Analogues of the Allosteric Heat Shock Protein 70 (Hsp70) Inhibitor, MKT-077, As Anti-Cancer Agents
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چکیده
منابع مشابه
molecular, evolution and stratification study of the heat shock protein 70 (hsp70) genes family in cattle
heat shock proteins (hsps), are highly important due to their association with such economically important traits in animals as resistance to temperature shock and mastitis. in the current study, to get a comprehensive information on molecular structure and evolution of the hsp70s, and the available hsp70 sequences of the cattle and other animals taken from ncbi and aligned together. then, nucl...
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Introduction: Breast cancer is the most common cancer diagnosed among women worldwide. Increased molecular and genetic information about cancer has improved diagnostic, screening, and treatment methods for cancer. Heat shock protein 70 (HSP70) is overexpressed in breast cancer patients and involved in malignant properties of breast cancer. Due to the noninvasive nature of saliva collection and ...
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Hop, an abundant and conserved protein of unresolved function, binds concomitantly with heat shock protein 70 (Hsp70) and Hsp90, participates with heat shock proteins at an intermediate stage of progesterone receptor assembly, and is required for efficient assembly of mature receptor complexes in vitro. A largely untested hypothesis is that Hop functions as an adaptor that targets Hsp90- to Hsp...
متن کاملAllosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones.
The 70-kDa heat shock protein (Hsp70) chaperones perform a wide array of cellular functions that all derive from the ability of their N-terminal nucleotide-binding domains (NBDs) to allosterically regulate the substrate affinity of their C-terminal substrate-binding domains in a nucleotide-dependent mechanism. To explore the structural origins of Hsp70 allostery, we performed NMR analysis on th...
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ژورنال
عنوان ژورنال: ACS Medicinal Chemistry Letters
سال: 2013
ISSN: 1948-5875,1948-5875
DOI: 10.1021/ml400204n