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Journal articles on the topic 'Chaperons'

Author: Grafiati

Published: 4 June 2021

Last updated: 26 July 2025

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1

Makarenko, M., D. Hovsyeyev, and L. Sydoryk. "Chaperonin as the normal controls and pathological anti-stress response in the human reproductive system." HEALTH OF WOMAN, no. 5(111) (June 20, 2016): 126–29. http://dx.doi.org/10.15574/hw.2016.111.126.

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Different kinds of physiological stress cause mass changes in the cells, including the changes in the structure and function of the protein complexes and in separate molecules. The protein functions is determined by its folding (the spatial conclusion), which depends on the functioning of proteins of thermal shock- molecular chaperons (HSPs) or depends on the stress proteins, that are high-conservative; specialized proteins that are responsible for the correct proteinaceous folding. The family of the molecular chaperones/ chaperonins/ Hsp60 has a special place due to the its unique properties

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2

Chen, Chih-Ling, Chien-Nan Lee, Yin-Hsiu Chien, Wuh-Liang Hwu, Tung-Ming Chang, and Ni-Chung Lee. "Novel Compound Heterozygous Variants in TBCD Gene Associated with Infantile Neurodegenerative Encephalopathy." Children 8, no. 12 (2021): 1140. http://dx.doi.org/10.3390/children8121140.

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Mutations in tubulin-specific chaperon D (TBCD), the gene encoding one of the co-chaperons required for the assembly and disassembly of the α/β-tubulin heterodimers, have been reported to cause perturbed microtubule dynamics, resulting in debilitating early-onset progressive neurodegenerative disorder. Here, we identified two novel TBCD variants, c.1340C>T (p.Ala447Val), and c.817+2T>C, presented as compound heterozygotes in two affected siblings born to unaffected carrier parents. Clinical features included early-onset neurodegeneration, failure to thrive, respiratory failure, hypotonia

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3

Morange, M. "Protéines chaperons." médecine/sciences 16, no. 5 (2000): 630. http://dx.doi.org/10.4267/10608/1706.

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4

Mendre, Christiane, and Bernard Mouillac. "Chaperons pharmacologiques." médecine/sciences 26, no. 6-7 (2010): 627–35. http://dx.doi.org/10.1051/medsci/2010266-7627.

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5

Germain, Dominique P., Karelle Benistan, and Lucia Echevarria. "Les chaperons pharmacologiques." médecine/sciences 29, no. 6-7 (2013): 579–82. http://dx.doi.org/10.1051/medsci/2013296009.

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6

Barouki, Robert. "Les chaperons de l’évolution." médecine/sciences 18, no. 12 (2002): 1200–1201. http://dx.doi.org/10.1051/medsci/200218121200.

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7

Pascoalino, Bruno, Gülcin Dindar, João P. Vieira-da-Rocha, Carlos Renato Machado, Christian J. Janzen, and Sergio Schenkman. "Characterization of two different Asf1 histone chaperones with distinct cellular localizations and functions in Trypanosoma brucei." Nucleic Acids Research 42, no. 5 (2013): 2906–18. http://dx.doi.org/10.1093/nar/gkt1267.

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Abstract The anti-silencing function protein 1 (Asf1) is a chaperone that forms a complex with histones H3 and H4 facilitating dimer deposition and removal from chromatin. Most eukaryotes possess two different Asf1 chaperones but their specific functions are still unknown. Trypanosomes, a group of early-diverged eukaryotes, also have two, but more divergent Asf1 paralogs than Asf1 of higher eukaryotes. To unravel possible different functions, we characterized the two Asf1 proteins in Trypanosoma brucei. Asf1A is mainly localized in the cytosol but translocates to the nucleus in S phase. In con

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8

Piacentini, Mirella. "Le Petit Chaperon Uf de Jean-Claude Grumberg : écrire pour « alerter les chaperons d’aujourd’hui »." Recherches & travaux, no. 87 (December 1, 2015): 105–16. http://dx.doi.org/10.4000/recherchestravaux.787.

