메뉴 건너뛰기




Volumn 2, Issue , 2001, Pages

Genomic organization of Tropomodulins 2 and 4 and unusual intergenic and intraexonic splicing of YL-I and Tropomodulin 4

Author keywords

[No Author keywords available]

Indexed keywords

DNA; GENE PRODUCT; PROTEIN YL 1; TROPOMODULIN; TROPOMODULIN 2; TROPOMODULIN 4; UNCLASSIFIED DRUG;

EID: 9144248619     PISSN: 14712164     EISSN: None     Source Type: Journal    
DOI: 10.1186/1471-2164-2-7     Document Type: Article
Times cited : (14)

References (42)
  • 2
    • 0026787699 scopus 로고
    • Molecular cloning and characterization of human fetal liver tropomodulin. A tropomyosin-binding protein
    • Sung LA, Fowler VM, Lambert K, Sussman MA, Karr D, Chien S: Molecular cloning and characterization of human fetal liver tropomodulin. A tropomyosin-binding protein. J Biol Chem 1992, 267:2616-2621
    • (1992) J. Biol. Chem. , vol.267 , pp. 2616-2621
    • Sung, L.A.1    Fowler, V.M.2    Lambert, K.3    Sussman, M.A.4    Karr, D.5    Chien, S.6
  • 3
    • 0028365626 scopus 로고
    • Tropomodulin in rat cardiac muscle. Localization of protein is independent of messenger RNA distribution during myofibrillar development
    • Sussman MA, Sakhi S, Barrientos P, Ito M, Kedes L: Tropomodulin in rat cardiac muscle. Localization of protein is independent of messenger RNA distribution during myofibrillar development. Circ Res 1994, 75:221-232
    • (1994) Circ. Res. , vol.75 , pp. 221-232
    • Sussman, M.A.1    Sakhi, S.2    Barrientos, P.3    Ito, M.4    Kedes, L.5
  • 4
    • 0028837458 scopus 로고
    • Cloning of tropomodulin cDNA and localization of gene transcripts during mouse embryogenesis
    • Ito M, Swanson B, Sussman MA, Kedes L, Lyons G: Cloning of tropomodulin cDNA and localization of gene transcripts during mouse embryogenesis. Dev Biol 1995, 167:317-328
    • (1995) Dev. Biol. , vol.167 , pp. 317-328
    • Ito, M.1    Swanson, B.2    Sussman, M.A.3    Kedes, L.4    Lyons, G.5
  • 5
    • 0029838840 scopus 로고    scopus 로고
    • N-tropomodulin: A novel isoform of tropomodulin identified as the major binding protein to brain tropomyosin
    • Watakabe A, Kobayashi R, Helfman DM: N-tropomodulin: a novel isoform of tropomodulin identified as the major binding protein to brain tropomyosin. J Cell Sci 1996, 109:2299-2310
    • (1996) J. Cell Sci. , vol.109 , pp. 2299-2310
    • Watakabe, A.1    Kobayashi, R.2    Helfman, D.M.3
  • 7
    • 0033214493 scopus 로고    scopus 로고
    • Identification of a novel tropomodulin isoform, skeletal tropomodulin, that caps actin filament pointed ends in fast skeletal muscle
    • Almenar-Queralt A, Lee A, Conley CA, Ribas de Pouplana L, Fowler VM: Identification of a novel tropomodulin isoform, skeletal tropomodulin, that caps actin filament pointed ends in fast skeletal muscle. J Biol Chem 1999, 274:28466-28475
    • (1999) J. Biol. Chem. , vol.274 , pp. 28466-28475
    • Almenar-Queralt, A.1    Lee, A.2    Conley, C.A.3    Ribas de Pouplana, L.4    Fowler, V.M.5
  • 8
    • 0034001356 scopus 로고    scopus 로고
    • Sequencing, expression analysis, and mapping of three unique human tropomodulin genes and their mouse orthologs
    • Cox PR, Zoghbi HY: Sequencing, expression analysis, and mapping of three unique human tropomodulin genes and their mouse orthologs. Genomics 2000, 63:97-107
