ArticleFEBS letters2011
Identification of endogenous ligands bound to bacterially expressed human and E. coli dihydrofolate reductase by 2D NMR.
Article in FEBS letters, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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Who cites it
12 citing papers in PubMed, 15 citations in OpenAlex.
- Protein Dynamics and Enzymatic Catalysis.The journal of physical chemistry. B · 2023Review
- NADP(H)-dependent biocatalysis without adding NADP(H).Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Modeling of Hidden Structures Using Sparse Chemical Shift Data from NMR Relaxation Dispersion.Biophysical journal · 2021Article
- Extending the Detection Limit in Fragment Screening of Proteins Using Reverse Micelle Encapsulation.ACS chemical biology · 2019Article
- Entropy in molecular recognition by proteins.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Systematic Analysis of Intracellular-targeting Antimicrobial Peptides, Bactenecin 7, Hybrid of Pleurocidin and Dermaseptin, Proline-Arginine-rich Peptide, and Lactoferricin B, by Using Escherichia coli Proteome Microarrays.Molecular & cellular proteomics : MCP · 2016Article
- The Effect of Protein Mass Modulation on Human Dihydrofolate Reductase.Biochemistry · 2016Article
- Cofactor-Mediated Conformational Dynamics Promote Product Release From Escherichia coli Dihydrofolate Reductase via an Allosteric Pathway.Journal of the American Chemical Society · 2015Article
- Preliminary joint X-ray and neutron protein crystallographic studies of ecDHFR complexed with folate and NADP+.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Side chain conformational averaging in human dihydrofolate reductase.Biochemistry · 2014Article
- Divergent evolution of protein conformational dynamics in dihydrofolate reductase.Nature structural & molecular biology · 2013Article
- Side-chain conformational heterogeneity of intermediates in the Escherichia coli dihydrofolate reductase catalytic cycle.Biochemistry · 2013Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Dihydrofolate reductase (DHFR) is a well-studied drug target and a paradigm for understanding enzyme catalysis. Preparation of pure DHFR samples, in defined ligand-bound states, is a prerequisite for in vitro studies and drug discovery efforts. We use NMR spectroscopy to monitor ligand content of human and Escherichia coli DHFR (ecDHFR), which bind different co-purifying ligands during expression in bacteria. An alternate purification strategy yields highly pure DHFR complexes, containing only the desired ligands, in the quantities required for structural studies. Interestingly, ecDHFR is bound to endogenous THF while human DHFR is bound to NADP. Consistent with these findings, a designed "humanized" mutant of ecDHFR switches binding specificity in the cell.
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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.