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9

Large, Andrew T., Martin D. Goldberg, and Peter A. Lund. "Chaperones and protein folding in the archaea." Biochemical Society Transactions 37, no. 1 (2009): 46–51. http://dx.doi.org/10.1042/bst0370046.

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A survey of archaeal genomes for the presence of homologues of bacterial and eukaryotic chaperones reveals several interesting features. All archaea contain chaperonins, also known as Hsp60s (where Hsp is heat-shock protein). These are more similar to the type II chaperonins found in the eukaryotic cytosol than to the type I chaperonins found in bacteria, mitochondria and chloroplasts, although some archaea also contain type I chaperonin homologues, presumably acquired by horizontal gene transfer. Most archaea contain several genes for these proteins. Our studies on the type II chaperonins of

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10

Fedorov, Alexey N. "Biosynthetic Protein Folding and Molecular Chaperons." Biochemistry (Moscow) 87, S1 (2022): S128—S145. http://dx.doi.org/10.1134/s0006297922140115.

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11

Nau, Jean-Yves. "Protéines chaperons et eau de Jouvence." Revue Médicale Suisse 4, no. 167 (2008): 1780. http://dx.doi.org/10.53738/revmed.2008.4.167.1780.

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12

Li, Xujian, Saisai Liu, Yapeng Wang, Wei Lu, Quanqi Zhang, and Jie Cheng. "Genomic and Transcriptomic Landscape and Evolutionary Dynamics of Heat Shock Proteins in Spotted Sea Bass (Lateolabrax maculatus) under Salinity Change and Alkalinity Stress." Biology 11, no. 3 (2022): 353. http://dx.doi.org/10.3390/biology11030353.

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The heat shock protein (Hsp) superfamily has received accumulated attention because it is ubiquitous and conserved in almost all living organisms and is involved in a wide spectrum of cellular responses against diverse environmental stresses. However, our knowledge about the Hsp co-chaperon network is still limited in non-model organisms. In this study, we provided the systematic analysis of 95 Hsp genes (LmHsps) in the genome of spotted sea bass (Lateolabrax maculatus), an important aquaculture species in China that can widely adapt to diverse salinities from fresh to sea water, and moderatel

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13

Scalia, Federica, Antonella Marino Gammazza, Everly Conway de Macario, Alberto J. L. Macario, and Francesco Cappello. "Myelin Pathology: Involvement of Molecular Chaperones and the Promise of Chaperonotherapy." Brain Sciences 9, no. 11 (2019): 297. http://dx.doi.org/10.3390/brainsci9110297.

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The process of axon myelination involves various proteins including molecular chaperones. Myelin alteration is a common feature in neurological diseases due to structural and functional abnormalities of one or more myelin proteins. Genetic proteinopathies may occur either in the presence of a normal chaperoning system, which is unable to assist the defective myelin protein in its folding and migration, or due to mutations in chaperone genes, leading to functional defects in assisting myelin maturation/migration. The latter are a subgroup of genetic chaperonopathies causing demyelination. In th

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14

Lechuga, Susana, Armando Marino-Melendez, Nayden G. Naydenov, Atif Zafar, Manuel B. Braga-Neto, and Andrei I. Ivanov. "Regulation of Epithelial and Endothelial Barriers by Molecular Chaperones." Cells 13, no. 5 (2024): 370. http://dx.doi.org/10.3390/cells13050370.

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The integrity and permeability of epithelial and endothelial barriers depend on the formation of tight junctions, adherens junctions, and a junction-associated cytoskeleton. The establishment of this junction–cytoskeletal module relies on the correct folding and oligomerization of its protein components. Molecular chaperones are known regulators of protein folding and complex formation in different cellular compartments. Mammalian cells possess an elaborate chaperone network consisting of several hundred chaperones and co-chaperones. Only a small part of this network has been linked, however,

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Scalia, Federica, Alessandra Maria Vitale, Radha Santonocito, Everly Conway de Macario, Alberto J. L. Macario, and Francesco Cappello. "The Neurochaperonopathies: Anomalies of the Chaperone System with Pathogenic Effects in Neurodegenerative and Neuromuscular Disorders." Applied Sciences 11, no. 3 (2021): 898. http://dx.doi.org/10.3390/app11030898.

