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Volumn 8, Issue 11, 1999, Pages 2258-2269

Crystal structure of brain-type creatine kinase at 1.41 Å resolution

Author keywords

Brain type creatine kinase; Cancer; Cellular energy metabolism; Guanidino kinase; Neurodegenerative disorders

Indexed keywords

ARGININE KINASE; CREATINE KINASE; CREATINE PHOSPHATE; GUANIDINE DERIVATIVE;

EID: 0032718703     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.11.2258     Document Type: Article
Times cited : (101)

References (76)
  • 1
    • 0031213840 scopus 로고    scopus 로고
    • The expression of creatine kinase isoenzymes in neocortex of patients with neurodegenerative disorders: Alzheimer's and Pick's disease
    • Aksenov MY, Aksenova, MV, Payne RM, Smith CD, Markesbery WR, Carney JM. 1997. The expression of creatine kinase isoenzymes in neocortex of patients with neurodegenerative disorders: Alzheimer's and Pick's disease. Exp Neurol 146:458-465.
    • (1997) Exp Neurol , vol.146 , pp. 458-465
    • Aksenov, M.Y.1    Payne, R.M.2    Smith, C.D.3    Markesbery, W.R.4    Carney, J.M.5
  • 3
    • 0344088960 scopus 로고
    • The active site of creatine kinase. Affinity labeling of cysteine 282 with epoxy-creatine
    • Beuchter DD, Medzihradsky, KF, Burlingame AL, Kenyon GL. 1992. The active site of creatine kinase. Affinity labeling of cysteine 282 with epoxy-creatine. J Biol Chem 267:2172-2178.
    • (1992) J Biol Chem , vol.267 , pp. 2172-2178
    • Beuchter, D.D.1    Medzihradsky, K.F.2    Burlingame, A.L.3    Kenyon, G.L.4
  • 4
    • 0024279342 scopus 로고
    • Crystallographic refinement by simulated annealing. Application to a 2.8 Å structure of aspartate aminotransferase
    • Brünger AT. 1988. Crystallographic refinement by simulated annealing. Application to a 2.8 Å structure of aspartate aminotransferase. J Mol Biol 203:803-816.
    • (1988) J Mol Biol , vol.203 , pp. 803-816
    • Brünger, A.T.1
  • 5
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger AT. 1992a. Free R value: A novel statistical quantity for assessing the accuracy of crystal structures. Nature 355:472-415.
    • (1992) Nature , vol.355 , pp. 472-415
    • Brünger, A.T.1
  • 8
    • 0028047586 scopus 로고
    • Transcriptional and posttranscriptional mechanisms modulate creatine kinase expression during differentiation of osteoblastic cells
    • Ch'ng JL, Ibrahim B. 1994. Transcriptional and posttranscriptional mechanisms modulate creatine kinase expression during differentiation of osteoblastic cells. J Biol Chem 269:2336-2341.
    • (1994) J Biol Chem , vol.269 , pp. 2336-2341
    • Ch'ng, J.L.1    Ibrahim, B.2
  • 9
    • 0025677199 scopus 로고
    • Purification and identification of creatine phosphokinase B as a substrate of protein kinase C in mouse skin in vivo
    • Chida K, Kasahara K, Tsunenage M, Kohno Y, Yamada S, Ohmi S, Kuroki T. 1990. Purification and identification of creatine phosphokinase B as a substrate of protein kinase C in mouse skin in vivo. Biochem Biophys Res Commun 173:351-357.
    • (1990) Biochem Biophys Res Commun , vol.173 , pp. 351-357
    • Chida, K.1    Kasahara, K.2    Tsunenage, M.3    Kohno, Y.4    Yamada, S.5    Ohmi, S.6    Kuroki, T.7
  • 10
    • 0032030854 scopus 로고    scopus 로고
    • Abnormal properties of creatine kinase in Alzheimer's disease brain: Correlation of reduced enzyme activity and active site photolabeling with aberrant cytosol-membrane partitioning
    • David S, Shoemaker M, Haley BE. 1998. Abnormal properties of creatine kinase in Alzheimer's disease brain: Correlation of reduced enzyme activity and active site photolabeling with aberrant cytosol-membrane partitioning. Mol Brain Res 54:276-287.
