ReviewProtein science : a publication of the Protein Society2017
A cell is more than the sum of its (dilute) parts: A brief history of quinary structure.
Review in Protein science : a publication of the Protein Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
67 citing papers in PubMed.
- Highly dynamic assemblies of glycolytic enzymes by quinary determinants.Nature communications · 2026Article
- Article
- In Vivo Ribosome-Amplified MetaBOlism, RAMBO, Effect Observed by Real Time Pulse Chase, RTPC, NMR Spectroscopy.Biochemistry · 2025Article
- Molecular determinants of condensate composition.Molecular cell · 2025Review
- Higher-order transient structures and the principle of dynamic connectivity in membrane signaling.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- RNA Structure: Past, Future, and Gene Therapy Applications.International journal of molecular sciences · 2024Review
- A quantitative intracellular peptide binding assay reveals recognition determinants and context dependence of short linear motifs.bioRxiv : the preprint server for biology · 2024Article
- Ribosome External Electric Field Regulates Metabolic Enzyme Activity: The RAMBO Effect.The journal of physical chemistry. B · 2024Article
- Amino Acids and Their Biological Derivatives Modulate Protein-Protein Interactions in an Additive Way.The journal of physical chemistry letters · 2024Article
- 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
- Using NMR-detected hydrogen-deuterium exchange to quantify protein stability in cosolutes, under crowded conditionsMagnetic resonance letters · 2023Review
- Intrinsically Disordered Flanking Regions Increase the Affinity of a Transcriptional Coactivator Interaction across Vertebrates.Biochemistry · 2023Article
- Intracellular environment can change protein conformational dynamics in cells through weak interactions.Science advances · 2023Article
- Progress toward Proteome-Wide Photo-Cross-Linking to Enable Residue-Level Visualization of Protein Structures and Networks In Vivo.Analytical chemistry · 2023Article
- Review
- Revitalizing an important field in biophysics: The new frontiers of molecular crowding.Frontiers in molecular biosciences · 2023Article
- The Protein Unfolded State: One, No One and One Hundred Thousand.Journal of the American Chemical Society · 2022Review
- Review
- Resolving molecular diffusion and aggregation of antibody proteins with megahertz X-ray free-electron laser pulses.Nature communications · 2022Article
7 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Most knowledge of protein structure and function is derived from experiments performed with purified protein resuspended in dilute, buffered solutions. However, proteins function in the crowded, complex cellular environment. Although the first four levels of protein structure provide important information, a complete understanding requires consideration of quinary structure. Quinary structure comprises the transient interactions between macromolecules that provides organization and compartmentalization inside cells. We review the history of quinary structure in the context of several metabolic pathways, and the technological advances that have yielded recent insight into protein behavior in living cells. The evidence demonstrates that protein behavior in isolated solutions deviates from behavior in the physiological environment.
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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.