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Volumn 450, Issue 7172, 2007, Pages 1036-1042

The structural basis of calcium transport by the calcium pump

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); ALUMINUM FLUORIDE; BERYLLIUM FLUORIDE; CALCIUM ION; FLUORIDE; UNCLASSIFIED DRUG;

EID: 37249043376     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature06418     Document Type: Article
Times cited : (390)

References (64)
  • 1
    • 0030854715 scopus 로고    scopus 로고
    • Cellular energy utilization and molecular origin of standard metabolic rate in mammals
    • Rolfe, D. F. & Brown, G. C. Cellular energy utilization and molecular origin of standard metabolic rate in mammals. Physiol. Rev. 77, 731-758 (1997).
    • (1997) Physiol. Rev , vol.77 , pp. 731-758
    • Rolfe, D.F.1    Brown, G.C.2
  • 2
    • 0037022309 scopus 로고    scopus 로고
    • Calcium signaling: A tale for all seasons
    • Carafoli, E. Calcium signaling: a tale for all seasons. Proc. Natl Acad. Sci. USA 99, 1115-1122 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 1115-1122
    • Carafoli, E.1
  • 3
    • 84968965880 scopus 로고
    • Adenosine triphosphate-linked concentration of calcium ions in a particulate fraction of rabbit muscle
    • Ebashi, S. & Lipmann, F. Adenosine triphosphate-linked concentration of calcium ions in a particulate fraction of rabbit muscle. J. Cell Biol. 14, 389-400 (1962).
    • (1962) J. Cell Biol , vol.14 , pp. 389-400
    • Ebashi, S.1    Lipmann, F.2
  • 4
    • 0018835338 scopus 로고
    • Quantitative aspects of the calcium concept of excitation contraction coupling - a critical evaluation
    • Hasselbach, W. Quantitative aspects of the calcium concept of excitation contraction coupling - a critical evaluation. Basic Res. Cardiol. 75, 2-12 (1980).
    • (1980) Basic Res. Cardiol , vol.75 , pp. 2-12
    • Hasselbach, W.1
  • 6
    • 0025245422 scopus 로고
    • 2+-ATPase during calcium transport in reconstituted proteoliposomes with low ionic permeability
    • 2+-ATPase during calcium transport in reconstituted proteoliposomes with low ionic permeability. J. Biol. Chem. 265, 19524-19534 (1990).
    • (1990) J. Biol. Chem , vol.265 , pp. 19524-19534
    • Levy, D.1    Seigneuret, M.2    Bluzat, A.3    Rigaud, J.L.4
  • 7
    • 0025775022 scopus 로고
    • 2+-ATPase reconstituted at high lipid/protein ratio
    • 2+-ATPase reconstituted at high lipid/protein ratio. FEBS Lett. 284, 46-50 (1991).
    • (1991) FEBS Lett , vol.284 , pp. 46-50
    • Cornelius, F.1    Moller, J.V.2
  • 9
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution
    • Toyoshima, C., Nakasako, M., Nomura, H. & Ogawa, H. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution. Nature 405, 647-655 (2000).
    • (2000) Nature , vol.405 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 10
    • 0037043709 scopus 로고    scopus 로고
    • Structural changes in the calcium pump accompanying the dissociation of calcium
    • Toyoshima, C. & Nomura, H. Structural changes in the calcium pump accompanying the dissociation of calcium. Nature 418, 605-611 (2002).
    • (2002) Nature , vol.418 , pp. 605-611
    • Toyoshima, C.1    Nomura, H.2
  • 11
    • 2942668632 scopus 로고    scopus 로고
    • Phosphoryl transfer and calcium ion occlusion in the calcium pump
    • Sorensen, T. L., Moller, J. V. & Nissen, P. Phosphoryl transfer and calcium ion occlusion in the calcium pump. Science 304, 1672-1675 (2004).
    • (2004) Science , vol.304 , pp. 1672-1675
    • Sorensen, T.L.1    Moller, J.V.2    Nissen, P.3
  • 12
    • 3242888769 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump with a bound ATP analogue
    • Toyoshima, C. & Mizutani, T. Crystal structure of the calcium pump with a bound ATP analogue. Nature 430, 529-535 (2004).
    • (2004) Nature , vol.430 , pp. 529-535
    • Toyoshima, C.1    Mizutani, T.2
  • 13
    • 9244232176 scopus 로고    scopus 로고
    • Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues
    • Toyoshima, C., Nomura, H. & Tsuda, T. Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues. Nature 432, 361-368 (2004).
