메뉴 건너뛰기




Volumn 13, Issue 2, 2012, Pages 164-179

V-ATPase Subunit interactions: The long road to therapeutic targeting

Author keywords

Bone loss pathology; Drug discovery; High throughput screening; Membrane transport; Osteolysis; Osteoporosis; Protein interaction; Tumor metastasis; Vacuolar proton translocating ATPase; Vesicular proton pump

Indexed keywords

3,4 DIHYDROXY N' (2 HYDROXYBENZYLIDENE)BENZOHYDRAZIDE; ADENOSINE TRIPHOSPHATASE (MAGNESIUM); OSTEOCLAST DIFFERENTIATION FACTOR; PROTEIN INHIBITOR; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; UNCLASSIFIED DRUG;

EID: 84860813774     PISSN: 13892037     EISSN: 18755550     Source Type: Journal    
DOI: 10.2174/138920312800493179     Document Type: Review
Times cited : (11)

References (152)
  • 1
    • 77953255215 scopus 로고    scopus 로고
    • Regulation and isoform function of the V-ATPases
    • Toei, M.; Saum, R.; Forgac, M., Regulation and isoform function of the V-ATPases. Biochemistry, 2010, 49, (23), 4715-4723.
    • (2010) Biochemistry , vol.49 , Issue.23 , pp. 4715-4723
    • Toei, M.1    Saum, R.2    Forgac, M.3
  • 2
    • 79952201156 scopus 로고    scopus 로고
    • Vacuolar-type proton pump ATPases: Roles of infunit isoforms in physiology and pathology
    • Sun-Wada, G.-H.; Wada, Y., Vacuolar-type proton pump ATPases: Roles of infunit isoforms in physiology and pathology. Histol. Histopathol., 2010, 25, (12), 1611-1620.
    • (2010) Histol. Histopathol , vol.25 , Issue.12 , pp. 1611-1620
    • Sun-Wada, G.-H.1    Wada, Y.2
  • 3
    • 66449120515 scopus 로고    scopus 로고
    • The little we know on the structure and machinery of V-ATPase
    • Saroussi, S.; Nelson, N., The little we know on the structure and machinery of V-ATPase. J. Exp. Biol., 2009, 212, (11), 1604-1610.
    • (2009) J. Exp. Biol , vol.212 , Issue.11 , pp. 1604-1610
    • Saroussi, S.1    Nelson, N.2
  • 4
    • 47349120492 scopus 로고    scopus 로고
    • +-ATPase in vesicular trafficking: Targeting, regulation and function
    • +-ATPase in vesicular trafficking: Targeting, regulation and function. Curr. Opin. Cell Biol., 2008, 20, (4), 415-426.
    • (2008) Curr. Opin. Cell Biol , vol.20 , Issue.4 , pp. 415-426
    • Marshansky, V.1    Futai, M.2
  • 6
    • 33749428456 scopus 로고    scopus 로고
    • The emerging structure of vacuolar ATPases
    • Drory, O.; Nelson, N., The emerging structure of vacuolar ATPases. Physiology, 2006, 21, 317-325.
    • (2006) Physiology , vol.21 , pp. 317-325
    • Drory, O.1    Nelson, N.2
  • 7
    • 33644935227 scopus 로고    scopus 로고
    • + ATPase: Molecular structure and function, physiological roles and regulation
    • + ATPase: Molecular structure and function, physiological roles and regulation. J. Exp. Biol., 2006, 209, (4), 577-589.
    • (2006) J. Exp. Biol , vol.209 , Issue.4 , pp. 577-589
    • Beyenbach, K.W.1    Wieczorek, H.2
  • 9
    • 4944246136 scopus 로고    scopus 로고
    • +/ATP coupling ratio
    • +/ATP coupling ratio. FEBS Lett., 2004, 576, (1-2), 1-4.
    • (2004) FEBS Lett , vol.576 , Issue.1-2 , pp. 1-4
    • Cross, R.L.1    Müller, V.2
  • 10
    • 79960112075 scopus 로고    scopus 로고
    • Structural divergence of the rotary ATPases
    • Muench, S.P.; Trinick, J.; Harrison, M.A., Structural divergence of the rotary ATPases. Q. Rev. Biophys., 2011, 44(3), 311-356.
    • (2011) Q. Rev. Biophys , vol.44 , Issue.3 , pp. 311-356
    • Muench, S.P.1    Trinick, J.2    Harrison, M.A.3
  • 11
    • 58149158078 scopus 로고    scopus 로고
    • 0)
    • Grüber, G.; Marshansky, V., New insights into structure-function relationships between archeal ATP synthase (A1A0) and vacuolar type ATPase (V1V0). Bioessays, 2008, 30, (11-12), 1096-1109.
    • (2008) Bioessays , vol.30 , Issue.11-12 , pp. 1096-1109
    • Grüber, G.1    Marshansky, V.2
  • 14
    • 0033960457 scopus 로고    scopus 로고
    • +transport to rotary catalysis in F-type ATP synthases: Structure and organization of the transmembrane rotary motor
    • + transport to rotary catalysis in F-type ATP synthases: Structure and organization of the transmembrane rotary motor. J. Exp. Biol., 2000, 203, (1), 9-17.
    • (2000) J. Exp. Biol , vol.203 , Issue.1 , pp. 9-17
    • Fillingame, R.H.1    Jiang, W.2    Dmitriev, O.Y.3
  • 16
    • 77949896724 scopus 로고    scopus 로고
    • An extended nomenclature for mammalian V-ATPase infunit genes and splice variants
    • Miranda, K.C.; Karet, F.E.; Brown, D., An extended nomenclature for mammalian V-ATPase infunit genes and splice variants. PLoS ONE, 2010, 5, (3), e9531.
    • (2010) PLoS ONE , vol.5 , Issue.3
    • Miranda, K.C.1    Karet, F.E.2    Brown, D.3
  • 18
    • 0023818529 scopus 로고
    • +-translocating adenosine triphosphatase from vacuolar membranes of Saccharomyces cerevisiae. A study with 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole
    • +-translocating adenosine triphosphatase from vacuolar membranes of Saccharomyces cerevisiae. A study with 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole. J. Biol. Chem., 1988, 263, (1), 45-51.
    • (1988) J. Biol. Chem , vol.263 , Issue.1 , pp. 45-51
    • Uchida, E.1    Ohsumi, Y.2    Anraku, Y.3
  • 19
    • 0024279650 scopus 로고
    • CDNA sequence and homologies of the 57-kDa nucleotide-binding infunit of the vacuolar ATPase from Arabidopsis
    • Manolson, M.F.; Ouellette, B.F.F.; Filion, M.; Poole, R.J., cDNA sequence and homologies of the 57-kDa nucleotide-binding infunit of the vacuolar ATPase from Arabidopsis. J. Biol. Chem., 1988, 263, (34), 17987-17994.
    • (1988) J. Biol. Chem , vol.263 , Issue.34 , pp. 17987-17994
    • Manolson, M.F.1    Ouellette, B.F.F.2    Filion, M.3    Poole, R.J.4
  • 21
    • 0029946927 scopus 로고    scopus 로고
    • +)-ATPase from bovine brain clathrin-coated vesicles by modification of a rapidly exchangeable, noncatalytic nucleotide binding site on the B infunit
    • +)-ATPase from bovine brain clathrin-coated vesicles by modification of a rapidly exchangeable, noncatalytic nucleotide binding site on the B infunit. J. Biol. Chem., 1996, 271, (22), 12775-12782.