    • (1998) Mol Brain Res , vol.54 , pp. 276-287
    • David, S.1    Shoemaker, M.2    Haley, B.E.3
  • 11
    • 0030915704 scopus 로고    scopus 로고
    • Improved R-factors for diffraction data analysis in macromolecular crystallography
    • Diederichs K, Karplus PA. 1997. Improved R-factors for diffraction data analysis in macromolecular crystallography. Nature Struct Biol 4:269-275.
    • (1997) Nature Struct Biol , vol.4 , pp. 269-275
    • Diederichs, K.1    Karplus, P.A.2
  • 12
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh RA, Huber R. 1991. Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallogr A 47:392-400.
    • (1991) Acta Crystallogr A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 13
    • 0014216037 scopus 로고
    • The comparative enzymology of creatine kinases. Isolation and characterization from chicken and rabbit tissues
    • Eppenberger HM, Dawson DM, Kaplan NO. 1967. The comparative enzymology of creatine kinases. Isolation and characterization from chicken and rabbit tissues. J Biol Chem 242:204-209.
    • (1967) J Biol Chem , vol.242 , pp. 204-209
    • Eppenberger, H.M.1    Dawson, D.M.2    Kaplan, N.O.3
  • 14
    • 0031848225 scopus 로고    scopus 로고
    • Structural changes of creatine kinase upon substrate binding
    • Forstner M, Kriechbaum M, Laggner P, Wallimann T. 1998. Structural changes of creatine kinase upon substrate binding. Biophys J 75(2):1016-1023.
    • (1998) Biophys J , vol.75 , Issue.2 , pp. 1016-1023
    • Forstner, M.1    Kriechbaum, M.2    Laggner, P.3    Wallimann, T.4
  • 15
    • 0342460542 scopus 로고    scopus 로고
    • The active site histidines of creatine kinase. A critical role of His61 situated on a flexible loop
    • Forstner M, Müller A, Stolz M, Wallimann T. 1997. The active site histidines of creatine kinase. A critical role of His61 situated on a flexible loop. Protein Sci 6:331-339.
    • (1997) Protein Sci , vol.6 , pp. 331-339
    • Forstner, M.1    Müller, A.2    Stolz, M.3    Wallimann, T.4
  • 16
    • 0026699158 scopus 로고
    • Purification and localization of brain-type creatine kinase in sodium chloride transporting epithelia of the spiny dogfish. Squalus acanthias
    • Friedman DL, Roberts R. 1992. Purification and localization of brain-type creatine kinase in sodium chloride transporting epithelia of the spiny dogfish. Squalus acanthias. J Biol Chem 267:4270-4276.
    • (1992) J Biol Chem , vol.267 , pp. 4270-4276
    • Friedman, D.L.1    Roberts, R.2
  • 18
    • 0027268548 scopus 로고
    • The reactive cysteine is required for synergism but is nonessential for catalysis
    • Furter R, Furter-Graves EM, Wallimann T. 1993. The reactive cysteine is required for synergism but is nonessential for catalysis. Biochemistry 32:7022-7029.
    • (1993) Biochemistry , vol.32 , pp. 7022-7029
    • Furter, R.1    Furter-Graves, E.M.2    Wallimann, T.3
  • 20
    • 0029143228 scopus 로고
    • Multiple-state equilibrium unfolding of guanidino kinases
    • Gross M, Lustig A, Wallimann T, Furter R. 1995. Multiple-state equilibrium unfolding of guanidino kinases. Biochemistry 34:10350-10357.
    • (1995) Biochemistry , vol.34 , pp. 10350-10357
    • Gross, M.1    Lustig, A.2    Wallimann, T.3    Furter, R.4
  • 21
    • 0024392614 scopus 로고
    • Resonance energy transfer between the active site of rabbit muscle creatine kinase by steady-state and time-resolved fluorescence
    • Grossman SH. 1990. Resonance energy transfer between the active site of rabbit muscle creatine kinase by steady-state and time-resolved fluorescence. Biochemistry 28:4894-4902.