    • (2004) Nature , vol.432 , pp. 361-368
    • Toyoshima, C.1    Nomura, H.2    Tsuda, T.3
  • 14
    • 11144330054 scopus 로고    scopus 로고
    • Dephosphorylation of the calcium pump coupled to counterion occlusion
    • Olesen, C., Sorensen, T. L., Nielsen, R. C., Moller, J. V. & Nissen, P. Dephosphorylation of the calcium pump coupled to counterion occlusion. Science 306, 2251-2255 (2004).
    • (2004) Science , vol.306 , pp. 2251-2255
    • Olesen, C.1    Sorensen, T.L.2    Nielsen, R.C.3    Moller, J.V.4    Nissen, P.5
  • 15
    • 33745762313 scopus 로고    scopus 로고
    • Modulatory and catalytic modes of ATP binding by the calcium pump
    • Jensen, A. M., Sorensen, T. L., Olesen, C., Moller, J. V. & Nissen, P. Modulatory and catalytic modes of ATP binding by the calcium pump. EMBO J. 25, 2305-2314 (2006).
    • (2006) EMBO J , vol.25 , pp. 2305-2314
    • Jensen, A.M.1    Sorensen, T.L.2    Olesen, C.3    Moller, J.V.4    Nissen, P.5
  • 16
    • 0020662713 scopus 로고
    • Determinants of calcium loading at steady state in sarcoplasmic reticulum
    • Feher, J. J. & Briggs, F. N. Determinants of calcium loading at steady state in sarcoplasmic reticulum. Biochim. Biophys. Acta 727, 389-402 (1983).
    • (1983) Biochim. Biophys. Acta , vol.727 , pp. 389-402
    • Feher, J.J.1    Briggs, F.N.2
  • 17
    • 0020576593 scopus 로고
    • 2+ efflux in the energized state of the calcium pump
    • 2+ efflux in the energized state of the calcium pump. Biochim. Biophys. Acta 734, 191-200 (1983).
    • (1983) Biochim. Biophys. Acta , vol.734 , pp. 191-200
    • Gerdes, U.1    Moller, J.V.2
  • 18
    • 0028905942 scopus 로고
    • 2+ transport by the sarcoplasmic reticulum ATPase
    • 2+ transport by the sarcoplasmic reticulum ATPase. J. Biol. Chem. 270, 4361-4367 (1995).
    • (1995) J. Biol. Chem , vol.270 , pp. 4361-4367
    • Yu, X.1    Inesi, G.2
  • 19
    • 0037458010 scopus 로고    scopus 로고
    • Na+/K+-pump ligands modulate gating of palytoxin-induced ion channels
    • Artigas, P. & Gadsby, D. C. Na+/K+-pump ligands modulate gating of palytoxin-induced ion channels. Proc. Natl Acad. Sci. USA 100, 501-505 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 501-505
    • Artigas, P.1    Gadsby, D.C.2
  • 20
    • 0020772059 scopus 로고
    • Translocation pathway in the catalysis of active transport
    • Tanford, C. Translocation pathway in the catalysis of active transport. Proc. Natl Acad. Sci. USA 80, 3701-3705 (1983).
    • (1983) Proc. Natl Acad. Sci. USA , vol.80 , pp. 3701-3705
    • Tanford, C.1
  • 21
  • 22
    • 34347247711 scopus 로고    scopus 로고
    • Interdomain communication in calcium pump as revealed in the crystal structures with transmembrane inhibitors
    • Takahashi, M., Kondou, Y. & Toyoshima, C. Interdomain communication in calcium pump as revealed in the crystal structures with transmembrane inhibitors. Proc. Natl Acad. Sci. USA 104, 5800-5805 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 5800-5805
    • Takahashi, M.1    Kondou, Y.2    Toyoshima, C.3
  • 23
    • 0019877491 scopus 로고
    • Sarcoplasmic reticulum ATPase catalyzes hydrolysis of adenyl-5′-yl imidodiphosphate
    • Taylor, J. S. Sarcoplasmic reticulum ATPase catalyzes hydrolysis of adenyl-5′-yl imidodiphosphate. J. Biol. Chem. 256, 9793-9795 (1981).
    • (1981) J. Biol. Chem , vol.256 , pp. 9793-9795
    • Taylor, J.S.1
  • 24
    • 0021343528 scopus 로고
    • Effects of pH, temperature, and calcium concentration on the stoichiometry of the calcium pump of sarcoplasmic reticulum
    • Meltzer, S. & Berman, M. C. Effects of pH, temperature, and calcium concentration on the stoichiometry of the calcium pump of sarcoplasmic reticulum. J. Biol. Chem. 259, 4244-4253 (1984).