    • (1996) J. Biol. Chem , vol.271 , Issue.22 , pp. 12775-12782
    • Vasilyeva, E.1    Forgac, M.2
  • 22
    • 0024279271 scopus 로고
    • Isolation of genes encoding the Neurospora vacuolar ATPase. Analysis of vma-2 encoding the 57-kDa polypeptide and comparison to vma-1
    • Bowman, B.J.; Allen, R.; Wechser, M.A.; Bowman, E.J., Isolation of genes encoding the Neurospora vacuolar ATPase. Analysis of vma-2 encoding the 57-kDa polypeptide and comparison to vma-1. J. Biol. Chem., 1988, 263, (28), 14002-14007.
    • (1988) J. Biol. Chem , vol.263 , Issue.28 , pp. 14002-14007
    • Bowman, B.J.1    Allen, R.2    Wechser, M.A.3    Bowman, E.J.4
  • 24
    • 0033527743 scopus 로고    scopus 로고
    • Structure of the vacuolar ATPase by electron microscopy
    • Wilkens, S.; Vasilyeva, E.; Forgac, M., Structure of the vacuolar ATPase by electron microscopy. J. Biol. Chem., 1999, 274, (45), 31804-31810.
    • (1999) J. Biol. Chem , vol.274 , Issue.45 , pp. 31804-31810
    • Wilkens, S.1    Vasilyeva, E.2    Forgac, M.3
  • 25
    • 0034698103 scopus 로고    scopus 로고
    • +-ATPase plays a role in coupling of proton transport and ATP hydrolysis
    • +-ATPase plays a role in coupling of proton transport and ATP hydrolysis. J. Biol. Chem., 2000, 275, (29), 22075-22081.
    • (2000) J. Biol. Chem , vol.275 , Issue.29 , pp. 22075-22081
    • Xu, T.1    Forgac, M.2
  • 26
    • 0344443771 scopus 로고    scopus 로고
    • Expression and function of the mouse V-ATPase d infunit isoforms
    • Nishi, T.; Kawasaki-Nishi, S.; Forgac, M., Expression and function of the mouse V-ATPase d infunit isoforms. J. Biol. Chem., 2003, 278, (47), 46396-46402.
    • (2003) J. Biol. Chem , vol.278 , Issue.47 , pp. 46396-46402
    • Nishi, T.1    Kawasaki-Nishi, S.2    Forgac, M.3
  • 27
    • 0030934380 scopus 로고    scopus 로고
    • Direct observation of the rotation of F1-ATPase
    • Noji, H.; Yasuda, R.; Yoshida, M.; Kinosita Jr., K., Direct observation of the rotation of F1-ATPase. Nature, 1997, 386, (6622), 299-302.
    • (1997) Nature , vol.386 , Issue.6622 , pp. 299-302
    • Noji, H.1    Yasuda, R.2    Yoshida, M.3    Kinosita, K.4
  • 30
    • 53849140811 scopus 로고    scopus 로고
    • Structural organization of the V-ATPase and its implications for regulatory assembly and disassembly
    • Diepholz, M.; Börsch, M.; Böttcher, B., Structural organization of the V-ATPase and its implications for regulatory assembly and disassembly. Biochem. Soc. Trans., 2008, 36, (5), 1027-1031.
    • (2008) Biochem. Soc. Trans , vol.36 , Issue.5 , pp. 1027-1031
    • Diepholz, M.1    Börsch, M.2    Böttcher, B.3
  • 31
    • 0035745766 scopus 로고    scopus 로고
    • Structure-function relationships of A-, F- and V-ATPases
    • Grüber, G.; Wieczorek, H.; Harvey, W.R.; Müller, V., Structure-function relationships of A-, F- and V-ATPases. J. Exp. Biol, 2001, 204, (15), 2597-2605.
    • (2001) J. Exp. Biol , vol.204 , Issue.15 , pp. 2597-2605
    • Grüber, G.1    Wieczorek, H.2    Harvey, W.R.3    Müller, V.4
  • 32
    • 60149087436 scopus 로고    scopus 로고
    • Cryo-electron microscopy of the vacuolar ATPase motor reveals its mechanical and regulatory complexity
    • Muench, S.P.; Huss, M.; Song, C.F.; Phillips, C; Wieczorek, H.; Trinick, J.; Harrison, M.A., Cryo-electron microscopy of the vacuolar ATPase motor reveals its mechanical and regulatory complexity. J. Mol. Biol., 2009, 386, (4), 989-999.
    • (2009) J. Mol. Biol , vol.386 , Issue.4 , pp. 989-999
    • Muench, S.P.1    Huss, M.2    Song, C.F.3    Phillips, C.4    Wieczorek, H.5    Trinick, J.6    Harrison, M.A.7
  • 33
    • 76549094484 scopus 로고    scopus 로고
    • o motor
    • Lau, W.C.Y.; Rubinstein, J.L., Structure of intact Thermus thermophilus V-ATPase by cryo-EM reveals organization of the membrane-bound Vo motor. Proc. Natl. Acad. Sci. U. S. A., 2010, 107, (4), 1367-1372.
    • (2010) Proc. Natl. Acad. Sci. U. S. A , vol.107 , Issue.4 , pp. 1367-1372
    • Lau, W.C.Y.1    Rubinstein, J.L.2
  • 34
    • 0142149158 scopus 로고    scopus 로고
    • Interacting helical surfaces of the transmembrane segments of infunits a and c' of the yeast V-ATPase defined by disulfide-mediated cross-linking
    • Kawasaki-Nishi, S.; Nishi, T.; Forgac, M., Interacting helical surfaces of the transmembrane segments of infunits a and c' of the yeast V-ATPase defined by disulfide-mediated cross-linking. J. Biol. Chem., 2003, 278, (43), 41908-41913.
    • (2003) J. Biol. Chem , vol.278 , Issue.43 , pp. 41908-41913
    • Kawasaki-Nishi, S.1    Nishi, T.2    Forgac, M.3
  • 35
    • 7244248726 scopus 로고    scopus 로고
    • TM2 but not TM4 of infunit c interacts with TM7 of infunit a of the yeast V-ATPase as defined by disulfide-mediated cross-linking
    • Wang, Y.; Inoue, T.; Forgac, M., TM2 but not TM4 of infunit c interacts with TM7 of infunit a of the yeast V-ATPase as defined by disulfide-mediated cross-linking. J. Biol. Chem., 2004, 279, (43), 44628-44638.
    • (2004) J. Biol. Chem , vol.279 , Issue.43 , pp. 44628-44638
    • Wang, Y.1    Inoue, T.2    Forgac, M.3
  • 36
    • 0029807877 scopus 로고    scopus 로고
    • 3 oligomer fixed by OSCP-b stator via the pDELSEED sequence
    • Kagawa, Y.; Hamamoto, T., The energy transmission in ATP synthase: From the rotor to the a3(33 oligomer fixed by OSCP-b stator via the pDELSEED sequence. J. Bioenerg. Biomembr., 1996, 28, (5), 421-431.
