ReviewCell stress & chaperones2021
Heat shock proteins and the biogenesis of cellular membranes.
Review in Cell stress & chaperones, 2021. 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
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed, 39 citations in OpenAlex.
- Genome-wide identification, characterization, and evolutionary analysis of the HSP70 gene family in rice (Oryza sativa L.).BMC plant biology · 2025Article
- The role of heat shock protein 70 on oocyte apoptosis during vitrification.Open veterinary journal · 2025Review
- Heat shock proteins in hypothermia: a review.Frontiers in molecular biosciences · 2025Review
- Two sexually compatible monokaryons from a heterokaryoticFrontiers in microbiology · 2025Article
- Extremophiles and Extremophilic Behaviour-New Insights and Perspectives.Life (Basel, Switzerland) · 2024Review
- Uncovering key steps in FGF12 cellular release reveals a common mechanism for unconventional FGF protein secretion.Cellular and molecular life sciences : CMLS · 2024Article
- The role of membrane physiology in sHSP Lo18-lipid interaction and lipochaperone activity.Scientific reports · 2024Article
- Heat Shock Proteins (HSPs) and Cardiovascular Complications of Obesity: Searching for Potential Biomarkers.Current issues in molecular biology · 2023Review
- Significant influence of four highly conserved amino-acids in lipochaperon-active sHsps on the structure and functions of the Lo18 protein.Scientific reports · 2023Article
- Human HSP70-escort protein 1 (hHep1) interacts with negatively charged lipid bilayers and cell membranes.Cell stress & chaperones · 2023Article
- Coping with harsh heat environments: molecular adaptation of metabolic depression in the intertidal snail Echinolittorina radiata.Cell stress & chaperones · 2023Article
- Is the lipochaperone activity of sHSP a key to the stress response encoded in its primary sequence?Cell stress & chaperones · 2023Review
- Genome-Wide Analyses of Heat Shock Protein Superfamily Provide New Insights on Adaptation to Sulfide-Rich Environments inInternational journal of molecular sciences · 2022Article
- The interaction of heat shock proteins with cellular membranes: a historical perspective.Cell stress & chaperones · 2021Review
- Comparative transcriptome analysis of Trichoderma reesei reveals different gene regulatory networks induced by synthetic mixtures of glucose and β-disaccharide.Bioresources and bioprocessing · 2021Article
- Human heat shock cognate protein (HSC70/HSPA8) interacts with negatively charged phospholipids by a different mechanism than other HSP70s and brings HSP90 into membranes.Cell stress & chaperones · 2021Article
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 at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The successful function of cells is importantly contributed by lipid membranes that are more than a simple physical barrier. The major components of cellular membranes are lipids, in particular glycerophospholipids, that have the capacity to assemble spontaneously into vesicles containing a lipid bilayer after exposure to an aqueous milieu due to their amphiphilic characteristics. The lipid capacity to form vesicles and encapsulate substrates has been proposed as a fundamental event during the biogenesis of cells. However, the stability of small vesicles is compromised during their expansion into larger and more complex particles. Recent observations by (Cornell et al. Proc Natl Acad Sci U S A 116:17239-17244, 2019) have shown that the insertion of amino acids into rudimentary vesicles could play a stabilizing role that was critical to the formation of early cells. Fatty acids were likely substituted by glycerophospholipids and amino acids replaced by polypeptides during the evolution of protocells. Thus, archaic peptides displaying lipid-binding and membrane-penetrating capacities could have played a key function in the development of current cells. In this regard, heat shock proteins (HSP), particularly the Hsp70 (HSPA) and small HSP (HSPB) families, could have portrayed that role. Indeed, bacterial DnaK is closest in sequence to the earliest members of the Hsp70 family and inserts into lipid membranes spontaneously. Moreover, extensive studies by the Vigh group have shown that, certainly, Hsp70s stabilize membranes. Thus, the ability of ancestral HSP70s and small HSPs to associate with lipids and stabilize membranes could have been a fundamental event in the genesis of cells.
Indexed as
Identifiers
What OpenQuestion holds
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.