Work

The CUL7 E3 Ubiquitin Ligase Targets Insulin Receptor Substrate 1 for Ubiquitin-Dependent Degradation

Year: 2008

Type: article

Source: Molecular Cell

DOI: 10.1016/j.molcel.2008.03.009

Authors: Xinsong Xu, Antonio Sarikas, Dora C. Dias-Santagata, Georgia Dolios, Pascal J. Lafontant, Shih-Chong Tsai, Wuqiang Zhu, Hidehiro Nakajima, Hisako O. Nakajima, Loren J. Field, Rong Wang, Zhen-Qiang Pan

Institutions: Icahn School of Medicine at Mount Sinai, Indiana University School of Medicine

Language: English

Topic: Ubiquitin and proteasome pathways

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: bronze

Funders: Deutsche Forschungsgemeinschaft, National Institutes of Health, National Heart, Lung, and Blood Institute, National Cancer Institute, National Institute of General Medical Sciences, National Center for Research Resources

Awards: G1053934161, G1076839231, G2326019417, The function and regulation of the cullin family E3 ubiquitin ligases, G2976715593, Cyclin D2 and Cardiac Regeneration, Genetics and Treatment of Heart Failure in the Young, G7517234395, MASS SPECTROMETRY SHARED RESOURCE, Studies on ROC1-dependent E3 ubiquitin ligases, MALD/ESI-Q-TOF Mass Spectrometer Shared Instrument

OpenAlex ID: W2164301822

FWCI: 6.079

Cites: 42

Cited by: 217

Related to: 10