Mutation of a single amino acid converts the human water channel aquaporin 5 into an anion channel (Q48031543)

7 February 2018

title

Mutation of a single amino acid converts the human water channel aquaporin 5 into an anion channel (English)

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7 February 2018

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7 February 2018

author name string

Xue Qin

series ordinal

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7 February 2018

publication date

10 July 2013

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7 February 2018

American Journal of Physiology - Cell Physiology

published in

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7 February 2018

volume

305

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7 February 2018

issue

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7 February 2018

page(s)

C663-72

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7 February 2018

Aquaporin water channels (Nobel Lecture).

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Evidence that aquaporin 1 is a major pathway for CO2 transport across the human erythrocyte membrane

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Characterization of aquaporin-6 as a nitrate channel in mammalian cells. Requirement of pore-lining residue threonine 63

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21 January 2018

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21 January 2018

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The human NBCe1-A mutant R881C, associated with proximal renal tubular acidosis, retains function but is mistargeted in polarized renal epithelia

21 January 2018

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The tobacco aquaporin NtAQP1 is a membrane CO2 pore with physiological functions

21 January 2018

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Gas-tight triblock-copolymer membranes are converted to CO₂ permeable by insertion of plant aquaporins

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In silico study of Aquaporin V: Effects and affinity of the central pore-occluding lipid

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10.1152/AJPCELL.00129.2013

21 January 2018

Identifiers

DOI

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7 February 2018

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7 February 2018