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Volumn 90, Issue 9, 2011, Pages 688-695

Vacuolar H +-ATPases: Intra- and intermolecular interactions

Author keywords

Interactions; Transport; V ATPases

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BAFILOMYCIN; CARRIER PROTEIN; ESTRADIOL BENZOATE PLUS PROGESTERONE; MACROLIDE;

EID: 79960564369     PISSN: 01719335     EISSN: 16181298     Source Type: Journal    
DOI: 10.1016/j.ejcb.2011.04.009     Document Type: Short Survey
Times cited : (23)

References (74)
  • 3
    • 0037262045 scopus 로고    scopus 로고
    • Novel marine and microbial natural product inhibitors of vacuolar ATPase
    • Beutler J.A., McKee T.C. Novel marine and microbial natural product inhibitors of vacuolar ATPase. Curr. Med. Chem. 2003, 10:787-796.
    • (2003) Curr. Med. Chem. , vol.10 , pp. 787-796
    • Beutler, J.A.1    McKee, T.C.2
  • 4
    • 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, 209:577-589.
    • (2006) J. Exp. Biol. , vol.209 , pp. 577-589
    • Beyenbach, K.W.1    Wieczorek, H.2
  • 5
    • 26244461164 scopus 로고    scopus 로고
    • Development and application of diazirines in biological and synthetic macromolecular systems
    • Blencowe A., Hayes W. Development and application of diazirines in biological and synthetic macromolecular systems. Soft Matter 2005, 1:178-205.
    • (2005) Soft Matter , vol.1 , pp. 178-205
    • Blencowe, A.1    Hayes, W.2
  • 7
    • 61349192268 scopus 로고    scopus 로고
    • The Ras/cAMP/protein kinase A pathway regulates glucose-dependent assembly of the vacuolar (H+)-ATPase in yeast
    • Bond S., Forgac M. The Ras/cAMP/protein kinase A pathway regulates glucose-dependent assembly of the vacuolar (H+)-ATPase in yeast. J. Biol. Chem. 2008, 283:36513-36521.
    • (2008) J. Biol. Chem. , vol.283 , pp. 36513-36521
    • Bond, S.1    Forgac, M.2
  • 8
    • 0037040244 scopus 로고    scopus 로고
    • Mutations in subunit c of the vacuolar ATPase confer resistance to bafilomycin and identify a conserved antibiotic binding site
    • Bowman B.J., Bowman E.J. Mutations in subunit c of the vacuolar ATPase confer resistance to bafilomycin and identify a conserved antibiotic binding site. J. Biol. Chem. 2002, 277:3965-3972.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3965-3972
    • Bowman, B.J.1    Bowman, E.J.2
  • 9
    • 33751085062 scopus 로고    scopus 로고
    • A model for the proteo lipid ring and bafilomycin/concanamycin-binding site in the vacuolar ATPase of Neurospora crassa
    • Bowman B.J., McCall M.E., Baertsch R., Bowman E.J. A model for the proteo lipid ring and bafilomycin/concanamycin-binding site in the vacuolar ATPase of Neurospora crassa. J. Biol. Chem. 2006, 281:31885-31893.
    • (2006) J. Biol. Chem. , vol.281 , pp. 31885-31893
    • Bowman, B.J.1    McCall, M.E.2    Baertsch, R.3    Bowman, E.J.4
  • 10
    • 4043065767 scopus 로고    scopus 로고
    • The bafilomycin/concanamycin binding site in subunit c of the V-ATPases from Neurospora crassa and Saccharomyces cerevisiae
    • Bowman E.J., Graham L.A., Stevens T.H., Bowman B.J. The bafilomycin/concanamycin binding site in subunit c of the V-ATPases from Neurospora crassa and Saccharomyces cerevisiae. J. Biol. Chem. 2004, 279:33131-33138.
    • (2004) J. Biol. Chem. , vol.279 , pp. 33131-33138
    • Bowman, E.J.1    Graham, L.A.2    Stevens, T.H.3    Bowman, B.J.4
  • 11
    • 0011913143 scopus 로고
    • Bafilomycins: a class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells
    • Bowman E.J., Siebers A., Altendorf K. Bafilomycins: a class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells. Proc. Natl. Acad. Sci. U.S.A. 1988, 85:7972-7976.
