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Academic Journal

Threonine 67 is a key component in the coupling of the NSS amino acid transporter KAAT1.

  • Authors : Giovanola M; Department of Pharmacological and Biomolecular Sciences, Università degli Studi di Milano, Via Trentacoste 2, 20134, Milano, Italy.; Vollero A

Subjects: Protein Interaction Domains and Motifs*/Protein Interaction Domains and Motifs*/Protein Interaction Domains and Motifs*/genetics; Amino Acid Transport Systems, Neutral/Amino Acid Transport Systems, Neutral/Amino Acid Transport Systems, Neutral/*chemistry ; Amino Acid Transport Systems, Neutral/Amino Acid Transport Systems, Neutral/Amino Acid Transport Systems, Neutral/*metabolism

  • Source: Biochimica et biophysica acta. Biomembranes [Biochim Biophys Acta Biomembr] 2018 May; Vol. 1860 (5), pp. 1179-1186. Date of Electronic Publication: 2018 Jan 31.Publisher: Elsevier Country of Publication: Netherlands NLM ID: 101731713 Publication Model: Print-Electronic Cited Medium: Print ISSN: 0005-2736

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Academic Journal

Role of a conserved glycine triplet in the NSS amino acid transporter KAAT1.

  • Authors : Giovanola M; Department of Molecular Sciences Applied to Biosystems, Universita degli Studi di Milano, Via Trentacoste 2, 20134 Milano, Italy.; D'Antoni F

Subjects: Mutation*; Amino Acid Transport Systems, Neutral/Amino Acid Transport Systems, Neutral/Amino Acid Transport Systems, Neutral/*genetics ; Glycine/Glycine/Glycine/*genetics

  • Source: Biochimica et biophysica acta [Biochim Biophys Acta] 2012 Jul; Vol. 1818 (7), pp. 1737-44.Publisher: Elsevier Pub. Co Country of Publication: Netherlands NLM ID: 0217513 Publication Model: Print Cited Medium: Print ISSN: 0006-3002

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Academic Journal

Passive water permeability of some wild type and mutagenized amino acid cotransporters of the SLC6/NSS family expressed in Xenopus laevis oocytes.

  • Authors : Santacroce M; Department of Molecular Sciences Applied to Biosystems, Università degli Studi di Milano, Milan, Italy. ; Castagna M

Subjects: Amino Acid Transport Systems, Neutral/Amino Acid Transport Systems, Neutral/Amino Acid Transport Systems, Neutral/*metabolism ; Carrier Proteins/Carrier Proteins/Carrier Proteins/*metabolism ; GABA Plasma Membrane Transport Proteins/GABA Plasma Membrane Transport Proteins/GABA Plasma Membrane Transport Proteins/*metabolism

  • Source: Comparative biochemistry and physiology. Part A, Molecular & integrative physiology [Comp Biochem Physiol A Mol Integr Physiol] 2010 Aug; Vol. 156 (4), pp. 509-17. Date of Electronic Publisher: Elsevier Science Country of Publication: United States NLM ID: 9806096 Publication Model: Print-Electronic Cited Medium: Internet ISSN:

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Academic Journal

An inverse relationship links temperature and substrate apparent affinity in the ion-coupled cotransporters rGAT1 and KAAT1.

  • Authors : Peres A; Department of Biotechnology and Life Sciences, University of Insubria, Via Dunant, 3, 21100 Varese, Italy. .; Vollero A

Subjects: Hot Temperature*; Amino Acid Transport Systems, Neutral/Amino Acid Transport Systems, Neutral/Amino Acid Transport Systems, Neutral/*metabolism ; GABA Plasma Membrane Transport Proteins/GABA Plasma Membrane Transport Proteins/GABA Plasma Membrane Transport Proteins/*metabolism

  • Source: International journal of molecular sciences [Int J Mol Sci] 2012 Nov 22; Vol. 13 (12), pp. 15565-74. Date of Electronic Publication: 2012 Nov 22.Publisher: MDPI Country of Publication: Switzerland NLM ID: 101092791 Publication Model: Electronic Cited Medium: Internet ISSN: 1422-0067

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Academic Journal

Interaction between lysine 102 and aspartate 338 in the insect amino acid cotransporter KAAT1.

  • Authors : Castagna M; Institute of General Physiology and Biological Chemistry G Esposito, Via Trentacoste 2, 20134, Milan, Italy.; Soragna A

Subjects: Amino Acid Transport Systems, Neutral/Amino Acid Transport Systems, Neutral/Amino Acid Transport Systems, Neutral/*metabolism ; Aspartic Acid/Aspartic Acid/Aspartic Acid/*metabolism ; Insect Proteins/Insect Proteins/Insect Proteins/*metabolism

  • Source: American journal of physiology. Cell physiology [Am J Physiol Cell Physiol] 2007 Oct; Vol. 293 (4), pp. C1286-95. Date of Electronic Publication: 2007 Jul 11.Publisher: American Physiological Society Country of Publication: United States NLM ID: 100901225 Publication Model: Print-Electronic Cited Medium:

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Academic Journal

Structural and functional basis of amino acid specificity in the invertebrate cotransporter KAAT1.

