RPUSD3 Inhibitors
RPUSD3 inhibitors encompass a spectrum of chemical entities that indirectly diminish the functional activity of RPUSD3, a protein essential for RNA modification, particularly within the mitochondria. Compounds like Dichloroacetate and Rapamycin operate through metabolic and mTOR signaling pathways, respectively, to potentially decrease the necessity for RPUSD3's RNA modification function. Dichloroacetate, by inhibiting pyruvate dehydrogenase kinase, shifts cellular metabolism towards a heightened mitochondrial activity, which may indirectly impose substrate competition on RPUSD3. Rapamycin, through its interaction with FKBP12 and subsequent inhibition of mTOR, attenuates protein synthesis, indirectly suggesting a reduced requirement for RPUSD3-mediated tRNA modification. 5-Fluorouracil, by being metabolized into nucleotide analogs, hampers RNA processing, potentially lowering the demand for RPUSD3's enzymatic activity. Chloroquine and Actinomycin D, through their respective nucleic acid intercalation and RNA polymerase inhibition, could lead to a decreased requirement for RNA processing enzymes, including RPUSD3.
Further, agents like α-Amanitin, Mycophenolic Acid, Cycloheximide, and Puromycin disrupt various stages of RNA and protein synthesis, indirectly suggesting a reduced load on RNA modification processes reliant on RPUSD3. α-Amanitin, by targeting RNA polymerase II, and Mycophenolic Acid, by depleting guanine nucleotides, exert effects that could ripple through to diminished RPUSD3 activity due to lower RNA turnover. Cycloheximide and Puromycin act as inhibitors of protein synthesis, which could correlate with a lesser need for RPUSD3's involvement in tRNA modification. Additionally, Tunicamycin, Anisomycin, and Emetine, through their distinct mechanisms of inhibiting glycosylation and peptide bond formation, might also indirectly suggest a reduced functional activity of RPUSD3 as they impact the overall protein homeostasis and biosynthesis, potentially leading to a decreased demand for modified RNA molecules necessary for efficient cellular function. Collectively, these inhibitors, by influencing various biochemical and cellular pathways, contribute to the potential diminution of RPUSD3 activity without directly binding to or altering the protein itself.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Sodium dichloroacetate | 2156-56-1 | sc-203275 sc-203275A | 10 g 50 g | $54.00 $205.00 | 6 | |
Dichloroacetate inhibits pyruvate dehydrogenase kinase, which results in the activation of pyruvate dehydrogenase, leading to a decrease in glycolytic flux and an increase in mitochondrial activity. Enhanced mitochondrial function can increase the demand for mitochondrial RNA editing, potentially diminishing RPUSD3 activity due to substrate competition. | ||||||
Rapamycin | 53123-88-9 | sc-3504 sc-3504A sc-3504B | 1 mg 5 mg 25 mg | $62.00 $155.00 $320.00 | 233 | |
Rapamycin specifically binds to FKBP12 and inhibits mTOR, a key regulator of protein synthesis and cell growth. By reducing mTOR activity, protein synthesis is diminished, which may decrease the need for tRNA modification and indirectly reduce the functional activity of RPUSD3. | ||||||
Fluorouracil | 51-21-8 | sc-29060 sc-29060A | 1 g 5 g | $36.00 $149.00 | 11 | |
5-Fluorouracil is metabolized into nucleotide analogs that interfere with RNA processing and function. This interference can lead to a reduced requirement for tRNA modification enzymes, thereby potentially decreasing the functional activity of RPUSD3 involved in tRNA modification. | ||||||
Chloroquine | 54-05-7 | sc-507304 | 250 mg | $68.00 | 2 | |
Chloroquine intercalates into DNA and RNA, which can disrupt nucleic acid function and replication. By destabilizing RNA structure, it may indirectly reduce the need for RNA modification enzymes such as RPUSD3, leading to a decrease in its activity. | ||||||
Actinomycin D | 50-76-0 | sc-200906 sc-200906A sc-200906B sc-200906C sc-200906D | 5 mg 25 mg 100 mg 1 g 10 g | $73.00 $238.00 $717.00 $2522.00 $21420.00 | 53 | |
Actinomycin D binds to DNA and inhibits RNA polymerase, which decreases RNA synthesis. Reduced RNA synthesis can lead to a lower demand for RNA processing and modification, indirectly diminishing the activity of RPUSD3. | ||||||
α-Amanitin | 23109-05-9 | sc-202440 sc-202440A | 1 mg 5 mg | $260.00 $1029.00 | 26 | |
α-Amanitin is a potent inhibitor of RNA polymerase II which halts mRNA synthesis. With decreased mRNA synthesis, there is a reduced requirement for mRNA processing and modification. This can indirectly reduce the activity of RPUSD3, which is involved in RNA modification. | ||||||
Mycophenolic acid | 24280-93-1 | sc-200110 sc-200110A | 100 mg 500 mg | $68.00 $261.00 | 8 | |
Mycophenolic Acid inhibits inosine monophosphate dehydrogenase, resulting in depleted guanine nucleotides. This depletion can affect the availability of substrates necessary for RNA processing and modification, indirectly diminishing the activity of RPUSD3. | ||||||
Cycloheximide | 66-81-9 | sc-3508B sc-3508 sc-3508A | 100 mg 1 g 5 g | $40.00 $82.00 $256.00 | 127 | |
Cycloheximide inhibits eukaryotic protein synthesis by interfering with the translocation step on the ribosome. This inhibition leads to a decreased demand for modified tRNAs, indirectly reducing the functional activity of RPUSD3 in tRNA modification. | ||||||
Puromycin dihydrochloride | 58-58-2 | sc-108071 sc-108071B sc-108071C sc-108071A | 25 mg 250 mg 1 g 50 mg | $40.00 $210.00 $816.00 $65.00 | 394 | |
Puromycin causes premature chain termination during protein synthesis by acting as an analog to aminoacyl-tRNA. With reduced protein synthesis, the demand for RNA modification by RPUSD3 is indirectly decreased. | ||||||
Tunicamycin | 11089-65-9 | sc-3506A sc-3506 | 5 mg 10 mg | $169.00 $299.00 | 66 | |
Tunicamycin inhibits N-linked glycosylation, which can affect protein folding and stability. By altering protein homeostasis, there is a potential indirect effect on RNA processing enzymes, including RPUSD3, reducing its functional activity. | ||||||