    • (1990) Biochemistry , vol.28 , pp. 4894-4902
    • Grossman, S.H.1
  • 23
    • 0029101502 scopus 로고
    • Autophosphorylation of creatine kinase: Characterization and identification of a specifically phosphorylated peptide
    • Hemmer W, Furter-Graves EM, Frank G, Wallimann T, Furter R. 1995. Autophosphorylation of creatine kinase: Characterization and identification of a specifically phosphorylated peptide. Biochim Biophys Acta 1251:81-90.
    • (1995) Biochim Biophys Acta , vol.1251 , pp. 81-90
    • Hemmer, W.1    Furter-Graves, E.M.2    Frank, G.3    Wallimann, T.4    Furter, R.5
  • 25
    • 0028273027 scopus 로고
    • The activity of S-thiomethyl modified creatine kinase is due to regeneration of free thiol at the active site
    • Hou ZX, Vollmer S. 1994. The activity of S-thiomethyl modified creatine kinase is due to regeneration of free thiol at the active site. Biochim Biophys Acta 1205:83-88.
    • (1994) Biochim Biophys Acta , vol.1205 , pp. 83-88
    • Hou, Z.X.1    Vollmer, S.2
  • 26
    • 84889120137 scopus 로고
    • Improved methods of building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou J-Y, Cowan SW, Kjeldgaard M. 1991. Improved methods of building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 47:110-119.
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 27
    • 85046526624 scopus 로고
    • Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector
    • Kabsch W. 1988. Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector. J Appl Crystallogr 21:916-924.
    • (1988) J Appl Crystallogr , vol.21 , pp. 916-924
    • Kabsch, W.1
  • 28
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. 1993. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J Appl Crystallogr 26:795-800.
    • (1993) J Appl Crystallogr , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 29
    • 0031469493 scopus 로고    scopus 로고
    • Mitochondrial creatine kinase - A square protein
    • Kabsch W, Fritz-Wolf K. 1997. Mitochondrial creatine kinase - A square protein. Curr Opin Struct Biol 7:811-818.
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 811-818
    • Kabsch, W.1    Fritz-Wolf, K.2
  • 30
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C. 1983. Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 32
    • 0027979405 scopus 로고
    • The N-terminal heptapeptide of mitochondrial creatine kinase is important for octamerization
    • Kaldis P, Furter R, Wallimann T. 1994. The N-terminal heptapeptide of mitochondrial creatine kinase is important for octamerization. Biochemistry 33:952-959.
    • (1994) Biochemistry , vol.33 , pp. 952-959
    • Kaldis, P.1    Furter, R.2    Wallimann, T.3
  • 33
    • 0029842655 scopus 로고    scopus 로고
    • Hot spots of creatine kinase localization in brain: Cerebellum, hippocampus and choroid plexus
    • Kaldis P, Hemmer W, Zanolla E, Holtzman D, Wallimann T. 1996. Hot spots of creatine kinase localization in brain: Cerebellum, hippocampus and choroid plexus. Dev Neurosci 18:542-554.
    • (1996) Dev Neurosci , vol.18 , pp. 542-554
    • Kaldis, P.1    Hemmer, W.2    Zanolla, E.3    Holtzman, D.4    Wallimann, T.5
  • 34
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 24:946-950.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 35
    • 0028912236 scopus 로고
    • Ion transport in gills of the euryhaline fish Gillichtys mirabilis is facilitated by a phosphocreatine circuit
    • Kültz D, Somero GN. 1995. Ion transport in gills of the euryhaline fish Gillichtys mirabilis is facilitated by a phosphocreatine circuit. Am J Physiol 268:R1003-R1012.
    • (1995) Am J Physiol , vol.268
    • Kültz, D.1    Somero, G.N.2
  • 36
  • 37
  • 38
    • 0028122461 scopus 로고
    • Interactions of nucleotides with fully unadenylylated glutamine synthetase from Salmonella typhimurium
    • Liaw SH, Jun G, Eisenberg D. 1994. Interactions of nucleotides with fully unadenylylated glutamine synthetase from Salmonella typhimurium. Biochemistry 33:11184-11188.
    • (1994) Biochemistry , vol.33 , pp. 11184-11188
    • Liaw, S.H.1    Jun, G.2    Eisenberg, D.3
  • 39
    • 0001099937 scopus 로고
    • Traitement statistique des erreurs dans la determination des structures cristallines
    • Luzatti V. 1952. Traitement statistique des erreurs dans la determination des structures cristallines. Acta Crystallogr 5:802-810.
