scopus 로고    scopus 로고
    • A molecular map of titin/connectin elasticity reveals two different mechanisms acting in series
    • Gautel, M., and D. Goulding. 1996. A molecular map of titin/connectin elasticity reveals two different mechanisms acting in series. FEBS (Fed. Eur. Biochem. Soc.) Lett. 385:11-14.
    • (1996) FEBS (Fed. Eur. Biochem. Soc.) Lett. , vol.385 , pp. 11-14
    • Gautel, M.1    Goulding, D.2
  • 30
    • 0022443306 scopus 로고
    • A microtubule-associated protein in Drosophila melanogaster, identification, characterization, and isolation of coding sequences
    • Goldstein, L.S.B., R.A. Laymon, and J.R. McIntosh. 1986. A microtubule-associated protein in Drosophila melanogaster, identification, characterization, and isolation of coding sequences. J. Cell Biol. 102:2076-2087.
    • (1986) J. Cell Biol. , vol.102 , pp. 2076-2087
    • Goldstein, L.S.B.1    Laymon, R.A.2    McIntosh, J.R.3
  • 31
    • 0030886602 scopus 로고    scopus 로고
    • A direct link between sister chromatid cohesion and chromosome condensation revealed through the analysis of MCD1 in S. cerevisiae
    • Guacci, V., D. Koshland, and A. Strunnikov. 1997. A direct link between sister chromatid cohesion and chromosome condensation revealed through the analysis of MCD1 in S. cerevisiae. Cell. 91:59-70.
    • (1997) Cell , vol.91 , pp. 59-70
    • Guacci, V.1    Koshland, D.2    Strunnikov, A.3
  • 32
    • 0003687473 scopus 로고
    • Cold Spring Harbor Laboratory Press, Plainview, New York
    • Hartenstein, V. 1993. Atlas of Drosophila development. Cold Spring Harbor Laboratory Press, Plainview, New York. 57 pp.
    • (1993) Atlas of Drosophila Development
    • Hartenstein, V.1
  • 33
    • 0029081926 scopus 로고
    • Biochemical and genetic dissection of mitotic chromosome condensation
    • Hirano, T. 1995. Biochemical and genetic dissection of mitotic chromosome condensation. Trends Biochem. Sci. 20:357-361.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 357-361
    • Hirano, T.1
  • 34
    • 0027943721 scopus 로고
    • A heterodimeric coiled-coil protein required for mitotic chromosome condensation in vitro
    • Hirano, T., and T.J. Mitchison. 1994. A heterodimeric coiled-coil protein required for mitotic chromosome condensation in vitro. Cell. 79:449-458.
    • (1994) Cell , vol.79 , pp. 449-458
    • Hirano, T.1    Mitchison, T.J.2
  • 35
    • 0030830639 scopus 로고    scopus 로고
    • Condensins, chromosome condensation protein complexes containing XCAP-C, XCAP-E and a Xenopus homolog of the Drosophila Barren protein
    • Hirano, T., R. Kobayashi, and M. Hirano. 1997. Condensins, chromosome condensation protein complexes containing XCAP-C, XCAP-E and a Xenopus homolog of the Drosophila Barren protein. Cell. 89:511-521.
    • (1997) Cell , vol.89 , pp. 511-521
    • Hirano, T.1    Kobayashi, R.2    Hirano, M.3
  • 36
    • 0029943216 scopus 로고    scopus 로고
    • An extragenic suppressor of the mitosis-defective bim6 mutation of Aspergillus nidulans codes for a chromosome scaffold protein
    • Holt, C.L., and G.S. May. 1996. An extragenic suppressor of the mitosis-defective bim6 mutation of Aspergillus nidulans codes for a chromosome scaffold protein. Genetics. 142:777-787.
    • (1996) Genetics , vol.142 , pp. 777-787
    • Holt, C.L.1    May, G.S.2
  • 37
    • 0030879072 scopus 로고    scopus 로고
    • Elasticity and structure of eukaryote chromosomes studied by micromanipulation and micropipette aspiration
    • Houchmandzadeh, B., J.F. Marko, D. Chatenay, and A. Libchaber. 1997. Elasticity and structure of eukaryote chromosomes studied by micromanipulation and micropipette aspiration. J. Cell Biol. 139:1-12.
