The INDRA Database: Results
IndraLab
Statements
databases
phosphosite
cbn
pc11
biopax
bel_lc
signor
biogrid
tas
lincs_drug
hprd
trrust
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geneways
tees
isi
trips
rlimsp
medscan
sparser
reach
reading
vemurafenib affects BRAF
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1
15
reach
"In these structures, signaling pathways become more diverse with 45% occupancy for the most optimal path in the Vemurafenib and BRAF complex and 55% occupancy in the PLX7904 and BRAF complex (XREF_FIG)."
reach
"Vemurafenib binding to the wild type BRAF inhibits BRAF but causes transactivation of CRAF, leading to MEK and ERK activation rather than inhibition."
reach
"Since vemurafenib binds less specifically to mutated BRAF than dabrafenib and binding to wildtype BRAF could inhibit ERK activation in immune cells."
reach
"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."
reach
"To model this possibility, we created MEMI1.2 in which binding of vemurafenib to monomeric or dimeric BRAF is explicitly specified by separate sentences, allowing the effects of different binding affinities to be explored (Fig XREF_FIG D)."
reach
"The crystal structures of the BRAF and V600E complex with PLX7904 (pdb id 4XV1), the BRAF V600E mutant bound with PLX7922 (pdb id 4XV3), and the BRAF and PLX5568 complex (pdb id 4XV9) have revealed a binding mode and interaction profiles that are highly reminiscent of the BRAF and Vemurafenib complex."
reach
"The small molecule inhibitors vemurafenib and dabrafenib selectively bind the active conformation of BRAF and inhibit signal transduction between BRAF and MEK."
reach
"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]."
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."
reach
"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."
reach
"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)."
BRAF affects vemurafenib
|
1
15
reach
"In these structures, signaling pathways become more diverse with 45% occupancy for the most optimal path in the Vemurafenib and BRAF complex and 55% occupancy in the PLX7904 and BRAF complex (XREF_FIG)."
reach
"Vemurafenib binding to the wild type BRAF inhibits BRAF but causes transactivation of CRAF, leading to MEK and ERK activation rather than inhibition."
reach
"Since vemurafenib binds less specifically to mutated BRAF than dabrafenib and binding to wildtype BRAF could inhibit ERK activation in immune cells."
reach
"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."
reach
"To model this possibility, we created MEMI1.2 in which binding of vemurafenib to monomeric or dimeric BRAF is explicitly specified by separate sentences, allowing the effects of different binding affinities to be explored (Fig XREF_FIG D)."
reach
"The crystal structures of the BRAF and V600E complex with PLX7904 (pdb id 4XV1), the BRAF V600E mutant bound with PLX7922 (pdb id 4XV3), and the BRAF and PLX5568 complex (pdb id 4XV9) have revealed a binding mode and interaction profiles that are highly reminiscent of the BRAF and Vemurafenib complex."
reach
"The small molecule inhibitors vemurafenib and dabrafenib selectively bind the active conformation of BRAF and inhibit signal transduction between BRAF and MEK."
reach
"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]."
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."
reach
"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."
reach
"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)."
BRAF affects V600, and vemurafenib
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1
BRAF affects F595, and vemurafenib
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1