    • (1996) J. Bioenerg. Biomembr , vol.28 , Issue.5 , pp. 421-431
    • Kagawa, Y.1    Hamamoto, T.2
  • 37
    • 35448946098 scopus 로고    scopus 로고
    • Vacuolar ATPases: Rotary proton pumps in physiology and pathophysiology
    • Forgac, M., Vacuolar ATPases: Rotary proton pumps in physiology and pathophysiology. Nat. Rev. Mol. Cell Biol, 2007, 8, (11), 917-929.
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , Issue.11 , pp. 917-929
    • Forgac, M.1
  • 39
    • 0034685544 scopus 로고    scopus 로고
    • 0 sector of the yeast V-ATPase, interacts directly with the Vma1p and Vma13p infunits of the V1 sector
    • Landolt-Marticorena, C; Williams, K.M.; Correa, J.; Chen, W.; Manolson, M.F., Evidence that the NH2 terminus of Vph1p, an integral infunit of the V0 sector of the yeast V-ATPase, interacts directly with the Vma1p and Vma13p infunits of the V1 sector. J. Biol. Chem., 2000, 275, (20), 15449-15457.
    • (2000) J. Biol. Chem , vol.275 , Issue.20 , pp. 15449-15457
    • Landolt-Marticorena, C.1    Williams, K.M.2    Correa, J.3    Chen, W.4    Manolson, M.F.5
  • 40
    • 0033543582 scopus 로고    scopus 로고
    • Infstrate- and inhibitor-induced conformational changes in the yeast V-ATPase provide evidence for communication between the catalytic and proton-translocating sectors
    • Landolt-Marticorena, C; Kahr, W.H.; Zawarinski, P.; Correa, J.; Manolson, M.F., Infstrate- and inhibitor-induced conformational changes in the yeast V-ATPase provide evidence for communication between the catalytic and proton-translocating sectors. J. Biol. Chem., 1999, 274, (37), 26057-26064.
    • (1999) J. Biol. Chem , vol.274 , Issue.37 , pp. 26057-26064
    • Landolt-Marticorena, C.1    Kahr, W.H.2    Zawarinski, P.3    Correa, J.4    Manolson, M.F.5
  • 41
    • 0035947711 scopus 로고    scopus 로고
    • Yeast V-ATPase complexes containing different isoforms of the 100-kDa a-infunit differ in coupling efficiency and in vivo dissociation
    • Kawasaki-Nishi, S.; Nishi, T.; Forgac, M., Yeast V-ATPase complexes containing different isoforms of the 100-kDa a-infunit differ in coupling efficiency and in vivo dissociation. J. Biol. Chem., 2001, 276, (21), 17941-17948.
    • (2001) J. Biol. Chem , vol.276 , Issue.21 , pp. 17941-17948
    • Kawasaki-Nishi, S.1    Nishi, T.2    Forgac, M.3
  • 42
    • 0035940474 scopus 로고    scopus 로고
    • Arg-735 of the 100-kDa infunit a of the yeast V-ATPase is essential for proton translocation
    • Kawasaki-Nishi, S.; Nishi, T.; Forgac, M., Arg-735 of the 100-kDa infunit a of the yeast V-ATPase is essential for proton translocation. Proc. Natl. Acad. Sci. U. S. A., 2001, 98, (22), 12397-12402.
    • (2001) Proc. Natl. Acad. Sci. U. S. A , vol.98 , Issue.22 , pp. 12397-12402
    • Kawasaki-Nishi, S.1    Nishi, T.2    Forgac, M.3
  • 43
    • 0035947648 scopus 로고    scopus 로고
    • Intra-endosomal pH-sensitive recruitment of the Arf-nucleotide exchange factor ARNO and Arf6 from cytoplasm to proximal tubule endosomes
    • Maranda, B.; Brown, D.; Bourgoin, S.; Casanova, J.E.; Vinay, P.; Ausiello, D.A.; Marshansky, V., Intra-endosomal pH-sensitive recruitment of the Arf-nucleotide exchange factor ARNO and Arf6 from cytoplasm to proximal tubule endosomes. J. Biol Chem., 2001, 276, (21), 18540-18550.
    • (2001) J. Biol Chem , vol.276 , Issue.21 , pp. 18540-18550
    • Maranda, B.1    Brown, D.2    Bourgoin, S.3    Casanova, J.E.4    Vinay, P.5    Ausiello, D.A.6    Marshansky, V.7
  • 44
    • 0024977948 scopus 로고
    • Cold inactivation of vacuolar proton-ATPases
    • Moriyama, Y.; Nelson, N., Cold inactivation of vacuolar proton-ATPases. J. Biol Chem., 1989, 264, (6), 3577-3582.
    • (1989) J. Biol Chem , vol.264 , Issue.6 , pp. 3577-3582
    • Moriyama, Y.1    Nelson, N.2
  • 45
    • 0035941232 scopus 로고    scopus 로고
    • Three-dimensional structure of the vacuolar ATPase proton channel by electron microscopy
    • Wilkens, S.; Forgac, M., Three-dimensional structure of the vacuolar ATPase proton channel by electron microscopy. J. Biol Chem., 2001, 276, (47), 44064-44068.
    • (2001) J. Biol Chem , vol.276 , Issue.47 , pp. 44064-44068
    • Wilkens, S.1    Forgac, M.2
  • 47
    • 0035861664 scopus 로고    scopus 로고
    • The amino-terminal domain of the vacuolar proton-translocating ATPase a infunit controls targeting and in vivo dissociation, and the carboxyl-terminal domain affects coupling of proton transport and ATP hydrolysis
    • Kawasaki-Nishi, S.; Bowers, K.; Nishi, T.; Forgac, M.; Stevens, T.H., The amino-terminal domain of the vacuolar proton-translocating ATPase a infunit controls targeting and in vivo dissociation, and the carboxyl-terminal domain affects coupling of proton transport and ATP hydrolysis. J. Biol. Chem., 2001, 276, (50), 47411-47420.
    • (2001) J. Biol. Chem , vol.276 , Issue.50 , pp. 47411-47420
    • Kawasaki-Nishi, S.1    Bowers, K.2    Nishi, T.3    Forgac, M.4    Stevens, T.H.5
  • 48
    • 1542677106 scopus 로고    scopus 로고
    • The a3 isoform of the 100-kDa V-ATPase infunit is highly but differentially expressed in large (≥10 nuclei) and small (≤5 nuclei) osteoclasts
    • Manolson, M.F.; Yu, H.; Chen, W.; Yao, Y.; Li, K.; Lees, R.L.; Heersche, J.N.M., The a3 isoform of the 100-kDa V-ATPase infunit is highly but differentially expressed in large (≥10 nuclei) and small (≤5 nuclei) osteoclasts. J. Biol. Chem., 2003, 278, (49), 49271-49278.
    • (2003) J. Biol. Chem , vol.278 , Issue.49 , pp. 49271-49278
    • Manolson, M.F.1    Yu, H.2    Chen, W.3    Yao, Y.4    Li, K.5    Lees, R.L.6    Heersche, J.N.M.7
  • 50
    • 65949119983 scopus 로고    scopus 로고
    • Atp6v0d2 Is an essential component of the osteoclast-specific proton pump that mediates extracellular acidification in bone resorption
    • Wu, H.; Xu, G.; Li, Y.-P., Atp6v0d2 Is an essential component of the osteoclast-specific proton pump that mediates extracellular acidification in bone resorption. J. Bone Miner. Res., 2009, 24, (5), 871-885.
