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Relevant bibliographies by topics / Excitatory amino acid transporter 1

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Academic literature on the topic 'Excitatory amino acid transporter 1'

Author: Grafiati

Published: 4 June 2025

Last updated: 1 August 2025

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Journal articles on the topic "Excitatory amino acid transporter 1"

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Vandenberg, Robert J., Cheryl A. Handford, Ewan M. Campbell, Renae M. Ryan, and Andrea J. Yool. "Water and urea permeation pathways of the human excitatory amino acid transporter EAAT1." Biochemical Journal 439, no. 2 (2011): 333–40. http://dx.doi.org/10.1042/bj20110905.

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Glutamate transport is coupled to the co-transport of 3 Na+ and 1 H+ followed by the counter-transport of 1 K+. In addition, glutamate and Na+ binding to glutamate transporters generates an uncoupled anion conductance. The human glial glutamate transporter EAAT1 (excitatory amino acid transporter 1) also allows significant passive and active water transport, which suggests that water permeation through glutamate transporters may play an important role in glial cell homoeostasis. Urea also permeates EAAT1 and has been used to characterize the permeation properties of the transporter. We have pr

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Canul-Tec, Juan C., Reda Assal, Erica Cirri, et al. "Structure and allosteric inhibition of excitatory amino acid transporter 1." Nature 544, no. 7651 (2017): 446–51. http://dx.doi.org/10.1038/nature22064.

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Hediger, M. A., and T. C. Welbourne. "Introduction: Glutamate transport, metabolism, and physiological responses." American Journal of Physiology-Renal Physiology 277, no. 4 (1999): F477—F480. http://dx.doi.org/10.1152/ajprenal.1999.277.4.f477.

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The material covered in this set of articles was originally presented at Experimental Biology ’98, in San Francisco, CA, on April 20, 1998. Here, the participants recount important elements of current research on the role of glutamate transporter activity in cellular signaling, metabolism, and organ function. W. A. Fairman and S. G. Amara discuss the five subtypes of human excitatory amino acid transporters, with emphasis on the EAAT4 subtype. M. A. Hediger discusses the expression and action of EAAC1 subtype of the human excitatory amino acid transporter. I. Nissim provides an overview of the

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Gebhardt, Christine, Rafael Körner, and Uwe Heinemann. "Delayed Anoxic Depolarizations in Hippocampal Neurons of Mice Lacking the Excitatory Amino Acid Carrier 1." Journal of Cerebral Blood Flow & Metabolism 22, no. 5 (2002): 569–75. http://dx.doi.org/10.1097/00004647-200205000-00008.

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Hypoxia leads to a rapid increase in vesicular release of glutamate. In addition, hypoxic glutamate release might be caused by reversed operation of neuronal glutamate transporters. An increase in extracellular glutamate concentration might be an important factor in generating anoxic depolarizations (AD) and subsequent neuronal damage. To study the AD and the vesicular release in hippocampal slices from CD1 wild-type mice and mice in which the neuronal glutamate transporter excitatory amino acid carrier 1 (EAAC1) had been knocked out, the authors performed recordings of field potentials and pa

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Watzke, Natalie, Thomas Rauen, Ernst Bamberg, and Christof Grewer. "On the Mechanism of Proton Transport by the Neuronal Excitatory Amino Acid Carrier 1." Journal of General Physiology 116, no. 5 (2000): 609–22. http://dx.doi.org/10.1085/jgp.116.5.609.

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Uptake of glutamate from the synaptic cleft is mediated by high affinity transporters and is driven by Na+, K+, and H+ concentration gradients across the membrane. Here, we characterize the molecular mechanism of the intracellular pH change associated with glutamate transport by combining current recordings from excitatory amino acid carrier 1 (EAAC1)–expressing HEK293 cells with a rapid kinetic technique with a 100-μs time resolution. Under conditions of steady state transport, the affinity of EAAC1 for glutamate in both the forward and reverse modes is strongly dependent on the pH on the cis

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Schmidt, Robert W., and Meghan L. Thompson. "Glycinergic signaling in the human nervous system: An overview of therapeutic drug targets and clinical effects." Mental Health Clinician 6, no. 6 (2016): 266–76. http://dx.doi.org/10.9740/mhc.2016.11.266.