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The chaperone (or chaperoning) system (CS) constitutes molecular chaperones, co-chaperones, and chaperone co-factors, interactors and receptors, and its canonical role is protein quality control. A malfunction of the CS may cause diseases, known as the chaperonopathies. These are caused by qualitatively and/or quantitatively abnormal molecular chaperones. Since the CS is ubiquitous, chaperonopathies are systemic, affecting various tissues and organs, playing an etiologic-pathogenic role in diverse conditions. In this review, we focus on chaperonopathies involved in the pathogenic mechanisms of

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16

Ghosh, Deepanjan, and Sureshkumar Ramasamy. "Engineering of the Tat pathway and chaperons." Acta Crystallographica Section A Foundations and Advances 73, a2 (2017): C273. http://dx.doi.org/10.1107/s2053273317093007.

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Verma, Saurabh, Gaurav K. Keshri, Manish Sharma, and Asheesh Gupta. "Role of H2S Supplementation on Burn Wound Healing and Molecular Chaperones." Defence Life Science Journal 6, no. 2 (2021): 171–76. http://dx.doi.org/10.14429/dlsj.6.16735.

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Treatment of non-healing burn injuries is a major challenge for the current scientific research. Hydrogen sulfide (H2S) is an endogenous gasotransmitter, which regulates redox homeostasis and cytoprotection during pathophysiological conditions. Similarly, heat shock proteins (HSPs) are molecular chaperones, which also confer cytoprotection during the wound repair process. Notably, the role of H2S as a regulator of HSPs during burn wound healing is still elusive. The present study investigated the effects of H2S supplementation on molecular chaperones during full-thickness, third-degree burn wo

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18

Hervás, Rubén, and Javier Oroz. "Mechanistic Insights into the Role of Molecular Chaperones in Protein Misfolding Diseases: From Molecular Recognition to Amyloid Disassembly." International Journal of Molecular Sciences 21, no. 23 (2020): 9186. http://dx.doi.org/10.3390/ijms21239186.

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Age-dependent alterations in the proteostasis network are crucial in the progress of prevalent neurodegenerative diseases, such as Alzheimer’s, Parkinson’s, or amyotrophic lateral sclerosis, which are characterized by the presence of insoluble protein deposits in degenerating neurons. Because molecular chaperones deter misfolded protein aggregation, regulate functional phase separation, and even dissolve noxious aggregates, they are considered major sentinels impeding the molecular processes that lead to cell damage in the course of these diseases. Indeed, members of the chaperome, such as mol

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19

Barbey, Frédéric, Pierre Monney, and Olivier Dormond. "Molécules chaperons : exemple de la maladie de Fabry." Néphrologie & Thérapeutique 17 (April 2021): S11—S22. http://dx.doi.org/10.1016/j.nephro.2020.02.005.

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20

Bensaude, O. "Chaperons moléculaires et cytosquelette, des archébactéries aux mammifères." médecine/sciences 8, no. 8 (1992): 846. http://dx.doi.org/10.4267/10608/3239.

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21

Martirosova, E. I., T. A. Karpekina, and G. I. El'-Registan. "Enzyme Modification by Natural Chemical Chaperons of Microorganisms." Microbiology 73, no. 5 (2004): 609–15. http://dx.doi.org/10.1023/b:mici.0000044252.10568.08.

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22

Heilman, Samuel C., and Eliezer Witztum. "Patients, chaperons and healers: Enlarging the therapeutic encounter." Social Science & Medicine 39, no. 1 (1994): 133–43. http://dx.doi.org/10.1016/0277-9536(94)90173-2.