    • (2009) J. Bone Miner. Res , vol.24 , Issue.5 , pp. 871-885
    • Wu, H.1    Xu, G.2    Li, Y.-P.3
  • 51
    • 23044497763 scopus 로고    scopus 로고
    • 0 Domain
    • Inoue, T.; Forgac, M., Cysteine-mediated cross-linking indicates that infunit C of the V-ATPase is in close proximity to infunits E and G of the V1 domain and infunit a of the V0 domain. J. Biol. Chem., 2005, 280, (30), 27896-27903.
    • (2005) J. Biol. Chem , vol.280 , Issue.30 , pp. 27896-27903
    • Inoue, T.1    Forgac, M.2
  • 52
    • 50349103459 scopus 로고    scopus 로고
    • Function and infunit interactions of the N-terminal domain of infunit a (Vph1p) of the yeast V-ATPase
    • Qi, J.; Forgac, M., Function and infunit interactions of the N-terminal domain of infunit a (Vph1p) of the yeast V-ATPase. J. Biol. Chem., 2008, 283, (28), 19274-19282.
    • (2008) J. Biol. Chem , vol.283 , Issue.28 , pp. 19274-19282
    • Qi, J.1    Forgac, M.2
  • 54
    • 77953807182 scopus 로고    scopus 로고
    • Specific motifs of the V-ATPase a2-infunit isoform interact with catalytic and regulatory domains of ARNO
    • Merkulova, M.; Bakulina, A.; Thaker, Y.R.; Grüber, G.; Marshansky, V., Specific motifs of the V-ATPase a2-infunit isoform interact with catalytic and regulatory domains of ARNO. Biochim. Biophys. Acta, 2010, 1797, (8), 1398-1409.
    • (2010) Biochim. Biophys. Acta , vol.1797 , Issue.8 , pp. 1398-1409
    • Merkulova, M.1    Bakulina, A.2    Thaker, Y.R.3    Grüber, G.4    Marshansky, V.5
  • 57
    • 34247872975 scopus 로고    scopus 로고
    • Genes required for osmoregulation and apical secretion in Caenorhabditis elegans
    • Liégeois, S.; Benedetto, A.; Michaux, G.; Belliard, G.; Labouesse, M., Genes required for osmoregulation and apical secretion in Caenorhabditis elegans. Genetics, 2007, 175, 709-724.
    • (2007) Genetics , vol.175 , pp. 709-724
    • Liégeois, S.1    Benedetto, A.2    Michaux, G.3    Belliard, G.4    Labouesse, M.5
  • 61
    • 3542998744 scopus 로고    scopus 로고
    • Diverse and essential roles of mammalian vacuolar-type proton pump ATPase: Toward the physiological understanding of inside acidic compartments
    • Sun-Wada, G.-H.; Wada, Y.; Futai, M., Diverse and essential roles of mammalian vacuolar-type proton pump ATPase: Toward the physiological understanding of inside acidic compartments. Biochim. Biophys. Acta, 2004, 1658, (1-2), 106-114.
    • (2004) Biochim. Biophys. Acta , vol.1658 , Issue.1-2 , pp. 106-114
    • Sun-Wada, G.-H.1    Wada, Y.2    Futai, M.3
  • 63
    • 42149139435 scopus 로고    scopus 로고
    • Intracellular pH homeostasis and serotonin-induced pH changes in Calliphora salivary glands: The contribution of V-ATPase and carbonic anhydrase
    • Schewe, B.; Schmälzlin, E.; Walz, B., Intracellular pH homeostasis and serotonin-induced pH changes in Calliphora salivary glands: The contribution of V-ATPase and carbonic anhydrase. J. Exp. Biol, 2008, 211, (5), 805-815.
    • (2008) J. Exp. Biol , vol.211 , Issue.5 , pp. 805-815
    • Schewe, B.1    Schmälzlin, E.2    Walz, B.3
  • 64
    • 66449088593 scopus 로고    scopus 로고
    • Regulation of the V-ATPase in kidney epithelial cells: Dual role in acid-base homeostasis and vesicle trafficking
    • Brown, D.; Paunescu, T.G.; Breton, S.; Marshansky, V., Regulation of the V-ATPase in kidney epithelial cells: Dual role in acid-base homeostasis and vesicle trafficking. J. Exp. Biol, 2009, 212, (11), 1762-1772.
    • (2009) J. Exp. Biol , vol.212 , Issue.11 , pp. 1762-1772
    • Brown, D.1    Paunescu, T.G.2    Breton, S.3    Marshansky, V.4
  • 65
    • 67650236818 scopus 로고    scopus 로고
    • Function of a infunit isoforms of the V-ATPase in pH homeostasis and in vitro invasion of MDA-MB231 human breast cancer cells
    • Hinton, A.; Sennoune, S.R.; Bond, S.; Fang, M.; Reuveni, M.; Sahagian, G.G.; Jay, D.; Martinez-Zaguilan, R.; Forgac, M., Function of a infunit isoforms of the V-ATPase in pH homeostasis and in vitro invasion of MDA-MB231 human breast cancer cells. J. Biol. Chem., 2009, 284, (24), 16400-16408.
    • (2009) J. Biol. Chem , vol.284 , Issue.24 , pp. 16400-16408
    • Hinton, A.1    Sennoune, S.R.2    Bond, S.3    Fang, M.4    Reuveni, M.5    Sahagian, G.G.6    Jay, D.7    Martinez-Zaguilan, R.8    Forgac, M.9
  • 66
    • 0030938766 scopus 로고    scopus 로고
    • Role of V-ATPase-rich cells in acidification of the male reproductive tract
    • Brown, D.; Smith, P.J.S.; Breton, S., Role of V-ATPase-rich cells in acidification of the male reproductive tract. J. Exp. Biol, 1997, 200, (2), 257-262.
    • (1997) J. Exp. Biol , vol.200 , Issue.2 , pp. 257-262
    • Brown, D.1    Smith, P.J.S.2    Breton, S.3
  • 68
    • 0029125907 scopus 로고
    • Characterization of the osteoclast vacuolar H(+)-ATPase B-infunit
    • Bartkiewicz, M.; Hernando, N.; Reddy, S.V.; Roodman, G.D.R.; Baron, R., Characterization of the osteoclast vacuolar H(+)-ATPase B-infunit. Gene, 1995, 160, (2), 157-164.
    • (1995) Gene , vol.160 , Issue.2 , pp. 157-164
    • Bartkiewicz, M.1    Hernando, N.2    Reddy, S.V.3    Roodman, G.D.R.4    Baron, R.5
  • 70
    • 0034629168 scopus 로고    scopus 로고
    • Molecular cloning and expression of three isoforms of the 100-kDa a infunit of the mouse vacuolar proton-translocating ATPase
    • Nishi, T.; Forgac, M., Molecular cloning and expression of three isoforms of the 100-kDa a infunit of the mouse vacuolar proton-translocating ATPase. J. Biol. Chem., 2000, 275, (10), 6824-6830.
    • (2000) J. Biol. Chem , vol.275 , Issue.10 , pp. 6824-6830
    • Nishi, T.1    Forgac, M.2
  • 71
    • 0034708665 scopus 로고    scopus 로고
    • +-ATPase: Preferential expression of the a 3 isoform during osteoclast differentiation
    • +-ATPase: Preferential expression of the a 3 isoform during osteoclast differentiation. J. Biol. Chem., 2000, 275, (12), 8760-8765.