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 7972-7976
    • Bowman, E.J.1    Siebers, A.2    Altendorf, K.3
  • 13
    • 0027203297 scopus 로고
    • New photolabeling and crosslinking methods
    • Brunner J. New photolabeling and crosslinking methods. Annu. Rev. Biochem. 1993, 62:483-514.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 483-514
    • Brunner, J.1
  • 15
    • 0028340169 scopus 로고
    • Bafilomycin inhibits proton flow through the H+ channel of vacuolar proton pumps
    • Crider B.P., Xie X.S., Stone D.K. Bafilomycin inhibits proton flow through the H+ channel of vacuolar proton pumps. J. Biol. Chem. 1994, 269:17379-17381.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17379-17381
    • Crider, B.P.1    Xie, X.S.2    Stone, D.K.3
  • 16
    • 0034840718 scopus 로고    scopus 로고
    • Fluorous reverse phase silica gel. A new tool for preparative separations in synthetic organic and organofluorine chemistry
    • Curran D.P. Fluorous reverse phase silica gel. A new tool for preparative separations in synthetic organic and organofluorine chemistry. Synlett 2001, 1488-1496.
    • (2001) Synlett , pp. 1488-1496
    • Curran, D.P.1
  • 17
    • 84958612634 scopus 로고    scopus 로고
    • Separations with fluorous silica gel and related materials
    • Curran D.P. Separations with fluorous silica gel and related materials. Handbook of Fluorous Chemistry 2004, pp. 101-127.
    • (2004) Handbook of Fluorous Chemistry , pp. 101-127
    • Curran, D.P.1
  • 18
    • 77954909378 scopus 로고    scopus 로고
    • Regulation of V-ATPase activity and assembly by extracellular pH
    • Diakov T.T., Kane P.M. Regulation of V-ATPase activity and assembly by extracellular pH. J. Biol. Chem. 2010, 285:23771-23778.
    • (2010) J. Biol. Chem. , vol.285 , pp. 23771-23778
    • Diakov, T.T.1    Kane, P.M.2
  • 19
    • 12144279605 scopus 로고    scopus 로고
    • Crystal structure of yeast V-ATPase subunit C reveals its stator function
    • Drory O., Frolow F., Nelson N. Crystal structure of yeast V-ATPase subunit C reveals its stator function. EMBO Rep. 2004, 5:1148-1152.
    • (2004) EMBO Rep. , vol.5 , pp. 1148-1152
    • Drory, O.1    Frolow, F.2    Nelson, N.3
  • 20
    • 0030711108 scopus 로고    scopus 로고
    • Salicylihalamides A and B, novel cytotoxic macrolides from the marine Sponge Haliclona sp.
    • Erickson K.L., Beutler J.A., Cardellina I.J., Boyd M.R. Salicylihalamides A and B, novel cytotoxic macrolides from the marine Sponge Haliclona sp. J. Org. Chem. 1997, 62:8188-8192.
    • (1997) J. Org. Chem. , vol.62 , pp. 8188-8192
    • Erickson, K.L.1    Beutler, J.A.2    Cardellina, I.J.3    Boyd, M.R.4
  • 21
    • 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, 8:917-925.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 917-925
    • Forgac, M.1
  • 22
    • 0000781941 scopus 로고    scopus 로고
    • Lobatamides A and B, novel cytotoxic macrolides from the tunicate Aplidium lobatum
    • Galinis D.L., McKee T.C., Pannell L.K., Cardellina J.H., Boyd M.R. Lobatamides A and B, novel cytotoxic macrolides from the tunicate Aplidium lobatum. J. Org. Chem. 1997, 62:8968-8969.
    • (1997) J. Org. Chem. , vol.62 , pp. 8968-8969
    • Galinis, D.L.1    McKee, T.C.2    Pannell, L.K.3    Cardellina, J.H.4    Boyd, M.R.5
  • 24
    • 0026563317 scopus 로고
    • Cloning and sequencing of cDNA encoding the putative insect plasma membrane V-ATPase subunit A
    • Gräf R., Novak F.J.S., Harvey W.R., Wieczorek H. Cloning and sequencing of cDNA encoding the putative insect plasma membrane V-ATPase subunit A. FEBS Lett. 1992, 300:119-122.
