ArticleNature communications2019
Design strategy for serine hydroxymethyltransferase probes based on retro-aldol-type reaction.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers, 1 of them a synthesis that pooled it.
What it found
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Who cites it
22 citing papers in PubMed, 1 synthesis or guideline pooled it, 42 citations in OpenAlex.
- A systematic review of omics discovery studies to identify pertinent metabolic pathways for locally advanced rectal cancer in response to neoadjuvant chemoradiotherapy.Metabolomics : Official journal of the Metabolomic Society · 2025Pooled it
- Chemical basis of fluorogenic substrate probe design: revisiting the past to discover the new in biochemistry.RSC chemical biology · 2026Review
- Comparative binding and activity analysis of known serine hydroxymethyltransferase inhibitors in biochemical assays.RSC advances · 2026Article
- Stimuli-Responsive Silsesquioxane Nanozymes for Organocatalysis in Water and Prodrug Activation in Cells.Angewandte Chemie (International ed. in English) · 2026Article
- The sulfur-related metabolic status ofVirulence · 2025Article
- Mitochondrial Metabolomics in Cancer: Mass Spectrometry-Based Approaches for Metabolic Rewiring Analysis and Therapeutic Discovery.Metabolites · 2025Review
- Subtractive proteo-genomics and model-based druggability analyses prioritized nitrate reductase-A subunit-α as potential therapeutic target against MDR pneumonia; a homology-based approach.BMC microbiology · 2025Article
- Universality of critical active site glutamate as an acid-base catalyst in serine hydroxymethyltransferase function.Chemical science · 2024Article
- Synergistic Antibacterial Efficacy of Melittin in Combination with Oxacillin against Methicillin-ResistantMicroorganisms · 2023Article
- Revealing protonation states and tracking substrate in serine hydroxymethyltransferase with room-temperature X-ray and neutron crystallography.Communications chemistry · 2023Article
- Characterization of thermostable serine hydroxymethyltransferase for β-hydroxy amino acids synthesis.Amino acids · 2023Article
- Serine-associated one-carbon metabolic reprogramming: a new anti-cancer therapeutic strategy.Frontiers in oncology · 2023Review
- Dihydrofolate reductase, thymidylate synthase, and serine hydroxy methyltransferase: successful targets against some infectious diseases.Molecular biology reports · 2022Review
- Article
- A Review of Small-Molecule Inhibitors of One-Carbon Enzymes: SHMT2 and MTHFD2 in the Spotlight.ACS pharmacology & translational science · 2021Review
- Therapeutic targeting of the mitochondrial one-carbon pathway: perspectives, pitfalls, and potential.Oncogene · 2021Review
- Metabolic supervision by PPIP5K, an inositol pyrophosphate kinase/phosphatase, controls proliferation of the HCT116 tumor cell line.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structural basis for selective inhibition of human serine hydroxymethyltransferase by secondary bile acid conjugate.iScience · 2021Article
- Plasma metabolites associated with chronic kidney disease and renal function in adults from the Baltimore Longitudinal Study of Aging.Metabolomics : Official journal of the Metabolomic Society · 2021Article
- Impaired folate binding of serine hydroxymethyltransferase 8 from soybean underlies resistance to the soybean cyst nematode.The Journal of biological chemistry · 2020Article
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Serine hydroxymethyltransferase (SHMT) is an enzyme that catalyzes the reaction that converts serine to glycine. It plays an important role in one-carbon metabolism. Recently, SHMT has been shown to be associated with various diseases. Therefore, SHMT has attracted attention as a biomarker and drug target. However, the development of molecular probes responsive to SHMT has not yet been realized. This is because SHMT catalyzes an essential yet simple reaction; thus, the substrates that can be accepted into the active site of SHMT are limited. Here, we focus on the SHMT-catalyzed retro-aldol reaction rather than the canonical serine-glycine conversion and succeed in developing fluorescent and
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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.