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Key Documents

Autres documents

I1911

Sigma-Aldrich

IU1

≥98% (HPLC)

Synonyme(s) :

1-[1-(4-Fluoro-phenyl)-2,5-dimethyl-1H-pyrrol-3-yl]-2-pyrrolidin-1-yl-ethanone

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About This Item

Formule empirique (notation de Hill):
C18H21FN2O
Numéro CAS:
314245-33-5
Poids moléculaire :
300.37
Numéro MDL:
MFCD01917473
Code UNSPSC :
12352200
ID de substance PubChem :
329815361
Nomenclature NACRES :
NA.77

Niveau de qualité

100

Pureté

≥98% (HPLC)

Forme

powder

Couleur

off-white to light brown

Solubilité

DMSO: >10 mg/mL

Température de stockage

2-8°C

Chaîne SMILES 

FC1=CC=C(N2C(C)=CC(C(CN3CCCC3)=O)=C2C)C=C1

InChI

1S/C18H21FN2O/c1-13-11-17(18(22)12-20-9-3-4-10-20)14(2)21(13)16-7-5-15(19)6-8-16/h5-8,11H,3-4,9-10,12H2,1-2H3

Clé InChI

JUWDSDKJBMFLHE-UHFFFAOYSA-N

Application

IU1 has been used for the inhibition of Ubiquitin Specific Peptidase 14 (USP14) in human neuroblastoma cells (SH-SY5Y) and in ubiquitin-rhodamine hydrolysis plate assay.

Actions biochimiques/physiologiques

IU1 is an inhibitor of USP14, a deubiquitinating enzyme associated with the proteasome. The proteasome mediates the cellular degradation of oxidized, damaged and misfolded proteins which, if not removed, accumulate and become toxic to cells. Proteins targeted for proteasomal degradation are first ubiquitinated, with longer length ubiquitin chains interacting more strongly with the proteasome. Deubiquitinating enzymes (DUBs) such as USP14 interfere with the degradation process. IU1 inhibits USP14-mediated ubiquitin "chain-trimming" thereby enhancing substrate degradation by the proteasome. The compound may help to eliminate toxic proteins more effectively by enhancing their degradation.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

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Consulter la Bibliothèque de documents

USP14 inhibition corrects an in vivo model of impaired mitophagy.
Chakraborty J, et al.
EMBO Molecular Medicine, 10(11), e9014-e9014 (2018)
Di Yun et al.
Neuropharmacology, 133, 354-365 (2018-02-07)
Posttranslational modification and degradation of proteins by the ubiquitin-proteasome system (UPS) is crucial to synaptic transmission. It is well established that 19S proteasome associated deubiquitinases (DUBs) reverse the process of ubiquitination by removing ubiquitin from their substrates. However, their potential
Ningning Liu et al.
Molecular and cellular biochemistry, 431(1-2), 87-96 (2017-04-02)
Persistent activation of nuclear factor B (NF-κB) is very important in the modulation of macrophages cellular response to microbial infections. The deubiquitinase USP14, which is critical for ubiquitin-mediated proteasomal degradation of proteins, is known to be involved in cancer, neurological
Inactive USP14 and inactive UCHL5 cause accumulation of distinct ubiquitinated proteins in mammalian cells.
Chadchankar J, et al.
bioRxiv, 10(11), 479758-479758 (2018)
Liu Xu et al.
International journal of biological sciences, 16(15), 2951-2963 (2020-10-17)
Previous studies have demonstrated that the antitumor potential of IU1 (a pharmacological compound), which was mediated by selective inhibition of proteasome-associated deubiquitinase ubiquitin-specific protease 14 (USP14). However, the underlying molecular mechanisms remain elusive. It has been well established that mdm2
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