    • (1992) FEBS Lett. , vol.300 , pp. 119-122
    • Gräf, R.1    Novak, F.J.S.2    Harvey, W.R.3    Wieczorek, H.4
  • 25
    • 0029812004 scopus 로고    scopus 로고
    • Purification and properties of a cytosolic V1-ATPase
    • Gräf R., Harvey W.R., Wieczorek H. Purification and properties of a cytosolic V1-ATPase. J. Biol. Chem. 1996, 271:20908-20913.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20908-20913
    • Gräf, R.1    Harvey, W.R.2    Wieczorek, H.3
  • 27
    • 62149142874 scopus 로고    scopus 로고
    • V-ATPase functions in normal and disease processes
    • Hinton A., Bond S., Forgac M. V-ATPase functions in normal and disease processes. Pflügers Arch. 2009, 457:589-598.
    • (2009) Pflügers Arch. , vol.457 , pp. 589-598
    • Hinton, A.1    Bond, S.2    Forgac, M.3
  • 32
    • 59149095897 scopus 로고    scopus 로고
    • Inhibitors of V-ATPases: old and new players
    • Huss M., Wieczorek H. Inhibitors of V-ATPases: old and new players. J. Exp. Biol. 2009, 212:341-346.
    • (2009) J. Exp. Biol. , vol.212 , pp. 341-346
    • Huss, M.1    Wieczorek, H.2
  • 33
    • 0029063512 scopus 로고
    • Disassembly and reassembly of the yeast vacuolar H(+)-ATPase in vivo
    • Kane P.M. Disassembly and reassembly of the yeast vacuolar H(+)-ATPase in vivo. J. Biol. Chem. 1995, 270:17025-17032.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17025-17032
    • Kane, P.M.1
  • 34
    • 26044453485 scopus 로고    scopus 로고
    • Actin redistribution in mosquito Malpighian tubules after a blood meal and cyclic AMP stimulation
    • Karas K., Brauer P., Petzel D. Actin redistribution in mosquito Malpighian tubules after a blood meal and cyclic AMP stimulation. J. Insect Physiol. 2005, 51:1041-1054.
    • (2005) J. Insect Physiol. , vol.51 , pp. 1041-1054
    • Karas, K.1    Brauer, P.2    Petzel, D.3
  • 35
    • 0001087954 scopus 로고    scopus 로고
    • Oximidines I and II: novel antitumor macrolides from Pseudomonas sp.
    • Kim J.W., Shin-Ya K., Furihata K., Hayakawa Y., Seto H. Oximidines I and II: novel antitumor macrolides from Pseudomonas sp. J. Org. Chem. 1999, 64:153-155.
    • (1999) J. Org. Chem. , vol.64 , pp. 153-155
    • Kim, J.W.1    Shin-Ya, K.2    Furihata, K.3    Hayakawa, Y.4    Seto, H.5
  • 36
    • 0000438917 scopus 로고
    • Neue Entwicklungen bei der Photoaffinitätsmarkierung
    • Kotzyba-Hibert F., Kapfer I., Goeldner M. Neue Entwicklungen bei der Photoaffinitätsmarkierung. Angewandte Chemie 1995, 107:1391-1408.
    • (1995) Angewandte Chemie , vol.107 , pp. 1391-1408
    • Kotzyba-Hibert, F.1    Kapfer, I.2    Goeldner, M.3
  • 37
    • 0032430828 scopus 로고    scopus 로고
    • Apicularens A and B, new cytostatic macrolides from Chondromyces species (myxobacteria): production, physico-chemical and biological properties
    • Kunze B., Jansen R., Sasse F., Höfle G., Reichenbach H. Apicularens A and B, new cytostatic macrolides from Chondromyces species (myxobacteria): production, physico-chemical and biological properties. J. Antibiot. (Tokyo) 1998, 51:1075-1080.
    • (1998) J. Antibiot. (Tokyo) , vol.51 , pp. 1075-1080
    • Kunze, B.1    Jansen, R.2    Sasse, F.3    Höfle, G.4    Reichenbach, H.5
  • 38
    • 34548300007 scopus 로고    scopus 로고
    • Physical interaction between aldolase and vacuolar H+-ATPase is essential for the assembly and activity of the proton pump
    • Lu M., Ammar D., Ives H., Albrecht F., Gluck S.L. Physical interaction between aldolase and vacuolar H+-ATPase is essential for the assembly and activity of the proton pump. J. Biol. Chem. 2007, 282:24495-24503.
