Results 11 to 20 of about 58,138 (243)
A Grp on the Hsp90 Mechanism [PDF]
Molecular Cell, 2007 In a recent issue of Molecular Cell, Dollins et al. (2007) present the crystal structure of Grp94, which highlights the similarity between Grp94 and Hsp90 and provides insight into the resting state of Grp94 and potentially other Hsp90 family members.
Richter, K., Reinstein, J., Buchner, J.
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bmc, 2011 Abstract Molecular chaperones are key components in the maintenance of cellular homeostasis and survival, not only during stress but also under optimal growth conditions. Among the ATP-dependent chaperones, heat shock proteins (Hsp90) proteins play a special role.
Stankiewicz Marta, Mayer Matthias P.
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Molecules, 2020 A series of benzo[g]benzothiazolo[2,3-b]quinazoline-7,12-quinones were prepared from 2-acylnaphthohydroquinones and 2-aminobenzothiazoles and were evaluated for their in vitro antiproliferative activity.
Jaime A. Valderrama +4 more
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Journal of Extracellular Vesicles, 2020 Evidence has been accumulating to indicate that extracellular vesicles (EVs), including exosomes, released by cancer cells can foster tumour progression.
Kisho Ono +16 more
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Inhibitors of HSP90 in melanoma [PDF]
Apoptosis, 2019 Abstract HSP90 (heat shock protein 90) is an ATP-dependent molecular chaperone involved in a proper folding and maturation of hundreds of proteins. HSP90 is abundantly expressed in cancer, including melanoma. HSP90 client proteins are the key oncoproteins of several signaling pathways controlling melanoma development, progression and response to ...
Aleksandra Mielczarek-Lewandowska +2 more
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Regulated Transport into the Nucleus of Herpesviridae DNA Replication Core Proteins
Viruses, 2013 The Herpesvirdae family comprises several major human pathogens belonging to three distinct subfamilies. Their double stranded DNA genome is replicated in the nuclei of infected cells by a number of host and viral products.
Alessandro Ripalti +6 more
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P53 in lung vascular barrier dysfunction
Vascular Biology, 2020 Endothelial barrier dysfunction is the hallmark of inflammatory lung disease, including Acute Lung Injury and Acute Respiratory Distress Syndrome. The purpose of the present editorial is to emphasize on recent advances in the corresponding field, as it ...
Nektarios Barabutis
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Regulatory Mechanisms of Hsp90 [PDF]
Biochemistry & Molecular Biology Journal, 2017 The ability of Hsp90 to activate a disparate clientele implicates this chaperone in diverse biological processes. To accommodate such varied roles, Hsp90 requires a variety of regulatory mechanisms that are coordinated in order to modulate its activity appropriately. Amongst these, the master-regulator heat shock factor 1 (HSF1) is critically important
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HSP90 Interacts with the Fibronectin N-terminal Domains and Increases Matrix Formation
Cells, 2020 Heat shock protein 90 (HSP90) is an evolutionarily conserved chaperone protein that controls the function and stability of a wide range of cellular client proteins.
Abir Chakraborty +2 more
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HSP90-Mediates Liraglutide Preconditioning-Induced Cardioprotection by Inhibiting C5a and NF-κB
Journal of Investigative Surgery, 2022 Objective We previously showed that HSP90 is involved in postconditioning cardioprotection by inhibiting complement C5a. Here, we investigated whether HSP90-mediated C5a/NF-κB inhibition is responsible for the cardioprotection conferred by liraglutide ...
Shi-Tao He +6 more
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