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23

Zierer, Bettina K., Matthias Weiwad, Martin Rübbelke, et al. "Aktivatoren des molekularen Chaperons Hsp90 erleichtern geschwindigkeitsbestimmende Konformationsänderungen." Angewandte Chemie 126, no. 45 (2014): 12454–59. http://dx.doi.org/10.1002/ange.201406578.

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24

Ito, Makoto, Kouhei Ohnishi, Yasufumi Hikichi, and Akinori Kiba. "Molecular chaperons and co-chaperons, Hsp90, RAR1, and SGT1 negatively regulate bacterial wilt disease caused by Ralstonia solanacearum in Nicotiana benthamiana." Plant Signaling & Behavior 10, no. 6 (2015): e970410. http://dx.doi.org/10.4161/15592316.2014.970410.

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25

Macario, Alberto J. L., Marianne Lange, Birgitte K. Ahring, and Everly Conway De Macario. "Stress Genes and Proteins in the Archaea." Microbiology and Molecular Biology Reviews 63, no. 4 (1999): 923–67. http://dx.doi.org/10.1128/mmbr.63.4.923-967.1999.

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SUMMARY The field covered in this review is new; the first sequence of a gene encoding the molecular chaperone Hsp70 and the first description of a chaperonin in the archaea were reported in 1991. These findings boosted research in other areas beyond the archaea that were directly relevant to bacteria and eukaryotes, for example, stress gene regulation, the structure-function relationship of the chaperonin complex, protein-based molecular phylogeny of organisms and eukaryotic-cell organelles, molecular biology and biochemistry of life in extreme environments, and stress tolerance at the cellul

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26

Al-Shafai,, Mashael, Abdelilah Arredouani,, Hamid Mesaeli,, Nasrin Mesaeli,, and Khaled Machaca. "Regulation of store-operated channels by endoplasmic reticulum chaperons." Qatar Foundation Annual Research Forum Proceedings, no. 2010 (December 13, 2010): BMPS11. http://dx.doi.org/10.5339/qfarf.2010.bmps11.

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27

Morello, JP, V. Bernier, M. Bouvier, and DG Bichet. "Des chaperons pharmacologiques pour corriger le diabète insipide néphrogénique ?" médecine/sciences 16, no. 10 (2000): 1109. http://dx.doi.org/10.4267/10608/1534.

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28

Zuehlke, Abbey D., Michael A. Moses, and Len Neckers. "Heat shock protein 90: its inhibition and function." Philosophical Transactions of the Royal Society B: Biological Sciences 373, no. 1738 (2017): 20160527. http://dx.doi.org/10.1098/rstb.2016.0527.

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The molecular chaperone heat shock protein 90 (Hsp90) facilitates metastable protein maturation, stabilization of aggregation-prone proteins, quality control of misfolded proteins and assists in keeping proteins in activation-competent conformations. Proteins that rely on Hsp90 for function are delivered to Hsp90 utilizing a co-chaperone–assisted cycle. Co-chaperones play a role in client transfer to Hsp90, Hsp90 ATPase regulation and stabilization of various Hsp90 conformational states. Many of the proteins chaperoned by Hsp90 (Hsp90 clients) are essential for the progression of various disea

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Filipovic, M., S. Ognjanovic, and M. Ognjanovic. "Evidence of molecular adaptation to extreme environments and applicability to space environments." Serbian Astronomical Journal, no. 176 (2008): 81–86. http://dx.doi.org/10.2298/saj0876081f.

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This is initial investigation of gene signatures responsible for adapting microscopic life to the extreme Earth environments. We present preliminary results on identification of the clusters of orthologous groups (COGs) common to several hyperthermophiles and exclusion of those common to a mesophile (non-hyperthermophile): Escherichia coli (E. coli K12), will yield a group of proteins possibly involved in adaptation to life under extreme temperatures. Comparative genome analyses represent a powerful tool in discovery of novel genes responsible for adaptation to specific extreme environments. M

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Zhou, Qin, Xin-Yuan Guan, and Yan Li. "Roles of heat shock proteins in tumor immune microenvironment." Visualized Cancer Medicine 5 (2024): 3. http://dx.doi.org/10.1051/vcm/2024002.