    • (2007) J. Biol. Chem. , vol.282 , pp. 24495-24503
    • Lu, M.1    Ammar, D.2    Ives, H.3    Albrecht, F.4    Gluck, S.L.5
  • 41
    • 33847147698 scopus 로고    scopus 로고
    • Design, synthesis, and biological evaluation of novel analogues of archazolid: a highly potent simplified V-ATPase inhibitor
    • Menche D., Hassfeld J., Sasse F., Huss M., Wieczorek H. Design, synthesis, and biological evaluation of novel analogues of archazolid: a highly potent simplified V-ATPase inhibitor. Bioorg. Med. Chem. Lett. 2007, 17:1732-1735.
    • (2007) Bioorg. Med. Chem. Lett. , vol.17 , pp. 1732-1735
    • Menche, D.1    Hassfeld, J.2    Sasse, F.3    Huss, M.4    Wieczorek, H.5
  • 42
    • 34249007040 scopus 로고    scopus 로고
    • Archazolid-7-O-beta-d-glucopyranoside-isolation, structural elucidation and solution conformation of a novel V-ATPase inhibitor from the myxobacterium Cystobacter violaceus
    • Menche D., Hassfeld J., Steinmetz H., Huss M., Wieczorek H., Sasse F. Archazolid-7-O-beta-d-glucopyranoside-isolation, structural elucidation and solution conformation of a novel V-ATPase inhibitor from the myxobacterium Cystobacter violaceus. Eur. J. Org. Chem. 2007, 2007:1196-1202.
    • (2007) Eur. J. Org. Chem. , vol.2007 , pp. 1196-1202
    • Menche, D.1    Hassfeld, J.2    Steinmetz, H.3    Huss, M.4    Wieczorek, H.5    Sasse, F.6
  • 43
    • 34548402968 scopus 로고    scopus 로고
    • The first hydroxylated archazolid from the myxobacterium Cystobacter violaceus: isolation, structural elucidation and V-ATPase inhibition
    • Menche D., Hassfeld J., Steinmetz H., Huss M., Wieczorek H., Sasse F. The first hydroxylated archazolid from the myxobacterium Cystobacter violaceus: isolation, structural elucidation and V-ATPase inhibition. J. Antibiot. (Tokyo) 2007, 60:328-331.
    • (2007) J. Antibiot. (Tokyo) , vol.60 , pp. 328-331
    • Menche, D.1    Hassfeld, J.2    Steinmetz, H.3    Huss, M.4    Wieczorek, H.5    Sasse, F.6
  • 44
    • 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, 386:989-999.
    • (2009) J. Mol. Biol. , vol.386 , 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
  • 46
    • 33745091487 scopus 로고    scopus 로고
    • Vacuolar ATPase as a drug discovery target
    • Niikura K. Vacuolar ATPase as a drug discovery target. Drug News Perspect. 2006, 19:139-144.
    • (2006) Drug News Perspect. , vol.19 , pp. 139-144
    • Niikura, K.1
  • 47
    • 0034647941 scopus 로고    scopus 로고
    • The H subunit (Vma13p) of the yeast V-ATPase inhibits the ATPase activity of cytosolic V1 complexes
    • Parra K.J., Keenan K.L., Kane P.M. The H subunit (Vma13p) of the yeast V-ATPase inhibits the ATPase activity of cytosolic V1 complexes. J. Biol. Chem. 2000, 275:21761-21767.
    • (2000) J. Biol. Chem. , vol.275 , pp. 21761-21767
    • Parra, K.J.1    Keenan, K.L.2    Kane, P.M.3
  • 48
    • 0031597366 scopus 로고    scopus 로고
    • +-ATPase is an unconventional glucose-induced effect
    • +-ATPase is an unconventional glucose-induced effect. Mol. Cell. Biol. 1998, 18:7064-7074.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7064-7074
    • Parra, K.J.1    Kane, P.M.2
  • 51
    • 0035912787 scopus 로고    scopus 로고
    • Crystal structure of the regulatory subunit H of the V-type ATPase of Saccharomyces cerevisiae
    • Sagermann M., Stevens T.H., Matthews B.W. Crystal structure of the regulatory subunit H of the V-type ATPase of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U.S.A. 2001, 98:7134-7139.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 7134-7139
    • Sagermann, M.1    Stevens, T.H.2    Matthews, B.W.3
  • 52
    • 0037588871 scopus 로고    scopus 로고
    • Archazolids, new cytotoxic macrolactones from Archangium gephyra (Myxobacteria). Production, isolation, physico-chemical and biological properties
    • Sasse F., Steinmetz H., Höfle G., Reichenbach H. Archazolids, new cytotoxic macrolactones from Archangium gephyra (Myxobacteria). Production, isolation, physico-chemical and biological properties. J. Antibiot. (Tokyo) 2003, 56:520-525.
