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Volumn 53, Issue 2, 2002, Pages 125-135

Amorphin is phosphorylase; phosphorylase is an alpha-actinin-binding protein

Author keywords

Enzyme; Green Fluorescent Protein; McArdle's Disease; Muscle; Sarcomere; Thin filaments; Z band

Indexed keywords

ALPHA ACTININ; AMORPHIN; BINDING PROTEIN; COMPLEMENTARY DNA; F ACTIN; GLYCOGEN PHOSPHORYLASE; GLYCOLYTIC ENZYME; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; MUSCLE PROTEIN; UNCLASSIFIED DRUG;

EID: 0036786003     PISSN: 08861544     EISSN: None     Source Type: Journal    
DOI: 10.1002/cm.10059     Document Type: Article
Times cited : (38)

References (50)
  • 1
    • 0033988021 scopus 로고    scopus 로고
    • Targeting of cardiac titin fragments to Z-bands and dense bodies of living muscle and non-muscle cells
    • Ayoob JC, Turnacioglu KK, Mittal B, Sanger JM and Sanger JW. 2000. Targeting of cardiac titin fragments to Z-bands and dense bodies of living muscle and non-muscle cells. Cell Motil Cytoskeleton 45:67-82.
    • (2000) Cell Motil Cytoskeleton , vol.45 , pp. 67-82
    • Ayoob, J.C.1    Turnacioglu, K.K.2    Mittal, B.3    Sanger, J.M.4    Sanger, J.W.5
  • 2
    • 0035089325 scopus 로고    scopus 로고
    • Expression of Green or Red Fluorescent Protein (GFP or DsRed) linked proteins in non-muscle and muscle cells
    • Ayoob JC, Shaner NC, Sanger JM, Sanger JW. 2001. Expression of Green or Red Fluorescent Protein (GFP or DsRed) linked proteins in non-muscle and muscle cells. Mol Biotechnol 17: 65-71.
    • (2001) Mol Biotechnol , vol.17 , pp. 65-71
    • Ayoob, J.C.1    Shaner, N.C.2    Sanger, J.M.3    Sanger, J.W.4
  • 3
  • 4
    • 0025957990 scopus 로고
    • Where is the glycolytic complex? A critical evaluation of present data from muscle tissue
    • Brooks SPJ, Storey KB. 1991. Where is the glycolytic complex? A critical evaluation of present data from muscle tissue. FEBS Lett 278:135-138.
    • (1991) FEBS Lett , vol.278 , pp. 135-138
    • Brooks, S.P.J.1    Storey, K.B.2
  • 5
    • 0020469148 scopus 로고
    • The Z-band: 85,000-Dalton amorphin and alpha-actinin and their relation to structure
    • Chowrashi PK, Pepe FA. 1982. The Z-band: 85,000-dalton amorphin and alpha-actinin and their relation to structure. J Cell Biol 94:565-573.
    • (1982) J Cell Biol , vol.94 , pp. 565-573
    • Chowrashi, P.K.1    Pepe, F.A.2
  • 7
    • 0032959430 scopus 로고    scopus 로고
    • Use of Green Fluorescent Proteins linked to cytoskeletal proteins to analyze myofibrillogenesis in living cells
    • Dabiri GA, Ayoob JP, Turnacioglu KK, Sanger JM, Sanger JW. 1999. Use of Green Fluorescent Proteins linked to cytoskeletal proteins to analyze myofibrillogenesis in living cells. Methods Enzymol 302:171-186.
    • (1999) Methods Enzymol , vol.302 , pp. 171-186
    • Dabiri, G.A.1    Ayoob, J.P.2    Turnacioglu, K.K.3    Sanger, J.M.4    Sanger, J.W.5
  • 8
    • 0016670453 scopus 로고
    • Immunolocalization of glycogenolytic and glycolytic enzyme proteins and of malate dehydrogenase isozymes in cross-striated skeletal muscle and heart of the rabbit
    • Doelken G, Leisner E, Pette D. 1975. Immunolocalization of glycogenolytic and glycolytic enzyme proteins and of malate dehydrogenase isozymes in cross-striated skeletal muscle and heart of the rabbit. Histochemistry 43:113-121.
