Results 51 to 60 of about 109,331 (244)

Dynamic control of selectivity in the ubiquitination pathway revealed by an ASP to GLU substitution in an intra-molecular salt-bridge network [PDF]

, 2012
Ubiquitination relies on a subtle balance between selectivity and promiscuity achieved through specific interactions between ubiquitin-conjugating enzymes (E2s) and ubiquitin ligases (E3s).
Bonvin, Alexandre M. J. J., Sjoerd J de Vries, Adrien S. J. Melquiond (122976), H Th Marc Timmers, Alexandre M. J. J. Bonvin (18079), Adrien S J Melquiond, Wijk, Sjoerd van, Alexandre M J J Bonvin, Melquiond, Adrien S. J., Timmers, H. Th. Marc, Sjoerd J. de Vries (110976), H. Th. Marc Timmers (10936), Sjoerd J. L. van Wijk (122975), Vries, Sjoerd J. de, Sjoerd J L van Wijk, van Wijk Sjoerd J. L., de Vries Sjoerd J., Timmers H. Th. Marc, Bonvin Alexandre M. J. J., Melquiond Adrien S. J.   +19 more
core   +1 more source

TRIM56 coiled-coil domain structure provides insights into its E3 ligase functions

Computational and Structural Biotechnology Journal, 2023
Protein ubiquitination is a post-translation modification mediated by E3 ubiquitin ligases. The RING domain E3 ligases are the largest family of E3 ubiquitin ligases, they act as a scaffold, bringing the E2-ubiquitin complex and its substrate together to
Xiaohua Lou, Binbin Ma, Yuan Zhuang, Xiang Xiao, Laurie J. Minze, Junji Xing, Zhiqiang Zhang, Xian C. Li   +7 more
doaj   +1 more source

E3 ubiquitin ligases in bone homeostasis: from regulatory mechanisms to skeletal diseases and therapeutic targeting

Frontiers in Cell and Developmental Biology
E3 ubiquitin ligases are key determinants of substrate specificity within the ubiquitin–proteasome system and have emerged as important regulators of skeletal biology.
Yutong Zhao, Nanjue Cao, Wenxiao Yang, Yuanfang Wang, Wei Wang   +4 more
doaj   +1 more source

Ubiquitin chain formation by RBR E3-ligases [PDF]

, 2013
Ubiquitination is an important posttranslational modification that plays a role in virtually all cellular pathways. Ubiquitin signals are made out of one or multiple ubiquitin proteins that are targeted towards substrates by a cascade of E1, E2 and E3 ...
Smit, J.J. (Judith)
core   +1 more source

Image_2_How to Inactivate Human Ubiquitin E3 Ligases by Mutation.jpg

, 2020
E3 ubiquitin ligases are the ultimate enzymes involved in the transfer of ubiquitin to substrate proteins, a process that determines the fate of the modified protein.
Ugo Mayor (404331), Cristina Garcia-Barcena (8395278), Nerea Osinalde (2989329), Juanma Ramirez (812674)   +3 more
core   +1 more source

Autophagy and mitophagy in pancreatic β‐cell homeostasis and their involvement in diabetes pathophysiology

FEBS Letters, EarlyView.
This review focuses on the role of autophagy and mitophagy in maintaining pancreatic β‐cell function and homeostasis. We discuss how genetic defects affecting these pathways contribute to the development of type 1, type 2, monogenic, and gestational diabetes. We further explore their potential as therapeutic targets. Created in BioRender.
Yunkyeong Lee, Mingming Tong, Anna L. Gloyn   +2 more
wiley   +1 more source

E3 ubiquitin ligases: structural diversity, dysregulation in disease, and their emerging role in targeted therapeutic strategies

Frontiers in Molecular Biosciences
The Ubiquitin-Proteasome System (UPS) is a key mechanism of cellular homeostasis. A central part of this mechanism is E3 ubiquitin ligases, which selectively direct proteins to be ubiquitinated for degradation via the UPS.
Srineevas Sriram, Prahalad Krishnakumar, C. Sudandiradoss   +2 more
doaj   +1 more source

A screen for E3 ubiquitination ligases that genetically interact with the adaptor protein Cindr during Drosophila eye patterning. [PDF]

PLoS ONE, 2017
Ubiquitination is a crucial post-translational modification that can target proteins for degradation. The E3 ubiquitin ligases are responsible for recognizing substrate proteins for ubiquitination, hence providing specificity to the process of protein ...
Kwami F Ketosugbo, Henry L Bushnell, Ruth I Johnson   +2 more
doaj   +1 more source

Emerging experimental and computational methods for studying redox‐regulated structural transitions

FEBS Letters, EarlyView.
Redox reactions can reshape proteins and alter how they behave in cells, with important consequences for health and disease. This review explores emerging experimental and computational approaches for discovering these redox‐sensitive protein switches, revealing their structural effects, and predicting their behavior, opening new opportunities to ...
Tasneem Rass, Dana Reichmann, Gábor Erdős   +2 more
wiley   +1 more source

Image_1_How to Inactivate Human Ubiquitin E3 Ligases by Mutation.jpg

, 2020
E3 ubiquitin ligases are the ultimate enzymes involved in the transfer of ubiquitin to substrate proteins, a process that determines the fate of the modified protein.
Ugo Mayor (404331), Cristina Garcia-Barcena (8395278), Nerea Osinalde (2989329), Juanma Ramirez (812674)   +3 more
core   +1 more source