    • (1997) J. Cell Biol. , vol.139 , pp. 1-12
    • Houchmandzadeh, B.1    Marko, J.F.2    Chatenay, D.3    Libchaber, A.4
  • 38
    • 0029593486 scopus 로고
    • Studies of the interaction between titin and myosin
    • Houmeida, A., J. Holt, L. Tskhovrebova, and J. Trinick. 1995. Studies of the interaction between titin and myosin. J. Cell Biol. 131:1471-1481.
    • (1995) J. Cell Biol. , vol.131 , pp. 1471-1481
    • Houmeida, A.1    Holt, J.2    Tskhovrebova, L.3    Trinick, J.4
  • 39
    • 0023756132 scopus 로고
    • Extensible and less-extensible domains of connectin filaments in stretched vertebrate skeletal muscle as detected by immunofluorescence and immunoelectron microscopy using monoclonal antibodies
    • Itoh, Y., T. Suzuki, S. Kimura, K. Ohashi, H. Higuchi, H. Sawada, T. Shimizu, M. Shibata, and K. Maruyama. 1988. Extensible and less-extensible domains of connectin filaments in stretched vertebrate skeletal muscle as detected by immunofluorescence and immunoelectron microscopy using monoclonal antibodies. J. Biochem. 104:504-508.
    • (1988) J. Biochem. , vol.104 , pp. 504-508
    • Itoh, Y.1    Suzuki, T.2    Kimura, S.3    Ohashi, K.4    Higuchi, H.5    Sawada, H.6    Shimizu, T.7    Shibata, M.8    Maruyama, K.9
  • 41
    • 0022761554 scopus 로고
    • Non-kinetochore directed autoantibodies in scleroderma/CREST. Identification of an activity recognizing a metaphase chromosome core non-histone protein
    • Jeppesen, P., and L. Nicol. 1986. Non-kinetochore directed autoantibodies in scleroderma/CREST. Identification of an activity recognizing a metaphase chromosome core non-histone protein. Mol. Biol. Med. 3:369-384.
    • (1986) Mol. Biol. Med. , vol.3 , pp. 369-384
    • Jeppesen, P.1    Nicol, L.2
  • 42
    • 0028955760 scopus 로고
    • Structure and function of titin and nebulin
    • Keller, T.C.S. 1995. Structure and function of titin and nebulin. Curr. Opin. Cell Biol. 7:32-33.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 32-33
    • Keller, T.C.S.1
  • 43
    • 0031002460 scopus 로고    scopus 로고
    • Folding-unfolding transitions in single titin molecules characterized with laser tweezers
    • Kellermayer, M.S.Z., S.B, Smith, H.L. Granzier, and C. Bustamante. 1997. Folding-unfolding transitions in single titin molecules characterized with laser tweezers. Science. 276:1112-1116.
    • (1997) Science , vol.276 , pp. 1112-1116
    • Kellermayer, M.S.Z.1    Smith, S.B.2    Granzier, H.L.3    Bustamante, C.4
  • 44
    • 0030874421 scopus 로고    scopus 로고
    • ATP-dependent positive supercoiling of DNA by 13S condensin: A biochemical implication for chromosome condensation
    • Kimura, K., and T. Hirano. 1997. ATP-dependent positive supercoiling of DNA by 13S condensin: a biochemical implication for chromosome condensation. Cell. 90:625-634.
    • (1997) Cell , vol.90 , pp. 625-634
    • Kimura, K.1    Hirano, T.2
  • 45
    • 0031172869 scopus 로고    scopus 로고
    • Muscle-specific calpain, p94, interacts with the extreme C-terminal region of connectin, a unique region flanked by two immunoglobulin C2 motifs
    • Kinbara, K., H. Sorimachi, S. Ishiura, and K. Suzuki. 1997. Muscle-specific calpain, p94, interacts with the extreme C-terminal region of connectin, a unique region flanked by two immunoglobulin C2 motifs. Arch. Biochem. Biophys. 342:99-107.
    • (1997) Arch. Biochem. Biophys. , vol.342 , pp. 99-107
    • Kinbara, K.1    Sorimachi, H.2    Ishiura, S.3    Suzuki, K.4
  • 46
    • 0029919189 scopus 로고    scopus 로고
    • Genomic organization of the M-line titin and its tissue-specific expression in two distinct isoforms
    • Kolmerer, B., N. Olivieri, C. Witt, B.G. Herrmann, and S. Labeit. 1996. Genomic organization of the M-line titin and its tissue-specific expression in two distinct isoforms. J. Mol. Biol. 256:556-563.
