Structural determinants of NH3 and NH4+ transport by mouse Rhbg, a renal Rh glycoprotein.

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Structural determinants of NH3 and NH4+ transport by mouse Rhbg, a renal Rh glycoprotein.

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http://www.wikidata.org/entity/Q39342876

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2016 nî lūn-bûn

@nan

2016年の論文

@ja

2016年論文

@yue

2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

@wuu

2016年论文

@zh

2016年论文

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Structural determinants of NH3 and NH4+ transport by mouse Rhbg, a renal Rh glycoprotein.

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Structural determinants of NH3 and NH4+ transport by mouse Rhbg, a renal Rh glycoprotein.

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Structural determinants of NH3 and NH4+ transport by mouse Rhbg, a renal Rh glycoprotein.

@en

Structural determinants of NH3 and NH4+ transport by mouse Rhbg, a renal Rh glycoprotein.

@nl

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Structural determinants of NH3 and NH4+ transport by mouse Rhbg, a renal Rh glycoprotein.

@en

Structural determinants of NH3 and NH4+ transport by mouse Rhbg, a renal Rh glycoprotein.

@nl

P1476

Structural determinants of NH3 and NH4+ transport by mouse Rhbg, a renal Rh glycoprotein.

@en

P2093

Edd Rabon

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L Lee Hamm

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Nazih L Nakhoul

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Solange Abdulnour-Nakhoul

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Trang Le

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P2860

Characterization of human RhCG and mouse Rhcg as novel nonerythroid Rh glycoprotein homologues predominantly expressed in kidney and testis

Rh type B glycoprotein is a new member of the Rh superfamily and a putative ammonia transporter in mammals

The human Rhesus-associated RhAG protein and a kidney homologue promote ammonium transport in yeast

RhBG and RhCG, the putative ammonia transporters, are expressed in the same cells in the distal nephron

Human Rhesus B and Rhesus C glycoproteins: properties of facilitated ammonium transport in recombinant kidney cells

NH3 is involved in the NH4+ transport induced by the functional expression of the human Rh C glycoprotein

Ammonium transport properties of HEK293 cells expressing RhCG mutants: preliminary analysis of structure/function by site-directed mutagenesis

Function of human Rh based on structure of RhCG at 2.1 A

Electroneutral ammonium transport by basolateral rhesus B glycoprotein

Substrate binding, deprotonation, and selectivity at the periplasmic entrance of the Escherichia coli ammonia channel AmtB

P304

F1280-F1293

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P31

scholarly article

P356

10.1152/AJPRENAL.00556.2015

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P433

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P478

311

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P577

2016-09-28T00:00:00Z

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P698

27681563

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P932

5210199

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