    • (2000) Genomics , vol.63 , pp. 97-107
    • Cox, P.R.1    Zoghbi, H.Y.2
  • 9
    • 0001027292 scopus 로고    scopus 로고
    • Gelsolin, a multifunctional actin regulatory protein
    • Sun HQ, Yamamoto M, Mejillano M, Yin HL: Gelsolin, a multifunctional actin regulatory protein. J Biol Chem 1999, 274:33179-33182
    • (1999) J. Biol. Chem. , vol.274 , pp. 33179-33182
    • Sun, H.Q.1    Yamamoto, M.2    Mejillano, M.3    Yin, H.L.4
  • 10
    • 0024421755 scopus 로고
    • Effects of CapZ, an actin capping protein of muscle, on the polymerization of actin
    • Caldwell JE, Heiss SG, Mermall V, Cooper JA: Effects of CapZ, an actin capping protein of muscle, on the polymerization of actin. Biochemistry 1989, 28:8506-8514
    • (1989) Biochemistry , vol.28 , pp. 8506-8514
    • Caldwell, J.E.1    Heiss, S.G.2    Mermall, V.3    Cooper, J.A.4
  • 11
    • 0030005249 scopus 로고    scopus 로고
    • A new function for adducin. Calcium/calmodulin-regulated capping of the barbed ends of actin filaments
    • Kuhlman PA, Hughes CA, Bennett V, Fowler VM: A new function for adducin. Calcium/calmodulin-regulated capping of the barbed ends of actin filaments. J Biol Chem 1996, 271:7986-7991
    • (1996) J. Biol. Chem. , vol.271 , pp. 7986-7991
    • Kuhlman, P.A.1    Hughes, C.A.2    Bennett, V.3    Fowler, V.M.4
  • 12
    • 0032407540 scopus 로고    scopus 로고
    • Defining actin filament length in striated muscle: Rulers and caps or dynamic stability?
    • Littlefield R, Fowler VM: Defining actin filament length in striated muscle: rulers and caps or dynamic stability? Annu Rev Cell Dev Biol 1998, 14:487-525
    • (1998) Annu. Rev. Cell. Dev. Biol. , vol.14 , pp. 487-525
    • Littlefield, R.1    Fowler, V.M.2
  • 13
    • 0029166140 scopus 로고
    • Requirement of pointed-end capping by tropomodulin to maintain actin filament length in embryonic chick cardiac myocytes
    • Gregorio CC, Weber A, Bondad M, Pennise CR, Fowler VM: Requirement of pointed-end capping by tropomodulin to maintain actin filament length in embryonic chick cardiac myocytes. Nature 1995, 377:83-86
    • (1995) Nature , vol.377 , pp. 83-86
    • Gregorio, C.C.1    Weber, A.2    Bondad, M.3    Pennise, C.R.4    Fowler, V.M.5
  • 16
    • 0028178083 scopus 로고
    • Alpha-tropomyosin and cardiac troponin T mutations cause familial hypertrophic cardiomyopathy: A disease of the sarcomere
    • Thierfelder L, Watkins H, MacRae C, Lamas R, McKenna W, Vosberg HP, Seidman JG, Seidman CE: Alpha-tropomyosin and cardiac troponin T mutations cause familial hypertrophic cardiomyopathy: a disease of the sarcomere. Cell 1994, 77:701-712
    • (1994) Cell , vol.77 , pp. 701-712
    • Thierfelder, L.1    Watkins, H.2    MacRae, C.3    Lamas, R.4    McKenna, W.5    Vosberg, H.P.6    Seidman, J.G.7    Seidman, C.E.8
  • 17
    • 0025164036 scopus 로고
    • A molecular basis for familial hypertrophic cardiomyopathy: An alpha/beta cardiac myosin heavy chain hybrid gene
    • Tanigawa G, Jarcho JA, Kass S, Solomon SD, Vosberg HP, Seidman JG, Seidman CE: A molecular basis for familial hypertrophic cardiomyopathy: an alpha/beta cardiac myosin heavy chain hybrid gene. Cell 1990, 62:991-998
    • (1990) Cell , vol.62 , pp. 991-998
    • Tanigawa, G.1    Jarcho, J.A.2    Kass, S.3    Solomon, S.D.4    Vosberg, H.P.5    Seidman, J.G.6    Seidman, C.E.7