    • (1996) J. Mol. Biol. , vol.256 , pp. 556-563
    • Kolmerer, B.1    Olivieri, N.2    Witt, C.3    Herrmann, B.G.4    Labeit, S.5
  • 48
    • 0028824480 scopus 로고
    • Titins, giant proteins in charge of muscle ultrastructure and elasticity
    • Labeit, S., and B. Kolmerer. 1995. Titins, giant proteins in charge of muscle ultrastructure and elasticity. Science. 270:293-296.
    • (1995) Science , vol.270 , pp. 293-296
    • Labeit, S.1    Kolmerer, B.2
  • 52
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 56
    • 0020324697 scopus 로고
    • Higher order metaphase chromosome structure: Evidence for metalloprotein interactions
    • Lewis, C.D., and U.K. Laemmli. 1982. Higher order metaphase chromosome structure: evidence for metalloprotein interactions. Cell. 29:171-181.
    • (1982) Cell , vol.29 , pp. 171-181
    • Lewis, C.D.1    Laemmli, U.K.2
  • 58
    • 0030851380 scopus 로고    scopus 로고
    • Actin-titin interaction in cardiac myofibrils: Probing a physiological role
    • Linke, W.A., M. Ivemeyer, S. Labeit, H. Hinssen, J.C. Ruegg, and M. Gautel. 1997. Actin-titin interaction in cardiac myofibrils: probing a physiological role. Biophys. J. 73:905-919.
    • (1997) Biophys. J. , vol.73 , pp. 905-919
    • Linke, W.A.1    Ivemeyer, M.2    Labeit, S.3    Hinssen, H.4    Ruegg, J.C.5    Gautel, M.6
  • 59
    • 0030982846 scopus 로고    scopus 로고
    • Connectin/titin, giant elastic protein of muscle
    • Maruyama, K. 1997. Connectin/titin, giant elastic protein of muscle. FASEB (Fed. Am. Soc. Exp. Biol.) J. 11:341-345.
    • (1997) FASEB (Fed. Am. Soc. Exp. Biol.) J. , vol.11 , pp. 341-345
    • Maruyama, K.1
  • 62
    • 0030885925 scopus 로고    scopus 로고
    • Cohesins: Chromosomal proteins that prevent premature separation of sister chromatids
    • Michaelis. C., R. Ciosk, and K. Nasmyth. 1997. Cohesins: chromosomal proteins that prevent premature separation of sister chromatids. Cell. 91:47-58.
    • (1997) Cell , vol.91 , pp. 47-58
    • Michaelis, C.1    Ciosk, R.2    Nasmyth, K.3
  • 63
    • 0023776666 scopus 로고
    • Identification and intracellular localization of the unc-22 gene product of Caenorhabditis elegans
    • Moerman, G.D., G.M. Benian, R.J. Barstead, L.A. Schrieffer, and R.H. Waterston. 1988. Identification and intracellular localization of the unc-22 gene product of Caenorhabditis elegans. Genes Dev. 2:93-105.
    • (1988) Genes Dev. , vol.2 , pp. 93-105
    • Moerman, G.D.1    Benian, G.M.2    Barstead, R.J.3    Schrieffer, L.A.4    Waterston, R.H.5
  • 64
    • 0025339387 scopus 로고
    • Autoantibodies from a patient with scleroderma CREST recognized kinetochores of the higher plant Haemanthus
    • Mole-Bajer, J., A.S. Bajer, R.P. Zinkowski, R.D. Balczon, and B.R. Brinkley. 1990. Autoantibodies from a patient with scleroderma CREST recognized kinetochores of the higher plant Haemanthus. Proc. Natl. Acad. Sci. USA. 17:1627-1631.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.17 , pp. 1627-1631
    • Mole-Bajer, J.1    Bajer, A.S.2    Zinkowski, R.P.3    Balczon, R.D.4    Brinkley, B.R.5
  • 65
    • 0020050314 scopus 로고
    • A catalogue of splice junction sequences
    • Mount, S.M. 1982. A catalogue of splice junction sequences. Nucleic Acids Res. 10:459-172.