    • (1975) Histochemistry , vol.43 , pp. 113-121
    • Doelken, G.1    Leisner, E.2    Pette, D.3
  • 9
    • 0013788789 scopus 로고
    • Localization of skeletal muscle phosphorylase using a fluorescent antibody technique and its correlation with histochemical observations
    • Dvorak HF, Cohen RB. 1965. Localization of skeletal muscle phosphorylase using a fluorescent antibody technique and its correlation with histochemical observations. J Histochem Cytochem 13:454-460.
    • (1965) J Histochem Cytochem , vol.13 , pp. 454-460
    • Dvorak, H.F.1    Cohen, R.B.2
  • 10
  • 12
    • 0002101212 scopus 로고
    • The isolation and crystallization of rabbit muscle phosphorylase b
    • Fischer EH, Krebs EG. 1958. The isolation and crystallization of rabbit muscle phosphorylase b. J Biol Chem 231:65-71.
    • (1958) J Biol Chem , vol.231 , pp. 65-71
    • Fischer, E.H.1    Krebs, E.G.2
  • 14
    • 0015527081 scopus 로고
    • Studies of temperature and tropomyosin on the alpha-actinin/F-actin interaction
    • Goll DE, Suzuki A, Temple J, Holmes GR. 1972. Studies of temperature and tropomyosin on the alpha-actinin/F-actin interaction. J Mol Biol 67:469-488.
    • (1972) J Mol Biol , vol.67 , pp. 469-488
    • Goll, D.E.1    Suzuki, A.2    Temple, J.3    Holmes, G.R.4
  • 17
    • 0018264524 scopus 로고
    • Isolation and characterization of glycogen phosphorylase b from chicken breast muscle: Comparison with a protein extracted from the M-line
    • Heizmann CW, Eppenberger HM. 1978. Isolation and characterization of glycogen phosphorylase b from chicken breast muscle: comparison with a protein extracted from the M-line. J Biol Chem 253:270-277.
    • (1978) J Biol Chem , vol.253 , pp. 270-277
    • Heizmann, C.W.1    Eppenberger, H.M.2
  • 18
    • 0035997135 scopus 로고    scopus 로고
    • Host focal adhesion protein domains that bind to the translocated intimin receptor (Tir) of enteropathogenic Escherichia coli (EPEC)
    • Huang L, Mittal B, Sanger JW, Sanger JM. 2002. Host focal adhesion protein domains that bind to the translocated intimin receptor (Tir) of enteropathogenic Escherichia coli (EPEC). Cell Motil Cytoskeleton 52:255-265.
    • (2002) Cell Motil Cytoskeleton , vol.52 , pp. 255-265
    • Huang, L.1    Mittal, B.2    Sanger, J.W.3    Sanger, J.M.4
  • 19
    • 0029246836 scopus 로고
    • Interaction between glycogen phosphorylase b and creatine kinase from rabbit skeletal muscle
    • Khakimova AK, Skolysheva LK, Shur SA, Vulfson IL. 1995. Interaction between glycogen phosphorylase b and creatine kinase from rabbit skeletal muscle. Biokhimia 60:278-288.
    • (1995) Biokhimia , vol.60 , pp. 278-288
    • Khakimova, A.K.1    Skolysheva, L.K.2    Shur, S.A.3    Vulfson, I.L.4
  • 20
    • 0018830142 scopus 로고
    • 125I-labeled protein A: Reactivity with IgG and use as a tracer in radioimmunoassay
    • Langone JJ. 1980. 125I-labeled protein A: reactivity with IgG and use as a tracer in radioimmunoassay. Methods Enzymol 70:356-375.
    • (1980) Methods Enzymol , vol.70 , pp. 356-375
    • Langone, J.J.1
  • 21
    • 0022455280 scopus 로고
    • Binding of phosphorylase a and b to skeletal muscle thin filament proteins
    • Marquetant RJ, Manfredi P, Holmes EW. 1986. Binding of phosphorylase a and b to skeletal muscle thin filament proteins. Arch Biochem Biophys 245:404-410.