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Heat shock proteins (HSPs) are the most abundant molecular chaperones in cells, categorized based on function and molecular weight into HSP families, namely, HSP40, HSP70, HSP90, HSP110, and HSPB (heat shock protein B), et al. HSPs are involved in protein homeostasis by assisting in the correct folding of proteins or incorrectly folded proteins, refolding partially denatured proteins, and degrading damaged proteins. High levels of HSPs have been shown to participate in oncogenesis, progression, and chemotherapy resistance in many cancers. Recently a new range of functions besides chaperons, mo

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Ranford, Julia C., Anthony R. M. Coates, and Brian Henderson. "Chaperonins are cell-signalling proteins: the unfolding biology of molecular chaperones." Expert Reviews in Molecular Medicine 2, no. 8 (2000): 1–17. http://dx.doi.org/10.1017/s1462399400002015.

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The chaperonins are a subgroup of oligomeric molecular chaperones; the best-studied examples are chaperonin 60 (GroEL) and chaperonin 10 (GroES), both from the bacterium Escherichia coli. At the end of the 20th century, the paradigm of chaperonins as protein folders had emerged, but it is likely that during the 21st century these proteins will come to be viewed as intercellular signals. Indeed, it is possible that the chaperonins were among the first intercellular signalling proteins to evolve. During the past few years, it has emerged that chaperonin 10 and chaperonin 60 can be found on the s

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Maslova, Ekaterina, Evgeny Pichkur, Pavel Semenyuk, Lidia Kurochkina, and Olga Sokolova. "Abstract P-45: Structure of the Bacteriophage AR9 Bacillus Subtilis Chaperonin According to Cryo-Electron Microscopy." International Journal of Biomedicine 11, Suppl_1 (2021): S32. http://dx.doi.org/10.21103/ijbm.11.suppl_1.p45.

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Background: Chaperonins are a family of molecular chaperones Hsp60 (heat shock proteins 60). GroEL is a bacterial chaperonin. It ensures the correct folding of proteins, using the energy of ATP hydrolysis. Three-dimensional reconstructions of its predicted orthologs were obtained and biochemically characterized in free and nucleotide-bound states for bacteriophages EL Pseudomonas aeruginosa, OBP Pseudomonas fluorescens (Kurochkina, L. P. et al., Journal of virology, 2012; Semenyuk, P. I. et al., Biochemical Journal, 2016; Stanishneva-Konovalova, T. B. et al., Journal of Structural Biology, 202

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33

Ba, Moly, Maëlle Paillat, Nolan Tronche, Amélie Vigneron-Bouquet, and Amel Latifi. "Le rôle des protéines chaperons dans les mécanismes d’adaptation bactériens." médecine/sciences 37, no. 3 (2021): 293–97. http://dx.doi.org/10.1051/medsci/2021020.

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34

van Calster, Paul. "Of Beardless Painters and Red Chaperons. A Fifteenth-Century Whodunit." Zeitschrift für Kunstgeschichte 66, no. 4 (2003): 465. http://dx.doi.org/10.2307/20055358.

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35

Zahn, Ralph. "Prion propagation and molecular chaperones." Quarterly Reviews of Biophysics 32, no. 4 (1999): 309–70. http://dx.doi.org/10.1017/s0033583500003553.

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1. Introduction 3102. Protein-only hypothesis 3123. The scrapie prion protein PrPSc3133.1 Purification of PrP 27–30 3133.2 Proteinase K resistance 3143.3 Scrapie-associated fibrils 3143.4 Smallest infectious unit 3163.5 Conformational properties 3163.6 Dissociation and stability 3194. The cellular prion protein PrPC3214.1 Prnp expression 3214.2 Biosynthetic pathway 3224.3 NMR structures 3244.4 Copper binding 3265. Post-translational PrP conversion 3275.1 Conformational isoforms 3275.2 Location of propagation 3295.3 Minimal PrP sequence 3305.4 Prion species barrier 3315.5 Prion strains 3326. Ef

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Austin, Publishing Group. "Basics of Alzheimer's Disease and Dementia." Austin Alzheimer's and Parkinson's Disease 6, no. 1 (2023): 1035. https://doi.org/10.26420/austinalzheimersjparkinsonsdis.2023.1035.

