Papers associated with proximal (and slc3a1)

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	HNF1B Alters an Evolutionarily Conserved Nephrogenic Program of Target Genes., Grand K., J Am Soc Nephrol. March 1, 2023; 34 (3): 412-432.
	Modeling congenital kidney diseases in Xenopus laevis., Blackburn ATM., Dis Model Mech. April 9, 2019; 12 (4):
	Heat-shock mediated overexpression of HNF1β mutations has differential effects on gene expression in the Xenopus pronephric kidney., Sauert K., PLoS One. January 1, 2012; 7 (3): e33522.
	Organization of the pronephric kidney revealed by large-scale gene expression mapping., Raciti D., Genome Biol. January 1, 2008; 9 (5): R84.
	Aminoaciduria and altered renal expression of luminal amino acid transporters in mice lacking novel gene collectrin., Malakauskas SM., Am J Physiol Renal Physiol. February 1, 2007; 292 (2): F533-44.
	The dopamine precursor L-dihydroxyphenylalanine is transported by the amino acid transporters rBAT and LAT2 in renal cortex., Quiñones H., Am J Physiol Renal Physiol. July 1, 2004; 287 (1): F74-80.
	Apical heterodimeric cystine and cationic amino acid transporter expressed in MDCK cells., Bauch C., Am J Physiol Renal Physiol. July 1, 2002; 283 (1): F181-9.
	Identification of a novel Na+-independent acidic amino acid transporter with structural similarity to the member of a heterodimeric amino acid transporter family associated with unknown heavy chains., Matsuo H., J Biol Chem. June 7, 2002; 277 (23): 21017-26.
	Human cystinuria-related transporter: localization and functional characterization., Mizoguchi K., Kidney Int. May 1, 2001; 59 (5): 1821-33.
	The molecular basis of cystinuria: an update., Goodyer P., Exp Nephrol. January 1, 2000; 8 (3): 123-7.
	LAT2, a new basolateral 4F2hc/CD98-associated amino acid transporter of kidney and intestine., Rossier G., J Biol Chem. December 3, 1999; 274 (49): 34948-54.
	Luminal heterodimeric amino acid transporter defective in cystinuria., Pfeiffer R., Mol Biol Cell. December 1, 1999; 10 (12): 4135-47.
	Obligatory amino acid exchange via systems bo,+-like and y+L-like. A tertiary active transport mechanism for renal reabsorption of cystine and dibasic amino acids., Chillarón J., J Biol Chem. July 26, 1996; 271 (30): 17761-70.
	The rBAT gene is responsible for L-cystine uptake via the b0,(+)-like amino acid transport system in a "renal proximal tubular" cell line (OK cells)., Mora C., J Biol Chem. May 3, 1996; 271 (18): 10569-76.
	Heavy metal mediated inhibition of rBAT-induced amino acid transport., Waldegger S., Kidney Int. June 1, 1995; 47 (6): 1677-81.
	A new family of proteins (rBAT and 4F2hc) involved in cationic and zwitterionic amino acid transport: a tale of two proteins in search of a transport function., Palacín M., J Exp Biol. November 1, 1994; 196 123-37.
	rBAT, related to L-cysteine transport, is localized to the microvilli of proximal straight tubules, and its expression is regulated in kidney by development., Furriols M., J Biol Chem. December 25, 1993; 268 (36): 27060-8.

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