ReviewFrontiers in molecular biosciences2018
The Energy Landscape of Human Serine Racemase.
Review in Frontiers in molecular biosciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
20 citing papers in PubMed, 36 citations in OpenAlex.
- Prenatal Exposure to Lipopolysaccharide or Valproate Leads to Abnormal Accumulation of the NMDA Receptor Agonist D-Aspartate in the Adolescent Rat Brain.Journal of neurochemistry · 2025Article
- α-Hydrazino Acids Inhibit Pyridoxal Phosphate-Dependent Decarboxylases via "Catalytically Correct" Ketoenamine Tautomers: A Special Motif for Chemical Biology and Drug Discovery?ACS catalysis · 2025Article
- Evolution and Functional Diversification of Serine Racemase Homologs in Bacteria.Journal of molecular evolution · 2025Article
- Modulating the serine metabolism in human differentiated astrocytes: an integrated multi omics approach.Frontiers in cellular neuroscience · 2025Article
- Phosphoserine Aminotransferase Pathogenetic Variants in Serine Deficiency Disorders: A Functional Characterization.Biomolecules · 2023Article
- L-serine biosynthesis in the human central nervous system: Structure and function of phosphoserine aminotransferase.Protein science : a publication of the Protein Society · 2023Article
- Information-Rich, Dual-FunctionJournal of the American Chemical Society · 2023Article
- Integrating human brain proteomic data with genome-wide association study findings identifies novel brain proteins in substance use traits.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2022Article
- Human Serine Racemase Weakly Binds the Third PDZ Domain of PSD-95.International journal of molecular sciences · 2022Article
- Tyrosine 121 moves revealing a ligandable pocket that couples catalysis to ATP-binding in serine racemase.Communications biology · 2022Article
- Integrated Bioinformatics Analysis of Serine Racemase as an Independent Prognostic Biomarker in Endometrial Cancer.Frontiers in genetics · 2022Article
- Structural Basis for Allostery in PLP-dependent Enzymes.Frontiers in molecular biosciences · 2022Review
- d-Amino Acids and pLG72 in Alzheimer's Disease and Schizophrenia.International journal of molecular sciences · 2021Review
- A Novel Assay for Phosphoserine Phosphatase Exploiting Serine Acetyltransferase as the Coupling Enzyme.Life (Basel, Switzerland) · 2021Article
- Biochemical and Biophysical Characterization of Recombinant Human 3-Phosphoglycerate Dehydrogenase.International journal of molecular sciences · 2021Article
- Racemization in Post-Translational Modifications Relevance to Protein Aging, Aggregation and Neurodegeneration: Tip of the Iceberg.Symmetry · 2021Article
- Roles of N-Methyl-D-Aspartate Receptors (NMDARs) in Epilepsy.Frontiers in molecular neuroscience · 2021Review
- Yin and Yang in Post-Translational Modifications of Human D-Amino Acid Oxidase.Frontiers in molecular biosciences · 2021Article
- d-amino Acids in Health and Disease: A Focus on Cancer.Nutrients · 2019Review
- Human Serine Racemase: Key Residues/Active Site Motifs and Their Relation to Enzyme Function.Frontiers in molecular biosciences · 2019Review
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human serine racemase is a pyridoxal 5'-phosphate (PLP)-dependent dimeric enzyme that catalyzes the reversible racemization of L-serine and D-serine and their dehydration to pyruvate and ammonia. As D-serine is the co-agonist of the N-methyl-D-aspartate receptors for glutamate, the most abundant excitatory neurotransmitter in the brain, the structure, dynamics, function, regulation and cellular localization of serine racemase have been investigated in detail. Serine racemase belongs to the fold-type II of the PLP-dependent enzyme family and structural models from several orthologs are available. The comparison of structures of serine racemase co-crystallized with or without ligands indicates the presence of at least one open and one closed conformation, suggesting that conformational flexibility plays a relevant role in enzyme regulation. ATP, Mg
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.