    • (1952) Acta Crystallogr , vol.5 , pp. 802-810
    • Luzatti, V.1
  • 40
    • 0023147598 scopus 로고
    • Only one of the two interconvertible forms of mitochondrial creatine kinase binds to heart mitoplasts
    • Marcillat O, Goldschmidt D, Eichenberger D, Vial C. 1987. Only one of the two interconvertible forms of mitochondrial creatine kinase binds to heart mitoplasts. Biochim Biophys Acta 890:233-241.
    • (1987) Biochim Biophys Acta , vol.890 , pp. 233-241
    • Marcillat, O.1    Goldschmidt, D.2    Eichenberger, D.3    Vial, C.4
  • 41
    • 0002705842 scopus 로고
    • A visual protein crystallographic software system for X11/ Xview
    • McRee DE. 1992. A visual protein crystallographic software system for X11/ Xview. J Mol Graph 10:44-46.
    • (1992) J Mol Graph , vol.10 , pp. 44-46
    • McRee, D.E.1
  • 42
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt EA, Bacon DJ. 1997. Raster3D: Photorealistic molecular graphics. Methods Enzymol 277:505-524.
    • (1997) Methods Enzymol , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 43
    • 0015052797 scopus 로고
    • Inhibition of adenosine 5′-triphosphate-creatine phosphotransferase by substrate-anion complexes. Evidence for the transition-state organization of the catalytic site
    • Milner-White EJ, Watts DC. 1971. Inhibition of adenosine 5′-triphosphate-creatine phosphotransferase by substrate-anion complexes. Evidence for the transition-state organization of the catalytic site. Biochem J 122(5):727-740.
    • (1971) Biochem J , vol.122 , Issue.5 , pp. 727-740
    • Milner-White, E.J.1    Watts, D.C.2
  • 44
    • 0032497392 scopus 로고    scopus 로고
    • Identification of the creatine binding domain of creatine kinase by photoaffinity labeling
    • Min KL, Steghens JP, Henry R, Doutheau A, Collombel C. 1998. Identification of the creatine binding domain of creatine kinase by photoaffinity labeling. Biochim Biophys Acta 1387:80-88.
    • (1998) Biochim Biophys Acta , vol.1387 , pp. 80-88
    • Min, K.L.1    Steghens, J.P.2    Henry, R.3    Doutheau, A.4    Collombel, C.5
  • 46
    • 84920325457 scopus 로고
    • AmoRe: An automated package for molecular replacement
    • Navaza J. 1994. AmoRe: An automated package for molecular replacement. Acta Crystallogr D 50:157-163.
    • (1994) Acta Crystallogr D , vol.50 , pp. 157-163
    • Navaza, J.1
  • 47
    • 0000649842 scopus 로고    scopus 로고
    • Improved structure refinement through maximum likelihood
    • Pannu NS, Read RJ. 1996. Improved structure refinement through maximum likelihood. Acta Crystallogr A 52:659-668.
    • (1996) Acta Crystallogr A , vol.52 , pp. 659-668
    • Pannu, N.S.1    Read, R.J.2
  • 48
    • 0027504514 scopus 로고
    • Creatine kinase isoenzymes are highly regulated during pregnancy in rat uterus and placenta
    • Payne MR, Friedman DL, Grant JW, Perryman MB, Strauss AW. 1993. Creatine kinase isoenzymes are highly regulated during pregnancy in rat uterus and placenta. Am J Physiol 265:E624-E635.
    • (1993) Am J Physiol , vol.265
    • Payne, M.R.1    Friedman, D.L.2    Grant, J.W.3    Perryman, M.B.4    Strauss, A.W.5
  • 49
    • 0024996554 scopus 로고
    • Phosphorylation of chicken brain-type creatine kinase affects a physiologically important kinetic parameter and gives rise to protein microheterogeneity in vivo
    • Quest AFG, Soldati T, Hemmer W, Perriard J-C, Eppenberger HM, Wallimann T. 1990. Phosphorylation of chicken brain-type creatine kinase affects a physiologically important kinetic parameter and gives rise to protein microheterogeneity in vivo. FEBS 2:457-464.