    • (1986) Arch Biochem Biophys , vol.245 , pp. 404-410
    • Marquetant, R.J.1    Manfredi, P.2    Holmes, E.W.3
  • 22
    • 0021790431 scopus 로고
    • Association of chicken pectoralis muscle phosphorylase with the Z-line and the M-line of myofibrils: Comparison with 'amorphin', the amorphous component of the Z-line
    • Maruyama KM, Kuroda M, Nonomura Y. 1985. Association of chicken pectoralis muscle phosphorylase with the Z-line and the M-line of myofibrils: comparison with 'amorphin', the amorphous component of the Z-line. Biochim Biophys Acta 829:229-237.
    • (1985) Biochim Biophys Acta , vol.829 , pp. 229-237
    • Maruyama, K.M.1    Kuroda, M.2    Nonomura, Y.3
  • 23
    • 0021129923 scopus 로고
    • Interactions between glycolytic enzymes and components of the cytomatrix
    • Masters C. 1984. Interactions between glycolytic enzymes and components of the cytomatrix. J Cell Biol 99:222s-225s.
    • (1984) J Cell Biol , vol.99
    • Masters, C.1
  • 24
    • 0024788703 scopus 로고
    • Antigenic probes locate binding sites for the glycolytic enzymes glyceraldehyde-3-phosphate dehydrogenase, aldolase and phosphofructokinase on the actin monomer in microfilaments
    • Mejean C, Pons F, Benyamin Y, Roustan C. 1989. Antigenic probes locate binding sites for the glycolytic enzymes glyceraldehyde-3-phosphate dehydrogenase, aldolase and phosphofructokinase on the actin monomer in microfilaments. Biochemistry 264: 671-677.
    • (1989) Biochemistry , vol.264 , pp. 671-677
    • Mejean, C.1    Pons, F.2    Benyamin, Y.3    Roustan, C.4
  • 26
    • 0032557642 scopus 로고    scopus 로고
    • Two immunoglobulin-like domains of the Z-disc portion of titin interact in a conformational-dependent way with telethonin
    • Mues A, van der Ven PFM, Young P, Furst DO, Gautel M. 1998. Two immunoglobulin-like domains of the Z-disc portion of titin interact in a conformational-dependent way with telethonin. FEBS Lett 428:111-114.
    • (1998) FEBS Lett , vol.428 , pp. 111-114
    • Mues, A.1    Van der Ven, P.F.M.2    Young, P.3    Furst, D.O.4    Gautel, M.5
  • 27
    • 0024077125 scopus 로고
    • Aldolase exists in both the fluid and solid phases of cytoplasm
    • Pagliaro L, Taylor DL. 1988. Aldolase exists in both the fluid and solid phases of cytoplasm. J Cell Biol 107:981-991.
    • (1988) J Cell Biol , vol.107 , pp. 981-991
    • Pagliaro, L.1    Taylor, D.L.2
  • 28
    • 0034618039 scopus 로고    scopus 로고
    • Characterization of palladin, a novel protein localized to stress fibers and cell adhesions
    • Parast MM, Otey CA. 2000. Characterization of palladin, a novel protein localized to stress fibers and cell adhesions. J Cell Biol 150:643-656.
    • (2000) J Cell Biol , vol.150 , pp. 643-656
    • Parast, M.M.1    Otey, C.A.2
  • 30
    • 0344759163 scopus 로고    scopus 로고
    • Myotilin, a novel sarcomeric protein with two Ig-like domains, is encoded by a candidate gene for two limb-girdle muscular dystrophy
    • Salmikangas P, Mykkanen O-M, Gronholm M, Heiska L, Carpen O. 1999. Myotilin, a novel sarcomeric protein with two Ig-like domains, is encoded by a candidate gene for two limb-girdle muscular dystrophy. Hum Mol Genet 8:1329-1336.
