d-glutamate and Gut Microbiota in Alzheimer’s Disease

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Homeostasis of the Intraparenchymal-Blood Glutamate Concentration Gradient: Maintenance, Imbalance, and Regulation

Bai, W., & Zhou, Y. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00400 · Cited by 61

Toxicity of β-amyloid in HEK293 cells expressing NR1/NR2A or NR1/NR2B N-methyl-d-aspartate receptor subunits

Domingues, A. M. D. J., Almeida, S., DACRUZESILVA, E., Oliveira, C. R., & Rego, A. C. (2007) · Neurochemistry International · doi:10.1016/j.neuint.2007.03.001 · Cited by 60

Reduced Hippocampal Glutamate and Posterior Cingulate N-Acetyl Aspartate in Mild Cognitive Impairment and Alzheimer’s Disease Is Associated with Episodic Memory Performance and White Matter Integrity in the Cingulum: A Pilot Study

Wong, D. Y., Atiya, S., Fogarty, J., Montero‐Odasso, M., Pasternak, S., Brymer, C., BORRIE, M. J., & Bartha, R. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-190773 · Cited by 56

Corynebacterium glutamicum mechanosensitive channels: towards unpuzzling “glutamate efflux” for amino acid production

Nakayama, Y., Hashimoto, K.-I., Sawada, Y., Sokabe, M., Kawasaki, H., & Martinac, B. (2018) · Biophysical Reviews · doi:10.1007/s12551-018-0452-1 · Cited by 49

Reaction Mechanism of Glutamate Racemase, a Pyridoxal Phosphate-Independent Amino Acid Racemase

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Determination of D‐Amino Acids in Some Processed Foods and Effect of Racemization on In Vitro Digestibility of Casein

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The Metabolic Formation and Utilization of 5‐Oxo‐ L ‐proline ( L ‐Pyroglutamate, L ‐Pyrrolidone Carboxylate)

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Amyloid β‐peptide activates nuclear factor‐κB through an N‐methyl‐D‐aspartate signaling pathway in cultured cerebellar cells

Kawamoto, E. M., Lepsch, L. B., Cury‐Boaventura, M. F., Munhoz, C. D., Lima, L. S., Yshii, L., Avellar, M. C. W., Curi, R., Mattson, M. P., & Scavone, C. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21548 · Cited by 43

Dietary Glutamate Is Almost Entirely Removed in Its First Pass Through the Splanchnic Bed in Premature Infants

Haÿs, S., Ordonez, J. M., Burrin, D. G., & Sunehag, A. L. (2007) · Pediatric Research · doi:10.1203/pdr.0b013e318123f719 · Cited by 42

Detection of free D ‐amino acids in food by chiral phase capillary gas chromatography

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Immunocytochemical visualization of d-glutamate in the rat brain

Mangas, A., Coveñas, R., Bodet, D., Geffard, M., Aguilar, L. A., & Yajeya, J. (2006) · Neuroscience · doi:10.1016/j.neuroscience.2006.09.045 · Cited by 39

smallcap˜D-Amino acids in dairy products: detection, origin and nutritional aspects. I. Milk, fermented milk, fresh cheese and acid curd cheese.

Brückner, H. J., & Hausch, M. (1990) · Milk science international/Milchwissenschaft · Cited by 31

Assessment of the Target Engagement and d-Serine Biomarker Profiles of the d-Amino Acid Oxidase Inhibitors Sodium Benzoate and PGM030756

Howley, E., Bestwick, M., Fradley, R. L., Harrison, H., Leveridge, M., Okada, K., Fieldhouse, C., Farnaby, W., Canning, H. E., Sykes, A. P., et al. (2017) · Neurochemical Research · doi:10.1007/s11064-017-2367-9 · Cited by 30

The Campylobacter jejuni RacRS two-component system activates the glutamate synthesis by directly upregulating γ-glutamyltranspeptidase (GGT)

van der Stel, A., van Mourik, A., Łaniewski, P., van Putten, J. P. M., Jagusztyn-Krynicka, E. K., & Wösten, M. M. S. M. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.00567 · Cited by 28

Biosynthesis of a Novel Glutamate Racemase Containing a Site-Specific 7-Hydroxycoumarin Amino Acid: Enzyme–Ligand Promiscuity Revealed at the Atomistic Level

Dean, S. F., Whalen, K. L., & Spies, M. A. (2015) · ACS Central Science · doi:10.1021/acscentsci.5b00211 · Cited by 26

Beta-amyloid oligomers induce early loss of presynaptic proteins in primary neurons by caspase-dependent and proteasome-dependent mechanisms

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Domain-Based Identification and Analysis of Glutamate Receptor Ion Channels and Their Relatives in Prokaryotes

Ger, M.-F., Rendon, G., Tilson, J. L., & Jakobsson, E. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012827 · Cited by 23

Glutamate Transporters in the Blood-Brain Barrier

Helms, H. C. C., Nielsen, C. U., Waagepetersen, H. S., & Brodin, B. (2017) · Advances in neurobiology · doi:10.1007/978-3-319-55769-4_15 · Cited by 21

Glutamatergic response to a low load working memory paradigm in the left dorsolateral prefrontal cortex in patients with mild cognitive impairment: a functional magnetic resonance spectroscopy study

Vijayakumari, A. A., Menon, R. N., Thomas, B., Arun, T. M., Mohanan, N., & Kesavadas, C. (2019) · Brain Imaging and Behavior · doi:10.1007/s11682-019-00122-7 · Cited by 20