    • (1982) Nucleic Acids Res. , vol.10 , pp. 459-1172
    • Mount, S.M.1
  • 66
    • 0026657738 scopus 로고
    • Splicing signals in Drosophila: Intron size, information content and consensus sequences
    • Mount, S.M., C. Burks, G. Hertz, G.D. Stormo, O. White, and C. Fields. 1992. Splicing signals in Drosophila: intron size, information content and consensus sequences. Nucleic Acids Res. 20:4255-4262.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 4255-4262
    • Mount, S.M.1    Burks, C.2    Hertz, G.3    Stormo, G.D.4    White, O.5    Fields, C.6
  • 67
    • 0026517110 scopus 로고
    • Update on autoantibodies to intracellular antigens in systemic rheumatic diseases
    • Nakamura, R.M., and E.M. Tan. 1992. Update on autoantibodies to intracellular antigens in systemic rheumatic diseases. Clin. Lab. Med. 12:1-23.
    • (1992) Clin. Lab. Med. , vol.12 , pp. 1-23
    • Nakamura, R.M.1    Tan, E.M.2
  • 68
    • 0029836627 scopus 로고    scopus 로고
    • The structure of the sarcomeric M band: Localization of defined domains of myomesin, M-protein, and the 250-kD carboxy-terminal region of titin by immunoelectron microscopy
    • Obermann, W.M., M. Gautel, F. Steiner, P.F. van der Ven, K. Weber, and D.O. Fürst. 1996. The structure of the sarcomeric M band: localization of defined domains of myomesin, M-protein, and the 250-kD carboxy-terminal region of titin by immunoelectron microscopy. J. Cell Biol. 134:1441-1453.
    • (1996) J. Cell Biol. , vol.134 , pp. 1441-1453
    • Obermann, W.M.1    Gautel, M.2    Steiner, F.3    Van Der Ven, P.F.4    Weber, K.5    Fürst, D.O.6
  • 69
    • 0031034775 scopus 로고    scopus 로고
    • Molecular structure of the sarcomeric M band: Mapping of titin and myosin binding domains in myomesin and the identification of a potential regulatory phosphorylation site in myomesin
    • Obermann, W.M., M. Gautel, K. Weber, and D.O. Fürst. 1997. Molecular structure of the sarcomeric M band: mapping of titin and myosin binding domains in myomesin and the identification of a potential regulatory phosphorylation site in myomesin. EMBO (Eur. Mol. Biol. Organ.) J. 16:211-220.
    • (1997) EMBO (Eur. Mol. Biol. Organ.) J. , vol.16 , pp. 211-220
    • Obermann, W.M.1    Gautel, M.2    Weber, K.3    Fürst, D.O.4
  • 70
    • 0031027371 scopus 로고    scopus 로고
    • Binding of the N-terminal 63 kD portion of connectin/titin to α-actinin as revealed by the yeast two-hybrid system
    • Ohtsuka, H., H. Yajima, K. Maruyama, and S. Kimura. 1997a. Binding of the N-terminal 63 kD portion of connectin/titin to α-actinin as revealed by the yeast two-hybrid system. FEBS (Fed. Eur. Biochem. Soc.) Lett. 401:65-67.
    • (1997) FEBS (Fed. Eur. Biochem. Soc.) Lett. , vol.401 , pp. 65-67
    • Ohtsuka, H.1    Yajima, H.2    Maruyama, K.3    Kimura, S.4
  • 71
    • 0031560933 scopus 로고    scopus 로고
    • The N-terminal Z-repeat 5 of connectin/titin binds to the C-terminal region of α-actinin
    • Ohtsuka, H., H. Yajima, K. Maruyama, and S. Kimura. 1997b. The N-terminal Z-repeat 5 of connectin/titin binds to the C-terminal region of α-actinin. Biochem. Biophys. Res. Commun. 235:1-3.
    • (1997) Biochem. Biophys. Res. Commun. , vol.235 , pp. 1-3
    • Ohtsuka, H.1    Yajima, H.2    Maruyama, K.3    Kimura, S.4
  • 72
    • 0017652886 scopus 로고
    • The structure of histone-depleted chromosomes
    • Paulson, J.R., and U.K. Laemmli. 1977. The structure of histone-depleted chromosomes. Cell. 12:817-828.
