Chemical Name: 5'-O-[(4-Cyanophenyl)methyl]-8-[[(3,4-dichlorophenyl)methyl]amino]-adenosine
Biological ActivityNovel adenosine-derived inhibitor of Heat Shock Protein 70 (Hsp70) (IC50 = 0.5 μM). Inhibits cell proliferation of multiple human tumor cell lines in vitro. Also binds Hsc70 and Grp78; displays selectivity against Hsp90β (IC50 >200 μM for Hsp90β).
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Tocris products are intended for laboratory research use only, unless stated otherwise.
Adenosine-derived inhibitors of 78 kDa glucose regulated protein (Grp78) ATPase: insights into isoform selectivity.
Macias et al.
A novel, small molecule inhibitor of Hsc70/Hsp70 potentiates Hsp90 inhibitor induced apoptosis in HCT116 colon carcinoma cells.
Massey et al.
Cancer Chemother.Pharmacol., 2009;66:535
Novel adenosine-derived inhibitors of 70 kDa heat shock protein, discovered through structure-based design.
Williamson et al.
ATPases as drug targets: insights from heat shock proteins 70 and 90.
Massey et al.
Citations for VER 155008
The citations listed below are publications that use Tocris products. Selected citations for VER 155008 include:
18 Citations: Showing 1 - 10
Hsp70 and DNAJA2 limit CFTR levels through degradation.
Authors: Chiaw Et al.
PLoS One 2019;14:e0220984
Feedback inhibition of cAMP effector signaling by a chaperone-assisted ubiquitin system.
Authors: Rinaldi Et al.
Nat Commun 2019;10:2572
N-Acetyl-l-Cysteine Protects Astrocytes against Proteotoxicity without Recourse to Glutathione.
Authors: Gleixner Et al.
Mol Pharmacol 2017;92:564
Hsc70 chaperone activity is required for the cytosolic slow axonal transport of synapsin.
Authors: Ganguly Et al.
J Cell Biol 2017;216:2059
Combined inhibition of heat shock proteins 90 and 70 leads to simultaneous degradation of the oncogenic signaling proteins involved in muscle invasive bladder cancer.
Authors: Cavanaugh Et al.
Oncogenic extracellular HSP70 disrupts the gap-junctional coupling between capillary cells.
Authors: Thuringer Et al.
J Cell Biol 2015;6:10267
Sequence-dependent internalization of aggregating peptides.
Authors: Couceiro Et al.
The regulation of TNFα production after heat and endotoxin stimulation is dependent on Annexin-A1 and HSP70.
Authors: Nair Et al.
Cell Stress Chaperones 2015;20:583
Hsp72 is targeted to the mitotic spindle by Nek6 to promote K-fiber assembly and mitotic progression.
Authors: O'Regan Et al.
J Biol Chem 2015;209:349
Hsp70 Isoforms Are Essential for the Formation of Kaposi's Sarcoma-Associated Herpesvirus Replication and Transcription Compartments.
Authors: Baquero-Perez and Whitehouse
PLoS Pathog 2015;11:e1005274
A novel mechanism of autophagic cell death in dystrophic muscle regulated by P2RX7 receptor large-pore formation and HSP90.
Authors: Young Et al.
Quantitative proteomics of the yeast Hsp70/Hsp90 interactomes during DNA damage reveal chaperone-dependent regulation of ribonucleotide reductase.
Authors: Truman Et al.
J Proteomics 2015;112:285
A cytosolic protein factor from the naked mole-rat activates proteasomes of other species and protects these from inhibition.
Authors: Rodriguez Et al.
Biochim Biophys Acta 2014;1842:2060
Mutation in integrin-linked kinase (ILK(R211A)) and heat-shock protein 70 comprise a broadly cardioprotective complex.
Authors: Traister Et al.
PLoS One 2013;8:e77331
The unfolded protein response selectively targets active smoothened mutants.
Authors: Marada Et al.
Mol Cell Biol 2013;33:2375
Molecular mechanism of mutant p53 stabilization: the role of HSP70 and MDM2.
Authors: Wiech Et al.
PLoS One 2012;7:e51426
The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system.
PLoS One 2011;6:e26319
A unique role for heat shock protein 70 and its binding partner tissue transglutaminase in cancer cell migration.
Authors: Boroughs Et al.
J Biol Chem 2011;286:37094
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Human osteosarcoma, U2OS, cells were incubated with VER 155008 (1 microM) for 24 h to follow PARP cleavage using Western blot. Hsp70 inhibition with VER 155008 significantly induced PARP cleavage in U2OS cells.