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PLoS ONE, ISSN 1932-6203, 11/2013, Volume 8, Issue 11, p. e78443
The molecular chaperones of the Hsp70 family have been recognized as targets for anti-cancer therapy. Since several paralogs of Hsp70 proteins exist in... 
CANCER-CELLS | HEAT-SHOCK-PROTEIN-70 | HSP90 | ATPASE ACTIVITY | NUCLEOTIDE EXCHANGE | SUBSTRATE-BINDING | MULTIDISCIPLINARY SCIENCES | CHAPERONE MACHINERY | HSC70 | SMALL-MOLECULE INHIBITOR | HEAT-SHOCK-PROTEIN | Protein Structure, Tertiary | Cell Survival - drug effects | Hydrolysis - drug effects | Purine Nucleosides - pharmacology | HSC70 Heat-Shock Proteins - metabolism | Humans | Molecular Conformation | Protein Refolding - drug effects | Sulfonamides - pharmacology | Adenosine Triphosphatases - antagonists & inhibitors | HSC70 Heat-Shock Proteins - chemistry | Protein Isoforms - metabolism | Protein Isoforms - chemistry | Adenosine Triphosphate - metabolism | Drug Design | Luciferases - chemistry | Cell Line, Tumor | HSC70 Heat-Shock Proteins - antagonists & inhibitors | Protein Isoforms - antagonists & inhibitors | Proteins | Heat shock proteins | Care and treatment | Health aspects | Cancer | Target recognition | Peptides | Biochemistry | Chaperones | Cytosol | Mitochondria | Allosteric properties | Adenosine triphosphate | Medical research | Research & development--R&D | Hsp70 protein | Functional analysis | Substrates | Mode of action | Inhibitors | Medical prognosis | Hsc70 protein | Alzheimers disease | Endoplasmic reticulum | Viability | Binding sites | Apoptosis | Conformation | Research & development | R&D
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Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 2/2010, Volume 107, Issue 7, pp. 3006 - 3011
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Chemosphere, ISSN 0045-6535, 02/2017, Volume 168, pp. 1248 - 1256
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