    • (1990) FEBS , vol.2 , pp. 457-464
    • Quest, A.F.G.1    Soldati, T.2    Hemmer, W.3    Perriard, J.-C.4    Eppenberger, H.M.5    Wallimann, T.6
  • 50
    • 0029820647 scopus 로고    scopus 로고
    • Changes of creatine kinase secondary structure induced by the release of nucleotides from caged compounds
    • Raimbault C, Buchet R, Vial C. 1996. Changes of creatine kinase secondary structure induced by the release of nucleotides from caged compounds. Eur J Biochem 240:134-142.
    • (1996) Eur J Biochem , vol.240 , pp. 134-142
    • Raimbault, C.1    Buchet, R.2    Vial, C.3
  • 51
    • 0032515099 scopus 로고    scopus 로고
    • Crystal structure of rabbit muscle creatine kinase
    • Rao JK, Bujacz, G, Wlodawer A. 1998. Crystal structure of rabbit muscle creatine kinase. FEBS 439:133-137.
    • (1998) FEBS , vol.439 , pp. 133-137
    • Rao, J.K.1    Bujacz, G.2    Wlodawer, A.3
  • 52
    • 84944812409 scopus 로고
    • Improved fourier coefficients for maps using phases from partial structures with errors
    • Read RJ. 1986. Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr A 42:140-149.
    • (1986) Acta Crystallogr A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 53
    • 0019492132 scopus 로고
    • Identification of the major component of the estrogen-induced protein of rat uterus as the BB isoenzyme of creatine kinase
    • Reiss NA, Kaye A. 1981. Identification of the major component of the estrogen-induced protein of rat uterus as the BB isoenzyme of creatine kinase. J Biol Chem 256:5741-5749.
    • (1981) J Biol Chem , vol.256 , pp. 5741-5749
    • Reiss, N.A.1    Kaye, A.2
  • 54
    • 0025942262 scopus 로고
    • Multiple positive and negative elements regulate human brain creatine kinase gene expression
    • Ritchie M-E, Trask RV, Fontanet HL, Billadello JJ. 1991. Multiple positive and negative elements regulate human brain creatine kinase gene expression. Nucl Acids Res 19:6231-6240.
    • (1991) Nucl Acids Res , vol.19 , pp. 6231-6240
    • Ritchie, M.-E.1    Trask, R.V.2    Fontanet, H.L.3    Billadello, J.J.4
  • 55
    • 0026035373 scopus 로고
    • Interaction of mitochondrial creatine kinase with model membranes. A monolayer study
    • Rojo M, Hovius R, Demel R, Wallimann T, Eppenberger HM, Nicolay K. 1991. Interaction of mitochondrial creatine kinase with model membranes. A monolayer study. FEBS 1,2:123-129.
    • (1991) FEBS , vol.1-2 , pp. 123-129
    • Rojo, M.1    Hovius, R.2    Demel, R.3    Wallimann, T.4    Eppenberger, H.M.5    Nicolay, K.6
  • 57
    • 0345382486 scopus 로고
    • Immunoenzymological evidence suggesting a change in conformation of adenylic acid deaminase and creatine kinase during substrate combination
    • Samuels AJ. 1961. Immunoenzymological evidence suggesting a change in conformation of adenylic acid deaminase and creatine kinase during substrate combination. Biochem J 1:437-444.
    • (1961) Biochem J , vol.1 , pp. 437-444
    • Samuels, A.J.1
  • 58
    • 0031712655 scopus 로고    scopus 로고
    • Functional aspects of the X-ray structure of mitochondrial creatine kinase: A molecular physiology approach
    • Schlattner U, Forstner M, Eder M, Stachowiak O, Fritz-Wolf K, Wallimann T. 1998. Functional aspects of the X-ray structure of mitochondrial creatine kinase: A molecular physiology approach. Mol Cell Biochem 184:125-140.