    • (1977) Cell , vol.12 , pp. 817-828
    • Paulson, J.R.1    Laemmli, U.K.2
  • 73
    • 0028134978 scopus 로고
    • The SMC family: Novel motor proteins for chromosome condensation?
    • Peterson, C.L. 1994. The SMC family: novel motor proteins for chromosome condensation? Cell. 79:389-392.
    • (1994) Cell , vol.79 , pp. 389-392
    • Peterson, C.L.1
  • 74
    • 0028225834 scopus 로고
    • Immunodetection of the ribosomal transcription factor UBF at the nucleolus organizer regions of fish cells
    • Rendon, M.C., J. Bolivar, M. Ortiz, and M.M. Valdivia. 1994. Immunodetection of the ribosomal transcription factor UBF at the nucleolus organizer regions of fish cells. Cell Struct. Funct. 19:153-158.
    • (1994) Cell Struct. Funct. , vol.19 , pp. 153-158
    • Rendon, M.C.1    Bolivar, J.2    Ortiz, M.3    Valdivia, M.M.4
  • 75
    • 0025602161 scopus 로고
    • Homeotic genes regulate the spatial expression of putative growth factors in the visceral mesoderm of Drosophila embryos
    • Reuter, R., G.E.F. Panganiban, F.M. Hoffmann, and M.P. Scott. 1990. Homeotic genes regulate the spatial expression of putative growth factors in the visceral mesoderm of Drosophila embryos. Development. 110:1031-1040
    • (1990) Development , vol.110 , pp. 1031-1040
    • Reuter, R.1    Panganiban, G.E.F.2    Hoffmann, F.M.3    Scott, M.P.4
  • 76
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • Rief, M., M. Gautel, F. Oesterhelt, J.M. Fernandez, and H.E. Gaub. 1997. Reversible unfolding of individual titin immunoglobulin domains by AFM. Science. 276:1109-1112.
    • (1997) Science , vol.276 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 77
    • 0022523423 scopus 로고
    • Identification and immunochemical analysis of biologically active Drosophila P-element transposase
    • Rio, D.C., F.A. Laski, and G.M. Rubin. 1986. Identification and immunochemical analysis of biologically active Drosophila P-element transposase. Cell 44: 21-32.
    • (1986) Cell , vol.44 , pp. 21-32
    • Rio, D.C.1    Laski, F.A.2    Rubin, G.M.3
  • 79
    • 0029360376 scopus 로고
    • The SMC proteins and the coming of age of the chromosome scaffold hypothesis
    • Saitoh, N., I. Goldberg, and W.C. Earnshaw. 1995. The SMC proteins and the coming of age of the chromosome scaffold hypothesis. BioEssays. 17:759-706.
    • (1995) BioEssays , vol.17 , pp. 759-1706
    • Saitoh, N.1    Goldberg, I.2    Earnshaw, W.C.3
  • 80
    • 0029143271 scopus 로고
    • Characterization of a 5.4 kb cDNa fragment from the Z-line of rabbit cardiac titin reveals phosphorylation sites for proline-directed kinases
    • Sebastyén, M.G., J.A. Wolff, and M.L. Greaser. 1995. Characterization of a 5.4 kb cDNA fragment from the Z-line of rabbit cardiac titin reveals phosphorylation sites for proline-directed kinases. J. Cell Sci. 108:3029-3037.
    • (1995) J. Cell Sci. , vol.108 , pp. 3029-3037
    • Sebastyén, M.G.1    Wolff, J.A.2    Greaser, M.L.3
  • 81
    • 0027242301 scopus 로고
    • Immunochemical and molecular characterization of anti-RNA polymerase I autoantibodies produced by tight skin mouse
    • Shibata, S., T. Muryos, Y. Saitoh, T.D. Brumeanu, C.A, Bona, and K.N. Katuri. 1993. Immunochemical and molecular characterization of anti-RNA polymerase I autoantibodies produced by tight skin mouse. J. Clin. Invest 92:984-992.