    • (2003) J. Antibiot. (Tokyo) , vol.56 , pp. 520-525
    • Sasse, F.1    Steinmetz, H.2    Höfle, G.3    Reichenbach, H.4
  • 53
    • 11844260070 scopus 로고    scopus 로고
    • +-ATPase assembly, translocation, and acidification of intracellular compartments in renal epithelial cells
    • +-ATPase assembly, translocation, and acidification of intracellular compartments in renal epithelial cells. Mol. Cell. Biol. 2005, 25:575-589.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 575-589
    • Sautin, Y.Y.1    Lu, M.2    Gaugler, A.3    Zhang, L.4    Gluck, S.L.5
  • 54
    • 0035067367 scopus 로고    scopus 로고
    • Skp1 forms multiple protein complexes, including RAVE, a regulator of V-ATPase assembly
    • Seol J.H., Shevchenko A., Deshaies R.J. Skp1 forms multiple protein complexes, including RAVE, a regulator of V-ATPase assembly. Nat. Cell Biol. 2001, 2:384-391.
    • (2001) Nat. Cell Biol. , vol.2 , pp. 384-391
    • Seol, J.H.1    Shevchenko, A.2    Deshaies, R.J.3
  • 55
    • 10344240424 scopus 로고    scopus 로고
    • Involvement of the nonhomologous region of subunit A of the yeast V-ATPase in coupling and in vivo dissociation
    • Shao E., Forgac M. Involvement of the nonhomologous region of subunit A of the yeast V-ATPase in coupling and in vivo dissociation. J. Biol. Chem. 2004, 279:48663-48670.
    • (2004) J. Biol. Chem. , vol.279 , pp. 48663-48670
    • Shao, E.1    Forgac, M.2
  • 56
    • 17744370342 scopus 로고    scopus 로고
    • Synthesis of photoactivatable acyclic analogues of the lobatamides
    • Shen R., Inoue T., Forgac M., Porco J.A. Synthesis of photoactivatable acyclic analogues of the lobatamides. J. Org. Chem. 2005, 70:3686-3692.
    • (2005) J. Org. Chem. , vol.70 , pp. 3686-3692
    • Shen, R.1    Inoue, T.2    Forgac, M.3    Porco, J.A.4
  • 57
    • 0037134525 scopus 로고    scopus 로고
    • The RAVE complex is essential for stable assembly of the yeast V-ATPase
    • Smardon A.M., Tarsio M., Kane P.M. The RAVE complex is essential for stable assembly of the yeast V-ATPase. J. Biol. Chem. 2002, 277:13831-13839.
    • (2002) J. Biol. Chem. , vol.277 , pp. 13831-13839
    • Smardon, A.M.1    Tarsio, M.2    Kane, P.M.3
  • 58
    • 34548826217 scopus 로고    scopus 로고
    • RAVE is essential for the efficient assembly of the C sub-unit with the vacuolar H(+)-ATPase
    • Smardon A.M., Kane P.M. RAVE is essential for the efficient assembly of the C sub-unit with the vacuolar H(+)-ATPase. J. Biol. Chem. 2007, 282:26185-26194.
    • (2007) J. Biol. Chem. , vol.282 , pp. 26185-26194
    • Smardon, A.M.1    Kane, P.M.2
  • 60
    • 0028898233 scopus 로고
    • Regulation of plasma membrane V-ATPase activity by dissociation of peripheral subunits
    • Sumner J.P., Dow J.A., Earley F.G., Klein U., Jäger D., Wieczorek H. Regulation of plasma membrane V-ATPase activity by dissociation of peripheral subunits. J. Biol. Chem. 1995, 270:5649-5653.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5649-5653
    • Sumner, J.P.1    Dow, J.A.2    Earley, F.G.3    Klein, U.4    Jäger, D.5    Wieczorek, H.6
  • 61
    • 33745841505 scopus 로고    scopus 로고
    • Differential gel electrophoresis and transgenic mitochondrial calcium reporters demonstrate spatiotemporal filtering in calcium control of mitochondria
    • Terhzaz S., Southall T.D., Lilley K.S., Kean L., Allan A.K., Davies S.A., Dow J.A. Differential gel electrophoresis and transgenic mitochondrial calcium reporters demonstrate spatiotemporal filtering in calcium control of mitochondria. J. Biol. Chem. 2006, 281:18849-18858.