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Abstract Alzheimer’s Disease (AD) is a disorder that causes degeneration of the cells in the brain and it is the main cause of dementia, which is characterized by a decline Independence in an individual’s daily activities. AD is considered a multifactorial disease. Two main hypotheses have been proposed as the cause of AD. The cholinergic hypothesis and the amyloid hypothesis. In addition, several risk factors have been implicated in this disease, including aging, genetic factors, head trauma, vascular disease, infections, and environmental factors. Currently, there are only two cl

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Galai, Geut, Hila Ben-David, Liron Levin, et al. "Pan-Cancer Analysis of Mitochondria Chaperone-Client Co-Expression Reveals Chaperone Functional Partitioning." Cancers 12, no. 4 (2020): 825. http://dx.doi.org/10.3390/cancers12040825.

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Metabolic reprogramming is a hallmark of cancer. Such reprogramming entails the up-regulation of the expression of specific mitochondrial proteins, thus increasing the burden on the mitochondrial protein quality control. However, very little is known about the specificity of interactions between mitochondrial chaperones and their clients, or to what extent the mitochondrial chaperone–client co-expression is coordinated. We hypothesized that a physical interaction between a chaperone and its client in mitochondria ought to be manifested in the co-expression pattern of both transcripts. Using Th

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38

Roobol, A., F. E. Holmes, N. V. Hayes, A. J. Baines, and M. J. Carden. "Cytoplasmic chaperonin complexes enter neurites developing in vitro and differ in subunit composition within single cells." Journal of Cell Science 108, no. 4 (1995): 1477–88. http://dx.doi.org/10.1242/jcs.108.4.1477.

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Chaperonins containing t-complex polypeptide-1 (CCT) are cytosolic molecular chaperone particles implicated especially in the biogenesis of cytoskeletal proteins by promoting the correct folding of the major ubiquitous cytoskeletal components, tubulin and actin. We have purified cytosolic chaperonins from the ND7/23 cell line, determined their subunit composition and examined changes in the intracellular locations of their components during differentiation of ND7/23 cells to a neuronal phenotype by using immunocytochemistry and immunoblots. Chaperonins containing the CCT alpha (TCP1) subunit e

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Cumova, Jana, Anna Potacova, Irena Kasalova, et al. "Proteomic Analysis of Multiple Myeloma Cells Targeted with Bortezomib." Blood 112, no. 11 (2008): 5133. http://dx.doi.org/10.1182/blood.v112.11.5133.5133.

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Abstract Introduction: Multiple myeloma (MM) is still an incurable disease characterized by clonal expansion of malignant plasma cells. New anticancer drugs further improve prognosis of myeloma patients. Despite promising clinical activity, some patients with MM failed to respond to bortezomib therapy. The aim of this study was to evaluate changes in protein expression of myeloma cell line ARH-77 after bortezomib treatment. Materials and methods: Myeloma cell line ARH-77 was treated with bortezomib (5–20nM) for various periods of time. The proteins contained in total myeloma cell lysate were s

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Macario, Alberto J. L., and Everly Conway de Macario. "The Archaeal Molecular Chaperone Machine: Peculiarities and Paradoxes." Genetics 152, no. 4 (1999): 1277–83. http://dx.doi.org/10.1093/genetics/152.4.1277.

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Abstract A major finding within the field of archaea and molecular chaperones has been the demonstration that, while some species have the stress (heat-shock) gene hsp70(dnaK), others do not. This gene encodes Hsp70(DnaK), an essential molecular chaperone in bacteria and eukaryotes. Due to the physiological importance and the high degree of conservation of this protein, its absence in archaeal organisms has raised intriguing questions pertaining to the evolution of the chaperone machine as a whole and that of its components in particular, namely, Hsp70(DnaK), Hsp40(DnaJ), and GrpE. Another arc

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Sokolova, Olga S., Evgeny B. Pichkur, Ekaterina S. Maslova, et al. "Local Flexibility of a New Single-Ring Chaperonin Encoded by Bacteriophage AR9 Bacillus subtilis." Biomedicines 10, no. 10 (2022): 2347. http://dx.doi.org/10.3390/biomedicines10102347.