    • (1993) J. Clin. Invest , vol.92 , pp. 984-992
    • Shibata, S.1    Muryos, T.2    Saitoh, Y.3    Brumeanu, T.D.4    Bona, C.A.5    Katuri, K.N.6
  • 82
    • 0024282772 scopus 로고
    • A gene important for chromosome segregation and other mitotic functions in S. cerevisiae
    • Snyder, M., and R.W. Davis. 1988. A gene important for chromosome segregation and other mitotic functions in S. cerevisiae. Cell. 54:743-754.
    • (1988) Cell , vol.54 , pp. 743-754
    • Snyder, M.1    Davis, R.W.2
  • 85
    • 0027536473 scopus 로고
    • A survey of the interactions made by the giant protein titin
    • Soteriou, A., M. Gamage, and J. Trinick. 1993. A survey of the interactions made by the giant protein titin. J. Cell Sci. 104:119-123.
    • (1993) J. Cell Sci. , vol.104 , pp. 119-123
    • Soteriou, A.1    Gamage, M.2    Trinick, J.3
  • 86
    • 0030967587 scopus 로고    scopus 로고
    • Architecture and function in the muscle sarcomere
    • Squire, J.M. 1997. Architecture and function in the muscle sarcomere. Curr. Opin. Struct. Biol. 7:247-257.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 247-257
    • Squire, J.M.1
  • 87
    • 0028942904 scopus 로고
    • SMC-2, a Saccharomyces cerevisiae gene essential for chromosome segregation and condensation defines a subgroup within the SMC-family
    • Strunnikov, A.V., E. Hogan, and D. Koshland. 1995. SMC-2, a Saccharomyces cerevisiae gene essential for chromosome segregation and condensation defines a subgroup within the SMC-family. Genes Dev. 9:587-599.
    • (1995) Genes Dev. , vol.9 , pp. 587-599
    • Strunnikov, A.V.1    Hogan, E.2    Koshland, D.3
  • 88
    • 0030826133 scopus 로고    scopus 로고
    • DNA renaturation activity of the SMC complex implicated in chromosome condensation
    • Sutani, T., and M. Yanagida. 1997. DNA renaturation activity of the SMC complex implicated in chromosome condensation. Nature. 388:798-801.
    • (1997) Nature , vol.388 , pp. 798-801
    • Sutani, T.1    Yanagida, M.2
  • 91
    • 0024518559 scopus 로고
    • Antinuclear antibodies: Diagnostic markers for autoimmune diseases and probes for cell biology
    • Tan, E.M. 1989. Antinuclear antibodies: diagnostic markers for autoimmune diseases and probes for cell biology. Adv. Immunol. 44:93-151.
    • (1989) Adv. Immunol. , vol.44 , pp. 93-151
    • Tan, E.M.1
  • 92
    • 0025786163 scopus 로고
    • Autoantibodies in pathology and cell biology
    • Tan, E.M. 1991. Autoantibodies in pathology and cell biology. Cell. 67:841-842.
    • (1991) Cell , vol.67 , pp. 841-842
    • Tan, E.M.1
  • 93
    • 0023484775 scopus 로고
    • Intracellular autoantigens: Diagnostic fingerprints but etiological dilemmas
    • D. Evered and J. Whelan, editors. John Wiley & Sons, Chichester, NY
    • Tan, E.M., G. Reimer, and K. Sullivan. 1987. Intracellular autoantigens: diagnostic fingerprints but etiological dilemmas. In Autoimmunity and autoimmune disease. D. Evered and J. Whelan, editors. John Wiley & Sons, Chichester, NY. 25-42.
    • (1987) Autoimmunity and Autoimmune Disease , pp. 25-42
    • Tan, E.M.1    Reimer, G.2    Sullivan, K.3
  • 94
    • 0024319520 scopus 로고
    • A non-radioactive in situ hybridization method for the localization of specific RNAs in Drosophila embryos reveals transtational control of the segmentation gene hunchback
    • Tautz, D., and C. Pfeifle. 1989. A non-radioactive in situ hybridization method for the localization of specific RNAs in Drosophila embryos reveals transtational control of the segmentation gene hunchback. Chromosoma. 98:81-85.
    • (1989) Chromosoma , vol.98 , pp. 81-85
    • Tautz, D.1    Pfeifle, C.2
  • 95
    • 0016373748 scopus 로고
    • Protein synthesis in salivary glands of Drosophila melanogaster. relation to chromosome puffs
    • Tissièrres, A., H.K. Mitchell, and U.M. Tracy. 1974. Protein synthesis in salivary glands of Drosophila melanogaster. relation to chromosome puffs. J. Mol. Biol. 84:389-398.