  • Authors : Miszner A; Laboratory of Cellular and Molecular Physiology, Department of Structural and Functional Biology, University of Insubria, Via Dunant 3, 21100 Varese, Italy.; Peres A

Subjects: Amino Acid Transport Systems, Neutral/Amino Acid Transport Systems, Neutral/Amino Acid Transport Systems, Neutral/*metabolism ; Amino Acids/Amino Acids/Amino Acids/*metabolism ; Carrier Proteins/Carrier Proteins/Carrier Proteins/*metabolism

  • Source: The Journal of physiology [J Physiol] 2007 Jun 15; Vol. 581 (Pt 3), pp. 899-913. Date of Electronic Publication: 2007 Apr 05.Publisher: Cambridge Univ. Press Country of Publication: England NLM ID: 0266262 Publication Model: Print-Electronic Cited Medium: Print ISSN:

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Academic Journal

Molecular physiology of the insect K-activated amino acid transporter 1 (KAAT1) and cation-anion activated amino acid transporter/channel 1 (CAATCH1) in the light of the structure of the homologous protein LeuT.

  • Authors : Castagna M; Institute of General Physiology and Biological Chemistry 'G. Esposito', University of Milan, Milano, Italy.; Bossi E

Subjects: Amino Acid Transport Systems, Neutral/Amino Acid Transport Systems, Neutral/Amino Acid Transport Systems, Neutral/*metabolism ; Carrier Proteins/Carrier Proteins/Carrier Proteins/*metabolism ; Insect Proteins/Insect Proteins/Insect Proteins/*metabolism

  • Source: Insect molecular biology [Insect Mol Biol] 2009 Jun; Vol. 18 (3), pp. 265-79. Date of Electronic Publication: 2009 Apr 06.Publisher: Blackwell Scientific For The Royal Entomological Society Country of Publication: England NLM ID: 9303579 Publication Model: Print-Electronic

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Academic Journal

NHE(VNAT): an H+ V-ATPase electrically coupled to a Na+:nutrient amino acid transporter (NAT) forms an Na+/H+ exchanger (NHE).

  • Authors : Harvey WR; Whitney Laboratory for Marine Bioscience, University of Florida, St Augustine, FL 32080, USA. ; Boudko DY

Subjects: Models, Molecular* ; Phylogeny*; Amino Acid Transport Systems/Amino Acid Transport Systems/Amino Acid Transport Systems/*metabolism

  • Source: The Journal of experimental biology [J Exp Biol] 2009 Feb; Vol. 212 (Pt 3), pp. 347-57.Publisher: Company Of Biologists Limited Country of Publication: England NLM ID: 0243705 Publication Model: Print Cited Medium: Print ISSN:

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Academic Journal

Oligomeric structure of the neutral amino acid transporters KAAT1 and CAATCH1.

  • Authors : Bossi E; Laboratory of Cellular and Molecular Physiology, Department of Structural and Functional Biology, University of Insubria, Via Dunant 3, 21100 Varese, Italy. ; Soragna A

Subjects: Amino Acid Transport Systems, Neutral/Amino Acid Transport Systems, Neutral/Amino Acid Transport Systems, Neutral/*physiology ; Carrier Proteins/Carrier Proteins/Carrier Proteins/*physiology ; Insect Proteins/Insect Proteins/Insect Proteins/*physiology

  • Source: American journal of physiology. Cell physiology [Am J Physiol Cell Physiol] 2007 Apr; Vol. 292 (4), pp. C1379-87. Date of Electronic Publication: 2006 Nov 29.Publisher: American Physiological Society Country of Publication: United States NLM ID: 100901225 Publication Model: Print-Electronic Cited Medium:

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Academic Journal

The D-amino acid transport by the invertebrate SLC6 transporters KAAT1 and CAATCH1 from Manduca sexta.

  • Authors : Vollero A; Department of Biotechnology and Life Sciences, University of Insubria, Varese, Italy.; Imperiali FG

Subjects: Amino Acid Transport Systems, Neutral/Amino Acid Transport Systems, Neutral/Amino Acid Transport Systems, Neutral/*metabolism ; Amino Acids/Amino Acids/Amino Acids/*metabolism ; Carrier Proteins/Carrier Proteins/Carrier Proteins/*metabolism

  • Source: Physiological reports [Physiol Rep] 2016 Feb; Vol. 4 (4).Publisher: published by Wiley Periodicals, Inc. on behalf of the American Physiological Society and The Physiological Society Country of Publication: United States NLM

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