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Abstract Glycine and related endogenous compounds (d-serine, d-alanine, sarcosine) serve critical roles in both excitatory and inhibitory neurotransmission and are influenced by a multitude of enzymes and transporters, including glycine transporter 1 and 2 (GlyT1 and GlyT2), d-amino acid oxidase (DAAO), serine racemase (SRR), alanine-serine-cysteine transporter 1 (Asc-1), and kynurenine aminotransferase (KAT). MEDLINE, Web of Science, and PsychINFO were searched for relevant human trials of compounds. Many studies utilizing exogenous administration of small molecule agonists of the glycineB si

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Fujita, Hiroko, Kohji Sato, Tong-Chun Wen, Yi Peng, and Masahiro Sakanaka. "Differential Expressions of Glycine Transporter 1 and Three Glutamate Transporter mRNA in the Hippocampus of Gerbils with Transient Forebrain Ischemia." Journal of Cerebral Blood Flow & Metabolism 19, no. 6 (1999): 604–15. http://dx.doi.org/10.1097/00004647-199906000-00003.

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The extracellular concentrations of glutamate and its co-agonist for the N-methyl-d-aspartate (NMDA) receptor, glycine, may be under the control of amino acid transporters in the ischemic brain, However, there is little information on changes in glycine and glutamate transporters in the hippocampal CA1 field of gerbils with transient forebrain ischemia. This study investigated the spatial and temporal expressions of glycine transporter 1 (GLYT 1) and three glutamate transporter (excitatory amino acid carrier 1, EAAC 1; glutamate/aspartate transporter, GLAST; glutamate transporter 1, GLT1) mRNA

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Scott, Heather L., David V. Pow, Anthony E. G. Tannenberg, and Peter R. Dodd. "Aberrant Expression of the Glutamate Transporter Excitatory Amino Acid Transporter 1 (EAAT1) in Alzheimer's Disease." Journal of Neuroscience 22, no. 3 (2002): RC206. http://dx.doi.org/10.1523/jneurosci.22-03-j0004.2002.

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Meyer, Thomas, Albert C. Ludolph, Markus Morkel, Christian Hagemeier, and Astrid Speer. "Genomic organization of the human excitatory amino acid transporter gene GLT-1." NeuroReport 8, no. 3 (1997): 775–77. http://dx.doi.org/10.1097/00001756-199702100-00039.

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Pant, Shashank, and Emad Tajkhorshid. "Modulation of Orientational Dynamics of Excitatory Amino Acid Transporter-1 by Cholesterol." Biophysical Journal 116, no. 3 (2019): 556a. http://dx.doi.org/10.1016/j.bpj.2018.11.2990.

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Dissertations / Theses on the topic "Excitatory amino acid transporter 1"

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Richards, Dannette Shanon. "CHARACTERIZATION OF EXCITATORY AMINO ACID NEUROTRANSMITTERS AT MOTONEURON SYNAPSES CONTACTING RENSHAW CELLS." Wright State University / OhioLINK, 2009. http://rave.ohiolink.edu/etdc/view?acc_num=wright1260896604.

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Ye, Ran. "Mass Spectrometric Characterization and Fluorophore-Assisted Light Inactivation of Human Excitatory Amino Acid Transporter." The University of Montana, 2009. http://etd.lib.umt.edu/theses/available/etd-05192009-104425/.

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Glia-expressing excitatory amino acid transporter 2 (EAAT2) mediates the bulk of glutamate re-uptake in the human central nervous system (CNS) and is associated with a variety of neurological disorders. Our understanding of the structure and mechanism of this integral membrane protein is limited. The goal of this study was to use pharmacological, mass spectrometric (MS) and photochemical approaches to probe EAAT2. For MS characterization, a hexahis epitope was incorporated into the N-terminus of human EAAT2. The recombinant protein was functionally expressed in HEK 293T cells and purified thro

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Leinenweber, Ariane [Verfasser]. "Regulation of Excitatory Amino Acid Transporter 2 (EAAT2) by Carboxy-terminal Domains / Ariane Leinenweber." Hannover : Bibliothek der Tierärztlichen Hochschule Hannover, 2010. http://d-nb.info/100962427X/34.

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Mavencamp, Terri Lynn. "Design, synthesis and biological evaluation of a family of excitatory amino acid transporter 3 (EAAT3) preferring inhibitors." [Missoula, Mont.] : The University of Montana, 2008. http://etd.lib.umt.edu/theses/available/etd-03212009-152926/unrestricted/Mavencamp_umt_0136D_10009.pdf.

