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Review
Biochemistry & Molecular Biology
Patricija van Oosten-Hawle
Summary: Heat shock protein 90 (Hsp90) is a highly conserved molecular chaperone that assists in the maturation of client proteins involved in cellular signal transduction. It plays a crucial role in maintaining cellular proteostasis and adapting to environmental stresses. Hsp90 also functions as an environmentally responsive chaperone in multicellular organisms, contributing to inter-tissue stress signaling responses and organismal health.
Review
Biochemistry & Molecular Biology
Chrisostomos Prodromou et al.
Summary: Hsp90, an ATP molecular chaperone, plays a crucial role in the activation and maturation of client proteins. Recent studies have shed light on the mechanism of Hsp90, including its ATP hydrolysis and the remodeling of client proteins for their activation.
Article
Oncology
Y. Kurokawa et al.
Summary: This randomized, placebo-controlled, phase III trial showed that pimitespib significantly improved progression-free survival (PFS) and overall survival (OS) in patients with advanced gastrointestinal stromal tumors (GIST) refractory to standard tyrosine kinase inhibitors (TKIs), with an acceptable safety profile.
ANNALS OF ONCOLOGY
(2022)
Review
Biochemistry & Molecular Biology
Sarah J. Backe et al.
Summary: This article reviews the literature on FNIP1, FNIP2, and Tsc1 as co-chaperones and discusses their potential impact on normal cellular function and human diseases.
Article
Biochemistry & Molecular Biology
Siddhi Omkar et al.
Summary: This study shows that APE2 and Apn2 proteins depend on the chaperone system in yeast and mammalian cells, and suggests that inhibiting chaperones may be a potential anticancer therapy targeting APE2-mediated processes.
Review
Biochemistry & Molecular Biology
Peter William Piper et al.
Summary: The folding of the myosin head requires a UCS chaperone protein. Different organisms have different types of UCS proteins, and their functions in animals and fungi diverged before a billion years ago. The UCS proteins in fungi and their interactions with Hsp70/Hsp90 chaperones are not well understood.
Review
Biochemistry & Molecular Biology
Jeffrey Lynham et al.
Summary: Hsp90 is a ubiquitous molecular chaperone that plays an important role in cell signaling pathways. Its interactions with specific chaperones and cochaperones determine the folding of client proteins. Although it has multiple roles in protein complex assembly, the detailed mechanisms are still not fully understood.
Review
Biochemistry & Molecular Biology
Abhinav Joshi et al.
Summary: TRAP1 is an important mitochondrial molecular chaperone that regulates mitochondrial respiration and homeostasis, while also displaying cytoprotective activity. It is involved in neurodegenerative diseases and multiple cancers.
Review
Biochemistry & Molecular Biology
Tanima Dutta et al.
Summary: Heat shock protein 90 (Hsp90) plays an important role in cellular protein homeostasis. In parasitic protozoans, such as Plasmodium falciparum, Hsp90 and its associated co-chaperones have unique properties and functions. Understanding these differences may lead to the development of drugs to combat malaria.
Review
Biochemistry & Molecular Biology
Laura A. Wengert et al.
Summary: Mitochondrial function relies on molecular chaperones, including heat shock proteins (Hsps) such as Hsp90 and its chaperone TNF-receptor-associated protein-1 (TRAP1). TRAP1, primarily localized in mitochondria, plays a crucial role in cellular metabolic reprogramming and mitochondrial apoptosis. Upregulation of TRAP1 promotes the growth of cancer cells by enhancing glycolytic metabolism and inhibiting mitochondrial permeability transition, while attenuation of TRAP1 induces apoptosis in cancer cells. Furthermore, TRAP1 is subject to post-translational modifications that regulate its function and downstream effectors.
Review
Biochemistry & Molecular Biology
Kalliopi Ziaka et al.
Summary: This review explores the role of Hsp90 in the proteostatic mechanisms of photoreceptors and elaborates on its function when retinal homeostasis is disturbed. It also discusses the impact of Hsp90 on retinal diseases through its interaction with specific client proteins.
Review
Biochemistry & Molecular Biology
Daniel Jay et al.
Summary: This review summarizes the research progress of extracellular Heat Shock Protein-90 (eHsp90) and provides recommendations for future studies and clinical relevance. Despite extensive research, there are still many fundamental questions about the origin, mechanisms, and differences from intracellular Hsp90 that remain unclear.
Review
Biochemistry & Molecular Biology
Anna G. Mankovich et al.
Summary: Heat shock protein 90 (Hsp90), a highly conserved molecular chaperone, not only maintains the stability of metastable proteins, but also plays a crucial role in protein transport. The specific contributions of Hsp90 to protein transport are still not well defined, despite numerous connections with factors involved in this process.
Review
Biochemistry & Molecular Biology
Samarpan Maiti et al.
Summary: The heat shock protein 90 (Hsp90) is a crucial molecular chaperone and regulator of protein stability in both normal and stressful conditions. In mammals, there are two cytosolic isoforms of Hsp90, Hsp90 alpha and Hsp90 beta, which have overlapping functions and interact with a majority of the proteome. Recent studies suggest that there may be differences in the specific functions of these isoforms, particularly in relation to certain tissues or cell types. Understanding the isoform-specific functions is important for designing therapeutic strategies.
Review
Biochemistry & Molecular Biology
Laurence H. Pearl et al.
BIOCHEMICAL JOURNAL
(2008)
Review
Oncology
L Whitesell et al.
NATURE REVIEWS CANCER
(2005)
