ArticleJournal of molecular biology2014
The extracellular protein VlsE is destabilized inside cells.
Article in Journal of molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 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
34 citing papers in PubMed, 81 citations in OpenAlex.
- Mimetics of in-cell and subcellular crowding and solvation for protein folding.Biochemical Society transactions · 2026Review
- Crowding-induced stabilization and destabilization in a single protein.Protein science : a publication of the Protein Society · 2025Article
- Weak, specific chemical interactions dictate barnase stability in diverse cellular environments.Protein science : a publication of the Protein Society · 2025Article
- 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
- Cellular ATP Levels Determine the Stability of a Nucleotide Kinase.Frontiers in molecular biosciences · 2021Article
- In-cell destabilization of a homodimeric protein complex detected by DEER spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- An in vitro mimic of in-cell solvation for protein folding studies.Protein science : a publication of the Protein Society · 2020Article
- Competition of individual domain folding with inter-domain interaction in WW domain engineered repeat proteins.Physical chemistry chemical physics : PCCP · 2019Article
- Proteins: "Boil 'Em, Mash 'Em, Stick 'Em in a Stew".The journal of physical chemistry. B · 2019Review
- Protein Folding Modulation in Cells Subject to Differentiation and Stress.Frontiers in molecular biosciences · 2019Article
- Heat shock-induced chaperoning by Hsp70 is enabled in-cell.PloS one · 2019Article
- A small single-domain protein folds through the same pathway on and off the ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Towards developing principles of protein folding and dynamics in the cell.Physical biology · 2018Review
- Toward an understanding of biochemical equilibria within living cells.Biophysical reviews · 2018Review
- Exploring the Denatured State Ensemble by Single-Molecule Chemo-Mechanical Unfolding: The Effect of Force, Temperature, and Urea.Journal of molecular biology · 2018Article
- Quinary interactions with an unfolded state ensemble.Protein science : a publication of the Protein Society · 2017Article
- Explicit Incorporation of Hard and Soft Protein-Protein Interactions into Models for Crowding Effects in Protein Mixtures. 2. Effects of Varying Hard and Soft Interactions upon Prototypical Chemical Equilibria.The journal of physical chemistry. B · 2017Article
- Physicochemical code for quinary protein interactions inProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Design and Properties of Genetically Encoded Probes for Sensing Macromolecular Crowding.Biophysical journal · 2017Article
- Protein folding, binding, and droplet formation in cell-like conditions.Current opinion in structural biology · 2017Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
We use U2OS cells as in vivo "test tubes" to study how the same cytoplasmic environment has opposite effects on the stability of two different proteins. Protein folding stability and kinetics were compared by fast relaxation imaging, which combines a temperature jump with fluorescence microscopy of FRET (Förster resonance energy transfer)-labeled proteins. While the stability of the cytoplasmic enzyme PGK (phosphoglycerate kinase) increases in cells, the stability of the cell surface antigen VlsE, which presumably did not evolve for stability inside cells, decreases. VlsE folding also slows down more than PGK folding in cells, relative to their respective aqueous buffer kinetics. Our FRET measurements provide evidence that VlsE is more compact inside cells than in aqueous buffer. Two kinetically distinct protein populations exist inside cells, making a connection with previous in vitro crowding studies. In addition, we confirm previous studies showing that VlsE is stabilized by 150mg/mL of the carbohydrate crowder Ficoll, even though it is destabilized in the cytoplasm relative to aqueous buffer. We propose two mechanisms for the observed destabilization of VlsE in U2OS cells: long-range interactions competing with crowding or shape-dependent crowding favoring more compact states inside the cell over the elongated aqueous buffer native state.
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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.