WDR23 Blocking Peptide
- Known as:
- WDR23 Blocking Peptide
- Catalog number:
- 33r-3582
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Fitzgerald industries international
- Gene target:
- WDR23 Blocking Peptide
Related genes to: WDR23 Blocking Peptide
- Gene:
- DCAF11 NIH gene
- Name:
- DDB1 and CUL4 associated factor 11
- Previous symbol:
- WDR23
- Synonyms:
- PRO2389, GL014
- Chromosome:
- 14q12
- Locus Type:
- gene with protein product
- Date approved:
- 2003-01-15
- Date modifiied:
- 2016-10-05
Related products to: WDR23 Blocking Peptide
Related articles to: WDR23 Blocking Peptide
- Osteosarcoma (OS) is a malignant tumor originating in bones with high morbidity rates among adolescents. Current approaches for early diagnosis of OS face significant challenges. This study aimed to construct a comprehensive diagnostic model for OS. - Source: PubMed
Publication date: 2026/02/24
Zou HuishuangFeng XiaoningYu HuaqiJiang RuntianSun GuangweiHuang LiliLu JieLi BinShi WeihanZhang Yaning - E3 ligases are crucial to PROTAC technology, and identifying novel E3 ligase ligands could accelerate the advancement of PROTACs. DCAF11 has shown considerable potential for PROTAC applications. However, the ligands targeting DCAF11 remain limited, highlighting the need for the development of novel ligands for this E3 ligase. In this study, leveraging previous research on DCAF11 ligands, we designed a class of arylidene-thiazoldione scaffolds and applied it to develop PROTACs, resulting in the identification of a potent BRD4 degrader, . Degradation activity and mechanistic studies demonstrated that the compound efficiently induces BRD4 degradation through the proteasomal pathway and via recruitment of DCAF11. This scaffold represents a reliable ligand, capable of facilitating the degradation of various proteins, including CDK4/6, BTK, and FKBP12. Therefore, this study introduces the arylidene-thiazoldione scaffold as a novel DCAF11 ligand and validates its application in PROTAC design, providing strong support for the development of DCAF11-based PROTACs. - Source: PubMed
Publication date: 2026/02/02
Liang JinyiLiu YuyangZhao ManChen LuQin JiajieMa WenjingWang YingWu HaiqiangTian RuilinWei TianziLao LingyinWang JingfeiQu HengyuWang HongboGao RongfangGuo SihanZhang MingHong LiangWang RuiLi Guofeng - Proteolysis-targeting chimeras (PROTACs) have recently gained popularity as targeted protein degradation (TPD) promises to overcome the limitations of occupancy-driven pharmacology. However, most degraders rely on a small number of E3 ligases. In this study, we present the first-in-class histone deacetylase (HDAC) PROTACs recruiting the DDB1- and CUL4- associated factor 11 (DCAF11). We established a synthesis route entirely on solid-phase to prepare a set of eleven degraders. The long and flexible spacer bearing FF2039 (1j) showed significant HDAC1 and 6 degradation in combination with cytotoxicity against the multiple myeloma cell line MM.1S. Further investigations revealed that 1j was also able to degrade HDAC isoforms of class I, IIa and IIb. Compared to our previously published cereblon-recruiting HDAC6 selective PROTAC A6, we succesfully transformed the selective degrader into a pan-HDAC degrader by switching the recruited E3 ligase. A detailed profiling of the anticancer properties of 1j demonstrated its significant antiproliferative activity against both hematological and solid cancer cell lines, driven by cell cycle arrest and apoptosis induction. - Source: PubMed
Publication date: 2025/03/24
Feller FelixWeber HeikoMiranda MartinaHonin IrinaHanl MariaHansen Finn K - Transcription factor NF-E2 p45-related factor 2 (Nrf2) orchestrates defenses against oxidants and thiol-reactive electrophiles. It is controlled at the protein stability level by several E3 ubiquitin ligases (CRL3, CRL4, SCF, and Hrd1). CRL3 is of the greatest importance because it constitutively targets Nrf2 for proteasomal degradation under homeostatic conditions but is prevented from doing so by oxidative stressors. Repression of Nrf2 by CRL3 is attenuated by SQSTM1/p62, and this is reinforced by phosphorylation of SQSTM1/p62. Repression by SCF requires phosphorylation of Nrf2 by GSK3, the activity of which is inhibited by PKB/Akt and other kinases. We discuss how Nrf2 activity is controlled by the ubiquitin ligases under different circumstances. We also describe endogenous signaling molecules that inactivate CRL3 to alleviate stress and restore homeostasis. - Source: PubMed
Publication date: 2025/01/27
Hayes John DDayalan Naidu SharadhaDinkova-Kostova Albena T - Targeted protein degradation (TPD) offers a promising approach for chemical probe and drug discovery that uses small molecules or biologics to direct proteins to the cellular machinery for destruction. Among the >600 human E3 ligases, CRBN and VHL have served as workhorses for ubiquitin-proteasome system-dependent TPD. Identification of additional E3 ligases capable of supporting TPD would unlock the full potential of this mechanism for both research and pharmaceutical applications. This perspective discusses recent strategies to expand the scope of TPD and the surprising convergence of these diverse screening efforts on a handful of E3 ligases, specifically DCAF16, DCAF11 and FBXO22. We speculate that a combination of properties, including superficial ligandability, potential for promiscuous substrate interactions and high occupancy in Cullin-RING complexes, may position these E3 ligases as 'low-hanging fruit' in TPD screens. We also discuss complementary approaches that might further expand the E3 ligase landscape supporting TPD. - Source: PubMed
Publication date: 2025/01/27
Zhang XiaoyuSimon Gabriel MCravatt Benjamin F