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Mavencamp, Terri Lynn. "Design, Synthesis and Biological Evaluation of a Family of Excitatory Amino Acid Transporter 3 (EAAT3) Preferring Inhibitors." The University of Montana, 2009. http://etd.lib.umt.edu/theses/available/etd-03212009-152926/.

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<p>This work describes the synthesis and initial characterization of the biological activity of a family of EAAT3 preferring inhibitors, L-β-benzyl aspartate (L-β-BA) and L-β-BA derivatives. L-β-BA and derivatives were initially synthesized in an approximate 2:1 ratio of diasteromers (threo:erythro), using base promoted enolate addition. Kinetic analysis of 3H-D-aspartate uptake into C17.2 cells expressing the hEAATs demonstrated that L-threo-β-BA is the more potent diastereomer (Ki values of 9 µM for EAAT1, 10.0 µM for EAAT2 and 0.8 µM for EAAT3), acts competitively,

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Barcelona, Stephanie Suazo. "Investigation of the Mechanism of Substrate Transport by the Glutamate Transporter EAAC1." Scholarly Repository, 2007. http://scholarlyrepository.miami.edu/oa_theses/91.

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The activity of glutamate transporters is essential for the temporal and spatial regulation of the neurotransmitter concentration in the synaptic cleft which is critical for proper neuronal signaling. Because of their role in controlling extracellular glutamate concentrations, dysfunctional glutamate transporters have been implicated in several neurodegenerative diseases and psychiatric disorders. Therefore, investigating the mechanism of substrate transport by these transporters is essential in understanding their behavior when they malfunction. A bacterial glutamate transporter hom

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Tian, Guilian. "The molecular mechanisms of the loss of glial glutamate transporter EAAT2 in neurodegenerative diseases." Columbus, Ohio : Ohio State University, 2007. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1187038549.

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Akohene-Mensah, Paul. "Examining the Role of L-Type Amino Acid Transporter 1 (SLC7A5) in Myoblasts." Thesis, Université d'Ottawa / University of Ottawa, 2020. http://hdl.handle.net/10393/41036.

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Skeletal muscles represent the largest tissue mass within the body and are primarily involved in the generation of force for voluntary movement. Skeletal muscles have a remarkable capacity to repair, due primarily to the actions of muscle stem cells (MuSCs). MuSCs are normally quiescent in adult skeletal muscle; however, in response to myotrauma (trauma to muscle tissue) from muscle injury or exercise, MuSCs become activated, either undergo self-renewal to replenish the quiescent population or commit to the myogenic lineage as myoblasts, proliferate, and differentiate into myotubes in vitro or

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Butchbach, Matthew E. R. "Regulation of glutamate transport by GTRAP3-18 and by lipid rafts." Connect to this title online, 2003. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1054650123.

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Thesis (Ph. D.)--Ohio State University, 2003.<br>Title from first page of PDF file. Document formatted into pages; contains xviii, 160 p.; also includes graphics Includes bibliographical references (p. 132-160). Available online via OhioLINK's ETD Center

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Linderholm, Klas. "Kynurenic acid in psychiatric disorders studies on the mechanisms of action /." Stockholm, 2010. http://diss.kib.ki.se/2010/978-91-7409-818-1/.

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Books on the topic "Excitatory amino acid transporter 1"

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Barnard, E. A. Allosteric Modulation of Amino Acid Receptors: Therapeutic Implications (Fidia Research Symposium Series, Vol 1). Raven Pr, 1989.

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Sebastio, Gianfranco, Manuel Schiff, and Hélène Ogier de Baulny. Lysinuric Protein Intolerance and Hartnup Disease. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780199972135.003.0025.

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Lysinuric protein intolerance (LPI) is an inherited aminoaciduria caused by defective cationic amino acid transport at the basolateral membrane of epithelial cells in intestine and kidney. LPI is caused by mutations in the SLC7A7 gene, which encodes the y+LAT-1 protein, the catalytic light chain subunit of a complex belonging to the heterodimeric amino acid transporter family. Symptoms usually begin after weaning with refusal of feeding, vomiting, and consequent failure to thrive. Hepatosplenomegaly, hematological anomalies, and neurological involvement including hyperammonemic coma will progr

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Servais, Aude, and Bertrand Knebelmann. Cystinuria. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780199972135.003.0024.