    • (1984) J. Biol. Chem , vol.259 , pp. 4244-4253
    • Meltzer, S.1    Berman, M.C.2
  • 25
    • 1842583783 scopus 로고    scopus 로고
    • 2+-ATPase from skeletal muscle is not compatible with a linear kinetic model
    • 2+-ATPase from skeletal muscle is not compatible with a linear kinetic model. Biochemistry 43, 4400-4416 (2004).
    • (2004) Biochemistry , vol.43 , pp. 4400-4416
    • Mahaney, J.E.1    Thomas, D.D.2    Froehlich, J.P.3
  • 26
    • 0023705151 scopus 로고
    • The Na,K-pump
    • Skou, J. C. The Na,K-pump. Methods Enzymol. 156, 1-25 (1988).
    • (1988) Methods Enzymol , vol.156 , pp. 1-25
    • Skou, J.C.1
  • 27
    • 4243471156 scopus 로고
    • Ch. 8 Sinauer Associates, Sunderland, Massachusetts
    • Läuger, P. in Electrogenic pumps Ch. 8 (Sinauer Associates, Sunderland, Massachusetts, 1991).
    • (1991) Electrogenic pumps
    • Läuger, P.1
  • 28
    • 2442504897 scopus 로고    scopus 로고
    • 2+-ATPase: Changes in catalytic and transport sites during phosphoenzyme hydrolysis
    • 2+-ATPase: changes in catalytic and transport sites during phosphoenzyme hydrolysis. J. Biol. Chem. 279, 14991-14998 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 14991-14998
    • Danko, S.1    Yamasaki, K.2    Daiho, T.3    Suzuki, H.4
  • 30
    • 0037064017 scopus 로고    scopus 로고
    • 2+-ATPase. Role of the A domain and its C-terminal link with the transmembrane region
    • 2+-ATPase. Role of the A domain and its C-terminal link with the transmembrane region. J. Biol. Chem. 277, 38647-38659 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 38647-38659
    • Moller, J.V.1
  • 31
    • 0141643093 scopus 로고    scopus 로고
    • 2+-ATPase result in almost complete inhibition of conformational transition and hydrolysis of phosphoenzyme intermediate
    • 2+-ATPase result in almost complete inhibition of conformational transition and hydrolysis of phosphoenzyme intermediate. J. Biol. Chem. 278, 39197-39204 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 39197-39204
    • Daiho, T.1
  • 32
    • 1542335434 scopus 로고    scopus 로고
    • 120, close to the A-domain
    • 120, close to the A-domain. J. Biol. Chem. 279, 9156-9166 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 9156-9166
    • Lenoir, G.1
  • 33
    • 36348994458 scopus 로고    scopus 로고
    • 48 loop linking actuator domain and 1st transmembrane helix of Ca2+-ATPase in Ca2+ deocclusion and release from ADP-insensitive phosphoenzyme
    • 48 loop linking actuator domain and 1st transmembrane helix of Ca2+-ATPase in Ca2+ deocclusion and release from ADP-insensitive phosphoenzyme. J. Biol. Chem. 282, 34429-34447 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 34429-34447
    • Daiho, T.1    Yamasaki, K.2    Danko, S.3    Suzuki, H.4
  • 34
    • 0028816888 scopus 로고
    • 2+- and Na+, K+-ATPases studied by site-directed mutagenesis
    • 2+- and Na+, K+-ATPases studied by site-directed mutagenesis. FEBS Lett. 359, 101-106 (1995).
    • (1995) FEBS Lett , vol.359 , pp. 101-106
    • Andersen, J.P.1    Vilsen, B.2
  • 35
    • 0032483082 scopus 로고    scopus 로고
    • 2+-ATPase affects cation binding from both sides of the membrane and destabilizes the occluded enzyme forms
    • 2+-ATPase affects cation binding from both sides of the membrane and destabilizes the occluded enzyme forms. Biochemistry 37, 10961-10971 (1998).
    • (1998) Biochemistry , vol.37 , pp. 10961-10971
    • Vilsen, B.1    Andersen, J.P.2
  • 36
    • 37249088547 scopus 로고    scopus 로고
    • Crystal structure of the sodium-potassium pump
    • doi:10.1038/nature06419 this issue
    • Morth, J. P. et al. Crystal structure of the sodium-potassium pump. Nature doi:10.1038/nature06419 (this issue).
    • Nature
    • Morth, J.P.1
  • 37
    • 33749169688 scopus 로고    scopus 로고
    • Ion permeation through the Na+,K+-ATPase
    • Reyes, N. & Gadsby, D. C. Ion permeation through the Na+,K+-ATPase. Nature 443, 470-474 (2006).