    • (2000) J. Biol. Chem , vol.275 , Issue.12 , pp. 8760-8765
    • Toyomura, T.1    Oka, T.2    Yamaguchi, C.3    Wada, Y.4    Futai, M.5
  • 73
    • 33751511196 scopus 로고    scopus 로고
    • The a 3 isoform of V-ATPase regulates insulin secretion from pancreatic 3-cells
    • Sun-Wada, G.-H.; Toyomura, T.; Murata, Y.; Yamamoto, A.; Futai, M.; Wada, Y., The a 3 isoform of V-ATPase regulates insulin secretion from pancreatic 3-cells. J. Cell Sci., 2006, 119, (21), 4531-4540.
    • (2006) J. Cell Sci , vol.119 , Issue.21 , pp. 4531-4540
    • Sun-Wada, G.-H.1    Toyomura, T.2    Murata, Y.3    Yamamoto, A.4    Futai, M.5    Wada, Y.6
  • 75
    • 45149125392 scopus 로고    scopus 로고
    • 0 domain infunits and efficient osteoclastic bone resorption
    • Feng, H.; Cheng, T.; Pavlos, N.J.; Yip, K.H.M.; Carrello, A.; Seeber, R.; Eidne, K.; Zheng, M.H.; Xu, J., Cytoplasmic terminus of vacuolar type proton pump accessory infunit Ac45 is required for proper interaction with V0 domain infunits and efficient osteoclastic bone resorption. J. Biol. Chem., 2008, 283, (19), 13194-13204.
    • (2008) J. Biol. Chem , vol.283 , Issue.19 , pp. 13194-13204
    • Feng, H.1    Cheng, T.2    Pavlos, N.J.3    Yip, K.H.M.4    Carrello, A.5    Seeber, R.6    Eidne, K.7    Zheng, M.H.8    Xu, J.9
  • 79
    • 0037265871 scopus 로고    scopus 로고
    • Novel mutations in the TCIRG1 gene encoding the a3 infunit of the vacuolar proton pump in patients affected by infantile malignant osteopetrosis
    • Scimeca, J.-C; Quincey, D.; Parrinello, H.; Romatet, D.; Grosgeorge, J.; Gaudray, P.; Philip, N.; Fischer, A.; Carle, G.F., Novel mutations in the TCIRG1 gene encoding the a3 infunit of the vacuolar proton pump in patients affected by infantile malignant osteopetrosis. Hum. Mutat., 2003, 21, (2), 151-157.
    • (2003) Hum. Mutat , vol.21 , Issue.2 , pp. 151-157
    • Scimeca, J.-C.1    Quincey, D.2    Parrinello, H.3    Romatet, D.4    Grosgeorge, J.5    Gaudray, P.6    Philip, N.7    Fischer, A.8    Carle, G.F.9
  • 81
    • 0032748995 scopus 로고    scopus 로고
    • Atp6i-deficient mice exhibit severe osteopetrosis due to loss of osteoclast-mediated extracellular acidification
    • Li, Y.-P.; Chen, W.; Liang, Y.; Li, E.; Stashenko, P., Atp6i-deficient mice exhibit severe osteopetrosis due to loss of osteoclast-mediated extracellular acidification. Nat. Genet, 1999, 23, 447-451.
    • (1999) Nat. Genet , vol.23 , pp. 447-451
    • Li, Y.-P.1    Chen, W.2    Liang, Y.3    Li, E.4    Stashenko, P.5
  • 82
    • 18344407785 scopus 로고    scopus 로고
    • The gene encoding the mouse homologue of the human osteoclast-specific 116-kDa V-ATPase infunit bears a deletion in osteosclerotic (oc/oc) mutants
    • Scimeca, J.-C.; Franchi, A.; Trojani, C.; Parrinello, H.; Grosgeorge, J.; Robert, C.; Jaillon, O.; Poirier, C.; Gaudray, P.; Carle, G.F., The gene encoding the mouse homologue of the human osteoclast-specific 116-kDa V-ATPase infunit bears a deletion in osteosclerotic (oc/oc) mutants. Bone, 2000, 26, (3), 207-213.
    • (2000) Bone , vol.26 , Issue.3 , pp. 207-213
    • Scimeca, J.-C.1    Franchi, A.2    Trojani, C.3    Parrinello, H.4    Grosgeorge, J.5    Robert, C.6    Jaillon, O.7    Poirier, C.8    Gaudray, P.9    Carle, G.F.10
  • 83
    • 33749542773 scopus 로고    scopus 로고
    • Endomembrane proton pumps: Connecting membrane and vesicle transport
    • Schumacher, K., Endomembrane proton pumps: connecting membrane and vesicle transport. Curr. Opin. Plant Biol., 2006, 9, (6), 595-600.
    • (2006) Curr. Opin. Plant Biol , vol.9 , Issue.6 , pp. 595-600
    • Schumacher, K.1
  • 84
    • 70350374082 scopus 로고    scopus 로고
    • +-ATPase prevent segregation of lysosomal- and secretory-pathway proteins
    • +-ATPase prevent segregation of lysosomal- and secretory-pathway proteins. J. Cell Sci., 2009, 122, (19), 3542-3553.
    • (2009) J. Cell Sci , vol.122 , Issue.19 , pp. 3542-3553
    • Sabota, J.A.1    Bäck, N.2    Eipper, B.A.3    Mains, R.E.4
  • 85
    • 0347382415 scopus 로고    scopus 로고
    • +ATPase a infunit to nerve terminals where it associates with both synaptic vesicles and the presynaptic plasma membrane
    • +ATPase a infunit to nerve terminals where it associates with both synaptic vesicles and the presynaptic plasma membrane. J. Cell Sci., 2003, 116, (23), 4751-4762.
    • (2003) J. Cell Sci , vol.116 , Issue.23 , pp. 4751-4762
    • Morel, N.1    Dedieu, J.-C.2    Philippe, J.-M.3
  • 86
    • 0035252348 scopus 로고    scopus 로고
    • Trans-complex formation by proteolipid channels in the terminal phase of membrane fusion
    • Peters, C.; Bayer, M.J.; Bühler, S.; Andersen, J.S.; Mann, M.; Mayer, A., Trans-complex formation by proteolipid channels in the terminal phase of membrane fusion. Nature, 2001, 409, (6820), 581-588.
    • (2001) Nature , vol.409 , Issue.6820 , pp. 581-588
    • Peters, C.1    Bayer, M.J.2    Bühler, S.3    Andersen, J.S.4    Mann, M.5    Mayer, A.6
  • 88
    • 0036197399 scopus 로고    scopus 로고
    • Genetic diseases of acid-base transporters
    • Alper, S.L., Genetic diseases of acid-base transporters. Annu. Rev. Physiol., 2002, 64, 899-923.
    • (2002) Annu. Rev. Physiol , vol.64 , pp. 899-923
    • Alper, S.L.1
  • 92
    • 0027373117 scopus 로고
    • Vacuolar-type H(+)-ATPases are functionally expressed in plasma membranes of human tumor cells
    • Martinez-Zaguilan, R.; Lynch, R.M.; Martinez, G.M.; Gillies, R.J., Vacuolar-type H(+)-ATPases are functionally expressed in plasma membranes of human tumor cells. Am. J. Physiol. Cell Physiol., 1993, 265, (4), C1015-C1029.