  • 18
    • 0025040392 scopus 로고
    • A molecular basis for familial hypertrophic cardiomyopathy: A beta cardiac myosin heavy chain gene missense mutation
    • Geisterfer-Lowrance AA, Kass S, Tanigawa G, Vosberg HP, McKenna W, Seidman CE, Seidman JG: A molecular basis for familial hypertrophic cardiomyopathy: a beta cardiac myosin heavy chain gene missense mutation. Cell 1990, 62:999-1006
    • (1990) Cell , vol.62 , pp. 999-1006
    • Geisterfer-Lowrance, A.A.1    Kass, S.2    Tanigawa, G.3    Vosberg, H.P.4    McKenna, W.5    Seidman, C.E.6    Seidman, J.G.7
  • 21
    • 0027830664 scopus 로고
    • Hypertrophic cardiomyopathy: An update
    • McKenna WJ: Hypertrophic cardiomyopathy: an update. Cardiologia 1993, 38:277-281
    • (1993) Cardiologia , vol.38 , pp. 277-281
    • McKenna, W.J.1
  • 23
    • 0030898109 scopus 로고    scopus 로고
    • Genetic localization of a newly recognized autosomal dominant limb-girdle muscular dystrophy with cardiac involvement (LGMD1B) to chromosome 1q11-21
    • van der Kooi AJ, van Meegen M, Ledderhof TM, McNally EM, de Visser M, Bolhuis PA: Genetic localization of a newly recognized autosomal dominant limb-girdle muscular dystrophy with cardiac involvement (LGMD1B) to chromosome 1q11-21. Am J Hum Genet 1997, 60:891-895
    • (1997) Am. J. Hum. Genet. , vol.60 , pp. 891-895
    • van der Kooi, A.J.1    van Meegen, M.2    Ledderhof, T.M.3    McNally, E.M.4    de Visser, M.5    Bolhuis, P.A.6
  • 24
    • 0034702027 scopus 로고    scopus 로고
    • Identification of mutations in the gene encoding lamins A/C in autosomal dominant limb girdle muscular dystrophy with atrioventricular conduction disturbances (LGMD1B)
    • Muchir A, Bonne G, van der Kooi AJ, van Meegen M, Baas F, Bolhuis PA, de Visser M, Schwartz K: Identification of mutations in the gene encoding lamins A/C in autosomal dominant limb girdle muscular dystrophy with atrioventricular conduction disturbances (LGMD1B). Hum Mol Genet 2000, 9:1453-1459
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 1453-1459
    • Muchir, A.1    Bonne, G.2    van der Kooi, A.J.3    van Meegen, M.4    Baas, F.5    Bolhuis, P.A.6    de Visser, M.7    Schwartz, K.8
  • 25
    • 0028969170 scopus 로고
    • Molecular cloning of a novel human cDNA on chromosome 1q21 and its mouse homolog encoding a nuclear protein with DNAbinding ability
    • Horikawa I, Tanaka H, Yuasa Y, Suzuki M, Oshimura M: Molecular cloning of a novel human cDNA on chromosome 1q21 and its mouse homolog encoding a nuclear protein with DNAbinding ability. Biochem Biophys Res Commun 1995, 208:999-1007
    • (1995) Biochem. Biophys. Res. Commun. , vol.208 , pp. 999-1007
    • Horikawa, I.1    Tanaka, H.2    Yuasa, Y.3    Suzuki, M.4    Oshimura, M.5
  • 26
    • 0029157381 scopus 로고
    • Forced expression of YL-1 protein suppresses the anchorage-independent growth of Kirsten sarcoma virus-transformed NIH3T3 cells
    • Horikawa I, Tanaka H, Yuasa Y, Suzuki M, Shimizu M, Oshimura M: Forced expression of YL-1 protein suppresses the anchorage-independent growth of Kirsten sarcoma virus-transformed NIH3T3 cells. Exp Cell Res 1995, 220:11-17
    • (1995) Exp. Cell Res. , vol.220 , pp. 11-17
    • Horikawa, I.1    Tanaka, H.2    Yuasa, Y.3    Suzuki, M.4    Shimizu, M.5    Oshimura, M.6
  • 27
    • 0034601690 scopus 로고    scopus 로고