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Chaperonins, a family of molecular chaperones, assist protein folding in all domains of life. They are classified into two groups: bacterial variants and those present in endosymbiotic organelles of eukaryotes belong to group I, while group II includes chaperonins from the cytosol of archaea and eukaryotes. Recently, chaperonins of a prospective new group were discovered in giant bacteriophages; however, structures have been determined for only two of them. Here, using cryo-EM, we resolved a structure of a new chaperonin encoded by gene 228 of phage AR9 B. subtilis. This structure has similari

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Pavlova, Iulia I., Vladimir B. Tsvetkov, Ekaterina A. Isaakova, et al. "Transcription-facilitating histone chaperons interact with genomic and synthetic G4 structures." International Journal of Biological Macromolecules 160 (October 2020): 1144–57. http://dx.doi.org/10.1016/j.ijbiomac.2020.05.173.

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Suryawanshi, Yogesh, Surekha Gupta, Hiral Mange, and Manisha Tripathi. "Efficient Production of Yeast Cu-Zn Superoxide Dismutase in the Periplasm of Escherichia coli by Co-expression of Skp Molecular Chaperone." International Journal of Pharmaceutical Sciences and Drug Research 13, no. 03 (2020): 311–17. http://dx.doi.org/10.25004/ijpsdr.2021.130311.

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Co-expression is a simultaneous expression of two or more proteins. Molecular chaperones are proteins that are naturally produced in the cell and have an essential role in restraining the aggregation of nonnative protein production. Co-expression of target protein alongside molecular chaperones is an efficient way to overcome the problems faced during the expression of recombinant proteins. The present study aims to a co-express protein highly useful in cosmetics, superoxide dismutase (SOD), in the periplasm of E. coli with molecular chaperone Skp. Superoxide dismutase and Skp were placed unde

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Yamaguchi, Atsushi, Osamu Hori, David M. Stern, Enno Hartmann, Satoshi Ogawa, and Masaya Tohyama. "Stress-Associated Endoplasmic Reticulum Protein 1 (Serp1)/Ribosome-Associated Membrane Protein 4 (Ramp4) Stabilizes Membrane Proteins during Stress and Facilitates Subsequent Glycosylation." Journal of Cell Biology 147, no. 6 (1999): 1195–204. http://dx.doi.org/10.1083/jcb.147.6.1195.

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Application of differential display to cultured rat astrocytes subjected to hypoxia allowed cloning of a novel cDNA, termed stress-associated endoplasmic reticulum protein 1 (SERP1). Expression of SERP1 was enhanced in vitro by hypoxia and/or reoxygenation or other forms of stress, causing accumulation of unfolded proteins in endoplasmic reticulum (ER) stress, and in vivo by middle cerebral artery occlusion in rats. The SERP1 cDNA encodes a 66–amino acid polypeptide which was found to be identical to ribosome-associated membrane protein 4 (RAMP4) and bearing 29% identity to yeast suppressor of

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Wang, Lisha, Liza Bergkvist, Rajnish Kumar, Bengt Winblad, and Pavel F. Pavlov. "Targeting Chaperone/Co-Chaperone Interactions with Small Molecules: A Novel Approach to Tackle Neurodegenerative Diseases." Cells 10, no. 10 (2021): 2596. http://dx.doi.org/10.3390/cells10102596.

