Results 61 to 70 of about 540 (119)

Epigenetic regulation of mycorrhizal symbioses: from plastic responses to transgenerational legacies

New Phytologist, Volume 250, Issue 3, Page 1438-1452, May 2026.
Summary Mycorrhizal symbioses represent one of the most widespread and ecologically significant plant–microbe interactions, shaping plant nutrition, stress resilience, and ecosystem functioning. Beyond their role in nutrient exchange and systemic defense, growing evidence suggests that these symbioses also influence plant plasticity within and across ...
Gerson Beltrán‐Torres, Henry J. De La Cruz, Stéphane Maury, Martina Janoušková, Claire Veneault‐Fourrey, Vít Latzel, Pierre‐Emmanuel Courty, Harold Duruflé, Jörg Tost, Iris Sammarco   +9 more
wiley   +1 more source

Chaperone‐Mediated Autophagic Degradation of USP9X in Macrophages Exacerbates Postmyocardial Infarction Inflammation and Cardiac Dysfunction

Advanced Science, Volume 13, Issue 19, 2 April 2026.
This study demonstrates that inflammatory stimuli induce the acetylation‐triggered, chaperone‐mediated autophagic degradation of ubiquitin‐specific peptidase 9 X‐linked (USP9X) in macrophages. USP9X acts as a macrophage “inflammation switch” after myocardial infarction (MI). USP9X loss destabilizes tumor necrosis factor receptor‐associated factor (TRAF)
Biqing Wang, Xiangheng Cai, Mengqi Li, Xue Liu, Junhui Xue, Ye Liu, Ding Ai, Xinyang Hu   +7 more
wiley   +1 more source

Recent advances in proteomic workflows to interrogate the SUMOylome in plants

New Phytologist, Volume 247, Issue 1, Page 90-96, July 2025.
Summary Protein posttranslational modifications (PTMs) are vital for regulating protein functions. SUMOylation, a PTM essential for plant survival, involves attaching a Small Ubiquitin‐like MOdifier (SUMO) to lysine residues of target proteins. SUMOylation influences stress tolerance, cell proliferation, protein stability, and gene expression.
Kishor D. Ingole, Elizaveta Alekseeva, Kathryn S. Lilley, Ari Sadanandom   +3 more
wiley   +1 more source

Ubiquitin‐specific protease 25 improves myocardial ischemia–reperfusion injury by deubiquitinating NLRP3 and negatively regulating NLRP3 inflammasome activity in cardiomyocytes

Clinical and Translational Medicine, Volume 15, Issue 2, February 2025.
Abstract Background Myocardial ischemia/reperfusion injury (MI/RI) restricts the effect of myocardial reperfusion therapy and lacks effective prevention and treatment methods. Deubiquitinating enzymes (DUBs), especially members of the ubiquitin‐specific protease (USP) family of DUBs, are key proteins in the ubiquitination modification process and play
Bozhi Ye, Diyun Xu, Lingfeng Zhong, Yi Wang, Wei Wang, Haowen Xu, Xue Han, Julian Min, Gaojun Wu, Wenhai Huang, Guang Liang   +10 more
wiley   +1 more source

Data-independent acquisition (DIA) approach for comprehensive ubiquitinome profiling in targeted protein degradation

Abstract Targeted protein degradation (TPD) has emerged as a highly promising therapeutic strategy for a wide range of diseases, including cancer and neurodegenerative disorders. The ubiquitin-proteasome system, which is responsible for protein degradation, plays a critical role in this process.
Sathe G, Röth S, Gelders G, Brewer A, Macartney TJ, Wood NT, De Muynck L, Nakasone MA, Phung TK, Buist A, Moechars D, Sapkota GP.   +11 more
europepmc   +2 more sources

Characterization of the Ubiquitin‐Modified Proteome of Recombinant Chinese Hamster Ovary Cells in Response to Endoplasmic Reticulum Stress

Biotechnology Journal, Volume 19, Issue 11, November 2024.
Graphical Abstract and Lay Summary Ubiquitination is an essential cellular process in which proteins are tagged with ubiquitin, marking them for proteasomal degradation. Beyond this role, ubiquitination plays key functions in ER stress, cell signalling, autophagy, and cell cycle regulation. To gain deep insights into ER stress mechanisms and changes to
Karuppuchamy Selvaprakash, Christiana‐Kondylo Sideri, Michael Henry, Esen Efeoglu, David Ryan, Paula Meleady   +5 more
wiley   +1 more source

Ubiquitin signalling in Drosophila innate immune responses

The FEBS Journal, Volume 291, Issue 20, Page 4397-4413, October 2024.
Drosophila innate immunity against bacterial infection relies on humoral responses regulated by the Imd and Toll pathways activating NF‐κB transcription factors, as well as JNK activation and JAK/STAT signalling. These pathways are characterised by E3 ligases and deubiquitinating enzymes that determine ubiquitination of signalling molecules followed by
Anna L. Aalto, Veera Luukkonen, Annika Meinander   +2 more
wiley   +1 more source

Genetic variation in ZmKW1 contributes to kernel weight and size in dent corn and popcorn

Plant Biotechnology Journal, Volume 22, Issue 6, Page 1453-1467, June 2024.
Summary Kernel weight is a critical factor that essentially affects maize (Zea mays) yield. In natural inbred lines, popcorn kernels exhibit overtly smaller sizes compared to dent corn kernels, and kernel weight, which is controlled by multiple genetic loci, varies widely.
Long Zhang, Miaomiao Fu, Wenyu Li, Yongbin Dong, Qiang Zhou, Qilei Wang, Xinyu Li, Jie Gao, Yan Wang, Han Wang, Yayong Li, Jiechen Wang, Yongrui Wu, Yuling Li   +13 more
wiley   +1 more source

Structural proteomics of the human ubiquitinome

Abstract The proteasome maintains the integrity of eukaryotic proteomes by selectively degrading ubiquitinated protein substrates. Ubiquitination targets a wide range of substrates for degradation, including translationally stalled nascent chains, misfolded proteins, and properly folded but short-lived proteins destined for regulatory ...
Anushka Jain, Naiyareen Mayeen, Michael E. Meadow, Nino Kalandadze, Kyle Swovick, Kevin A. Welle, Jennifer R. Hryhorenko, Sina Ghaemmaghami   +7 more
openaire   +1 more source

The functional landscape of the human ubiquitinome.

bioRxiv : the preprint server for biology
Protein ubiquitination regulates cell biology through diverse avenues, from quality control-linked protein degradation to signaling functions such as modulating protein-protein interactions and enzyme activation. Mass spectrometry-based proteomics has allowed proteome-scale quantification of hundreds of thousands of ubiquitination sites (ubi-sites ...
van Gerwen, Julian, Fottner, Maximilian, Wang, Shengbo, Busby, Bede, Boswell, Ellen, Schnacke, Paul, Carrano, Andrea C., Bakowski, Malina A., Troemel, Emily R., Studer, Romain, Strumillo, Marta, Martin, Maria-Jesus, Harper, J. Wade, Lang, Kathrin, Jones, Andrew R., Bennett, Eric J., Vizcaíno, Juan Antonio, Barrio-Hernandez, Inigo, Beltrao, Pedro   +18 more
openaire   +2 more sources