ArticleBiophysical journal2011
Protein stability and folding kinetics in the nucleus and endoplasmic reticulum of eucaryotic cells.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 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.
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Who cites it
68 citing papers in PubMed, 151 citations in OpenAlex.
- Mimetics of in-cell and subcellular crowding and solvation for protein folding.Biochemical Society transactions · 2026Review
- How Does Genetic Information Enable Life?Bulletin of mathematical biology · 2026Article
- Marginal Stability of the YB1 Cold-Shock Domain in Cells Enables Binding of Multiple Nucleic Acids.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- PHASE SEPARATION TUNES THE STABILITY AND DYNAMICS OF G-QUADRUPLEX AND I-MOTIF DNA IN THE NUCLEI OF LIVING CELLS.bioRxiv : the preprint server for biology · 2025Article
- Exploring the effects of excipients on complex coacervation.Journal of colloid and interface science · 2025Article
- Dynamic Cytoplasm: A Physical Regulator of Enzymatic Function.Biochemistry · 2025Review
- Weak, specific chemical interactions dictate barnase stability in diverse cellular environments.Protein science : a publication of the Protein Society · 2025Article
- Protein misfolding involving entanglements providesa structural explanation for the origin of stretched-exponential refolding kinetics.Science advances · 2025Article
- Simulating Crowding In Vitro: Not an Elusive Goal Any Longer.Sub-cellular biochemistry · 2025Review
- Endogenous Cu(II) Labeling for Distance Measurements on Proteins by EPR.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024Article
- Protein folding and quality control during nuclear transport.Current opinion in cell biology · 2024Review
- Molecular Crowding: The History and Development of a Scientific Paradigm.Chemical reviews · 2024Review
- Exploring the dynamics and structure of PpiB in living Escherichia coli cells using electron paramagnetic resonance spectroscopy.Protein science : a publication of the Protein Society · 2024Article
- Metastable States in the Hinge-Bending Landscape of an Enzyme in an Atomistic Cytoplasm Simulation.The journal of physical chemistry letters · 2024Article
- Using NMR-detected hydrogen-deuterium exchange to quantify protein stability in cosolutes, under crowded conditionsMagnetic resonance letters · 2023Review
- In silico protein dynamics in the human cytoplasm: Partial folding, misfolding, fold switching, and non-native interactions.Protein science : a publication of the Protein Society · 2023Article
- Chemical interactions modulate λProtein science : a publication of the Protein Society · 2023Article
- Protein stability [determination] problems.Frontiers in molecular biosciences · 2022Article
- Disease-Related Protein Variants of the Highly Conserved Enzyme PAPSS2 Show Marginal Stability and Aggregation in Cells.Frontiers in molecular biosciences · 2022Article
- Stabilization and Kinetics of an Adsorbed Protein Depends on the Poly(Biomacromolecules · 2021Article
8 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We measure the stability and folding relaxation rate of phosphoglycerate kinase (PGK) Förster resonance energy transfer (FRET) constructs localized in the nucleus or in the endoplasmic reticulum (ER) of eukaryotic cells. PGK has a more compact native state in the cellular compartments than in aqueous solution. Its native FRET signature is similar to that previously observed in a carbohydrate-crowding matrix, consistent with crowding being responsible for the compact native state of PGK in the cell. PGK folds through multiple states in vitro, but its folding kinetics is more two-state-like in the ER, so the folding mechanism can be modified by intracellular compartments. The nucleus increases PGK stability and folding rate over the cytoplasm and ER, even though the density of crowders in the nucleus is no greater than in the ER or cytoplasm. Nuclear folding kinetics (and to a lesser extent, thermodynamics) vary less from cell to cell than in the cytoplasm or ER, indicating a more homogeneous crowding and chemical environment in the nucleus.
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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.