Results 221 to 230 of about 278,733 (404)

SUMO-1 Modification of Mdm2 Prevents Its Self-Ubiquitination and Increases Mdm2 Ability to Ubiquitinate p53 [PDF]

, 2000
Thomas Buschmann, Serge Y. Fuchs, Chee-Gun Lee, Zhen-Qiang Pan, Ze’ev A. Ronai   +4 more
openalex   +1 more source

Post‐Translational Modifications in Cilia and Ciliopathies

Advanced Science, EarlyView.
This review synthesizes current understanding of post‐translational modifications (PTMs) in ciliary proteins and emphasizes their roles in ciliary formation, homeostasis, and signaling. This review also discusses the implication of PTM dysregulation in ciliopathies and explores therapeutic strategies targeting PTM‐modifying enzymes.
Jie Ran, Jun Zhou
wiley   +1 more source

Ubiquitination contributes to the regulation of GDP-mannose pyrophosphorylase B activity

Frontiers in Molecular Neuroscience
GDP-mannose pyrophosphorylase B (GMPPB) loss-of-function is associated with muscular dystrophy and variable additional neurological symptoms. GMPPB facilitates the catalytic conversion of mannose-1-phosphate and GTP to GDP-mannose, which serves as a ...
Patricia Franzka, Sonnhild Mittag, Abhijnan Chakraborty, Otmar Huber, Christian A. Hübner   +4 more
doaj   +1 more source

The short-lived MATα2 transcriptional regulator is ubiquitinated in vivo [PDF]

, 1991
The substrates of ubiquitin-dependent proteolytic pathways include both damaged or otherwise abnormal proteins and undamaged proteins that are naturally short-lived. Few specific examples of the latter class have been identified, however.
Chau, Vincent, Ellison, Michael J., Hochstrasser, Mark, Varshavsky, Alexander   +3 more
core  

Nuclear‐Localized BCKDK Facilitates Homologous Recombination Repair to Support Breast Cancer Progression and Therapy Resistance

Advanced Science, EarlyView.
Under DNA damage, tumor cells rely on efficient DNA repair for survival and therapy resistance. This study has demonstrated that BCKDK localizes to breast cancer cell nuclei, where it binds to and phosphorylates RNF8, thereby blocking ubiquitin‐mediated degradation of RAD51 and enhancing HRR. A selective BCKDK inhibitor synergizes with clinical agents,
Haiying Liu, Jiaqian Feng, Tingting Pan, Pinggen Zhang, Ling Ye, Zetan Jiang, Zilong Zhou, Qiankun Mao, Jian Li, Xinyi Yang, Ping Gao, De Huang, Huafeng Zhang   +12 more
wiley   +1 more source

Ligand-induced ubiquitination of the platelet-derived growth factor beta-receptor plays a negative regulatory role in its mitogenic signaling.

, 1993
Seijiro Mori, Carl‐Henrik Heldin, Lena Claesson‐Welsh   +2 more
openalex   +1 more source

The hPLIC Proteins May Provide a Link between the Ubiquitination Machinery and the Proteasome [PDF]

, 2000
Maurits F. Kleijnen, Alan H. Shih, Pengbo Zhou, Sushant Kumar, Raymond E. Soccio, Nancy Kedersha, Grace Gill, Peter M. Howley   +7 more
openalex   +1 more source

Pyruvate Carboxylase in Macrophages Aggravates Atherosclerosis by Regulating Metabolism Reprogramming to Promote Inflammatory Responses Through the Hypoxia‐Inducible Factor‐1 Signaling Pathway

Advanced Science, EarlyView.
This study investigates the role of macrophage pyruvate carboxylase (PC) in atherosclerosis (AS) demonstrating that PC upregulation in macrophages promotes metabolism reprogramming to enhance inflammatory responses via the HIF‐1 signaling pathway.
Ling‐Na Zhao, Rui‐Ling Wang, Ran‐Xin Liu, Meng‐Ru Zheng, Li Zhao, Bao‐Feng Li, Jia‐Le Li, De‐Shen Liu, Xiao‐Xia He, Qin‐Bao Peng, Kai Li, Tian‐Xiao Lin, Ying‐Ying Liu, Sheng‐Ping He, Jun Lu, Shao‐Yi Zheng, Xiu Liu, Fang‐Ze Huang   +17 more
wiley   +1 more source

Structure-guided engineering enables E3 ligase-free and versatile protein ubiquitination via UBE2E1

Nature Communications
Ubiquitination, catalyzed usually by a three-enzyme cascade (E1, E2, E3), regulates various eukaryotic cellular processes. E3 ligases are the most critical components of this catalytic cascade, determining both substrate specificity and ...
Xiangwei Wu, Yunxiang Du, Lu-Jun Liang, Ruichao Ding, Tianyi Zhang, Hongyi Cai, Xiaolin Tian, Man Pan, Lei Liu   +8 more
doaj   +1 more source

Hypoxia-inducible factor 1α protein expression is controlled by oxygen-regulated ubiquitination that is disrupted by deletions and missense mutations [PDF]

, 2000
Thomas R. Sutter, Erik Laughner, Gregg L. Semenza   +2 more
openalex   +1 more source