Multi-kinase inhibitors can associate with heat shock proteins through their NH2-termini by which they suppress chaperone function
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Rationally Repurposing Ruxolitinib (Jakafi (®)) as a Solid Tumor TherapeuticRuxolitinib synergizes with DMF to kill via BIM+BAD-induced mitochondrial dysfunction and via reduced SOD2/TRX expression and ROSMulti-kinase inhibitors interact with sildenafil and ERBB1/2/4 inhibitors to kill tumor cells in vitro and in vivo.The HDAC inhibitor AR42 interacts with pazopanib to kill trametinib/dabrafenib-resistant melanoma cells in vitro and in vivo.[pemetrexed + sildenafil], via autophagy-dependent HDAC down-regulation, enhances the immunotherapy response of NSCLC cells.Sorafenib impedes Rift Valley fever virus egress by inhibiting Valosin-containing protein function in the cellular secretory pathway.Exploring the in vitro potential of celecoxib derivative AR-12 as an effective antiviral compound against four dengue virus serotypes.PDE5 inhibitors enhance the lethality of [pemetrexed + sorafenib].[Pemetrexed + Sorafenib] lethality is increased by inhibition of ERBB1/2/3-PI3K-NFκB compensatory survival signaling.AR-12 Inhibits Chaperone Proteins Preventing Virus Replication and the Accumulation of Toxic Misfolded Proteins.Effect of glycosides of Cistanche on the expression of mitochondrial precursor protein and keratin type II cytoskeletal 6A in a rat model of vascular dementia.PDE5 inhibitors enhance the lethality of pemetrexed through inhibition of multiple chaperone proteins and via the actions of cyclic GMP and nitric oxideHDAC inhibitors enhance the immunotherapy response of melanoma cells.HDAC inhibitors enhance neratinib activity and when combined enhance the actions of an anti-PD-1 immunomodulatory antibody in vivo.Curcumin interacts with sildenafil to kill GI tumor cells via endoplasmic reticulum stress and reactive oxygen/ nitrogen species.Protein biosynthesis, a target of sorafenib, interferes with the unfolded protein response (UPR) and ferroptosis in hepatocellular carcinoma cells.Glucose-regulated protein 78 substrate-binding domain alters its conformation upon EGCG inhibitor binding to nucleotide-binding domain: Molecular dynamics studies.
P2860
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P2860
Multi-kinase inhibitors can associate with heat shock proteins through their NH2-termini by which they suppress chaperone function
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 12 February 2016
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
@cs
name
Multi-kinase inhibitors can as ...... ey suppress chaperone function
@en
Multi-kinase inhibitors can as ...... y suppress chaperone function.
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type
label
Multi-kinase inhibitors can as ...... ey suppress chaperone function
@en
Multi-kinase inhibitors can as ...... y suppress chaperone function.
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prefLabel
Multi-kinase inhibitors can as ...... ey suppress chaperone function
@en
Multi-kinase inhibitors can as ...... y suppress chaperone function.
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P2093
P2860
P356
P1433
P1476
Multi-kinase inhibitors can as ...... ey suppress chaperone function
@en
P2093
Alexander Zukiwski
Brian Shuch
Ching-Shih Chen
Dasheng Wang
Don Bottaro
Iryna O Lebedyeva
Jane L Roberts
Laurence Booth
Mehrad Tavallai
Stefan Proniuk
P2860
P304
12975-12996
P356
10.18632/ONCOTARGET.7349
P407
P577
2016-02-12T00:00:00Z