    • (1998) Mol Cell Biochem , vol.184 , pp. 125-140
    • Schlattner, U.1    Forstner, M.2    Eder, M.3    Stachowiak, O.4    Fritz-Wolf, K.5    Wallimann, T.6
  • 59
    • 0023806487 scopus 로고
    • Mitochondrial creatine kinase from cardiac muscle and brain are two distinct isoenzymes but both form octameric molecules
    • Schlegel J, Wyss M, Schürch U, Schnyder T, Quest A, Wegmann G, Eppenberger HM, Wallimann T. 1988a. Mitochondrial creatine kinase from cardiac muscle and brain are two distinct isoenzymes but both form octameric molecules. J Biol Chem 263:16963-16969.
    • (1988) J Biol Chem , vol.263 , pp. 16963-16969
    • Schlegel, J.1    Wyss, M.2    Schürch, U.3    Schnyder, T.4    Quest, A.5    Wegmann, G.6    Eppenberger, H.M.7    Wallimann, T.8
  • 60
    • 0023775251 scopus 로고
    • Native mitochondrial creatine kinase (Mi-CK) forms octameric structures. I. Isolation of two interconvertible Mi-CK isoforms: Dimeric and octameric Mi-CK
    • Schlegel J, Zurbriggen B, Wegmann G, Wyss M, Eppenberger HM, Wallimann T. 1988b. Native mitochondrial creatine kinase (Mi-CK) forms octameric structures. I. Isolation of two interconvertible Mi-CK isoforms: Dimeric and octameric Mi-CK. J Biol Chem 263:16942-16953.
    • (1988) J Biol Chem , vol.263 , pp. 16942-16953
    • Schlegel, J.1    Zurbriggen, B.2    Wegmann, G.3    Wyss, M.4    Eppenberger, H.M.5    Wallimann, T.6
  • 61
    • 0018348257 scopus 로고
    • Creatine kinase activity and isoenzyme composition in normal tissue and neoplasms of rat and mice
    • Shatton JB, Morris HP, Weinhouse S. 1979. Creatine kinase activity and isoenzyme composition in normal tissue and neoplasms of rat and mice. Cancer Res 39:492-501.
    • (1979) Cancer Res , vol.39 , pp. 492-501
    • Shatton, J.B.1    Morris, H.P.2    Weinhouse, S.3
  • 64
    • 0025217034 scopus 로고
    • Alternative ribosomal initiation gives rise to chicken brain-type creatine kinase isoproteins with heterogeneous amino termini
    • Soldati T, Schäfer B, Perriard J-C. 1990. Alternative ribosomal initiation gives rise to chicken brain-type creatine kinase isoproteins with heterogeneous amino termini. J Biol Chem 265:4498-4506.
    • (1990) J Biol Chem , vol.265 , pp. 4498-4506
    • Soldati, T.1    Schäfer, B.2    Perriard, J.-C.3
  • 65
    • 3042643717 scopus 로고
    • Direct and sex-specific stimulation by sex steroids of creatine kinase activity and DNA synthesis in rat bone
    • Sömjen D, Weisman Y, Harell A, Berger E, Kaye AM. 1989. Direct and sex-specific stimulation by sex steroids of creatine kinase activity and DNA synthesis in rat bone. Proc Natll Acad Sci USA 86:3361-3365.
    • (1989) Proc Natll Acad Sci USA , vol.86 , pp. 3361-3365
    • Sömjen, D.1    Weisman, Y.2    Harell, A.3    Berger, E.4    Kaye, A.M.5
  • 66
    • 0031781884 scopus 로고    scopus 로고
    • Myofibrillar interaction of cytosolic creatine kinase (CK) isoenzymes: Allocation of N-terminal binding epitope in MM-CK and BB-CK
    • Stolz M, Wallimann T. 1998. Myofibrillar interaction of cytosolic creatine kinase (CK) isoenzymes: Allocation of N-terminal binding epitope in MM-CK and BB-CK. J Cell Sci 111:1207-1216.
    • (1998) J Cell Sci , vol.111 , pp. 1207-1216
    • Stolz, M.1    Wallimann, T.2
  • 67
    • 0029992890 scopus 로고    scopus 로고
    • Balancing ATP in the cell
    • Stroud RM. 1996. Balancing ATP in the cell. Nature Struct Biol 3:567-569.
