ArticleProceedings of the National Academy of Sciences of the United States of America2000
An essential intermediate in the folding of dihydrofolate reductase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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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.
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Who cites it
21 citing papers in PubMed, 45 citations in OpenAlex.
- Quantifying protein unfolding kinetics with a high-throughput microfluidic platform.Cell systems · 2026Article
- Kinetic Dissection of the Reaction of Human GDP-l-Fucose Synthase.ACS catalysis · 2025Article
- How synonymous mutations alter enzyme structure and function over long timescales.Nature chemistry · 2023Article
- Differentiating between the sequence of structural events on alternative pathways of folding of a heterodimeric protein.Protein science : a publication of the Protein Society · 2022Article
- FtsH degrades dihydrofolate reductase by recognizing a partially folded species.Protein science : a publication of the Protein Society · 2022Article
- Protein folding in vitro and in the cell: From a solitary journey to a team effort.Biophysical chemistry · 2022Review
- The Right-Handed Parallel β-Helix Topology ofBiomolecules · 2021Article
- Behavior of Proteins under Pressure from Experimental Pressure-Dependent Structures.The journal of physical chemistry. B · 2021Article
- Cotranslational folding allows misfolding-prone proteins to circumvent deep kinetic traps.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- How cooperative are protein folding and unfolding transitions?Protein science : a publication of the Protein Society · 2016Review
- Structure of a partially unfolded form of Escherichia coli dihydrofolate reductase provides insight into its folding pathway.Protein science : a publication of the Protein Society · 2014Article
- Folding pathway of a multidomain protein depends on its topology of domain connectivity.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Protein mass-modulated effects in the catalytic mechanism of dihydrofolate reductase: beyond promoting vibrations.Journal of the American Chemical Society · 2014Article
- Practical approaches to protein folding and assembly: spectroscopic strategies in thermodynamics and kinetics.Methods in enzymology · 2009Article
- The rough energy landscape of superfolder GFP is linked to the chromophore.Journal of molecular biology · 2007Article
- The folding pathway of T4 lysozyme: an on-pathway hidden folding intermediate.Journal of molecular biology · 2007Article
- A protein folding pathway with multiple folding intermediates at atomic resolution.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Multiple folding pathways of the SH3 domain.Biophysical journal · 2004Article
- Integrating folding kinetics and protein function: biphasic kinetics and dual binding specificity in a WW domain.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- An amino acid code for protein folding.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The folding of Escherichia coli dihydrofolate reductase was examined at pH 7.8 and 15 degrees C by using stopped-flow fluorescence and absorbance spectroscopies. The formation of a highly fluorescent intermediate occurs with relaxation times ranging between 142 and 343 msec, whereas stopped-flow absorbance spectroscopy using methotrexate binding assays shows a distinct lag phase during these time frames for the native state. The lag in absorbance kinetics and the lack of fast-track folding events indicate that the formation of this ensemble of intermediates is an obligatory step in the folding reaction.
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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.