    • (1974) J. Mol. Biol. , vol.84 , pp. 389-398
    • Tissièrres, A.1    Mitchell, H.K.2    Tracy, U.M.3
  • 96
    • 0028091960 scopus 로고
    • Titin and nebulin: Protein rulers in muscle?
    • Trinick, J. 1994. Titin and nebulin: protein rulers in muscle? Trends Biochem. Sci. 19:405-408.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 405-408
    • Trinick, J.1
  • 97
    • 0030091595 scopus 로고    scopus 로고
    • Titin as a scaffold and spring
    • Trinick, J. 1996. Titin as a scaffold and spring. Cytoskeleton Curr. Biol. 6:258-260.
    • (1996) Cytoskeleton Curr. Biol. , vol.6 , pp. 258-260
    • Trinick, J.1
  • 98
    • 0030821918 scopus 로고    scopus 로고
    • Actin removal from cardiac myocytes shows that near Z line titin attaches to actin while under tension
    • Trombitas, K., and H. Granzier. 1997. Actin removal from cardiac myocytes shows that near Z line titin attaches to actin while under tension. Am. J. Physiol. 273:662-670.
    • (1997) Am. J. Physiol. , vol.273 , pp. 662-670
    • Trombitas, K.1    Granzier, H.2
  • 99
    • 0030976481 scopus 로고    scopus 로고
    • Interaction between titin and thin filaments in intact cardiac muscle
    • Trombitas, K., M.L. Greaser, and G.H. Pollack. 1997. Interaction between titin and thin filaments in intact cardiac muscle. J. Muscle Res. Cell Motil 18:345-351.
    • (1997) J. Muscle Res. Cell Motil , vol.18 , pp. 345-351
    • Trombitas, K.1    Greaser, M.L.2    Pollack, G.H.3
  • 100
    • 0032559640 scopus 로고    scopus 로고
    • Titin extensibility in situ: Entropie elasticity of permanently folded and permanently unfolded molecular segments
    • Trombitas, K., M. Greaser, S. Labeit, J.-P. Jin, M. Kellermayer, M. Helmes, and H. Granzier. 1998. Titin extensibility in situ: entropie elasticity of permanently folded and permanently unfolded molecular segments. J. Cell Biol. 140:853-859.
    • (1998) J. Cell Biol. , vol.140 , pp. 853-859
    • Trombitas, K.1    Greaser, M.2    Labeit, S.3    Jin, J.-P.4    Kellermayer, M.5    Helmes, M.6    Granzier, H.7
  • 101
    • 0031006659 scopus 로고    scopus 로고
    • Elasticity and unfolding of single molecules of the giant muscle protein titin
    • Tskhovrebova, L., J. Trinick, J.A. Sleep, and R.M. Simmons. 1997. Elasticity and unfolding of single molecules of the giant muscle protein titin. Nature. 387:308-312.
    • (1997) Nature. , vol.387 , pp. 308-312
    • Tskhovrebova, L.1    Trinick, J.2    Sleep, J.A.3    Simmons, R.M.4
  • 102
    • 0029949254 scopus 로고    scopus 로고
    • Partial characterization of zeugmatin indicates that it is part of the Z-band region of titin
    • Turnacioglu, K.K., B. Mittal, J.M. Sanger, and J.W. Sanger. 1996. Partial characterization of zeugmatin indicates that it is part of the Z-band region of titin. Cell Motil Cytoskeleton. 34:108-121.
    • (1996) Cell Motil Cytoskeleton. , vol.34 , pp. 108-121
    • Turnacioglu, K.K.1    Mittal, B.2    Sanger, J.M.3    Sanger, J.W.4
  • 103
    • 0031004299 scopus 로고    scopus 로고
    • An N-terminal fragment of titin coupled to green fluorescent protein localizes to the Z-bands in living muscle cells: Overexpression leads to myofibril disassembly
    • Turnacioglu, K.K., B. Mittal, G.A. Dabiri, J.M. Sanger, and J.W. Sanger. 1997. An N-terminal fragment of titin coupled to green fluorescent protein localizes to the Z-bands in living muscle cells: overexpression leads to myofibril disassembly. Mol. Biol. Cell. 8:705-717.
