If you were to design an experiment to get p53 back into cancer cells, how would you go about that work? How would you direct p53 into the nucleus of cancer cells without directing it to the nucleus of healthy cells? As an overabundance of p53 in healthy cells would cause problems. Could someone in depth answer these questions for me and explain them cellularly.

If you were to design an experiment to get p53 back into cancer cells, how would you go about that work? How would you direct p53 into the nucleus of cancer cells without directing it to the nucleus of healthy cells? As an overabundance of p53 in healthy cells would cause problems. Could someone in depth answer these questions for me and explain them cellularly.

Biology Today and Tomorrow without Physiology (MindTap Course List)

5th Edition

ISBN:9781305117396

Author:Cecie Starr, Christine Evers, Lisa Starr

Publisher:Cecie Starr, Christine Evers, Lisa Starr

Chapter7: Gene Expression And Control

Section: Chapter Questions

Problem 3CT

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Similar questions

Can you think of two ways in which the function of p53 can be disrupted?
Name four downstream effects of p53 activation.
As the most junior member of a lab, you are tasked with generating cell lines that accumulate DNA damage to investigate how random mutations affect transformation of cells into cancer cells. You decide to mutate proteins in the p53 pathway. Which three proteins would you mutate? Explain your reasoning.
What protein does the P53 code for and why is it important?
Since all cells contain the same number of chromosomes and the overall same/similar genome how would the genome in a nerve cell work differently than the genome of a muscle cell? In other words what epigenetic processes cause these differences between cell types at the molecular level
The p53 pathway is important for regulating the cell cycle. In a normal cell, there is a protein called mdm2 that can bind to p53 and deactivate it. A diseased individual has amutation in the gene that codes for mdm2, resulting in an mdm2 protein that is less able to bind to p53. Will this mutation increase, decrease, or cause no change in the rate of cell death? Explain.
Let’s suppose you were interested in developing drugs to preventepigenetic changes that may contribute to cancer. What cellularproteins would be the target of your drugs? What possible sideeffects might your drugs cause?
"Changes to the p53 protein structure can be caused by differences in DNA and can affect protein function." Can you give detailed explanation why this is causation and not correlation? The explanation should be related with mutation, structure changes during protein synthesis, chemical property changes in amino acids, and functions of p53 protein.
is the p53 protein an activator or a repressor? How do you know?
why is it important for all somatic cells to be genetically identical?
In a few sentences, describe how p53 guards the genome. Include at least two specific ways that p53 guards the genome. In a few more sentences, describe the structure and function of the p53 protein. Structure: what domains are present in the p53 protein? Do p53 work as a single protein or as part of a complex? Function: what do the different domains do? How can p53 do so many different things?
Can you please help me by drawing a serie of schematic figures that demonstrates the information in the paragraph below? In addition to phosphorylation, the C-terminal domain of p53 can also be acetylated and sumolated in response to DNA damage. Acetylation and sumolation both result in an increase in the transactivation ability of p53 and may account for this finding. In vivo, IR induces the acetylation of p53 at Lys320 by PCAF and Lys382 by CBP/p300. Acetylation at these sites is dependent on N-terminal phosphorylation at Ser15 and to a lesser extent on phosphorylation at Ser6, Ser9, and Thr18 (Saito et al., 2002; Wahl and Carr, 2001). All of these phosphorylation events are ATM-dependent, although only Ser15 has been shown to be phosphorylated directly by ATM. Sumolation occurs at Lys386 after DNA damage (Muller et al., 2000). Sumolation refers to the covalent attachment of a small ubiquitin-like molecule (SUMO-1) to Lys residues, but in contrast to ubiquitination, does not result…