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Cystinuria (OMIM #220100) is an autosomal recessive disorder of a dibasic amino acid transport in the apical membrane of epithelial cells of the renal proximal tubule and small intestine. It leads to increased urinary cystine excretion and recurrent urolithiasis. The cystine transporter is an heterodimeric transporter which is composed of a heavy subunit, rBAT, linked to a light subunit, b0,+AT. Two genes, SLC3A1 (solute carrier family 3 member 1) and SLC7A9, coding for rBAT and b0,+AT, account for the genetic basis of cystinuria. Cystinuria may lead to obstruction, infections, and ultimately

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Johnson, Nicholas J., and Judd E. Hollander. Management of cocaine poisoning. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780199600830.003.0324.

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Cocaine is powerful central nervous system (CNS) stimulant derived from the coca plant. It affects the body via a number of mechanisms including blockade of fast sodium channels, increased catecholamine release, inhibition of catecholamine reuptake, and increased concentration of excitatory amino acid concentrations in the CNS. It is rapidly absorbed via the aerodigestive, respiratory, gastrointestinal, and genitourinary mucosa, and also may be injected. When injected intravenously or inhaled, cocaine is rapidly distributed throughout the body and CNS, with peak effects in 3–5 minutes. With na

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Book chapters on the topic "Excitatory amino acid transporter 1"

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Sarthy, Vijay, and David Pow. "Excitatory Amino Acid Transporters in the Retina." In Ocular Transporters In Ophthalmic Diseases And Drug Delivery. Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-375-2_15.

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Ueda, T. "Glutamate Transport in the Synaptic Vesicle." In Excitatory Amino Acids. Palgrave Macmillan UK, 1986. http://dx.doi.org/10.1007/978-1-349-08479-1_12.

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Beschorner, Rudi. "Differentiating Choroid Plexus Tumors from Metastatic Carcinomas: Use of Inwardly Rectifying K+ Channel KIR7.1 and Excitatory Amino Acid Transporter-1." In Tumors of the Central Nervous System. Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-7602-9_21.

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Langford, Marlyn P., Thomas B. Redens, and Donald E. Texada. "Excitatory Amino Acid Transporters, Xc− Antiporter, γ-Glutamyl Transpeptidase, Glutamine Synthetase, and Glutathione in Human Corneal Epithelial Cells." In Oxidative Stress in Applied Basic Research and Clinical Practice. Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-1935-2_4.

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Gillessen, Thomas, Samantha L. Budd, and Stuart A. Lipton. "Excitatory Amino Acid Neurotoxicity." In Advances in Experimental Medicine and Biology. Springer US, 2003. http://dx.doi.org/10.1007/978-1-4615-0123-7_1.

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Schwarcz, R., E. Okuno, and C. Köhler. "Endogenous Excitotoxins: Focus on Quinolinic Acid." In Excitatory Amino Acids. Palgrave Macmillan UK, 1986. http://dx.doi.org/10.1007/978-1-349-08479-1_25.

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Roberts, P. J. "Presynaptic Receptors for Excitatory Amino Acid Transmitters." In Excitatory Amino Acids. Palgrave Macmillan UK, 1986. http://dx.doi.org/10.1007/978-1-349-08479-1_13.

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Watkins, J. C. "Twenty-five Years of Excitatory Amino Acid Research." In Excitatory Amino Acids. Palgrave Macmillan UK, 1986. http://dx.doi.org/10.1007/978-1-349-08479-1_1.

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Stone, T. W., J. H. Connick, J. I. Addae, D. A. S. Smith, and P. A. Brooks. "The Neuropharmacology of Quinolinic Acid and the Kynurenines." In Excitatory Amino Acids. Palgrave Macmillan UK, 1986. http://dx.doi.org/10.1007/978-1-349-08479-1_24.

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Zaczek, R., K. Koller, D. O. Carpenter, R. Fisher, J. M. ffrench-Mullen, and J. T. Coyle. "Interactions of Acidic Peptides: Excitatory Amino Acid Receptors." In Excitatory Amino Acids. Palgrave Macmillan UK, 1986. http://dx.doi.org/10.1007/978-1-349-08479-1_26.

