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Volumn 13, Issue 2, 1996, Pages 85-93

The action of carboxyl modifying reagents on the ryanodine receptor/Ca2+ release channel of skeletal muscle sarcoplasmic reticulum

Author keywords

Ca2+ release channel; Carboxyl modifying reagents; Ryanodine receptor; Sarcoplasmic reticulum

Indexed keywords

1 (3 DIMETHYLAMINOPROPYL) 3 ETHYLCARBODIIMIDE; 2 ETHOXY 1(2H) QUINOLINECARBOXYLIC ACID ETHYL ESTER; CAFFEINE; CALCIUM CHANNEL; CALCIUM ION; DICYCLOHEXYLCARBODIIMIDE; RYANODINE; RYANODINE RECEPTOR;

EID: 0029761984     PISSN: 09687688     EISSN: None     Source Type: Journal    
DOI: 10.3109/09687689609160581     Document Type: Article
Times cited : (9)

References (42)
  • 1
    • 0025982123 scopus 로고
    • Exitation-contraction coupling and the mechanism of muscle contraction
    • Ebashi, S. (1991) Exitation-contraction coupling and the mechanism of muscle contraction. Annual Review of Physiology, 53, 1-16.
    • (1991) Annual Review of Physiology , vol.53 , pp. 1-16
    • Ebashi, S.1
  • 2
    • 0021646029 scopus 로고
    • 2+ release from sarcoplasmic reticulum of skeletal muscle
    • 2+ release from sarcoplasmic reticulum of skeletal muscle. Physiology Review, 64, 1240-1319.
    • (1984) Physiology Review , vol.64 , pp. 1240-1319
    • Martonosi, A.N.1
  • 5
    • 0024342717 scopus 로고
    • The muscle ryanodine receptor and its intrinsic calcium channel activity
    • Lai, F. A. and Meissner, G. (1989) The muscle ryanodine receptor and its intrinsic calcium channel activity. Journal of Bioenergetics and Biomembranes, 21, 227-245.
    • (1989) Journal of Bioenergetics and Biomembranes , vol.21 , pp. 227-245
    • Lai, F.A.1    Meissner, G.2
  • 6
    • 0023241909 scopus 로고
    • Isolation of the ryanodine receptor from cardiac sarcoplasmic reticulum and identity with the feet structures
    • Inui, M., Saito, A. and Fleischer, S. (1987) Isolation of the ryanodine receptor from cardiac sarcoplasmic reticulum and identity with the feet structures. Journal of Biological Chemistry, 262, 15637-15642.
    • (1987) Journal of Biological Chemistry , vol.262 , pp. 15637-15642
    • Inui, M.1    Saito, A.2    Fleischer, S.3
  • 7
    • 0023903046 scopus 로고
    • Purification and reconstitution of the calcium release channel from skeletal muscle
    • Lai, F. A., Enckson, H. P., Rousseau, E., Liu, Q-Y. and Meissner. G. (1988) Purification and reconstitution of the calcium release channel from skeletal muscle. Nature (London), 331, 315-319.
    • (1988) Nature (London) , vol.331 , pp. 315-319
    • Lai, F.A.1    Enckson, H.P.2    Rousseau, E.3    Liu, Q.-Y.4    Meissner, G.5
  • 9
    • 0023884309 scopus 로고
    • Ryanodine binding to sarcoplasmic reticulum membranes: Companson between cardiac and skeletal muscle
    • Michalak, M., Dupraz, P. and Shoshan-Barmatz, V. (1988) Ryanodine binding to sarcoplasmic reticulum membranes: companson between cardiac and skeletal muscle. Biochimica et Biophysica Acta, 939, 587-594.
    • (1988) Biochimica et Biophysica Acta , vol.939 , pp. 587-594
    • Michalak, M.1    Dupraz, P.2    Shoshan-Barmatz, V.3
  • 11
    • 0024280913 scopus 로고
    • Ryanodine receptor of skeletal muscle is a gap junction-type channel
    • Ma, J. J. Fill, M., Knudson. M., Campbell, K. P. and Coronado, R. (1988) Ryanodine receptor of skeletal muscle is a gap junction-type channel. Science, 242, 99-102.
    • (1988) Science , vol.242 , pp. 99-102
    • Ma, J.J.1    Fill, M.2    Knudson, M.3    Campbell, K.P.4    Coronado, R.5
  • 13
    • 0026613088 scopus 로고
    • 2- release channel (ryanodine receptor) of rabbit skeletal muscle sarcoplasmic reticulum
    • 2- release channel (ryanodine receptor) of rabbit skeletal muscle sarcoplasmic reticulum. Journal of Biological Chemistry. 267, 23318-23326.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 23318-23326
