Pages that link to "Q39500057"
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The following pages link to Fully activated MEK1 exhibits compromised affinity for binding of allosteric inhibitors U0126 and PD0325901. (Q39500057):
Displaying 12 items.
- Mechanism of Action and Epitopes of Clostridium difficile Toxin B-neutralizing Antibody Bezlotoxumab Revealed by X-ray Crystallography (Q27683753) (← links)
- Mechanism of MEK inhibition determines efficacy in mutant KRAS- versus BRAF-driven cancers (Q27685364) (← links)
- Selectively targeting an inactive conformation of interleukin-2-inducible T-cell kinase by allosteric inhibitors (Q27689430) (← links)
- A Protoberberine derivative HWY336 selectively inhibits MKK4 and MKK7 in mammalian cells: the importance of activation loop on selectivity (Q28538148) (← links)
- MEK and the inhibitors: from bench to bedside (Q34036341) (← links)
- An Automated Microscale Thermophoresis Screening Approach for Fragment-Based Lead Discovery (Q35861440) (← links)
- Assessing adaptation of the cancer kinome in response to targeted therapies (Q38238603) (← links)
- Intrinsic and acquired resistance to MEK1/2 inhibitors in cancer (Q38238605) (← links)
- Signaling pathways as therapeutic targets in biliary tract cancer. (Q38747573) (← links)
- Allosteric modulators of MEK1: drug design and discovery (Q38817910) (← links)
- Molecular pathways: adaptive kinome reprogramming in response to targeted inhibition of the BRAF-MEK-ERK pathway in cancer (Q39697330) (← links)
- The effect of dual inhibition of Ras-MEK-ERK and GSK3β pathways on development of in vitro cultured rabbit embryos (Q90464791) (← links)