    • (2006) J. Biol. Chem. , vol.281 , pp. 18849-18858
    • Terhzaz, S.1    Southall, T.D.2    Lilley, K.S.3    Kean, L.4    Allan, A.K.5    Davies, S.A.6    Dow, J.A.7
  • 62
    • 0037470438 scopus 로고    scopus 로고
    • Activation of lysosomal function during dendritic cell maturation
    • Trombetta E.S., Ebersold M., Garrett W., Pypaert M., Mellman I. Activation of lysosomal function during dendritic cell maturation. Science 2003, 299:1400-1403.
    • (2003) Science , vol.299 , pp. 1400-1403
    • Trombetta, E.S.1    Ebersold, M.2    Garrett, W.3    Pypaert, M.4    Mellman, I.5
  • 64
    • 12544249243 scopus 로고    scopus 로고
    • The V-ATPase subunit C binds to polymeric F-actin as well as to monomeric G-actin and induces cross-linking of actin filaments
    • Vitavska O., Merzendorfer H., Wieczorek H. The V-ATPase subunit C binds to polymeric F-actin as well as to monomeric G-actin and induces cross-linking of actin filaments. J. Biol. Chem. 2005, 280:1070-1076.
    • (2005) J. Biol. Chem. , vol.280 , pp. 1070-1076
    • Vitavska, O.1    Merzendorfer, H.2    Wieczorek, H.3
  • 65
    • 36348958588 scopus 로고    scopus 로고
    • Stimulus-induced phosphorylation of plasma membrane V-ATPase by protein kinase A
    • Voss M., Vitavska O., Walz B., Wieczorek H., Baumann O. Stimulus-induced phosphorylation of plasma membrane V-ATPase by protein kinase A. J. Biol. Chem. 2007, 282:33735-33742.
    • (2007) J. Biol. Chem. , vol.282 , pp. 33735-33742
    • Voss, M.1    Vitavska, O.2    Walz, B.3    Wieczorek, H.4    Baumann, O.5
  • 66
    • 28844433952 scopus 로고    scopus 로고
    • Subunit a of the yeast V-ATPase participates in binding of bafilomycin
    • Wang Y., Inoue T., Forgac M. Subunit a of the yeast V-ATPase participates in binding of bafilomycin. J. Biol. Chem. 2005, 280:40481-40488.
    • (2005) J. Biol. Chem. , vol.280 , pp. 40481-40488
    • Wang, Y.1    Inoue, T.2    Forgac, M.3
  • 68
    • 0021331201 scopus 로고
    • Metabolic products of microorganisms. 224. Bafilomycins, a new group of macrolide antibiotics. Production, isolation, chemical structure and biological activity
    • Werner G., Hagenmaier H., Drautz H., Baumgartner A., Zahner H. Metabolic products of microorganisms. 224. Bafilomycins, a new group of macrolide antibiotics. Production, isolation, chemical structure and biological activity. J. Antibiot. (Tokyo) 1984, 37:110-117.
    • (1984) J. Antibiot. (Tokyo) , vol.37 , pp. 110-117
    • Werner, G.1    Hagenmaier, H.2    Drautz, H.3    Baumgartner, A.4    Zahner, H.5
  • 69
    • 0006260685 scopus 로고
    • Energization of animal plasma membranes by the proton-motive force
    • Wieczorek H., Harvey W.R. Energization of animal plasma membranes by the proton-motive force. Physiol. Zool. 1995, 68:15-23.
    • (1995) Physiol. Zool. , vol.68 , pp. 15-23
    • Wieczorek, H.1    Harvey, W.R.2
  • 71
    • 0035816719 scopus 로고    scopus 로고
    • Microtubules are involved in glucose-dependent dissociation of the yeast vacuolar ATPase
    • Xu T., Forgac M. Microtubules are involved in glucose-dependent dissociation of the yeast vacuolar ATPase. J. Biol. Chem. 2001, 276:24855-24861.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24855-24861
    • Xu, T.1    Forgac, M.2
  • 72
    • 0027978351 scopus 로고
    • Proton conduction and bafilomycin binding by the V0 domain of the coated vesicle V-ATPase
    • Zhang J., Feng Y., Forgac M. Proton conduction and bafilomycin binding by the V0 domain of the coated vesicle V-ATPase. J. Biol. Chem. 1994, 269:23518-23523.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23518-23523
    • Zhang, J.1    Feng, Y.2    Forgac, M.3


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