    • Chen, S.R.W.1    Zhang, L.2    MacLennan, D.H.3
  • 17
    • 0000249418 scopus 로고
    • Dicyclohexylcarbodiimide as a probe for proton translocating enzymes
    • Solioz, M. (1984) Dicyclohexylcarbodiimide as a probe for proton translocating enzymes. Trends in Biochemical Science, 7, 309-312.
    • (1984) Trends in Biochemical Science , vol.7 , pp. 309-312
    • Solioz, M.1
  • 22
    • 0022423882 scopus 로고
    • 2O = E + Pi reaction and ATP = Pi exchange in sarcoplasmic reticulum adenosinetriphosphatase
    • 2O = E + Pi reaction and ATP = Pi exchange in sarcoplasmic reticulum adenosinetriphosphatase. Biochemistry, 24, 1025-1029.
    • (1985) Biochemistry , vol.24 , pp. 1025-1029
    • Scofans, H.M.1    Barrabin, H.2    Lewis, D.3    Inesi, G.4
  • 24
    • 0028351176 scopus 로고
    • Diethylpyrocarbonate modification of ryanodine receptor from skeletal muscle sarcoplasmic retiulum
    • Shoshan-Barmatz, V. and Well, S. (1994) Diethylpyrocarbonate modification of ryanodine receptor from skeletal muscle sarcoplasmic retiulum. Biochemical Journal, 299, 177-181.
    • (1994) Biochemical Journal , vol.299 , pp. 177-181
    • Shoshan-Barmatz, V.1    Well, S.2
  • 25
    • 3042941582 scopus 로고
    • Structural involvment of carboxyl residues in the photocycle of bacteriorhodopsin
    • Herz, S. M. and Packer, L. (1981) Structural involvment of carboxyl residues in the photocycle of bacteriorhodopsin FEBS Letters, 131, 158-164.
    • (1981) FEBS Letters , vol.131 , pp. 158-164
    • Herz, S.M.1    Packer, L.2
  • 26
    • 0023008143 scopus 로고
    • 2+ release channel of sarcoplasmic reticulum
    • 2+ release channel of sarcoplasmic reticulum. Journal of Biological Chemistry, 261, 6300-6306.
    • (1986) Journal of Biological Chemistry , vol.261 , pp. 6300-6306
    • Meissner, G.1
  • 27
    • 0028238477 scopus 로고
    • Surface charge potentiates conduction through the cardiac ryanodine receptor channel
    • Tu, Q., Velez, P., Cortes-Gurierrez, M. and Fill, M (1994) Surface charge potentiates conduction through the cardiac ryanodine receptor channel. Journal of General Physiology, 103, 853-867.
    • (1994) Journal of General Physiology , vol.103 , pp. 853-867
    • Tu, Q.1    Velez, P.2    Cortes-Gurierrez, M.3    Fill, M.4
  • 28
    • 0018785338 scopus 로고
    • 2+ binding site in a hydrophobic region
    • 2+ binding site in a hydrophobic region. Biochemistry, 18, 103-113.
    • (1979) Biochemistry , vol.18 , pp. 103-113
    • Pick, U.1    Racker, E.2
  • 29
    • 0023856595 scopus 로고
    • Patterns of proteolytic cleavage and carbodiimide derivatization in sarcoplasmic reticulum adenosinetriphosphatase
    • de Ancos, J. G. and Inesi, G (1988) Patterns of proteolytic cleavage and carbodiimide derivatization in sarcoplasmic reticulum adenosinetriphosphatase. Biochemistry, 27, 1793-1803.
    • (1988) Biochemistry , vol.27 , pp. 1793-1803
    • Ancos, J.G.1    Inesi, G.2
  • 30
    • 0025280251 scopus 로고
    • Purification, calcium binding properties, and ultrastructural localization of the 53,000- And 160,000 (sarcalumenin)-Dalton glycoproteins of the sarcoptasmic reticulum
    • Leberer, E., Timms, B. G., Campbell, K. P. and MacLennan, D. H. (1990) Purification, calcium binding properties, and ultrastructural localization of the 53,000- and 160,000 (sarcalumenin)-Dalton glycoproteins of the sarcoptasmic reticulum. Journal of Biological Chemistry, 265, 10118-10124.
    • (1990) Journal of Biological Chemistry , vol.265 , pp. 10118-10124
    • Leberer, E.1    Timms, B.G.2    Campbell, K.P.3    MacLennan, D.H.4
  • 32
    • 0024992021 scopus 로고
    • Isolation of a terminal cistema protein which may link the dihydropyridine receptor to the junctional foot protein in skeletal muscle
    • Kim, K. C., Caswell, A. H., Talvenheirno, J. A and Brandt, N. R. (1990) Isolation of a terminal cistema protein which may link the dihydropyridine receptor to the junctional foot protein in skeletal muscle. Biochemistry, 29, 9281-9292.