    • (1997) Mol. Biol. Cell. , vol.8 , pp. 705-717
    • Turnacioglu, K.K.1    Mittal, B.2    Dabiri, G.A.3    Sanger, J.M.4    Sanger, J.W.5
  • 104
    • 1842334510 scopus 로고    scopus 로고
    • Assembly of titin, myomesin and M-protein into the sarcomeric M band in differentiating human skeletal muscle cells in vitro
    • van der Ven, P.F., and D.O. Fürst. 1997. Assembly of titin, myomesin and M-protein into the sarcomeric M band in differentiating human skeletal muscle cells in vitro. Cell Struct. Funct. 22:163-171.
    • (1997) Cell Struct. Funct. , vol.22 , pp. 163-171
    • Van Der Ven, P.F.1    Fürst, D.O.2
  • 106
    • 0024400452 scopus 로고
    • Electrophoretic transfer of high-molecular weight proteins for immunostaining
    • Wang, K., B.O. Fanger, C.A. Guyer, and J.V. Staros. 1989. Electrophoretic transfer of high-molecular weight proteins for immunostaining. Methods Enzymol. 172:687-696.
    • (1989) Methods Enzymol. , vol.172 , pp. 687-696
    • Wang, K.1    Fanger, B.O.2    Guyer, C.A.3    Staros, J.V.4
  • 107
    • 0025816649 scopus 로고
    • Regulation of skeletal muscle stiffness and elasticity by titin isoforms: A test of segmental extension model of resting tension
    • Wang, K., R. McCarter, R. Wright, J. Beverly, and R. Ramirez-Mitchell. 1991. Regulation of skeletal muscle stiffness and elasticity by titin isoforms: a test of segmental extension model of resting tension. Proc. Natl. Acad. Sci. USA. 88:7101-7105.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7101-7105
    • Wang, K.1    McCarter, R.2    Wright, R.3    Beverly, J.4    Ramirez-Mitchell, R.5
  • 108
    • 0031081432 scopus 로고    scopus 로고
    • Untangling the role of DNA topo-isomerase II in mitotic chromosome structure and function
    • Warburton, P.E., and W.C. Earnshaw. 1997. Untangling the role of DNA topo-isomerase II in mitotic chromosome structure and function. BioEssays. 19: 97-99.
    • (1997) BioEssays , vol.19 , pp. 97-99
    • Warburton, P.E.1    Earnshaw, W.C.2
  • 109
    • 0018961312 scopus 로고
    • Mutants with altered muscle structure in Caenorhabditis elegans
    • Waterston, R.H., J.N. Thomson, and S. Brenner. 1980. Mutants with altered muscle structure in Caenorhabditis elegans. Dev. Biol. 77:271-302.
    • (1980) Dev. Biol. , vol.77 , pp. 271-302
    • Waterston, R.H.1    Thomson, J.N.2    Brenner, S.3
  • 110
    • 0029963412 scopus 로고    scopus 로고
    • Immunopathogenesis of systemic sclerosis
    • White, B. 1996. Immunopathogenesis of systemic sclerosis. Rheum. Dis. Clin. N. Am. 22:695-735.
    • (1996) Rheum. Dis. Clin. N. Am. , vol.22 , pp. 695-735
    • White, B.1
  • 111
    • 0024961666 scopus 로고
    • Does titin regulate the length of muscle thick filaments?
    • Whiting, A., J. Wardale, and J. Trinick. 1989. Does titin regulate the length of muscle thick filaments? J. Mol. Biol. 205:163-169.
    • (1989) J. Mol. Biol. , vol.205 , pp. 163-169
    • Whiting, A.1    Wardale, J.2    Trinick, J.3
  • 113
    • 0024292597 scopus 로고
    • Sequence analysis and neuronal expression of Fasciclin I in grasshopper and Drosophila
    • Zinn, K., L. McAllister, and C.S. Goodman. 1988. Sequence analysis and neuronal expression of Fasciclin I in grasshopper and Drosophila. Cell. 53:577-587.
    • (1988) Cell , vol.53 , pp. 577-587
    • Zinn, K.1    McAllister, L.2    Goodman, C.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.