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Volumn 26, Issue 1, 2015, Pages 1-3

Cutting it out: ENaC processing in the human nephron

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY; FURIN; KALLIKREIN; PROSTASIN; SODIUM CHANNEL; EPITHELIAL SODIUM CHANNEL; SCNN1G PROTEIN, HUMAN;

EID: 84924167802     PISSN: 10466673     EISSN: 15333450     Source Type: Journal    
DOI: 10.1681/ASN.2014060618     Document Type: Editorial
Times cited : (10)

References (15)
  • 1
    • 34250207969 scopus 로고    scopus 로고
    • Epithelial Na+ channels are fully activated by furin- and prostasin-dependent release of an inhibitory peptide from the gamma-subunit
    • Bruns JB, Carattino MD, Sheng S, Maarouf AB, Weisz OA, Pilewski JM, Hughey RP, Kleyman TR: Epithelial Na+ channels are fully activated by furin- and prostasin-dependent release of an inhibitory peptide from the gamma-subunit. J Biol Chem 282: 6153-6160, 2007
    • (2007) J Biol Chem , vol.282 , pp. 6153-6160
    • Bruns, J.B.1    Carattino, M.D.2    Sheng, S.3    Maarouf, A.B.4    Weisz, O.A.5    Pilewski, J.M.6    Hughey, R.P.7    Kleyman, T.R.8
  • 2
    • 54449088865 scopus 로고    scopus 로고
    • Proteolytic processing of the epithelial sodium channel gamma subunit has a dominant role in channel activation
    • Carattino MD, Hughey RP, Kleyman TR: Proteolytic processing of the epithelial sodium channel gamma subunit has a dominant role in channel activation. J Biol Chem 283: 25290-25295, 2008
    • (2008) J Biol Chem , vol.283 , pp. 25290-25295
    • Carattino, M.D.1    Hughey, R.P.2    Kleyman, T.R.3
  • 3
    • 80053374793 scopus 로고    scopus 로고
    • ENaC structure and function in the wake of a resolved structure of a family member
    • Kashlan OB, Kleyman TR: ENaC structure and function in the wake of a resolved structure of a family member. Am J Physiol Renal Physiol 301: F684-F696, 2011
    • (2011) Am J Physiol Renal Physiol , vol.301 , pp. F684-F696
    • Kashlan, O.B.1    Kleyman, T.R.2
  • 4
    • 68949094195 scopus 로고    scopus 로고
    • ENaC at the cutting edge: Regulation of epithelial sodium channels by proteases
    • Kleyman TR, Carattino MD, Hughey RP: ENaC at the cutting edge: Regulation of epithelial sodium channels by proteases. J Biol Chem 284: 20447-20451, 2009
    • (2009) J Biol Chem , vol.284 , pp. 20447-20451
    • Kleyman, T.R.1    Carattino, M.D.2    Hughey, R.P.3
  • 7
    • 33748439266 scopus 로고    scopus 로고
    • Regulation of maturation and processing of ENaC subunits in the rat kidney
    • Ergonul Z, Frindt G, Palmer LG: Regulation of maturation and processing of ENaC subunits in the rat kidney. Am J Physiol Renal Physiol 291: F683-F693, 2006
    • (2006) Am J Physiol Renal Physiol , vol.291 , pp. F683-F693
    • Ergonul, Z.1    Frindt, G.2    Palmer, L.G.3
  • 8
    • 70350719352 scopus 로고    scopus 로고
    • Surface expression of sodium channels and transporters in rat kidney: Effects of dietary sodium
    • Frindt G, Palmer LG: Surface expression of sodium channels and transporters in rat kidney: effects of dietary sodium. Am J Physiol Renal Physiol 297: F1249-F1255, 2009
    • (2009) Am J Physiol Renal Physiol , vol.297 , pp. F1249-F1255
    • Frindt, G.1    Palmer, L.G.2
  • 15
    • 59449104675 scopus 로고    scopus 로고
    • ENaC proteolytic regulation by channel-activating protease 2
    • García-Caballero A, Dang Y, He H, Stutts MJ: ENaC proteolytic regulation by channel-activating protease 2. J Gen Physiol 132: 521-535, 2008
    • (2008) J Gen Physiol , vol.132 , pp. 521-535
    • García-Caballero, A.1    Dang, Y.2    He, H.3    Stutts, M.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.