    • (1996) Nature Struct Biol , vol.3 , pp. 567-569
    • Stroud, R.M.1
  • 68
    • 0031555335 scopus 로고    scopus 로고
    • Evolution of phosphagen kinase. VI. Isolation, characterization and cdna-derived amino acid sequence of lombricine kinase from the earthworm Eisenia foetida, and identification of a possible candidate for the guanidine substrate recognition site
    • Suzuki T, Kawasaki Y, Furukohri T, Ellington WR. 1997. Evolution of phosphagen kinase. VI. Isolation, characterization and cDNA-derived amino acid sequence of lombricine kinase from the earthworm Eisenia foetida, and identification of a possible candidate for the guanidine substrate recognition site. Biochim Biophys Acta 1348:152-159.
    • (1997) Biochim Biophys Acta , vol.1348 , pp. 152-159
    • Suzuki, T.1    Kawasaki, Y.2    Furukohri, T.3    Ellington, W.R.4
  • 69
  • 70
    • 0028017704 scopus 로고
    • Creatine kinase in non-muscle tissues and cells
    • Wallimann T, Hemmer W. 1994. Creatine kinase in non-muscle tissues and cells. Mol Cell Biochem 133/134:193-220.
    • (1994) Mol Cell Biochem , vol.133-134 , pp. 193-220
    • Wallimann, T.1    Hemmer, W.2
  • 71
    • 0020805791 scopus 로고
    • Isoenzyme-specific localization of M-line hound creatine kinase in myogenic cells
    • Wallimann T, Moser H, Eppenberger HM. 1983. Isoenzyme-specific localization of M-line hound creatine kinase in myogenic cells. J Muscle Res Cell Motil 4:429-441.
    • (1983) J Muscle Res Cell Motil , vol.4 , pp. 429-441
    • Wallimann, T.1    Moser, H.2    Eppenberger, H.M.3
  • 72
    • 0026585611 scopus 로고
    • Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: The "phosphocreatine circuit" for cellular energy homeostasis
    • Wallimann T, Wyss M, Brdicka D, Nicolay K, Eppenberger HM. 1992. Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: The "phosphocreatine circuit" for cellular energy homeostasis. Biochem J 281: 21-40.
    • (1992) Biochem J , vol.281 , pp. 21-40
    • Wallimann, T.1    Wyss, M.2    Brdicka, D.3    Nicolay, K.4    Eppenberger, H.M.5
  • 73
    • 0025353852 scopus 로고
    • A unique chicken B-creatine kinase gene gives rise to two B-creatine kinase isoproteins with distinct N-termini by alternative splicing
    • Wirz T, Brandle U, Soldati T, Hossle JP, Perriard J-C. 1990. A unique chicken B-creatine kinase gene gives rise to two B-creatine kinase isoproteins with distinct N-termini by alternative splicing. J Biol Chem 265:11656-11666.
    • (1990) J Biol Chem , vol.265 , pp. 11656-11666
    • Wirz, T.1    Brandle, U.2    Soldati, T.3    Hossle, J.P.4    Perriard, J.-C.5
  • 74
    • 0029993078 scopus 로고    scopus 로고
    • Phosphocreatine-dependent glutamate uptake by synaptic vesicles. A comparison with ATP-dependent glutamate uptake
    • Xu CJ, Klunk WE, Kanfer JN, Xiong Q, Miller G, Pettegrew JW. 1996. Phosphocreatine-dependent glutamate uptake by synaptic vesicles. A comparison with ATP-dependent glutamate uptake. J Biol Chem 271:13435-13440.
    • (1996) J Biol Chem , vol.271 , pp. 13435-13440
    • Xu, C.J.1    Klunk, W.E.2    Kanfer, J.N.3    Xiong, Q.4    Miller, G.5    Pettegrew, J.W.6
  • 75
    • 0028125271 scopus 로고
    • Mouse p53 represses the rat brain creatine kinase gene but activates the rat muscle creatine kinase gene
    • Zhao J, Schmieg FI, Simmons DT, Molloy GR. 1994. Mouse p53 represses the rat brain creatine kinase gene but activates the rat muscle creatine kinase gene. Mol Cell Biol 14:8483-8492.
    • (1994) Mol Cell Biol , vol.14 , pp. 8483-8492
    • Zhao, J.1    Schmieg, F.I.2    Simmons, D.T.3    Molloy, G.R.4


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