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Conference papers on the topic "Excitatory amino acid transporter 1"

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Kostić, Marina D., Jovana S. Marjanović, Sven Mangelinckx, and Vera M. Divac. "In silico Drug-Likeness, Pharmacokinetic and other ADME properties of 2- (aminomethyl)cyclopropane-1,1-dicarboxylic acid." In 2nd International Conference on Chemo and Bioinformatics. Institute for Information Technologies, University of Kragujevac, 2023. http://dx.doi.org/10.46793/iccbi23.455k.

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Herein we present the results of in silico determination of Drug-Likeness, Pharmacokinetic and other ADME properties of 2-(aminomethyl)cyclopropane-1,1-dicarboxylic acid as an example constrained γ-amino dicarboxylic acid. The results of in silico screening of drug-likeness, pharmacokinetic and other ADME (absorption, distribution, metabolism and elimination) properties of 2-(aminomethyl)cyclopropane-1,1-dicarboxylic acid have revealed that this compound is not able to cross the blood-brain barrier, but it shows good solubility and gastrointestinal absorption. The possible target screening has

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Iino, Ichirota, Hirotoshi Kikuchi, Shinichiro Miyazaki, et al. "Abstract 404: Effect of miR-122 and its target gene cationic amino acid transporter 1 on colorectal liver metastasis." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-404.

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Liang, Zhongxing, Heidi T. Cho, Ke Liang, et al. "Abstract 2736: Overexpression of L-type amino acid transporter-1 in breast cancer cells and tissues: potential association with growth and progression of tumors." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-2736.

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Rabbani, Naila, Alberto de a Fuente, and Paul Thornalley. "Risk prediction of early decline in renal function in diabetic kidney disease with algorithm including fractional excretion of glycated amino acids." In Qatar University Annual Research Forum & Exhibition. Qatar University Press, 2021. http://dx.doi.org/10.29117/quarfe.2021.0096.

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Background and aims: Diabetic kidney disease occurs in ca. 40% patients with diabetes. Approximately 1 in 5 patients with type 1 diabetes mellitus (T1DM) and 1 in 3 patients with type 2 diabetes mellitus (T2DM) develop early decline in renal function (EDRF), requiring renal dialysis after 5 - 20 years. Currently, at the time of normoalbuminuria or new onset microalbuminuria (incipient diabetic nephropathy), it is uncertain which patients are at risk of EDRF. With Joslin Kidney Study investigators, we found patients with T1DM who later developed EDRF (Decliners) have higher fractional excretion

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Tahseen Taha AL-TAEE, Nidhal. "EFFECT OF FATTY EXTRACT OF AZOLLA PLANT WITH DIFFERENT SOLVENTS ON HEMATOLOGICAL AND BIOCHEMICAL PARAMETERS OF COMMON CARP CYPRINUS CARPIO L." In VI.International Scientific Congress of Pure,Applied and Technological Sciences. Rimar Academy, 2022. http://dx.doi.org/10.47832/minarcongress6-51.

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The study was conducted in the fish laboratory of the Department of Animal Production in the College of Agriculture and Forestry / the University of Mosul. The experiment included feeding common carp fish using ten experimental diets containing Azolla plant extract at percentages (0.5%, 1%, 1.5%) of each solvent, ether, acetone, and ethanol, and the control was free of additives. Glass tanks were used in the growth experiment of carp fish for a period of 49 days. The results of the statistical analysis showed that the average hemoglobin concentration and the percentage of the volume of compact

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Reports on the topic "Excitatory amino acid transporter 1"

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Wong, Eric A., and Zehava Uni. Nutrition of the Developing Chick Embryo: Nutrient Uptake Systems of the Yolk Sac Membrane and Embryonic Intestine. United States Department of Agriculture, 2012. http://dx.doi.org/10.32747/2012.7697119.bard.

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We have examined the developmental changes in composition, amount, and uptake of yolk nutrients (fat, protein, water and carbohydrates) and the expression ofnutrient transporters in the yolk sac membrane (YSM) from embryonic day 11 (Ell) to 21 (E21) and small intestine from embryonic day 15 (E15) to E21 in embryos from young (22-25 wk) and old (45-50 wk) Cobb and Leghorn breeder flocks. The developmental expression profiles for the peptide transporter 1 (PepTl), the amino acid transporters, EAAT3, CAT-1 and BOAT, the sodium glucose transporter (SGLTl), the fructose transporter (GLUT5), the dig

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