메뉴 건너뛰기




Volumn 278, Issue 17, 2011, Pages 3025-3031

Motion of the Ca 2+-pump captured

Author keywords

atomic force microscopy; ion pump; P type ATPase; SERCA; single molecular reaction analysis

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); CALCIUM ION; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE; THAPSIGARGIN; ADENOSINE TRIPHOSPHATE; CALCIUM; DEOXYCHOLIC ACID; ENZYME INHIBITOR; IMMOBILIZED ENZYME; MUSCLE PROTEIN; SURFACTANT;

EID: 80051837144     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2011.08222.x     Document Type: Article
Times cited : (26)

References (32)
  • 1
    • 0033939421 scopus 로고    scopus 로고
    • Calcium ion in skeletal muscle: Its crucial role for muscle function, plasticity, and disease
    • Berchtold MW, Brinkmeier H, &, Muntener M, (2000) Calcium ion in skeletal muscle: its crucial role for muscle function, plasticity, and disease. Physiol Rev 80, 1215-1265. (Pubitemid 30452014)
    • (2000) Physiological Reviews , vol.80 , Issue.3 , pp. 1215-1265
    • Berchtold, M.W.1    Brinkmeier, H.2    Muntener, M.3
  • 2
    • 40849094355 scopus 로고    scopus 로고
    • Troponin: Regulatory function and disorders
    • Ohtsuki I, &, Morimoto S, (2008) Troponin: regulatory function and disorders. Biochem Biophys Res Commun 369, 62-73.
    • (2008) Biochem Biophys Res Commun , vol.369 , pp. 62-73
    • Ohtsuki, I.1    Morimoto, S.2
  • 3
    • 72949126637 scopus 로고
    • The calcium pump of the 'relaxing granules' of muscle and its dependence on ATP-splitting
    • Hasselbach W, &, Makinose M, (1961) The calcium pump of the 'relaxing granules' of muscle and its dependence on ATP-splitting. Biochem Z 333, 518-528.
    • (1961) Biochem Z , vol.333 , pp. 518-528
    • Hasselbach, W.1    Makinose, M.2
  • 4
    • 3242701547 scopus 로고    scopus 로고
    • Biology, structure and mechanism of P-type ATPases
    • DOI 10.1038/nrm1354
    • Kuhlbrandt W, (2004) Biology, structure and mechanism of P-type ATPases. Nat Rev Mol Cell Biol 5, 282-295. (Pubitemid 38480609)
    • (2004) Nature Reviews Molecular Cell Biology , vol.5 , Issue.4 , pp. 282-295
    • Kuhlbrandt, W.1
  • 5
    • 0001714579 scopus 로고
    • Third component participating in the superprecipitation of 'natural actomyosin'
    • Ebashi S, (1963) Third component participating in the superprecipitation of 'natural actomyosin'. Nature 200, 1010.
    • (1963) Nature , vol.200 , pp. 1010
    • Ebashi, S.1
  • 6
    • 84968965880 scopus 로고
    • Adenosine triphosphate-linked concentration of calcium ions in a particulate fraction of rabbit muscle
    • Ebashi S, &, Lipmann F, (1962) Adenosine triphosphate-linked concentration of calcium ions in a particulate fraction of rabbit muscle. J Cell Biol 14, 389-400.
    • (1962) J Cell Biol , vol.14 , pp. 389-400
    • Ebashi, S.1    Lipmann, F.2
  • 7
    • 0013790350 scopus 로고
    • A new protein factor promoting aggregation of tropomyosin
    • Ebashi S, &, Kodama A, (1965) A new protein factor promoting aggregation of tropomyosin. J Biochem 58, 107-108.
    • (1965) J Biochem , vol.58 , pp. 107-108
    • Ebashi, S.1    Kodama, A.2
  • 8
    • 33749339997 scopus 로고    scopus 로고
    • Fast-scanning atomic force microscopy reveals the ATP/ADP-dependent conformational changes of GroEL
    • DOI 10.1038/sj.emboj.7601326, PII 7601326
    • Yokokawa M, Wada C, Ando T, Sakai N, Yagi A, Yoshimura SH, &, Takeyasu K, (2006) Fast-scanning atomic force microscopy reveals the ATP/ADP-dependent conformational changes of GroEL. EMBO J 25, 4567-4576. (Pubitemid 44498130)
    • (2006) EMBO Journal , vol.25 , Issue.19 , pp. 4567-4576
    • Yokokawa, M.1    Wada, C.2    Ando, T.3    Sakai, N.4    Yagi, A.5    Yoshimura, S.H.6    Takeyasu, K.7
  • 11
    • 26944478236 scopus 로고    scopus 로고
    • Polymer-supported membranes as models of the cell surface
    • DOI 10.1038/nature04164, PII N04164
    • Tanaka M, &, Sackmann E, (2005) Polymer-supported membranes as models of the cell surface. Nature 437, 656-663. (Pubitemid 41486528)
    • (2005) Nature , vol.437 , Issue.7059 , pp. 656-663
    • Tanaka, M.1    Sackmann, E.2
  • 12
    • 2942657752 scopus 로고    scopus 로고
    • Time-resolved charge translocation by sarcoplasmic reticulum Ca-ATpase measured on a solid supported membrane
    • DOI 10.1529/biophysj.103.036608
    • Tadini Buoninsegni F, Bartolommei G, Moncelli MR, Inesi G, &, Guidelli R, (2004) Time-resolved charge translocation by sarcoplasmic reticulum Ca-ATPase measured on a solid supported membrane. Biophys J 86, 3671-3686. (Pubitemid 38780246)