    • (1993) Am. J. Physiol. Cell Physiol , vol.265 , Issue.4
    • Martinez-Zaguilan, R.1    Lynch, R.M.2    Martinez, G.M.3    Gillies, R.J.4
  • 94
    • 33947513226 scopus 로고    scopus 로고
    • Structure and function of V-ATPases in osteoclasts: Potential therapeutic targets for the treatment of osteolysis
    • Xu, J.; Cheng, T.; Feng, H.T.; Pavlos, N.J.; Zheng, M.H., Structure and function of V-ATPases in osteoclasts: Potential therapeutic targets for the treatment of osteolysis. Histol. Histopathol., 2007, 22, (4), 443-454.
    • (2007) Histol. Histopathol , vol.22 , Issue.4 , pp. 443-454
    • Xu, J.1    Cheng, T.2    Feng, H.T.3    Pavlos, N.J.4    Zheng, M.H.5
  • 95
    • 77956977479 scopus 로고    scopus 로고
    • The vacuolar ATPase in bone cells: A potential therapeutic target in osteoporosis
    • Yuan, F.-L.; Li, X.; Lu, W.-G.; Li, C.-W.; Li, J.-P.; Wang, Y., The vacuolar ATPase in bone cells: A potential therapeutic target in osteoporosis. Mol. Biol. Rep., 2010, 37, (7), 3561-3566.
    • (2010) Mol. Biol. Rep , vol.37 , Issue.7 , pp. 3561-3566
    • Yuan, F.-L.1    Li, X.2    Lu, W.-G.3    Li, C.-W.4    Li, J.-P.5    Wang, Y.6
  • 96
    • 77951951499 scopus 로고    scopus 로고
    • Proton pump inhibitors as anti vacuolar-ATPases drug: A novel anticancer strategy
    • Spugnini, E.P.; Citro, G.; Fais, S., Proton pump inhibitors as anti vacuolar-ATPases drug: A novel anticancer strategy. J. Exp. Clin. Cancer Res., 2010, 29, 44.
    • (2010) J. Exp. Clin. Cancer Res , vol.29 , pp. 44
    • Spugnini, E.P.1    Citro, G.2    Fais, S.3
  • 97
    • 36349001899 scopus 로고    scopus 로고
    • +-ATPases as a new strategy against cancer
    • +-ATPases as a new strategy against cancer. Cancer Res., 2007, 67, (22), 10627-10630.
    • (2007) Cancer Res , vol.67 , Issue.22 , pp. 10627-10630
    • Fais, S.1    de Milito, A.2    You, H.3    Qin, W.4
  • 98
    • 0017834718 scopus 로고
    • Bioenergetic process in chromaffin granules: A new perspective on some old problems
    • Njus, D.; Radda, G.K., Bioenergetic process in chromaffin granules: A new perspective on some old problems. Biochim. Biophys. Acta, 1978, 463, (3-4), 219-244.
    • (1978) Biochim. Biophys. Acta , vol.463 , Issue.3-4 , pp. 219-244
    • Njus, D.1    Radda, G.K.2
  • 99
    • 0019834321 scopus 로고
    • +-translocating adenosine triphosphatase in vacuolar membranes of Saccharomyces cerevisiae
    • +-translocating adenosine triphosphatase in vacuolar membranes of Saccharomyces cerevisiae. J. Biol. Chem., 1981, 256, (21), 10859-10863.
    • (1981) J. Biol. Chem , vol.256 , Issue.21 , pp. 10859-10863
    • Kakinuma, Y.1    Ohsumi, Y.2    Anraku, Y.3
  • 100
    • 0019411588 scopus 로고
    • Active transport of basic amino acids driven by a proton motive force in vacuolar membrane vesicles of Saccharomyces cerevisiae
    • Ohsumi, Y.; Anraku, Y., Active transport of basic amino acids driven by a proton motive force in vacuolar membrane vesicles of Saccharomyces cerevisiae. J. Biol. Chem., 1981, 256, (5), 2079-2082.
    • (1981) J. Biol. Chem , vol.256 , Issue.5 , pp. 2079-2082
    • Ohsumi, Y.1    Anraku, Y.2
  • 101
    • 0000600604 scopus 로고
    • +-translocating ATPases: Advances using membrane vesicles
    • +-translocating ATPases: Advances using membrane vesicles. Annu. Rev. Plant Physiol, 1985, 36, 175-208.
    • (1985) Annu. Rev. Plant Physiol , vol.36 , pp. 175-208
    • Sze, H.1
  • 102
    • 0021959611 scopus 로고
    • 2+-adenosine triphosphatase from vacuolar membranes of Saccharomyces cerevisiae
    • 2+-adenosine triphosphatase from vacuolar membranes of Saccharomyces cerevisiae. J. Biol. Chem., 1985, 260, (2), 1090-1095.
    • (1985) J. Biol. Chem , vol.260 , Issue.2 , pp. 1090-1095
    • Uchida, E.1    Ohsumi, Y.2    Anraku, Y.3
  • 103
    • 0022878225 scopus 로고
    • +-ATPases from mithochondria, plasma membranes, and vacuoles of fungal cells
    • +-ATPases from mithochondria, plasma membranes, and vacuoles of fungal cells. J. Membr. Biol., 1986, 94, 83-97.
    • (1986) J. Membr. Biol , vol.94 , pp. 83-97
    • Bowman, B.J.1    Bowman, E.J.2
  • 104
    • 0022559211 scopus 로고
    • + pumping into intracellular organelles
    • + pumping into intracellular organelles. Annu. Rev. Physiol., 1986, 48, 403-413.
    • (1986) Annu. Rev. Physiol , vol.48 , pp. 403-413
    • Rudnick, G.1
  • 105
    • 0022978965 scopus 로고
    • Isolation and reconstitution of the clathrin-coated vesicle proton translocating complex
    • Xie, X.-S.; Stone, D.K., Isolation and reconstitution of the clathrin-coated vesicle proton translocating complex. J. Biol. Chem., 1986, 261, (6), 2492-2495.
    • (1986) J. Biol. Chem , vol.261 , Issue.6 , pp. 2492-2495
    • Xie, X.-S.1    Stone, D.K.2
  • 106
    • 0023645189 scopus 로고
    • The purified ATPase from chromaffin granule membranes is an anion-dependent proton pump
    • Moriyama, Y.; Nelson, N., The purified ATPase from chromaffin granule membranes is an anion-dependent proton pump. J. Biol. Chem., 1987, 262, (19), 9175-9180.
    • (1987) J. Biol. Chem , vol.262 , Issue.19 , pp. 9175-9180
    • Moriyama, Y.1    Nelson, N.2
  • 108
    • 0022555867 scopus 로고
    • Acidification of the endocytic and exocytic pathways
    • Mellman, I.; Fuchs, R.; Helenius, A., Acidification of the endocytic and exocytic pathways. Annu. Rev. Biochem., 1986, 55, 663-700.
