Date published: 2025-10-15

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ZFP110 Inhibitors

ZFP110 inhibitors are a class of chemical compounds designed to specifically target zinc finger protein 110 (ZFP110), a transcription factor that plays a pivotal role in regulating gene expression by binding to specific DNA sequences. ZFP110, like other zinc finger proteins, contains zinc finger motifs that are essential for its ability to recognize and bind to precise DNA regions. These motifs are stabilized by the coordination of zinc ions, which are critical for maintaining the three-dimensional structure necessary for the protein's function. Through its binding to DNA, ZFP110 influences the transcription of various genes, impacting a range of cellular processes. Inhibitors of ZFP110 work by disrupting this interaction with DNA, either by destabilizing the zinc finger motifs or by preventing the protein from effectively binding to its target DNA sequences, leading to altered gene regulation and changes in cellular activity.

The mechanisms by which ZFP110 inhibitors function are varied and depend on the specific chemical properties of the compounds. One common mechanism involves chelating the zinc ions that are required to stabilize the zinc finger domains. By binding to these zinc ions, the inhibitors cause the structural collapse of the zinc finger motifs, rendering ZFP110 unable to maintain its functional conformation and bind to DNA. This disruption impairs ZFP110's role in regulating transcription, resulting in altered gene expression. Other inhibitors may block essential protein-protein interactions that are critical for ZFP110 to form transcriptional complexes or interact with other regulatory proteins, further hindering its regulatory functions. Research into ZFP110 inhibitors provides insights into the broader mechanisms of transcriptional control and the role of zinc finger proteins in maintaining cellular function and gene expression networks. Understanding how ZFP110 inhibitors operate sheds light on the intricate processes governing genetic regulation in various biological systems.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Actinomycin D

50-76-0sc-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
(3)

Actinomycin D inhibits ZNF110 expression by binding to DNA, preventing RNA polymerase from elongating.

Resveratrol

501-36-0sc-200808
sc-200808A
sc-200808B
100 mg
500 mg
5 g
$60.00
$185.00
$365.00
64
(2)

Resveratrol inhibits ZNF110 expression through its ability to modulate various signaling pathways.

Curcumin

458-37-7sc-200509
sc-200509A
sc-200509B
sc-200509C
sc-200509D
sc-200509F
sc-200509E
1 g
5 g
25 g
100 g
250 g
1 kg
2.5 kg
$36.00
$68.00
$107.00
$214.00
$234.00
$862.00
$1968.00
47
(1)

Curcumin inhibits ZNF110 by affecting multiple pathways involved in gene expression and protein synthesis.

Etoposide (VP-16)

33419-42-0sc-3512B
sc-3512
sc-3512A
10 mg
100 mg
500 mg
$32.00
$170.00
$385.00
63
(1)

Etoposide inhibits ZNF110 expression by interfering with topoisomerase II, leading to DNA damage and repair.

Ellagic Acid, Dihydrate

476-66-4sc-202598
sc-202598A
sc-202598B
sc-202598C
500 mg
5 g
25 g
100 g
$57.00
$93.00
$240.00
$713.00
8
(1)

Ellagic acid may inhibit ZNF110 by modulating transcription factors and impacting gene expression pathways.

Berberine

2086-83-1sc-507337
250 mg
$90.00
1
(0)

Berberine inhibits ZNF110 through its ability to modulate gene expression and interfere with DNA transcription.

Flavopiridol

146426-40-6sc-202157
sc-202157A
5 mg
25 mg
$78.00
$254.00
41
(3)

Flavopiridol inhibits ZNF110 by targeting cyclin-dependent kinases, which are involved in gene transcription.

Camptothecin

7689-03-4sc-200871
sc-200871A
sc-200871B
50 mg
250 mg
100 mg
$57.00
$182.00
$92.00
21
(2)

Camptothecin inhibits ZNF110 expression by trapping topoisomerase I-DNA complexes, leading to DNA damage.

Ellipticine

519-23-3sc-200878
sc-200878A
10 mg
50 mg
$142.00
$558.00
4
(1)

Ellipticine inhibits ZNF110 expression by intercalating DNA and affecting the function of DNA topoisomerases.