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The dysfunction of the proteostasis network is a molecular hallmark of neurodegenerative diseases such as Alzheimer’s disease, Parkinson’s disease, Huntington’s disease, and amyotrophic lateral sclerosis. Molecular chaperones are a major component of the proteostasis network and maintain cellular homeostasis by folding client proteins, assisting with intracellular transport, and interfering with protein aggregation or degradation. Heat shock protein 70 kDa (Hsp70) and 90 kDa (Hsp90) are two of the most important chaperones whose functions are dependent on ATP hydrolysis and collaboration with

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Muronetz, Vladimir I., Sofia S. Kudryavtseva, Evgeniia V. Leisi, Lidia P. Kurochkina, Kseniya V. Barinova, and Elena V. Schmalhausen. "Regulation by Different Types of Chaperones of Amyloid Transformation of Proteins Involved in the Development of Neurodegenerative Diseases." International Journal of Molecular Sciences 23, no. 5 (2022): 2747. http://dx.doi.org/10.3390/ijms23052747.

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The review highlights various aspects of the influence of chaperones on amyloid proteins associated with the development of neurodegenerative diseases and includes studies conducted in our laboratory. Different sections of the article are devoted to the role of chaperones in the pathological transformation of alpha-synuclein and the prion protein. Information about the interaction of the chaperonins GroE and TRiC as well as polymer-based artificial chaperones with amyloidogenic proteins is summarized. Particular attention is paid to the effect of blocking chaperones by misfolded and amyloidoge

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Lund, Peter. "Insights into chaperonin function from studies on archaeal thermosomes." Biochemical Society Transactions 39, no. 1 (2011): 94–98. http://dx.doi.org/10.1042/bst0390094.

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It is now well understood that, although proteins fold spontaneously (in a thermodynamic sense), many nevertheless require the assistance of helpers called molecular chaperones to reach their correct and active folded state in living cells. This is because the pathways of protein folding are full of traps for the unwary: the forces that drive proteins into their folded states can also drive them into insoluble aggregates, and, particularly when cells are stressed, this can lead, without prevention or correction, to cell death. The chaperonins are a family of molecular chaperones, practically u

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Winkler, Camilla, Christian Hasberg, and Willi Jahnen-Dechent. "Biologische Mineralisation vs. Pathologische Kalzifizierung – die Rolle des Mineral-Chaperons Fetuin-A." Osteologie 31, no. 04 (2022): 270–79. http://dx.doi.org/10.1055/a-1963-7406.

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ZusammenfassungDie Mineralien Kalzium und Phosphat sind für den Zellstoffwechsel aller lebenden Organismen unverzichtbar. Beide Ionen kommen in biologischen Flüssigkeiten normalerweise in millimolaren Konzentrationen vor. Dies führt zu einem Löslichkeits- und Transportproblem, da Kalziumphosphate in Wasser kaum löslich sind und leicht aus übersättigten Lösungen ausfallen. Mineral-Chaperone stabilisieren Mineral als Kolloid und ermöglichen so den Transport und die Clearance nominell übersättigter Mineral-Lösungen. Am Beispiel des Plasmaproteins Fetuin-A erklären wir die Rolle systemischer Miner

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Qi, Ou Kai, Zhen Ning Wong, and Zhen Yu Wong. "Perception of Patients, Physicians, and Chaperones Regarding the Use of Chaperones During Patient Examinations for Plastic Surgery: A Systematic Review." Plastic and Aesthetic Nursing 44, no. 2 (2024): 140–46. http://dx.doi.org/10.1097/psn.0000000000000560.

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In this systematic review, we searched electronic databases for literature addressing physician use of chaperones during examinations of patients undergoing plastic surgery from the perspective of the patient, physician, and chaperone from inception of the database until April 2023. After screening 939 articles, we included seven studies in a systematic review. We conducted an inductive thematic analysis of four domains (physician perspective, patient perspective, chaperone perspective, and chaperone documentation). The results of the analysis showed that surgeons who are experienced, are men,

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GROMOV, P. "Identification of two molecular chaperons (HSX70, HSC70) in mature human erythrocytes*1." Experimental Cell Research 195, no. 2 (1991): 556–59. http://dx.doi.org/10.1016/0014-4827(91)90412-n.

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