IndraLab

Statements

Vemurafenib binds BRAF-V600E. 9 / 9
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reach
"The kinase domain of B-raf V600E has strong structural homology with the kinase domains of hRIPK1 and hRIPK3, which explains the similarities between the crystal structure of Nec-1 bound to RIPK1 and the structure of Vemurafenib bound to B-Raf V600E."
28661484
reach
"This was also shown to be the case for vemurafenib binding to BRAF V600E."
30926642
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"It has been shown that vemurafenib binding to BRAF V600E paradoxically activates downstream MAPK signaling via dimerization with non mutant RAF family members and allosteric activation of the non mutant partner [XREF_BIBR]."
26405815
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"Comparison of this structure to the inactive conformation seen in the structure of vemurafenib bound to BRAF V600E reveals significant differences in the orientation of alphaC."
26996308
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"Additionally, vemurafenib has been found to induce the trans-activation of WT-BRAF or CRAF through hetero-dimerization between vemurafenib bound BRAF V600E and WT-BRAF or CRAF."
28174173
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"Comparison of alphaC position in the dabrafenib bound and vemurafenib bound BRAF V600E indicates that vemurafenib induces a greater alphaC shift then dabrafenib."
26996308
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"Crystal structures of vemurafenib bound to BRAF V600E reveal a solvent exposed chloride at the para-position on the phenyl ring, which we posited would be ideal for linker addition (PDB : 3OG7) 34."
33568647
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"Based on prior structural data of MEK1-BRAF, vemurafenib bound V600E BRAF, and MEK1-KSR2 and structural alignments of vemurafenib bound V600E BRAF with BRAF or KSR2, we hypothesized a regulatory V600E BRAF- MUT MEK complex where V600E BRAF arginine 662 makes critical contacts with MEK residues in one complex interface (XREF_FIG)."
25600339
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"PLX4032 binds V600E mutant BRAF with high affinity and inhibits ERK signaling output."
24460976