    • Genomic organization of mouse and human erythrocyte tropomodulin genes encoding the pointed end capping protein for the actin filaments
    • Chu X, Thompson D, Yee LJ, Sung LA: Genomic organization of mouse and human erythrocyte tropomodulin genes encoding the pointed end capping protein for the actin filaments. Gene 2000, 256 271-281
    • (2000) Gene , vol.256 , pp. 271-281
    • Chu, X.1    Thompson, D.2    Yee, L.J.3    Sung, L.A.4
  • 28
    • 0033804469 scopus 로고    scopus 로고
    • Genomic sequence, splicing, and gene annotation
    • Mount SM: Genomic sequence, splicing, and gene annotation. Am J Hum Genet 2000, 67:788-792
    • (2000) Am. J. Hum. Genet. , vol.67 , pp. 788-792
    • Mount, S.M.1
  • 29
    • 0034326362 scopus 로고    scopus 로고
    • Analysis of canonical and non-canonical splice sites in mammalian genomes
    • Burset M, Seledtsov LA, Solovyev VV: Analysis of canonical and non-canonical splice sites in mammalian genomes. Nucleic Acids Res 2000, 28:4364-4375
    • (2000) Nucleic Acids Res. , vol.28 , pp. 4364-4375
    • Burset, M.1    Seledtsov, L.A.2    Solovyev, V.V.3
  • 30
    • 0029867018 scopus 로고    scopus 로고
    • Intergenic splicing of MDS1 and EVI1 occurs in normal tissues as well as in myeloid leukemia and produces a new member of the PR domain family
    • Fears S, Mathieu C, ZeIeznik-Le N, Huang S, Rowley JD, Nucifora G: Intergenic splicing of MDS1 and EVI1 occurs in normal tissues as well as in myeloid leukemia and produces a new member of the PR domain family. Proc Natl Acad Sci USA 1996, 93: 642-1647
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1642-1647
    • Fears, S.1    Mathieu, C.2    ZeIeznik-Le, N.3    Huang, S.4    Rowley, J.D.5    Nucifora, G.6
  • 31
    • 0030894543 scopus 로고    scopus 로고
    • The leukemia-associated gene MDS1/EVI1 is a new type of GATA-binding transactivator
    • Soderholm J, Kobayashi H, Mathieu C, Rowley JD, Nucifora G: The leukemia-associated gene MDS1/EVI1 is a new type of GATA-binding transactivator. Leukemia 1997, 11:352-358
    • (1997) Leukemia , vol.11 , pp. 352-358
    • Soderholm, J.1    Kobayashi, H.2    Mathieu, C.3    Rowley, J.D.4    Nucifora, G.5
  • 32
    • 17144434438 scopus 로고    scopus 로고
    • Cotranscription and intergenic splicing of human galactose- 1-phosphate uridylyltransferase and interleukin-11 receptor alpha-chain genes generate a fusion mRNA in normal cells. Implication for the production of multidomain proteins during evolution
    • Magrangeas F, Pitiot G, Dubois S, Bragado-Nilsson E, Cherel M, Jobert S, Lebeau B, Boisteau O, Lethe B, Mallet J, Jacques Y, Minvielle S: Cotranscription and intergenic splicing of human galactose- 1-phosphate uridylyltransferase and interleukin-11 receptor alpha-chain genes generate a fusion mRNA in normal cells. Implication for the production of multidomain proteins during evolution. J Biol Chem 1998, 273:16005-16010
    • (1998) J. Biol. Chem. , vol.273 , pp. 16005-16010
    • Magrangeas, F.1    Pitiot, G.2    Dubois, S.3    Bragado-Nilsson, E.4    Cherel, M.5    Jobert, S.6    Lebeau, B.7    Boisteau, O.8    Lethe, B.9    Mallet, J.10    Jacques, Y.11    Minvielle, S.12
  • 33
    • 0033135012 scopus 로고    scopus 로고
    • Intergenic splicing between a HERV-H endogenous retrovirus and two adjacent human genes