    • (1999) Hum Mol Genet , vol.8 , pp. 1329-1336
    • Salmikangas, P.1    Mykkanen, O.-M.2    Gronholm, M.3    Heiska, L.4    Carpen, O.5
  • 31
    • 0033648297 scopus 로고    scopus 로고
    • Microinjection of fluorescently labeled alpha-actinin into living cells
    • Tuan RS, Lo CW, editors. Totowa, NJ: Humana Press
    • Sanger JM, Danowski BA, Sanger JW. 2000. Microinjection of fluorescently labeled alpha-actinin into living cells. In: Tuan RS, Lo CW, editors. Methods in molecular biology: developmental biology protocols, vol. III. Totowa, NJ: Humana Press. p 449-456.
    • (2000) Methods in molecular biology: developmental biology protocols , vol.3 , pp. 449-456
    • Sanger, J.M.1    Danowski, B.A.2    Sanger, J.W.3
  • 32
    • 0021349790 scopus 로고
    • Analysis of myofibrillar structure and assembly using fluorescent labeled contractile proteins
    • Sanger JW, Mittal B, Sanger JM. 1984. Analysis of myofibrillar structure and assembly using fluorescent labeled contractile proteins. J Cell Biol 98, 825-833.
    • (1984) J Cell Biol , vol.98 , pp. 825-833
    • Sanger, J.W.1    Mittal, B.2    Sanger, J.M.3
  • 33
    • 0000812264 scopus 로고    scopus 로고
    • Myofibrillogenesis in cardiac muscle cells
    • Dube D, editor. New York: Springer Verlag
    • Sanger JW, Sanger JM. 2001a. Myofibrillogenesis in cardiac muscle cells. In: Dube D, editor. Myofibrillogenesis. New York: Springer Verlag. p 3-20.
    • (2001) Myofibrillogenesis , pp. 3-20
    • Sanger, J.W.1    Sanger, J.M.2
  • 34
    • 0035833258 scopus 로고    scopus 로고
    • Fishing out proteins that bind to titin
    • Sanger JM, Sanger JW. 2001b. Fishing out proteins that bind to titin. J Cell Biol 154:1-4.
    • (2001) J Cell Biol , vol.154 , pp. 1-4
    • Sanger, J.M.1    Sanger, J.W.2
  • 37
    • 0000379923 scopus 로고
    • Characterization and study of sarcoplasmic proteins
    • Briskey EJ, Cassens RG, Marsh BB, editors. Madison: University of Wisconsin Press
    • Scopes RK. 1970. Characterization and study of sarcoplasmic proteins. In: Briskey EJ, Cassens RG, Marsh BB, editors. The physiology and biochemistry of muscle as a food, Vol. 2. Madison: University of Wisconsin Press. p 471-492.
    • (1970) The physiology and biochemistry of muscle as a food , vol.2 , pp. 471-492
    • Scopes, R.K.1
  • 38
    • 0018899656 scopus 로고
    • Interaction of adolase with actin-containing filaments
    • Stewart M, Morton DJ, Clarke FM. 1980. Interaction of adolase with actin-containing filaments. Biochem J 186:99-104.
    • (1980) Biochem J , vol.186 , pp. 99-104
    • Stewart, M.1    Morton, D.J.2    Clarke, F.M.3
  • 39
    • 0017392812 scopus 로고
    • M-protein from chicken pectoralis muscle: Isolation and characterization
    • Trinick J, Lowey S. 1977. M-protein from chicken pectoralis muscle: isolation and characterization. J Mol Biol 113:343-368.
    • (1977) J Mol Biol , vol.113 , pp. 343-368
    • Trinick, J.1    Lowey, S.2
  • 42
    • 0031967863 scopus 로고    scopus 로고
    • Sites of monomeric actin incorporation in living PtK2 and REF-52 cells
    • Turnacioglu KK, Sanger JW, Sanger JM. 1998. Sites of monomeric actin incorporation in living PtK2 and REF-52 cells. Cell Motil Cytoskeleton 40:59-70.
    • (1998) Cell Motil Cytoskeleton , vol.40 , pp. 59-70
    • Turnacioglu, K.K.1    Sanger, J.W.2    Sanger, J.M.3
  • 43
    • 0028283285 scopus 로고
    • The muscle Z band: Lessons in stress management
    • Vigoreaux JO. 1994. The muscle Z band: lessons in stress management. J Mus Res Cell Motil 15:237-255.