    • (2006) Nature , vol.443 , pp. 470-474
    • Reyes, N.1    Gadsby, D.C.2
  • 38
    • 0022998517 scopus 로고
    • Factors influencing calcium release from the ADP-sensitive phosphoenzyme intermediate of the sarcoplasmic reticulum ATPase
    • Wakabayashi, S., Ogurusu, T. & Shigekawa, M. Factors influencing calcium release from the ADP-sensitive phosphoenzyme intermediate of the sarcoplasmic reticulum ATPase. J. Biol. Chem. 261, 9762-9769 (1986).
    • (1986) J. Biol. Chem , vol.261 , pp. 9762-9769
    • Wakabayashi, S.1    Ogurusu, T.2    Shigekawa, M.3
  • 39
    • 1142280082 scopus 로고    scopus 로고
    • Structure-function relationship in P-type ATPases-a biophysical approach
    • Apell, H. J. Structure-function relationship in P-type ATPases-a biophysical approach. Rev. Physiol. Biochem. Pharmacol. 150, 1-35 (2003).
    • (2003) Rev. Physiol. Biochem. Pharmacol , vol.150 , pp. 1-35
    • Apell, H.J.1
  • 40
    • 0014029736 scopus 로고
    • Simple allosteric model for membrane pumps
    • Jardetzky, O. Simple allosteric model for membrane pumps. Nature 211, 969-970 (1966).
    • (1966) Nature , vol.211 , pp. 969-970
    • Jardetzky, O.1
  • 41
    • 0013875762 scopus 로고
    • Inhibition of parallel flux and augmentation of counter flux shown by transport models not involving a mobile carrier
    • Vidaver, G. A. Inhibition of parallel flux and augmentation of counter flux shown by transport models not involving a mobile carrier. J. Theor. Biol. 10, 301-306 (1966).
    • (1966) J. Theor. Biol , vol.10 , pp. 301-306
    • Vidaver, G.A.1
  • 43
    • 0041353145 scopus 로고    scopus 로고
    • Structure and mechanism of the lactose permease of Escherichia coli
    • Abramson, J. et al. Structure and mechanism of the lactose permease of Escherichia coli. Science 301, 610-615 (2003).
    • (2003) Science , vol.301 , pp. 610-615
    • Abramson, J.1
  • 44
    • 33846505059 scopus 로고    scopus 로고
    • Coupling substrate and ion binding to extracellular gate of a sodium-dependent aspartate transporter
    • Boudker, O., Ryan, R. M., Yernool, D., Shimamoto, K. & Gouaux, E. Coupling substrate and ion binding to extracellular gate of a sodium-dependent aspartate transporter. Nature 445, 387-393 (2007).
    • (2007) Nature , vol.445 , pp. 387-393
    • Boudker, O.1    Ryan, R.M.2    Yernool, D.3    Shimamoto, K.4    Gouaux, E.5
  • 45
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • Dawson, R. J. & Locher, K. P. Structure of a bacterial multidrug ABC transporter. Nature 443, 180-185 (2006).
    • (2006) Nature , vol.443 , pp. 180-185
    • Dawson, R.J.1    Locher, K.P.2
  • 46
    • 34548671159 scopus 로고    scopus 로고
    • Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF
    • Hvorup, R. N. et al. Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF. Science 317, 1387-1390 (2006).
    • (2006) Science , vol.317 , pp. 1387-1390
    • Hvorup, R.N.1
  • 47
    • 14244272868 scopus 로고    scopus 로고
    • PHENIX: Building new software for automated crystallographic structure determination
    • Adams, P. D. et al. PHENIX: building new software for automated crystallographic structure determination. Acta Crystallogr. D 58, 1948-1954 (2002).
    • (2002) Acta Crystallogr. D , vol.58 , pp. 1948-1954
    • Adams, P.D.1
  • 48
    • 0036405236 scopus 로고    scopus 로고
    • Evidence for phosphotransferases phosphorylated on aspartate residue in N-terminal DXDX(T/V) motif
    • Collet, J. F., Stroobant, V. & Van Schaftingen, E. Evidence for phosphotransferases phosphorylated on aspartate residue in N-terminal DXDX(T/V) motif. Methods Enzymol. 354, 177-188 (2002).
    • (2002) Methods Enzymol , vol.354 , pp. 177-188
    • Collet, J.F.1    Stroobant, V.2    Van Schaftingen, E.3
  • 49
    • 0036403574 scopus 로고    scopus 로고
    • Use of sodium borohydride to detect acyl-phosphate linkages in enzyme reactions
    • Purich, D. L. Use of sodium borohydride to detect acyl-phosphate linkages in enzyme reactions. Methods Enzymol. 354, 168-177 (2002).
