Mutations in Ras are found in a majority of cancers. Which of these mutations will lead to permanent activation of Ras-signaling? Mutations that inhibit Raf-activity Mutations that activate Ras-GAP Mutations that inhibit Ras-GTPase activity Mutations that inhibit Ras-GEF activity O O O O
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- Answer both to get a like or don't attempt.Thanks Question 9 Listen Transphosphorylation, the bidirectional recpiprocal phosphorylation of growth factor dimers, results in the phosphorylation of an array of tyrosine residues present in cytoplasmic portions of the growth factor receptor outside the kinase domain. Question 9 options: TRUE FALSE Question 10 Listen For the EGF receptor: Question 10 options: Spontaneous receptor dimerization precedes receptor binding. The EGF ligand serves as a bridge to dimerize receptors. Are overexpressed in many human cancers making them hyper-responsive to low levels of ligand. A and C are both correct. B and C are both correct.Explain why in cells that are genetically NF1–/–, basal levels of GTP-bound activated Ras are higher than normal and respond to growth factor stimulation by increasing rapidly to far higher levels.which of hthe following would result in a persisting proliferation response to growth factor receptor activation after the ligand is no longer binding to its rceptor kinase? 1. Both a mutation that blocks the GTPas activity of Ras and a mutation that blocks the exchange of GDP with GTP would cause the response to persist. 2. a mutation that blocks the GTPas activity of Ras 3. neither a mutation that blocks the GTPas activity of Ras nor a mutation that blocks the exchange of GDP with GTP would cause the response to persist 4. a mutatiaon that blocks the exchange of GDP with GTP
- Why do signals indicating damage to cells result in increase in the expression of p21Cip1? I need new answerSignal-transducing heterotrimeric G proteins consist of three subunits designated α, β, and γ. The Gα subunit is a GTPase switch protein that cycles between active and inactive states depending on whether it is bound to GTP or to GDP. Review the steps for ligand-induced activation of effector proteins mediated by the heterotrimeric G proteins. Suppose that you have isolated a mutant Gα subunit that has an increased GTPase activity. What effect would this mutation have on the G protein and the effector protein?a change that decreases the rate of hydrolysis of GTP by Ras a change that increases the affinity of Ras for GDP a change that decreases the affinity of Ras for GTP O a change that prevents Ras from being made
- Which of the following mutations would produce a form of the Ras protein that would be more difficult to inactivate than normal Ras? Briefly explain your reasoning.(i) A mutation that allows Ras to cleave (hydrolyze) GTP more rapidly than usual(ii) A mutation that causes Ras to bind Ras-GAP more tightly than usual(iii) A mutation that causes Ras to cleave (hydrolyze) GTP more slowly than usualHow would a mutation that prevents the Ras proteinfrom hydrolyzing GTP affect the cell-signaling pathway in 25.11?This is the full question.. "Both the cytokinin receptor encoded by CRE1 and the ethylene receptor encoded by ETR1 are examples of" Both the cytokinin receptor encoded by CRE1 and the ethylene receptor encoded by ETR1 are examples of O Leucine-rich repeat receptor kinase • The response regulator component of a two-component sensor histidine kinase (i.e., the component that directly activates transcription (type B ARRS, in the case of cytokinin) or directly mediates a response (type A ARRS)) O Regulatory molecules that bind calcium O The sensor histidine kinase component of a two-component sensor histidine kinase (i.e., the part that receives the signal and passes it to other components of the signal transduction cascade) O Proteins that shuttle from the cytoplasm to the nucleus to alter gene expression
- I just read an abstract of the paper “Disulfide bond-disrupting agents activate the tumor necrosis family-related apoptosis-inducing ligand/death receptor 5 pathway” and noted that “DDAs and TRAIL synergize to kill cancer cells and are cytotoxic to HER2+ cancer cells with acquired resistance to the EGFR/HER2 tyrosine kinase inhibitor Lapatinib.” For the last sentence, I am not sure the meaning of the “acquired resistance to the EGFR/HER2 tyrosine kinase inhibitor Lapatinib”. Is the “acquired resistance ... to inhibitor” a good thing or bad thing, as far as the synergize effect of DDAs and TRAIL”? Hope that expert can help.Compare and contrast the regulation of Ras with trimeric G proteins.The oscillatory clock that drives somite forma-tion in vertebrates involves three essential componentsHer7 (an unstable repressor of its own synthesis), Delta (atransmembrane signaling molecule), and Notch (a trans-membrane receptor for Delta). Notch is bound by Delta onneighboring cells, activating the Notch signaling pathway,which then activates Her7 transcription. Normally, thissystem works flawlessly to create sharply defined somites(Figure Q21–2A). In the absence of Delta, however, onlythe first five somites form normally, and the rest are poorlydefined (Figure Q21–2B). If a pulse of Delta is suppliedlater, somite formation returns to normal in the regionswhere Delta was present (Figure Q21–2C). A diagram ofthe connections between the components of the clockand how they interact in adjacent cells is shown in FigureQ21–2D. In the absence of Delta, why do the cells becomeunsynchronized? What is it about the presence of Deltathat keeps adjacent cells oscillating in synchrony?