    • (2004) Biophysical Journal , vol.86 , Issue.6 , pp. 3671-3686
    • Buoninsegni, F.T.1    Bartolommei, G.2    Moncelli, M.R.3    Inesi, G.4    Guidelli, R.5
  • 13
    • 0025019294 scopus 로고
    • Three-dimensional crystals of CaATPase from sarcoplasmic reticulum. Symmetry and molecular packing
    • Stokes DL, &, Green NM, (1990) Three-dimensional crystals of CaATPase from sarcoplasmic reticulum. Symmetry and molecular packing. Biophys J 57, 1-14. (Pubitemid 20033741)
    • (1990) Biophysical Journal , vol.57 , Issue.1 , pp. 1-14
    • Stokes, D.L.1    Green, N.M.2
  • 14
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å; resolution
    • DOI 10.1038/35015017
    • Toyoshima C, Nakasako M, Nomura H, &, Ogawa H, (2000) Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution. Nature 405, 647-655. (Pubitemid 30428644)
    • (2000) Nature , vol.405 , Issue.6787 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 16
    • 0037043709 scopus 로고    scopus 로고
    • Structural changes in the calcium pump accompanying the dissociation of calcium
    • Toyoshima C, &, Nomura H, (2002) Structural changes in the calcium pump accompanying the dissociation of calcium. Nature 418, 605-611.
    • (2002) Nature , vol.418 , pp. 605-611
    • Toyoshima, C.1    Nomura, H.2
  • 17
    • 3242888769 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump with a bound ATP analogue
    • DOI 10.1038/nature02680
    • Toyoshima C, &, Mizutani T, (2004) Crystal structure of the calcium pump with a bound ATP analogue. Nature 430, 529-535. (Pubitemid 38998620)
    • (2004) Nature , vol.430 , Issue.6999 , pp. 529-535
    • Toyoshima, C.1    Mizutani, T.2
  • 18
    • 9244232176 scopus 로고    scopus 로고
    • Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues
    • DOI 10.1038/nature02981
    • Toyoshima C, Nomura H, &, Tsuda T, (2004) Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues. Nature 432, 361-368. (Pubitemid 39555518)
    • (2004) Nature , vol.432 , Issue.7015 , pp. 361-368
    • Toyoshima, C.1    Nomura, H.2    Tsuda, T.3
  • 19
    • 2942668632 scopus 로고    scopus 로고
    • Phosphoryl transfer and calcium ion occlusion in the calcium pump
    • DOI 10.1126/science.1099366
    • Sorensen TL, Moller JV, &, Nissen P, (2004) Phosphoryl transfer and calcium ion occlusion in the calcium pump. Science 304, 1672-1675. (Pubitemid 38765859)
    • (2004) Science , vol.304 , Issue.5677 , pp. 1672-1675
    • Sorensen, T.L.-M.1    Moller, J.V.2    Nissen, P.3
  • 21
    • 0025737973 scopus 로고
    • 2+ transport ATPase by thapsigargin at subnanomolar concentrations
    • 2+ transport ATPase by thapsigargin at subnanomolar concentrations. J Biol Chem 266, 13503-13506. (Pubitemid 21907377)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.21 , pp. 13503-13506
    • Sagara, Y.1    Inesi, G.2
  • 23
    • 0018401053 scopus 로고
    • 2+-dependent ATPase of the sarcoplasmic reticulum
    • 2+-dependent ATPase of the sarcoplasmic reticulum. Annu Rev Biochem 48, 275-292.
    • (1979) Annu Rev Biochem , vol.48 , pp. 275-292
    • De Meis, L.1    Vianna, A.L.2
  • 27
  • 28
    • 33745762313 scopus 로고    scopus 로고
    • Modulatory and catalytic modes of ATP binding by the calcium pump
    • DOI 10.1038/sj.emboj.7601135, PII 7601135
    • Jensen AM, Sorensen TL, Olesen C, Moller JV, &, Nissen P, (2006) Modulatory and catalytic modes of ATP binding by the calcium pump. EMBO J 25, 2305-2314. (Pubitemid 44012214)
    • (2006) EMBO Journal , vol.25 , Issue.11 , pp. 2305-2314
    • Jensen, A.-M.L.1    Sorensen, T.L.-M.2    Olesen, C.3    Moller, J.V.4    Nissen, P.5
  • 29
    • 0015523849 scopus 로고
    • Activation by adenosine triphosphate in the phosphorylation kinetics of sodium and potassium ion transport adenosine triphosphatase
    • Post RL, Hegyvary C, &, Kume S, (1972) Activation by adenosine triphosphate in the phosphorylation kinetics of sodium and potassium ion transport adenosine triphosphatase. J Biol Chem 247, 6530-6540.
    • (1972) J Biol Chem , vol.247 , pp. 6530-6540
    • Post, R.L.1    Hegyvary, C.2    Kume, S.3
  • 31
    • 0014150624 scopus 로고
    • ++-dependent ATPase of sarcoplasmic reticulum from skeletal muscle. I. Kinetic studies
    • ++-dependent ATPase of sarcoplasmic reticulum from skeletal muscle. I. Kinetic studies. J Biochem 62, 558-575.
    • (1967) J Biochem , vol.62 , pp. 558-575
    • Yamamoto, T.1    Tonomura, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.