A History of Molecular Chaperone Structures in the Protein Data Bank

Bascos, Neil Andrew D.; Landry, Samuel J.

doi:10.3390/ijms20246195

Cited by 32 publications

(25 citation statements)

References 63 publications

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“…Chaperones belong to five major families that are classified on the basis of their approximate molecular mass and function: small heat shock proteins (sHSPs), HSP60, HSP70, HSP90, and HSP100 (Park and Seo, 2015;Bascos and Landry, 2019). Among them, one of the chaperones most extensively studied in different organisms is HSP70.…”

Section: Introduction Protein Folding and Chaperonesmentioning

confidence: 99%

HOP, a Co-chaperone Involved in Response to Stress in Plants

et al. 2020

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Protein folding is an essential step for protein functionality. In eukaryotes this process is carried out by multiple chaperones that act in a cooperative manner to maintain the proteome homeostasis. Some of these chaperones are assisted during protein folding by different co-chaperones. One of these co-chaperones is HOP, the HSP70-HSP90 organizing protein. This assistant protein, due to its importance, has been deeply analyzed in other eukaryotes, but its function has only recently started to be envisaged in plants. In this kingdom, the role of HOP has been associated to plant response to different cellular, biotic and abiotic stresses. In this article, we analyze the current knowledge about HOP in eukaryotes, paying a special attention to the recently described roles of HOP in plants. In addition, we discuss the recent breakthroughs in the field and the possible new avenues for the study of plant HOP proteins in the future.

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Section: Introduction Protein Folding and Chaperonesmentioning

confidence: 99%

HOP, a Co-chaperone Involved in Response to Stress in Plants

et al. 2020

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“…HSP70 and small HSP use modular “clamps” to protect the extended hydrophobic structure in the target protein. HSP60 adopts barrel “Anfinsen” cage structure for isolation and folding of target protein ( Bascos and Landry, 2019 ).…”

Section: Heat Shock Proteins and Ferroptosismentioning

confidence: 99%

Heat Shock Proteins and Ferroptosis

Liu

Zhou

et al. 2022

Front. Cell Dev. Biol.

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Ferroptosis is a new form of regulatory cell death named by Dixon in 2012, which is characterized by the accumulation of lipid peroxides and iron ions. Molecular chaperones are a class of evolutionarily conserved proteins in the cytoplasm. They recognize and bind incompletely folded or assembled proteins to help them fold, transport or prevent their aggregation, but they themselves do not participate in the formation of final products. As the largest number of molecular chaperones, heat shock proteins can be divided into five families: HSP110 (HSPH), HSP90 (HSPC), HSP70 (HSPA), HSP40 (DNAJ) and small heat shock proteins (HSPB). Different heat shock proteins play different roles in promoting or inhibiting ferroptosis in different diseases. It is known that ferroptosis is participated in tumors, nervous system diseases, renal injury and ischemia-reperfusion injury. However, there are few reviews about the relationship of heat shock proteins and ferroptosis. In this study, we systematically summarize the roles of heat shock proteins in the occurrence of ferroptosis, and predict the possible mechanisms of different families of heat shock proteins in the development of ferroptosis.

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“…Chaperone proteins are a complex family of proteins with various structural characteristics [11,12]. Because chaperone proteins provide cellular tolerance to environmental stressors, the cell stress response, more often known as HSPs, refers to the majority of the chaperone protein family's members [13].…”

Section: Background On Hsps As Molecular Chaperones Proteinsmentioning

confidence: 99%

Implications of sperm heat shock protein 70-2 in bull fertility

et al. 2022

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Heat shock protein 70 (HSP70) is one of the most abundant chaperone proteins. Their function is well documented in facilitating the protein synthesis, translocation, de novo folding, and ordering of multiprotein complexes. HSP70 in bovine consists of four genes: HSP70-1, HSP70-2, HSP70-3, and HSP70-4. HSP70-2 was found to be involved in fertility. Current knowledge implicates HSP70-2 in sperm quality, sperm capacitation, sperm–egg recognition, and fertilization essential for bull reproduction. HSP70-2 is also involved in the biological processes of spermatogenesis, as it protects cells from the effects of apoptosis and oxidative stress. Fertilization success is not only determined by the amount of sperm found in the female reproductive tract but also by the functional ability of the sperm. However, subfertility is more likely to be associated with changes in sperm molecular dynamics not detectable using conventional methods. As such, molecular analyses and omics methods have been developed to monitor crucial aspects of sperm molecular morphology that are important for sperm functions, which are the objectives of this review.

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A History of Molecular Chaperone Structures in the Protein Data Bank

Cited by 32 publications

References 63 publications

HOP, a Co-chaperone Involved in Response to Stress in Plants

HOP, a Co-chaperone Involved in Response to Stress in Plants

Heat Shock Proteins and Ferroptosis

Implications of sperm heat shock protein 70-2 in bull fertility

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