ReviewInternational journal of molecular sciences2019
A History of Molecular Chaperone Structures in the Protein Data Bank.
Review in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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
22 citing papers in PubMed.
- The function of chaperones in the radioresistance of glioblastoma: a new insight into the current knowledge.Brain tumor pathology · 2025Review
- The function of chaperones in the radioresistance of glioblastoma: a new insight into the current knowledge.Brain tumor pathology · 2025Review
- Extracellular vesicles from cartilage progenitors stimulate type II collagen expression and wound healing in meniscal cells.Journal of orthopaedic research : official publication of the Orthopaedic Research Society · 2025Article
- A temperature-responsive regulator that enhances virulence in the kiwifruit canker pathogenComputational and structural biotechnology journal · 2025Article
- Review
- Chaperones-A New Class of Potential Therapeutic Targets in Alzheimer's Disease.International journal of molecular sciences · 2024Review
- Enzymatic and synthetic regulation of polypeptide folding.Chemical science · 2024Review
- Heat Shock Proteins and Breast Cancer.International journal of molecular sciences · 2024Review
- Chaperones vs. oxidative stress in the pathobiology of ischemic stroke.Frontiers in molecular neuroscience · 2024Review
- Exploring Scoring Function Space: Developing Computational Models for Drug Discovery.Current medicinal chemistry · 2024Review
- The HSP40 family chaperone isoform DNAJB6b prevents neuronal cells from tau aggregation.BMC biology · 2023Article
- Heat Shock Proteins (HSPs) and Cardiovascular Complications of Obesity: Searching for Potential Biomarkers.Current issues in molecular biology · 2023Review
- Uncovering the Role of Natural and Synthetic Small Molecules in Counteracting the Burden of α-Synuclein Aggregates and Related Toxicity in Different Models of Parkinson's Disease.International journal of molecular sciences · 2023Review
- MicroRNAs in Age-Related Proteostasis and Stress Responses.Non-coding RNA · 2023Review
- Single-molecule mechanical studies of chaperones and their clients.Biophysics reviews · 2022Review
- Implications of sperm heat shock protein 70-2 in bull fertility.Veterinary world · 2022Review
- Heat Shock Proteins and Ferroptosis.Frontiers in cell and developmental biology · 2022Review
- Viral Induced Protein Aggregation: A Mechanism of Immune Evasion.International journal of molecular sciences · 2021Review
- At elevated temperatures, heat shock protein genes show altered ratios of different RNAs and expression of new RNAs, including several novel HSPB1 mRNAs encoding HSP27 protein isoforms.Experimental and therapeutic medicine · 2021Article
- Molecular Chaperones and Proteolytic Machineries Regulate Protein Homeostasis In Aging Cells.Cells · 2020Review
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
Thirty years ago a class of proteins was found to prevent the aggregation of Rubisco. These proteins' ability to prevent unwanted associations led to their being called chaperones. These chaperone proteins also increased in expression as a response to heat shock, hence their label as heat shock proteins (Hsps). However, neither label encompasses the breadth of these proteins' functional capabilities. The term "unfoldases" has been proposed, as this basic function is shared by most members of this protein family. Onto this is added specializations that allow the different family members to perform various cellular functions. This current article focuses on the resolved structural bases for these functions. It reviews the currently available molecular structures in the Protein Data Bank for several classes of Hsps (Hsp60, Hsp70, Hsp90, and Hsp104). When possible, it discusses the complete structures for these proteins, and the types of molecular machines to which they have been assigned. The structures of domains and the associated functions are discussed in order to illustrate the rationale for the proposed unfoldase function.
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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.