    • (1986) Annu. Rev. Biochem , vol.55 , pp. 663-700
    • Mellman, I.1    Fuchs, R.2    Helenius, A.3
  • 112
    • 0024297266 scopus 로고
    • oF1 type ATP synthase from the acidothermophilic archaebacterium, Sulfolobus acidocaldarius
    • Denda, K.; Konishi, J.; Oshima, T; Date, T.; Yoshida, M., Molecular cloning of the (3-infunit of a possible non-FoF1 type ATP synthase from the acidothermophilic archaebacterium, Sulfolobus acidocaldarius. J. Biol. Chem., 1988, 263, (33), 17251-17254.
    • (1988) J. Biol. Chem , vol.263 , Issue.33 , pp. 17251-17254
    • Denda, K.1    Konishi, J.2    Oshima, T.3    Date, T.4    Yoshida, M.5
  • 114
    • 33646830005 scopus 로고
    • Ion motive ATPases. I. Ubiquity, properties, and significance to cell function
    • Pedersen, P.L.; Carafoli, E., Ion motive ATPases. I. Ubiquity, properties, and significance to cell function. Trends Biochem. Sci., 1987, 12, 146-150.
    • (1987) Trends Biochem. Sci , vol.12 , pp. 146-150
    • Pedersen, P.L.1    Carafoli, E.2
  • 115
    • 0342713241 scopus 로고
    • Head and stalk structures of soybean vacuolar membranes
    • Morré, D.J.; Liedtke, C; Brightman, A.O.; Scherer, G.F.E., Head and stalk structures of soybean vacuolar membranes. Planta, 1991, 184, (3), 343-349.
    • (1991) Planta , vol.184 , Issue.3 , pp. 343-349
    • Morré, D.J.1    Liedtke, C.2    Brightman, A.O.3    Scherer, G.F.E.4
  • 116
    • 0344465252 scopus 로고
    • Assay of vacuolar pH in yeast and identification of acidification-defective mutants
    • Preston, R.A.; Murphy, R.F.; Jones, E.W., Assay of vacuolar pH in yeast and identification of acidification-defective mutants. Proc. Natl. Acad. Sci. U. S. A., 1989, 86, (18), 7027-7031.
    • (1989) Proc. Natl. Acad. Sci. U. S. A , vol.86 , Issue.18 , pp. 7027-7031
    • Preston, R.A.1    Murphy, R.F.2    Jones, E.W.3
  • 118
    • 0025059465 scopus 로고
    • Cloning of a cDNA for a T cell produced molecule with a putative immune regulatory cycle
    • Lee, C; Ghoshal, K.; Beaman, K.D., Cloning of a cDNA for a T cell produced molecule with a putative immune regulatory cycle. Mol. Immunol., 1990, 27, (11), 1137-1144.
    • (1990) Mol. Immunol , vol.27 , Issue.11 , pp. 1137-1144
    • Lee, C.1    Ghoshal, K.2    Beaman, K.D.3
  • 119
    • 0026948003 scopus 로고
    • Evidence for a conserved 95-120 kDa infunit associated with and essential for activity of V-ATPases
    • Manolson, M.F.; Proteau, D.; Jones, E.W., Evidence for a conserved 95-120 kDa infunit associated with and essential for activity of V-ATPases. J. Exp. Biol., 1992, 172, (105), 105-112.
    • (1992) J. Exp. Biol , vol.172 , Issue.105 , pp. 105-112
    • Manolson, M.F.1    Proteau, D.2    Jones, E.W.3
  • 120
    • 0030048278 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a putative novel human osteoclast-specific 116-kDa vacuolar proton pump infunit
    • Li, Y.-P.; Chen, W.; Stashenko, P., Molecular cloning and characterization of a putative novel human osteoclast-specific 116-kDa vacuolar proton pump infunit. Biochem. Biophys. Res. Commun., 1996, 218, (3), 813-821.
    • (1996) Biochem. Biophys. Res. Commun , vol.218 , Issue.3 , pp. 813-821
    • Li, Y.-P.1    Chen, W.2    Stashenko, P.3
  • 122
    • 31944432438 scopus 로고    scopus 로고
    • Seventeen a-infunit isoforms of Paramecium V-ATPase provide high specialization in location and function
    • Wassmer, T.; Kissmehl, R.; Cohen, J.; Plattner, H., Seventeen a-infunit isoforms of Paramecium V-ATPase provide high specialization in location and function. Mol. Biol. Cell, 2006, 17, (2), 917-930.
    • (2006) Mol. Biol. Cell , vol.17 , Issue.2 , pp. 917-930
    • Wassmer, T.1    Kissmehl, R.2    Cohen, J.3    Plattner, H.4
  • 123
    • 0024971242 scopus 로고
    • The vacuolar ATPase of Neurospora crassa contains an F1-like structure
    • Bowman, B.J.; Dschida, W.J.; Harris, T.; Bowman, E.J., The vacuolar ATPase of Neurospora crassa contains an F1-like structure. J. Biol. Chem., 1989, 264, (26), 15606-15612.
    • (1989) J. Biol. Chem , vol.264 , Issue.26 , pp. 15606-15612
    • Bowman, B.J.1    Dschida, W.J.2    Harris, T.3    Bowman, E.J.4
  • 124
    • 0026947915 scopus 로고
    • Vacuolar ATPase of Neurospora crassa: Electron microscopy, gene characterization and gene inactivation/mutation
    • Bowman, B.J.; Dschida, W.J.; Bowman, E.J., Vacuolar ATPase of Neurospora crassa: Electron microscopy, gene characterization and gene inactivation/mutation. J. Exp. Biol, 1992, 172, (1), 57-66.
    • (1992) J. Exp. Biol , vol.172 , Issue.1 , pp. 57-66
    • Bowman, B.J.1    Dschida, W.J.2    Bowman, E.J.3
  • 125
    • 0031445914 scopus 로고    scopus 로고
    • Visualization of a peripheral stalk in V-type ATPase: Evidence for the stator structure essential to rotational catalysis
    • Boekema, E.J.; Ubbink-Kok, T.; Lolkema, J.S.; Brisson, A.; Konings, W.N., Visualization of a peripheral stalk in V-type ATPase: Evidence for the stator structure essential to rotational catalysis. Proc. Natl. Acad. Sci. USA., 1997, 94, (26), 14291-14293.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , Issue.26 , pp. 14291-14293
    • Boekema, E.J.1    Ubbink-Kok, T.2    Lolkema, J.S.3    Brisson, A.4    Konings, W.N.5
  • 126
    • 0033531950 scopus 로고    scopus 로고
    • +)-ATPases
    • +)-ATPases. J. Biol. Chem., 1999, 274, (19), 12951-12954.
    • (1999) J. Biol. Chem , vol.274 , Issue.19 , pp. 12951-12954
    • Forgac, M.1
  • 128
    • 4043065767 scopus 로고    scopus 로고
    • The bafilomycin/concanamycin binding site in infunit c of the V-ATPase from Neurospora crassa and Saccharomyces cerevisiae
    • Bowman, E.J.; Graham, L.A.; Stevens, T.H.; Bowman, B.J., The bafilomycin/concanamycin binding site in infunit c of the V-ATPase from Neurospora crassa and Saccharomyces cerevisiae. J. Biol. Chem., 2004, 279, (32), 33131-33138.