How Glutamate Is Managed by the Blood-Brain BarrierPreprint

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Treponema denticola cystalysin exhibits significant alanine racemase activity accompanied by transamination: mechanistic implications

Bertoldi, M., Cellini, B., Paiardini, A., di Salvo, M. L., & BORRIVOLTATTORNI, C. (2003) · Biochemical Journal · doi:10.1042/bj20020875 · Cited by 19

Brain d-amino acids: a novel class of neuromodulators

Mothet, J., & Snyder, S. H. (2012) · Amino Acids · doi:10.1007/s00726-012-1403-y · Cited by 18

Investigation of the Essentiality of Glutamate Racemase in Mycobacterium smegmatis

Li, Y., Mortuza, R., Milligan, D. L., Tran, S. L., Strych, U., Cook, G. M., & Krause, K. L. (2014) · Journal of Bacteriology · doi:10.1128/jb.02090-14 · Cited by 18

Regulatory responses to an oral d -glutamate load: formation of d -pyrrolidone carboxylic acid in humans

Raj, D. S., Langford, M. P., Krueger, S., Shelton, M., & Welbourne, T. (2001) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.2001.280.2.e214 · Cited by 16

The Chain of Chirality Transfer as Determinant of Brain Functional Laterality. Breaking the Chirality Silence: Search for New Generation of Biomarkers; Relevance to Neurodegenerative Diseases, Cognitive Psychology, and Nutrition Science

Dyakin, V. V., Lucas, J., Dyakina‐Fagnano, N. V., & Posner, E. V. (2017) · Neurology and Neuroscience Research · doi:10.24983/scitemed.nnr.2017.00028 · Cited by 15

Isolation of themurIgene fromBrevibacterium lactofermentumATCC 13869 encoding d-glutamate racemase

Malathi, K. C., Wachi, M., & Nagai, K. (1999) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1999.tb13619.x · Cited by 13

Recombinant expression, purification and characterisation of the native glutamate racemase from Lactobacillus plantarum NC8

Böhmer, N., Dautel, A., EISELE, T. A., & Fischer, L. (2012) · Protein Expression and Purification · doi:10.1016/j.pep.2012.11.012 · Cited by 12

Chirality and drugs used to treat psychiatric disorders

Baker, G. B., Prior, T. I., & Coutts, R. T. (2002) · Journal of Psychiatry and Neuroscience · doi:10.1139/jpn.0260 · Cited by 11

Generation of specific antisera directed against D-amino acids: focus on the neuroanatomical distribution of D-glutamate and other D-amino acids

Coveñas, R., Mangas, A., Sánchez, M. L., Cadena, D., Husson, M., & Geffard, M. (2018) · Folia Histochemica et Cytobiologica · doi:10.5603/fhc.a2017.0023 · Cited by 8

Isolation of the murI gene from Brevibacterium lactofermentum ATCC 13869 encoding ?-glutamate racemase

Malathi, K. C. (1999) · FEMS Microbiology Letters · doi:10.1016/s0378-1097(99)00192-5 · Cited by 2

Microbiota–gut–brain axis and its therapeutic applications in neurodegenerative diseases

Loh, J. S., Mak, W. Q., Tan, L. K. S., Ng, C. X., Chan, H. H., Yeow, S. H., Foo, J. B., Ong, Y. S., How, C. W., & Khaw, K. Y. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01743-1 · Cited by 1,193

Regulation of Neurotransmitters by the Gut Microbiota and Effects on Cognition in Neurological Disorders

Chen, Y., Xu, J., & Chen, Y. (2021) · Nutrients · doi:10.3390/nu13062099 · Cited by 917

Gut Bacteria and Neurotransmitters

Dicks, L. M. T. (2022) · Microorganisms · doi:10.3390/microorganisms10091838 · Cited by 482

Brain–gut–microbiota axis in depression: A historical overview and future directions

Chang, L., Wei, Y., & Hashimoto, K. (2022) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2022.02.004 · Cited by 407

The Microbiota–Gut–Brain Axis and Alzheimer’s Disease: Neuroinflammation Is to Blame?

Megur, A., Baltriukienė, D., Bukelskienė, V., & Burokas, A. (2020) · Nutrients · doi:10.3390/nu13010037 · Cited by 323

The Gut Microbiota and Alzheimer’s Disease

Jiang, C., Li, G., Huang, P., Liu, Z., & Zhao, B. (2017) · Journal of Alzheimer's Disease · doi:10.3233/jad-161141 · Cited by 852

The Influence of the Gut Microbiota on Alzheimer's Disease: A Narrative Review

Yin, J.-T., Xu, X., Jin, C.-Y., Yuan, X., & Wang, X. (2023) · Journal of Integrative Neuroscience · doi:10.31083/j.jin2202038 · Cited by 15

The role of gut microbiota in the pathogenesis of Alzheimer’s disease: A review of the literature

Steć, G., Brzyska, A., Siemianowski, J., Kotnis, W., Pawlak, M., Prolejko, S., Gajęcki, B., Kopala, J., Kucharski, T., & Buczek, W. (2025) · Medical Science · doi:10.54905/disssi.v29i163.e165ms3654

The impact of the microbiota-gut-brain axis on Alzheimer’s disease pathophysiology

Doifode, T., Giridharan, V. V., Generoso, J. S., Bhatti, G., Collodel, A., Schulz, P. E., Forlenza, O. V., & Barichello, T. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2020.105314 · Cited by 347

The Role of Gut Microbiota in the Pathogenesis of Alzheimer’s Disease

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