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Volumn 60, Issue , 1998, Pages 719-739

Functional properties and physiological roles of organic solute channels

Author keywords

Anion channels; Cell volume regulation; Metabolites; Organic osmolytes; Porins

Indexed keywords

ACETIC ACID; ANION; ANION CHANNEL; BETAINE; GAP JUNCTION PROTEIN; INOSITOL; LACTIC ACID; MALIC ACID; PORIN; PROPIONIC ACID; SORBITOL; SUCCINIC ACID; TAURINE; URATE;

EID: 0031896999     PISSN: 00664278     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.physiol.60.1.719     Document Type: Review
Times cited : (83)

References (23)
  • 1
    • 0029907916 scopus 로고    scopus 로고
    • Structure and functional mechanism of porins
    • Jap BK, Walian PJ. 1996. Structure and functional mechanism of porins. Physiol. Rev. 76:1073-88
    • (1996) Physiol. Rev. , vol.76 , pp. 1073-1088
    • Jap, B.K.1    Walian, P.J.2
  • 2
    • 0024154771 scopus 로고
    • Structure and function of porins from gram-negative bacteria
    • Benz R. 1988. Structure and function of porins from gram-negative bacteria. Annu. Rev. Microbiol. 42:359-93
    • (1988) Annu. Rev. Microbiol. , vol.42 , pp. 359-393
    • Benz, R.1
  • 4
    • 0026730943 scopus 로고
    • The 'ins' and 'outs' of mitochondrial membrane channels
    • Mannella CA. 1992. The 'ins' and 'outs' of mitochondrial membrane channels. Trends Biochem. Sci. 17:315-20
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 315-320
    • Mannella, C.A.1
  • 5
    • 0029685882 scopus 로고    scopus 로고
    • VDAC, a channel in the outer mitochondrial membrane
    • Colombini M, Blachly-Dyson E, Forte M. 1996. VDAC, a channel in the outer mitochondrial membrane. Ion Channels 4:169-202
    • (1996) Ion Channels , vol.4 , pp. 169-202
    • Colombini, M.1    Blachly-Dyson, E.2    Forte, M.3
  • 6
    • 0029081876 scopus 로고
    • The membrane of leaf peroxisomes contains a porin-like channel
    • Reumann S, Maier E, Benz R, Heldt HW. 1995. The membrane of leaf peroxisomes contains a porin-like channel. J. Biol. Chem. 270:17559-65
    • (1995) J. Biol. Chem. , vol.270 , pp. 17559-17565
    • Reumann, S.1    Maier, E.2    Benz, R.3    Heldt, H.W.4
  • 7
    • 0027527234 scopus 로고
    • The outer mitochondrial membrane channel, VDAC, is modulated by a protein localized in the intermembrane space
    • Holden MJ, Colombini M. 1993. The outer mitochondrial membrane channel, VDAC, is modulated by a protein localized in the intermembrane space. Biochim. Biophys. Acta 1144:396-402
    • (1993) Biochim. Biophys. Acta , vol.1144 , pp. 396-402
    • Holden, M.J.1    Colombini, M.2
  • 8
    • 0028158479 scopus 로고
    • NADH regulates the gating of VDAC, the mitochondrial outer membrane channel
    • Zizi M, Forte M, Blachly-Dyson E, Colombini M. 1994. NADH regulates the gating of VDAC, the mitochondrial outer membrane channel. J. Biol. Chem. 269:1614-16
    • (1994) J. Biol. Chem. , vol.269 , pp. 1614-1616
    • Zizi, M.1    Forte, M.2    Blachly-Dyson, E.3    Colombini, M.4
  • 9
    • 0030958679 scopus 로고    scopus 로고
    • Regulation of metabolite flux through voltage-gating of VDAC channels
    • Hodge T, Colombini M. 1997. Regulation of metabolite flux through voltage-gating of VDAC channels. J. Membr. Biol. 157:271-79
    • (1997) J. Membr. Biol. , vol.157 , pp. 271-279
    • Hodge, T.1    Colombini, M.2
  • 10
    • 0030947935 scopus 로고    scopus 로고
    • VDAC channels mediate and gate the flow of ATP: Implication on regulation of mitochondrial function
    • Rostovtseva T, Colombini M. 1997. VDAC channels mediate and gate the flow of ATP: implication on regulation of mitochondrial function. Biophys. J. 72:1954-62
    • (1997) Biophys. J. , vol.72 , pp. 1954-1962
    • Rostovtseva, T.1    Colombini, M.2
  • 11