    • (2002) Methods Enzymol , vol.354 , pp. 168-177
    • Purich, D.L.1
  • 50
    • 0000154206 scopus 로고
    • The colorimetric determination of phosphours
    • Fiske, C. H. & Subbarow, Y. The colorimetric determination of phosphours. J. Biol. Chem. 26, 375-400 (1925).
    • (1925) J. Biol. Chem , vol.26 , pp. 375-400
    • Fiske, C.H.1    Subbarow, Y.2
  • 53
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch, W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Cryst. 26, 795-800 (1993).
    • (1993) J. Appl. Cryst , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 55
    • 0033896691 scopus 로고    scopus 로고
    • Maximum-likelihood density modification
    • Terwilliger, T. C. Maximum-likelihood density modification. Acta Crystallogr. D 56, 965-972 (2000).
    • (2000) Acta Crystallogr. D , vol.56 , pp. 965-972
    • Terwilliger, T.C.1
  • 56
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 57
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brunger, A. T. et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brunger, A.T.1
  • 58
    • 0027169515 scopus 로고
    • Main-chain bond lengths and bond angles in protein structures
    • Laskowski, R. A., Moss, D. S. & Thornton, J. M. Main-chain bond lengths and bond angles in protein structures. J. Mol. Biol. 231, 1049-1067 (1993).
    • (1993) J. Mol. Biol , vol.231 , pp. 1049-1067
    • Laskowski, R.A.1    Moss, D.S.2    Thornton, J.M.3
  • 59
    • 0035260293 scopus 로고    scopus 로고
    • Phosphoamino acid analysis
    • Sickmann, A. & Meyer, H. E. Phosphoamino acid analysis. Proteomics 1, 200-206 (2001).
    • (2001) Proteomics , vol.1 , pp. 200-206
    • Sickmann, A.1    Meyer, H.E.2
  • 60
    • 0035823603 scopus 로고    scopus 로고
    • Bovine cytosolic 5′-nucleotidase acts through the formation of an aspartate 52-phosphoenzyme intermediate
    • Allegrini, S. et al. Bovine cytosolic 5′-nucleotidase acts through the formation of an aspartate 52-phosphoenzyme intermediate. J. Biol. Chem. 276, 33526-33532 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 33526-33532
    • Allegrini, S.1
  • 61
    • 0033607641 scopus 로고    scopus 로고
    • Mechanistic studies of phosphoserine phosphatase, an enzyme related to P-type ATPases
    • Collet, J. F., Stroobant, V. & Van Schaftingen, E. Mechanistic studies of phosphoserine phosphatase, an enzyme related to P-type ATPases. J. Biol. Chem. 274, 33985-33990 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 33985-33990
    • Collet, J.F.1    Stroobant, V.2    Van Schaftingen, E.3
  • 62
    • 0024787464 scopus 로고
    • Identification of the site of phosphorylation of the chemotaxis response regulator protein, CheY
    • Sanders, D. A., Gillece-Castro, B. L., Stock, A. M., Burlingame, A. L. & Koshland, D. E. Jr. Identification of the site of phosphorylation of the chemotaxis response regulator protein, CheY. J. Biol. Chem. 264, 21770-21778 (1989).
    • (1989) J. Biol. Chem , vol.264 , pp. 21770-21778
    • Sanders, D.A.1    Gillece-Castro, B.L.2    Stock, A.M.3    Burlingame, A.L.4    Koshland Jr., D.E.5
  • 63
    • 0026657678 scopus 로고
    • Fluoride is a slow, tight-binding inhibitor of the calcium ATPase of sarcoplasmic reticulum
    • Murphy, A. J. & Coll, R. J. Fluoride is a slow, tight-binding inhibitor of the calcium ATPase of sarcoplasmic reticulum. J. Biol. Chem. 267, 5229-5235 (1992).
    • (1992) J. Biol. Chem , vol.267 , pp. 5229-5235
    • Murphy, A.J.1    Coll, R.J.2
  • 64
    • 0037728118 scopus 로고
    • 2+)-activated ATPase from sarcoplasmic reticulum. Effect of protein-protein interactions
    • 2+)-activated ATPase from sarcoplasmic reticulum. Effect of protein-protein interactions. J. Biol. Chem. 255, 1912-1920 (1980).
    • (1980) J. Biol. Chem , vol.255 , pp. 1912-1920
    • Moller, J.V.1    Lind, K.E.2    Andersen, J.P.3


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