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Volumn 357, Issue 1, 2001, Pages 1-10

Functional role of polar amino acid residues in Na+/H+ exchangers

Author keywords

Cation co ordination; Charge relay system; Membrane protein; pH regulation; Salt tolerance

Indexed keywords

AMINO ACIDS; BINDING ENERGY; ESCHERICHIA COLI; ION EXCHANGERS; PHYSIOLOGY; YEAST;

EID: 0035396616     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3570001     Document Type: Review
Times cited : (62)

References (86)
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  • 45
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    • + antiporter of Escherichia coli. Cysteine (H226C) or serine (H226S) retain both normal activity and pH sensitivity, aspartate (H226D) shifts the pH profile toward basic pH, and alanine (H226A) inactivates the carrier at all pH values
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    • + 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
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    • Gerchman, Y.1    Rimon, A.2    Padan, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.