    • (2004) J. Biol. Chem , vol.279 , Issue.32 , pp. 33131-33138
    • Bowman, E.J.1    Graham, L.A.2    Stevens, T.H.3    Bowman, B.J.4
  • 129
    • 28844433952 scopus 로고    scopus 로고
    • Infunit a of the yeast V-ATPase participates in binding of bafilomycin
    • Wang, Y.; Inoue, T.; Forgac, M., Infunit a of the yeast V-ATPase participates in binding of bafilomycin. J. Biol. Chem., 2005, 280, (49), 40481-40488.
    • (2005) J. Biol. Chem , vol.280 , Issue.49 , pp. 40481-40488
    • Wang, Y.1    Inoue, T.2    Forgac, M.3
  • 130
    • 0027169669 scopus 로고
    • +-ATPase in mutants lacking one infunit of the enzyme
    • +-ATPase in mutants lacking one infunit of the enzyme. J. Biol. Chem., 1993, 268, (22), 16845-16851.
    • (1993) J. Biol. Chem , vol.268 , Issue.22 , pp. 16845-16851
    • Doherty, R.D.1    Kane, P.M.2
  • 134
    • 0036051171 scopus 로고    scopus 로고
    • A novel natural product compound enhances cAMP-regulated chloride conductance of cells expressing CFTRAF508
    • deCarvalho, A.C.V.; Ndi, C.P.; Tsopmo, A.; Tane, P.; Ayafor, J.; Connolly, J.D.; Teem, J.L., A novel natural product compound enhances cAMP-regulated chloride conductance of cells expressing CFTRAF508. Mol. Med., 2002, 8, (2), 75-87.
    • (2002) Mol. Med , vol.8 , Issue.2 , pp. 75-87
    • Decarvalho, A.C.V.1    Ndi, C.P.2    Tsopmo, A.3    Tane, P.4    Ayafor, J.5    Connolly, J.D.6    Teem, J.L.7
  • 135
    • 0018180802 scopus 로고
    • Functional macrophage cell lines transformed by Abelson leukemia virus
    • Raschke, W.C.; Baird, S.; Ralph, P.; Nakoinz, I., Functional macrophage cell lines transformed by Abelson leukemia virus. Cell, 1978, 15, (1), 261-267.
    • (1978) Cell , vol.15 , Issue.1 , pp. 261-267
    • Raschke, W.C.1    Baird, S.2    Ralph, P.3    Nakoinz, I.4
  • 137
    • 0037711384 scopus 로고    scopus 로고
    • RANKL-mediated osteoclast formation from murine RAW 264.7 cells
    • Collin-Osdoby, P.; Yu, X.; Zheng, H.; Osdoby, P., RANKL-mediated osteoclast formation from murine RAW 264.7 cells. Methods Mol. Med., 2003, 80, 153-166.
    • (2003) Methods Mol. Med , vol.80 , pp. 153-166
    • Collin-Osdoby, P.1    Yu, X.2    Zheng, H.3    Osdoby, P.4
  • 138
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • Fields, S.; Song, O.-k., A novel genetic system to detect protein-protein interactions. Nature, 1989, 340, (6230), 245-246.
    • (1989) Nature , vol.340 , Issue.6230 , pp. 245-246
    • Fields, S.1    Song, O.-K.2
  • 139
    • 0023649184 scopus 로고
    • A new class of yeast transcriptional activators
    • Ma, J.; Ptashne, M., A new class of yeast transcriptional activators. Cell, 1987, 51, (1), 113-119.
    • (1987) Cell , vol.51 , Issue.1 , pp. 113-119
    • Ma, J.1    Ptashne, M.2
  • 141
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith, D.B.; Johnson, K.S., Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene, 1988, 67, (1), 31-40.
    • (1988) Gene , vol.67 , Issue.1 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 142
    • 14744292185 scopus 로고
    • A thioredoxin gene fusion expression system that circumvents inclusion body formation in the E. coli cytoplasm
    • LaVallie, E.R.; DiBlasio, E.A.; Kovacic, S.; Grant, K.L.; P.F., S.; McCoy, J.M., A thioredoxin gene fusion expression system that circumvents inclusion body formation in the E. coli cytoplasm. Biotechnology, 1993, 11, (2), 187-193.
    • (1993) Biotechnology , vol.11 , Issue.2 , pp. 187-193
    • Lavallie, E.R.1    Diblasio, E.A.2    Kovacic, S.3    Grant, K.L.4    McCoy, J.M.5
  • 145
    • 0023130372 scopus 로고
    • Evaluation of a tetrazolium-based semiautomated colorimetric assay: Assessment of chemosensitivity testing
    • Carmichael, J.; DeGraff, W.G.; Gazdar, A.F.; Minna, J.D.; Mitchell, J.B., Evaluation of a tetrazolium-based semiautomated colorimetric assay: Assessment of chemosensitivity testing. Cancer Res., 1987, 47, (4), 936-942.
    • (1987) Cancer Res , vol.47 , Issue.4 , pp. 936-942
    • Carmichael, J.1    Degraff, W.G.2    Gazdar, A.F.3    Minna, J.D.4    Mitchell, J.B.5
  • 146
    • 58849164046 scopus 로고    scopus 로고
    • Molecular mechanisms in coupling of bone formation to resorption
    • Martin, J.T.; Gooi, J.H.; Sims, N.A., Molecular mechanisms in coupling of bone formation to resorption. Crit. Rev. Eukaryot. Gene Expr., 2009, 19, (1), 73-88.
    • (2009) Crit. Rev. Eukaryot. Gene Expr , vol.19 , Issue.1 , pp. 73-88
    • Martin, J.T.1    Gooi, J.H.2    Sims, N.A.3
  • 149
    • 3242762388 scopus 로고    scopus 로고
    • Differential effects of teriparatide on BMD after treatment with raloxifene or alendronate
    • Ettinger, B.; San Martin, J.; Crans, G.; Pavo, I., Differential effects of teriparatide on BMD after treatment with raloxifene or alendronate. J. Bone Miner. Res., 2004, 19, (5), 745-751.
    • (2004) J. Bone Miner. Res , vol.19 , Issue.5 , pp. 745-751
    • Ettinger, B.1    San Martin, J.2    Crans, G.3    Pavo, I.4
  • 150
    • 0141796739 scopus 로고    scopus 로고
    • The effects of parathyroid hormone, alendronate, or both in men with osteoporosis
    • Finkelstein, J.S.; Hayes, A.; Hunzelman, J.L.; Wyland, J.J.; Lee, H.; Neer, R.M., The effects of parathyroid hormone, alendronate, or both in men with osteoporosis. New Engl. J. Med., 2003, 349, (13), 1216-1226.
    • (2003) New Engl. J. Med , vol.349 , Issue.13 , pp. 1216-1226
    • Finkelstein, J.S.1    Hayes, A.2    Hunzelman, J.L.3    Wyland, J.J.4    Lee, H.5    Neer, R.M.6
  • 152
    • 85027917619 scopus 로고    scopus 로고
    • A rationale for osteoclast selectivity of inhibiting the lysosomal V-ATPase a3 isoform
    • Nyman, J.; Väänänen, H., A rationale for osteoclast selectivity of inhibiting the lysosomal V-ATPase a3 isoform. Calcif. Tissue Int., 2010, 87, (3), 273-283.
    • (2010) Calcif. Tissue Int , vol.87 , Issue.3 , pp. 273-283
    • Nyman, J.1    Väänänen, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.