ReviewInternational journal of molecular sciences2013
The role of short-chain conjugated poly-(R)-3-hydroxybutyrate (cPHB) in protein folding.
Review in International journal of molecular sciences, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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
16 citing papers in PubMed, 29 citations in OpenAlex.
- Animal degradation of microbial storage polyhydroxyalkanoates.Nature ecology & evolution · 2026Article
- Article
- Hunting the Cell CycleLife (Basel, Switzerland) · 2024Article
- Inorganic polyphosphate and ion transport across biological membranes.Biochemical Society transactions · 2024Review
- P3HB from CHFrontiers in bioengineering and biotechnology · 2023Review
- Challenges in Discovering Drugs That Target the Protein-Protein Interactions of Disordered Proteins.International journal of molecular sciences · 2022Review
- Inorganic polyphosphate as an energy source in tumorigenesis.Oncotarget · 2020Article
- Article
- Calcium Regulation of Bacterial Virulence.Advances in experimental medicine and biology · 2020Review
- Effect of poly(3-hydroxyalkanoates) as natural polymers on mesenchymal stem cells.World journal of stem cells · 2019Review
- Survival Mechanisms ofFrontiers in microbiology · 2019Article
- Nontemplate-driven polymers: clues to a minimal form of organization closure at the early stages of living systems.Theory in biosciences = Theorie in den Biowissenschaften · 2015Article
- To be or not to be a poly(3-hydroxybutyrate) (PHB) depolymerase: PhaZd1 (PhaZ6) and PhaZd2 (PhaZ7) of Ralstonia eutropha, highly active PHB depolymerases with no detectable role in mobilization of accumulated PHB.Applied and environmental microbiology · 2014Article
- Gene regulatory and metabolic adaptation processes of Dinoroseobacter shibae DFL12T during oxygen depletion.The Journal of biological chemistry · 2014Article
- Role of β-hydroxybutyrate, its polymer poly-β-hydroxybutyrate and inorganic polyphosphate in mammalian health and disease.Frontiers in physiology · 2014Review
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Poly-(R)-3-hydroxybutyrate (PHB), a linear polymer of R-3-hydroxybutyrate (R-3HB), is a fundamental constituent of biological cells. Certain prokaryotes accumulate PHB of very high molecular weight (10,000 to >1,000,000 residues), which is segregated within granular deposits in the cytoplasm; however, all prokaryotes and all eukaryotes synthesize PHB of medium-chain length (~100-200 residues) which resides within lipid bilayers or lipid vesicles, and PHB of short-chain length (<12 residues) which is conjugated to proteins (cPHB), primarily proteins in membranes and organelles. The physical properties of cPHB indicate it plays important roles in the targeting and folding of cPHB-proteins. Here we review the occurrence, physical properties and molecular characteristics of cPHB, and discuss its influence on the folding and structure of outer membrane protein A (OmpA) of Escherichia coli.
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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.