    • Kowalski PE, Freeman JD, Mager DL: Intergenic splicing between a HERV-H endogenous retrovirus and two adjacent human genes. Genomics 1999, 57:371-379
    • (1999) Genomics , vol.57 , pp. 371-379
    • Kowalski, P.E.1    Freeman, J.D.2    Mager, D.L.3
  • 35
    • 0029122980 scopus 로고
    • A 2.4-megabase physical map spanning the CYP2C gene cluster on chromosome 10q24
    • Gray IC, Nobile C, Muresu R, Ford S, Spurr NK: A 2.4-megabase physical map spanning the CYP2C gene cluster on chromosome 10q24. Genomics 1995, 28:328-332
    • (1995) Genomics , vol.28 , pp. 328-332
    • Gray, I.C.1    Nobile, C.2    Muresu, R.3    Ford, S.4    Spurr, N.K.5
  • 36
    • 0025763625 scopus 로고
    • Cloning and expression of complementary DNAs for multiple members of the human cytochrome P450IIC subfamily
    • [published erratum appears in Biochemistry 1993 Feb 9;32(5):1390]
    • Romkes M, Faletto MB, Blaisdell JA, Raucy JL, Goldstein JA: Cloning and expression of complementary DNAs for multiple members of the human cytochrome P450IIC subfamily [published erratum appears in Biochemistry 1993 Feb 9;32(5):1390]. Biochemistry 1991, 30: 247-3255
    • (1991) Biochemistry , vol.30 , pp. 3247-3255
    • Romkes, M.1    Faletto, M.B.2    Blaisdell, J.A.3    Raucy, J.L.4    Goldstein, J.A.5
  • 37
    • 0033168090 scopus 로고    scopus 로고
    • RNA molecules containing exons originating from different members of the cytochrome P450 2C gene subfamily (CYP2C) in human epidermis and liver
    • Zaphiropoulos PG: RNA molecules containing exons originating from different members of the cytochrome P450 2C gene subfamily (CYP2C) in human epidermis and liver. Nucleic Acids Res 1999, 27:2585-2590
    • (1999) Nucleic Acids Res. , vol.27 , pp. 2585-2590
    • Zaphiropoulos, P.G.1
  • 38
    • 0034144388 scopus 로고    scopus 로고
    • The human CYP2C locus: A prototype for intergenic and exon repetition splicing events
    • Finta C, Zaphiropoulos PG: The human CYP2C locus: a prototype for intergenic and exon repetition splicing events. Genomics 2000, 63:433-438
    • (2000) Genomics , vol.63 , pp. 433-438
    • Finta, C.1    Zaphiropoulos, P.G.2
  • 39
    • 0034235003 scopus 로고    scopus 로고
    • Chromosomal location and genomic structure of the human translin-associated factor X gene (TRAX; TSNAX) revealed by intergenic splicing to DISCI, a gene disrupted by a translocation segregating with schizophrenia
    • [In Process Citation]
    • Millar JK, Christie S, Semple CA, Porteous DJ: Chromosomal location and genomic structure of the human translin-associated factor X gene (TRAX; TSNAX) revealed by intergenic splicing to DISCI, a gene disrupted by a translocation segregating with schizophrenia [In Process Citation]. Genomics 2000, 67:69-77
    • (2000) Genomics , vol.67 , pp. 69-77
    • Millar, J.K.1    Christie, S.2    Semple, C.A.3    Porteous, D.J.4
  • 42
    • 0034976418 scopus 로고    scopus 로고
    • Actin dynamics at pointed ends regulates thin filament length in striated muscle
    • Littlefield R, Almenar Queralt A, Fowler VM: Actin dynamics at pointed ends regulates thin filament length in striated muscle. Nat Cell Biol 2001, 6:544-51
    • (2001) Nat. Cell Biol. , vol.6 , pp. 544-551
    • Littlefield, R.1    Almenar Queralt, A.2    Fowler, V.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.