A look at ubiquitination.
1/ Cells make, regulate and break down proteins constantly. They have a system to control the regulation of the proteins they produce. This is to remove unwanted proteins when no longer used.
2/ It also maintains healthy proteins as they degrade slowly over time. The process of ubiquitination is the tagging of these proteins by the cell for destruction. There are 3 enzymes that work in the process of ubiquitination.
3/ They are the enzymes E1, E2 and E3. There are only 2 types of E1 enzymes, 30 types of E2 enzymes and estimated to be 600 possible E3 enzymes. Lets take a look at how a protein get tagged for destruction.
4/ The E1 ligase take the actual ubiquitin molecule and puts a phosphate on it. This is called phosphorylation. Once its got that phosphate group added, it passes the ubiquitin to the E2 enzyme.
5/ The E2 ligase takes the phosphorylated ubiquitin and binds to the E3 ligase with it. This creates a complex of the E2 and E3 ligases. The E3 ligase will bind to the protein it recognizes and add that ubiquitin to the protein.
6/ The addition of the ubiquitin to the protein is done on a lysine amino acid. It can be done to several lysine amino acids on that same protein by multiple E3 ligases.
7/ After the E3 adds the ubiquitin to the protein, it releases the E2 ligase and binds another which contains another ubiquitin.
8/ It keeps adding these ubiquitin molecules to the lysine in a long chain called a poly ubiquitin chain. It can create a chain of more than 10 ubiquitin molecules long.
9/ This long tail of ubiquitin on the protein flags it for destruction by the organelle called the Proteasome.

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More from @Biotech2k1

15 Sep
#Cancer_Immunology TME

A look into the Tumor Micro Environment (TME).
1/ There is a complex set of interactions that must go on between a tumor and its surroundings. It has to interact with the tissue cells, it needs nutrients, it needs oxygen, it needs to survive and proliferate in a hostile environment.
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My Game Plan:

$BPMC 3.37% core position
$MRTX 3.37% core position
$TPTX 3.37% core position
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$RVMD 2.7%
$RLAY 2.7%
$ERAS 0% considering but way too expensive
$RPTX 2.02%
$KNTE sold out as it was my weakest link
Protein Degraders:
$ARVN 1.35%
$KYMR 1.35% paying down a core position
$CCCC 2.02% paying down a core position
$GLUE 1.35% paying down a core position
CRISPR/Old Antibodies
$CRBU 1.35% paying down a core position
$BCAB 2.7% will sell out when I think its good opportunity.

CRISPR is way to crazy on values to waste money on here. It will implode someday, and I will be waiting.
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A look into protein degraders.
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2/ The monoDAC will bind with a covalent chemical bonding to the E3 ligase and alter its targeted function. It changes the shape of the E3 and directs it to place the ubiquitin molecule onto a protein it directs.
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I look at how the Proteasome works.
1/ The Proteasome is a cellular organelle. Its like the recycling bin for proteins. When a cell is done with a protein, it tags it for destruction in the process called ubiquitination.
2/ The proteasome will load these tagged proteins and break them down into peptides of about 7 to 10 amino acids in length for recycling. They will further be broken down after into single amino acids for reuse to build new proteins.
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Looking at Protein Degraders:

Looking at the pathway coverage of the deragers.
1/ $ARVN
AR - Androgen receptor
ER - Estrogen receptor
BCL6 - transcription factor
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MYC - transcription factor
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