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Volumn 268, Issue 17, 2001, Pages 4674-4685

Functional analysis of polar amino-acid residues in membrane associated regions of the NHE1 isoform of the mammalian NA+/H+ exchanger

Author keywords

Cation binding; Crown ether; Membrane; NHE1; pH regulation

Indexed keywords

AMINO ACID; ASPARTIC ACID; GLUCOSAMINE; GLYCINE; LITHIUM; OXYGEN; PLASMA PROTEIN; PROTON; SODIUM ION;

EID: 0035726207     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2001.02391.x     Document Type: Article
Times cited : (87)

References (48)
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  • 40
    • 0033609818 scopus 로고    scopus 로고
    • + antiporter of Escherichia coli involves loop VIII-IX, plays a role in the pH response of the protein, and is maintained by the pure protein in dodecyl maltoside
    • (1999) J. Biol. Chem. , vol.274 , pp. 24617-24624
    • Gerchman, Y.1    Rimon, A.2    Padan, E.3
  • 41
    • 0023825249 scopus 로고
    • Bioenergetic coupling to protonmotive force: Should we be considering hydronium ion coordination and not group protonation?
    • (1988) Trends Biochem. Sci. , vol.13 , pp. 5-7
    • Boyer, P.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.