    • (1994) J Mus Res Cell Motil , vol.15 , pp. 237-255
    • Vigoreaux, J.O.1
  • 44
    • 0020957201 scopus 로고
    • Non-uniform staining of myofibril A-bands by a monoclonal antibody to skeletal muscle myosin S1 heavy chain
    • Wachsberger P, Lampson L, Pepe FA. 1983. Non-uniform staining of myofibril A-bands by a monoclonal antibody to skeletal muscle myosin S1 heavy chain. Tissue Cell 15:3412-349.
    • (1983) Tissue Cell , vol.15 , pp. 3412-4349
    • Wachsberger, P.1    Lampson, L.2    Pepe, F.A.3
  • 45
    • 0019523287 scopus 로고
    • An immunological approach to myosin light chain function in thick filament-linked regulation. I. Characterization, specificity, and cross reactivity of anti-scallop myosin heavy- and light-chain antibodies by competitive solid-phase radioimmunoassay
    • Walliman T, Szent-Gyorgyi AG. 1981. An immunological approach to myosin light chain function in thick filament-linked regulation. I. Characterization, specificity, and cross reactivity of anti-scallop myosin heavy- and light-chain antibodies by competitive solid-phase radioimmunoassay. Biochemistry 20:176-1187.
    • (1981) Biochemistry , vol.20 , pp. 176-1187
    • Walliman, T.1    Szent-Gyorgyi, A.G.2
  • 46
    • 0030768060 scopus 로고    scopus 로고
    • Flight muscle function in Drosopila requires colocalization of glycolytic enzymes
    • Wojtas K, Slepecky N, von Kalm L, Sullivan D. 1997. Flight muscle function in Drosopila requires colocalization of glycolytic enzymes. Mol Biol Cell 8:1665-1675.
    • (1997) Mol Biol Cell , vol.8 , pp. 1665-1675
    • Wojtas, K.1    Slepecky, N.2    Von Kalm, L.3    Sullivan, D.4
  • 47
    • 0030827949 scopus 로고    scopus 로고
    • Actinin-associated LIM protein: Identification of a domain interaction between PDZ and spectrin-like repeat motifs
    • Xia H, Winokur ST, Kuo W-L, Altherr MR, Bredt DS. 1997. Actinin-associated LIM protein: identification of a domain interaction between PDZ and spectrin-like repeat motifs. J Cell Biol 139: 507-515.
    • (1997) J Cell Biol , vol.139 , pp. 507-515
    • Xia, H.1    Winokur, S.T.2    Kuo, W.-L.3    Altherr, M.R.4    Bredt, D.S.5
  • 48
    • 0021112289 scopus 로고
    • Quantitative determination of myosin and actin in rabbit skeletal muscle
    • Yates LD, Greaser ML. 1983. Quantitative determination of myosin and actin in rabbit skeletal muscle. J Mol Biol 168:123-141.
    • (1983) J Mol Biol , vol.168 , pp. 123-141
    • Yates, L.D.1    Greaser, M.L.2
  • 49
    • 0035833261 scopus 로고    scopus 로고
    • Obscurin, a giant sarcomeric Rho-GEF protein involved in sarcomere assembly
    • Young P, Ehler E, Gautel M. 2001. Obscurin, a giant sarcomeric Rho-GEF protein involved in sarcomere assembly. J Cell Biol 154:123-136.
    • (2001) J Cell Biol , vol.154 , pp. 123-136
    • Young, P.1    Ehler, E.2    Gautel, M.3
  • 50
    • 0033538565 scopus 로고    scopus 로고
    • Cypher, a striated muscle-restricted PDZ and LIM domain-containing protein, binds to alpha-actinin-2 and protein kinase C
    • Zhou Q, Ruiz-Lozano P, Martone ME, Chen J. 1999. Cypher, a striated muscle-restricted PDZ and LIM domain-containing protein, binds to alpha-actinin-2 and protein kinase C. J Biol Chem 274:19807-19813.
    • (1999) J Biol Chem , vol.274 , pp. 19807-19813
    • Zhou, Q.1    Ruiz-Lozano, P.2    Martone, M.E.3    Chen, J.4


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