scholarly journals Design, synthesis and pharmacological evaluation of 4,5-diarylisoxazols bearing amino acid residues within the 3-amido motif as potent heat shock protein 90 (Hsp90) inhibitors

2017 ◽  
Vol 125 ◽  
pp. 315-326 ◽  
Author(s):  
Chi Zhang ◽  
Xin Wang ◽  
Hongchun Liu ◽  
Minmin Zhang ◽  
Meiyu Geng ◽  
...  
Keyword(s):  
Amino Acid ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 90 ◽  
Amino Acid Residues ◽  
Hsp90 Inhibitors ◽  
Design Synthesis ◽  
Pharmacological Evaluation

Molecular cloning and characterization of novel heat shock protein 90 gene from a wild Vitis pseduoreticulata native to China

Biologia ◽  
2009 ◽  
Vol 64 (1) ◽  
Author(s):  
Yan Xu ◽  
Yuejin Wang
Keyword(s):  
Amino Acid ◽  
Nicotiana Tabacum ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 90 ◽  
Amino Acid Residues ◽  
Higher Plant ◽  
Phylogenetic Tree Analysis ◽  
Ancestral Gene ◽  
Reading Frame

AbstractHeat shock protein 90 (Hsp90), known as molecular chaperone, is involved in protein folding and assembly in the cell. In the present study, a full-length cDNA named Vitis pseduoreticulta heat shock protein 90 (VpHsp90) (GenBank accession Number:EU239815), encoding a heat shock protein 90, was obtained by degenerated primers and 3′-and 5′-RACE from Vitis pseudoreticulata according to our previously obtained EST sequence (GenBnak accession number:DV182112), putatively known as Hsp90. Comparison of VpHsp90 sequence has revealed that an open reading frame (ORF) consists of 2,100 bp nucleotides and the translated proteins of 699 amino acid residues. The molecular mass of VpHsp90 calculated from the deduced amino acid sequence was 80.2 kDa, Isolectric Point was 4.893, which is in close proximity of Hsp90. The maximum similarity of VpHsp90 at nucleotides level (85%) and protein level (96%) was found to be with Nicotiana tabacum. Phylogenetic tree analysis at both the nucleotides and amino acids levels indicates that Vitis pseduoreticulata, Nicotiana tabacum, and Arabidopsis thaliana Hsp90 sequences comprise one clade, which is closely related to Oryza sativa, Hordeum vulgare and Triticum aestivum Hsp90s. It may be reasonably concluded that VpHsp90 possesses the ancestral gene of Hsp90 similar to that of higher plant species.

Design, Synthesis, and Evaluation of Heat Shock Protein 90 Inhibitors in Human Breast Cancer and Its Metastasis

2016 ◽  
Vol 17 (14) ◽  
pp. 1231-1245 ◽  
Author(s):  
Mehmet Gümus ◽  
Aykut Ozgur ◽  
Lutfi Tutar ◽  
Ali Disli ◽  
Irfan Koca ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Human Breast Cancer ◽  
Heat Shock Protein 90 ◽  
Human Breast ◽  
Design Synthesis

Ligand Desolvation Steers On-Rate and Impacts Drug Residence Time of Heat Shock Protein 90 (Hsp90) Inhibitors

2018 ◽  
Vol 61 (10) ◽  
pp. 4397-4411 ◽  
Author(s):  
Doris A. Schuetz ◽  
Lars Richter ◽  
Marta Amaral ◽  
Melanie Grandits ◽  
Ulrich Grädler ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Residence Time ◽  
Heat Shock Protein 90 ◽  
Hsp90 Inhibitors

Identification of Limonol Derivatives as Heat Shock Protein 90 (Hsp90) Inhibitors through a Multidisciplinary Approach

2016 ◽  
Vol 22 (37) ◽  
pp. 13236-13250 ◽  
Author(s):  
Maria G. Chini ◽  
Nicola Malafronte ◽  
Maria C. Vaccaro ◽  
Maria J. Gualtieri ◽  
Antonio Vassallo ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Multidisciplinary Approach ◽  
Heat Shock Protein 90 ◽  
Hsp90 Inhibitors

scholarly journals Heat-shock protein 90 and Cdc37 interact with LKB1 and regulate its stability

2003 ◽  
Vol 370 (3) ◽  
pp. 849-857 ◽  
Author(s):  
Jérôme BOUDEAU ◽  
Maria DEAK ◽  
Margaret A. LAWLOR ◽  
Nick A. MORRICE ◽  
Dario R. ALESSI
Keyword(s):  
Heat Shock ◽  
Protein Kinase ◽  
Heat Shock Protein ◽  
Heat Shock Protein 90 ◽  
Kinase Domain ◽  
Cancer Syndrome ◽  
Hsp90 Inhibitors ◽  
Detailed Mechanism ◽  
Anti Cancer ◽  
Hsp90 Chaperone

LKB1 is a widely expressed serine/threonine protein kinase that is mutated in the inherited Peutz—Jeghers cancer syndrome. Recent findings indicate that LKB1 functions as a tumour suppressor, but little is known regarding the detailed mechanism by which LKB1 regulates cell growth. In this study we have purified LKB1 from cells and establish that it is associated with the heat-shock protein 90 (Hsp90) chaperone and the Cdc37 kinase-specific targetting subunit for Hsp90. We demonstrate that Cdc37 and Hsp90 bind specifically to the kinase domain of LKB1. We also perform experiments using Hsp90 inhibitors, which indicate that the association of Hsp90 and Cdc37 with LKB1 regulates LKB1 stability and prevents its degradation by the proteasome. Hsp90 inhibitors are being considered as potential anti-cancer agents. However, our observations indicate that prolonged usage of these drugs could possibly lead to tumour development by decreasing cellular levels of LKB1.

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