    • (1990) Biochemistry , vol.29 , pp. 9281-9292
    • Kim, K.C.1    Caswell, A.H.2    Talvenheirno, J.A.3    Brandt, N.R.4
  • 33
    • 0023372321 scopus 로고
    • The structure of calsequestrin in triads of vertebrate skeletal muscle: A deep-etch study
    • Franzini-Armstrong, C., Kenney, L. J. and Varriano-Marston, E. (1987) The structure of calsequestrin in triads of vertebrate skeletal muscle: a deep-etch study. Journal of Cell Biology, 105, 49-56.
    • (1987) Journal of Cell Biology , vol.105 , pp. 49-56
    • Franzini-Armstrong, C.1    Kenney, L.J.2    Varriano-Marston, E.3
  • 34
    • 0025255311 scopus 로고
    • Identification of a region of calsequestrin that binds to the junctional face membrane of sarcoplasmic reticulum
    • Collins, J. H., Tarcsafalvi, A. and Ikemoto, N. (1990) Identification of a region of calsequestrin that binds to the junctional face membrane of sarcoplasmic reticulum. Biochemical Biophysical Research Communication, 167, 189-193.
    • (1990) Biochemical Biophysical Research Communication , vol.167 , pp. 189-193
    • Collins, J.H.1    Tarcsafalvi, A.2    Ikemoto, N.3
  • 35
    • 0028352967 scopus 로고
    • Regulation of calcium channel in sarcoplasmic reticulum by calsequestrin
    • Kawasaki, T. and Kasai, M. (1994) Regulation of calcium channel in sarcoplasmic reticulum by calsequestrin. Biochemical Biophysical Research Communication, 199, 1120-1127.
    • (1994) Biochemical Biophysical Research Communication , vol.199 , pp. 1120-1127
    • Kawasaki, T.1    Kasai, M.2
  • 37
    • 0021137066 scopus 로고
    • Preparation and morphology of sarcoptasmic reticulum terminal cisternae from rabbit skeletal muscle
    • Saito, A., Seiler, S., Chu, A. and Fleischer, S. (1984) Preparation and morphology of sarcoptasmic reticulum terminal cisternae from rabbit skeletal muscle. Journal of Cell Biology, 99, 875-885.
    • (1984) Journal of Cell Biology , vol.99 , pp. 875-885
    • Saito, A.1    Seiler, S.2    Chu, A.3    Fleischer, S.4
  • 38
    • 0014940130 scopus 로고
    • Purification and properties of an adenosine triphosphatase from sarcoplasmic reticulum
    • MacLennan, D. H. (1970) Purification and properties of an adenosine triphosphatase from sarcoplasmic reticulum. Journal of Biological Chemistry, 245, 4508-4518.
    • (1970) Journal of Biological Chemistry , vol.245 , pp. 4508-4518
    • MacLennan, D.H.1
  • 40
    • 0026689240 scopus 로고
    • A simple, fast, one-step method for the purification of the skeletal muscle ryanodine receptor
    • Shoshan-Barmatz, V. and Zarka, A. (1992) A simple, fast, one-step method for the purification of the skeletal muscle ryanodine receptor Biochemical Journal, 285, 61-64.
    • (1992) Biochemical Journal , vol.285 , pp. 61-64
    • Shoshan-Barmatz, V.1    Zarka, A.2
  • 41
    • 0022229182 scopus 로고
    • Determination of microgram quantities of protein in the presence of milligram levels of lipid with amido black 10B
    • Kaplan, R. S. and Pedersen, F. L. (1985) Determination of microgram quantities of protein in the presence of milligram levels of lipid with amido black 10B. Analytic Biochemistry, 150, 95-104.
    • (1985) Analytic Biochemistry , vol.150 , pp. 95-104
    • Kaplan, R.S.1    Pedersen, F.L.2
  • 42
    • 0024201809 scopus 로고
    • Computer programs for calculating total from specific free or free from specific total ionic concentrations in aqueous solutions containing multiple metals and ligands
    • Fabiato, A. (1988) Computer programs for calculating total from specific free or free from specific total ionic concentrations in aqueous solutions containing multiple metals and ligands. Methods in Enzymology, 157, 378-417.
    • (1988) Methods in Enzymology , vol.157 , pp. 378-417
    • Fabiato, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.