    • 0028946962 scopus 로고
    • Structural basis for sugar translocation through maltoporin channels at 3.1 Å resolution
    • Schirmer T, Keller TA, Wang YF, Rosenbusch JP. 1995. Structural basis for sugar translocation through maltoporin channels at 3.1 Å resolution. Science 267:512-14
    • (1995) Science , vol.267 , pp. 512-514
    • Schirmer, T.1    Keller, T.A.2    Wang, Y.F.3    Rosenbusch, J.P.4
  • 13
    • 0025934347 scopus 로고
    • Renal medullary organic osmolytes
    • Garcia-Perez A, Burg MB. 1991. Renal medullary organic osmolytes. Physiol. Rev. 71:1081-115
    • (1991) Physiol. Rev. , vol.71 , pp. 1081-1115
    • Garcia-Perez, A.1    Burg, M.B.2
  • 15
    • 0029972423 scopus 로고    scopus 로고
    • Cellular and molecular physiology of volume-sensitive anion channels
    • Strange K, Emma F, Jackson PS. 1996. Cellular and molecular physiology of volume-sensitive anion channels. Am. J. Physiol. 270:C711-30
    • (1996) Am. J. Physiol. , vol.270
    • Strange, K.1    Emma, F.2    Jackson, P.S.3
  • 16
    • 0029103366 scopus 로고
    • Swelling-activated organic osmolyte efflux: A new role for anion channels
    • Strange K, Jackson PS. 1995. Swelling-activated organic osmolyte efflux: a new role for anion channels. Kidney Intl. 48:994-1003
    • (1995) Kidney Intl. , vol.48 , pp. 994-1003
    • Strange, K.1    Jackson, P.S.2
  • 17
    • 0030759645 scopus 로고    scopus 로고
    • Physiological roles and functional properties of swelling-activated organic osmolyte channels
    • Kirk K. 1997. Physiological roles and functional properties of swelling-activated organic osmolyte channels. J. Membr. Biol. 158:1-16
    • (1997) J. Membr. Biol. , vol.158 , pp. 1-16
    • Kirk, K.1
  • 18
    • 0030946888 scopus 로고    scopus 로고
    • Characterization of volume-sensitive organic osmolyte efflux and anion current in Xenopus oocytes
    • Hand M, Morrison R, Strange K. 1997. Characterization of volume-sensitive organic osmolyte efflux and anion current in Xenopus oocytes. J. Membr. Biol. 157:9-16
    • (1997) J. Membr. Biol. , vol.157 , pp. 9-16
    • Hand, M.1    Morrison, R.2    Strange, K.3
  • 20
    • 0028029012 scopus 로고
    • The volume-sensitive organic osmolyteanion channel VSOAC is regulated by non-hydrolytic ATP binding
    • Jackson PS, Morrison R, Strange K. 1994. The volume-sensitive organic osmolyteanion channel VSOAC is regulated by non-hydrolytic ATP binding. Am. J. Physiol. 267:01203-9
    • (1994) Am. J. Physiol. , vol.267 , pp. 1203-1209
    • Jackson, P.S.1    Morrison, R.2    Strange, K.3
  • 21
    • 0029019691 scopus 로고
    • Single channel properties of a swelling-activated anion conductance. Current activation occurs by abrupt switching of closed channels to an open state
    • Jackson PS, Strange K. 1995. Single channel properties of a swelling-activated anion conductance. Current activation occurs by abrupt switching of closed channels to an open state. J. Gen. Physiol. 105:643-60
    • (1995) J. Gen. Physiol. , vol.105 , pp. 643-660
    • Jackson, P.S.1    Strange, K.2
  • 22
    • 0029760934 scopus 로고    scopus 로고
    • - channels in M-1 mouse cortical collecting duct cells
    • - channels in M-1 mouse cortical collecting duct cells. J. Gen. Physiol. 108:177-93
    • (1996) J. Gen. Physiol. , vol.108 , pp. 177-193
    • Meyer, K.1    Korbmacher, C.2
  • 23
    • 0029796710 scopus 로고    scopus 로고
    • - current in IMCD cells activated by hypotonicity: Time course, ATP dependence, and inhibitors
    • - current in IMCD cells activated by hypotonicity: time course, ATP dependence, and inhibitors. Am. J. Physiol. 271:F552-59
    • (1996) Am. J. Physiol. , vol.271
    • Volk, K.A.1    Zhang, C.2    Husted, R.F.3    Stokes, J.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.