Date published: 2026-5-9

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DDX34 Inhibitors

DDX34 inhibitors refer to a specific class of chemical compounds that target and inhibit the activity of the DDX34 protein, a member of the DEAD-box family of RNA helicases. DDX34 is involved in RNA processing, unwinding RNA structures, and facilitating the assembly or disassembly of ribonucleoprotein complexes. It plays a vital role in various aspects of RNA metabolism, such as RNA splicing, translation, and degradation. Inhibitors of DDX34 specifically interfere with the helicase's ability to hydrolyze ATP, which is critical for its RNA-unwinding function. By disrupting this ATPase activity, DDX34 inhibitors affect the protein's capacity to carry out its roles in RNA processing, potentially altering downstream molecular processes that depend on properly regulated RNA structures.

DDX34 inhibitors are diverse, consisting of small molecules designed to bind either to the ATP-binding site or to regions of the protein that regulate its interaction with RNA substrates. These molecules are typically characterized by high affinity for DDX34, leading to selective inhibition of its helicase function without affecting other related enzymes. Structural modifications within these compounds allow fine-tuning of their binding efficiency and specificity. The ability of DDX34 inhibitors to selectively inhibit a particular member of the DEAD-box family is crucial for their utility in studying the biological functions of DDX34, as well as their broader influence on RNA dynamics. These inhibitors serve as valuable tools for researchers aiming to explore the complex regulatory mechanisms of RNA helicases and their role in post-transcriptional gene expression.

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Items 1 to 10 of 11 total

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Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Suramin sodium

129-46-4sc-507209
sc-507209F
sc-507209A
sc-507209B
sc-507209C
sc-507209D
sc-507209E
50 mg
100 mg
250 mg
1 g
10 g
25 g
50 g
$152.00
$214.00
$728.00
$2601.00
$10965.00
$21838.00
$41096.00
5
(1)

Suramin is known to inhibit various ATP-utilizing enzymes. It may compete for the ATP-binding site on DHX34, impairing its function.

Quercetin

117-39-5sc-206089
sc-206089A
sc-206089E
sc-206089C
sc-206089D
sc-206089B
100 mg
500 mg
100 g
250 g
1 kg
25 g
$11.00
$17.00
$110.00
$250.00
$936.00
$50.00
33
(2)

Quercetin has been reported to inhibit certain helicases by preventing their ATPase activity. It may exhibit similar inhibitory effects on DHX34.

Myricetin

529-44-2sc-203147
sc-203147A
sc-203147B
sc-203147C
sc-203147D
25 mg
100 mg
1 g
25 g
100 g
$97.00
$188.00
$260.00
$510.00
$1022.00
3
(1)

Like Quercetin, Myricetin can inhibit some helicase activities. It might obstruct DHX34's RNA unwinding function.

Roscovitine

186692-46-6sc-24002
sc-24002A
1 mg
5 mg
$94.00
$265.00
42
(2)

Roscovitine inhibits cyclin-dependent kinases. As an ATP competitor, it could impair the ATP-dependent activity of DHX34.

5-Iodotubercidin

24386-93-4sc-3531
sc-3531A
1 mg
5 mg
$153.00
$464.00
20
(2)

This adenosine analog might compete for ATP binding, possibly reducing the ATP-dependent function of DHX34.

Alsterpaullone

237430-03-4sc-202453
sc-202453A
1 mg
5 mg
$68.00
$312.00
2
(1)

As a kinase inhibitor and ATP competitor, Alsterpaullone might interfere with the ATPase activity of DHX34.

Ellagic Acid, Dihydrate

476-66-4sc-202598
sc-202598A
sc-202598B
sc-202598C
500 mg
5 g
25 g
100 g
$58.00
$95.00
$245.00
$727.00
8
(1)

Some studies suggest ellagic acid can inhibit helicase. It might impair DHX34's RNA unwinding activity.

KU 0063794

938440-64-3sc-361219
10 mg
$209.00
(1)

As an mTOR inhibitor, it may compete for ATP binding, potentially hampering the ATP-dependent function of DHX34.

Olaparib

763113-22-0sc-302017
sc-302017A
sc-302017B
250 mg
500 mg
1 g
$210.00
$305.00
$495.00
10
(1)

Though primarily a PARP inhibitor, its mechanism of ATP-competition might affect ATP-dependent functions like that of DHX34.

Silvestrol

697235-38-4sc-507504
1 mg
$920.00
(0)

Known to inhibit DEAD-box helicases. It may block the helicase action of DHX34 by affecting its ATPase activity.