Results 91 to 100 of about 54,326 (298)

SUMO Modification Stabilizes Enterovirus 71 Polymerase 3D To Facilitate Viral Replication. [PDF]

, 2016
Accumulating evidence suggests that viruses hijack cellular proteins to circumvent the host immune system. Ubiquitination and SUMOylation are extensively studied posttranslational modifications (PTMs) that play critical roles in diverse biological ...
Gong, P, Hu, Q, Ke, X, Liu, Y, Meng, J, Shu, B, Wang, H, Zhang, Y, Zheng, C, Zheng, Z   +9 more
core   +1 more source

A WLM Protein with SUMO-Directed Protease Activity [PDF]

Molecular and Cellular Biology, 2010
Covalent modification of eukaryotic proteins by ubiquitin and the distantly related ubiquitin-like protein called SUMO contributes to an extraordinary assortment of biological regulatory mechanisms (2). These attachments have different consequences, depending not only on which of the proteins is attached but also on whether they are in the form of a ...
Dan, Su, Mark, Hochstrasser
openaire   +2 more sources

PFOS Disrupts Oocyte Maturation and Early Embryonic Development via Ovarian FOXK1 O‐GlcNAcylation in Mice

Advanced Science, EarlyView.
Perfluorooctane sulfonate (PFOS) exposure disrupts oocyte maturation and early embryonic development. This study elucidates the mechanism by which enhanced O‐GlcNAcylation of FOXK1 underlies the PFOS‐induced reduction of progesterone levels in granulosa cells and the disturbance of follicular microenvironment.
Shuwen Han, Qin Yuan, Zhu Wu, Yaohui Fang, Hong Qian, Jiale Zhu, Yuchen Zhang, Ke Deng, Liangliang Su, Haibo Xu, Haotian Shu, Yiming Gong, Qiaoqiao Xu, Guizhen Du, Di Wu, Yun Fan, Chuncheng Lu   +16 more
wiley   +1 more source

The C-terminus of p63 contains multiple regulatory elements with different functions [PDF]

, 2010
The transcription factor p63 is expressed as at least six different isoforms, of which two have been assigned critical biological roles within ectodermal development and skin stem cell biology on the one hand and supervision of the genetic stability of ...
Candi, Eleonora, Durst, Florian, Dötsch, Volker, Melino, Gennaro, Ou, Horng Der, Rajalingam, Krishnaraj, Schäfer, Birgit, Straub, Wesley E., Weber, Tobias Alexander   +8 more
core   +2 more sources

Super Resolution Microscopy of SUMO Proteins in Neurons [PDF]

Frontiers in Cellular Neuroscience, 2019
The ubiquitously expressed SUMO proteins regulate a plethora of cellular pathways and processes. While they have a predominantly nuclear localization, extranuclear roles of SUMO isoforms at the synapse have also been described, making SUMOylation one of the major post-translational regulators of nerve functions.
Colnaghi L, Russo L, Natale C, Restelli E, Cagnotto A, Salmona M, Chiesa R, Fioriti L   +7 more
openaire   +4 more sources

Targeting DESI2 as a Novel Therapeutic Strategy for JAK2‐Mutant Leukemias

Advanced Science, EarlyView.
Mass spectrometry‐based proteomics identify DESI2 as a novel component of the JAK2‐V617F complex, which associates with and stabilizes mutant JAK2 through deSUMOylation and deubiquitination, therefore promoting JAK2 mutant cell growth and MPN disease onset in vivo.
Husheng Mei, Wuqiang Wen, Wenjun Zhang, Shujing Zhang, Ting Sun, Guiming Li, Jing Zhang, Shuang Qi, Jie Zhou, Bing Li, Yunshuo Zhao, Xiaotong Chen, Bowen Li, Yiying Xue, Wang Lu, Yanli Sun, Jingyao Wang, Hengyue Shan, Shengzhe Zhang, Yushan Huang, Yisa Chen, Wenchao Wang, Qingsong Liu, Wenchao Lu, Li Tan, Yi Ding, Jianfei Fu, Jun Long, Lei Zhang, Baobing Zhao, Aibin Liang, Baishan Jiang, Jing Yang   +32 more
wiley   +1 more source

Mechanism of Adenovirus E4-ORF3-Mediated SUMO Modifications

mBio, 2019
Regulation of a variety of different cellular processes, including posttranslational modifications, is critical for the ability of many viruses to replicate efficiently within host cells.
Sook-Young Sohn, Patrick Hearing
doaj   +1 more source

Tissue-specific inhibition of protein sumoylation uncovers diverse SUMO functions during C. elegans vulval development.

PLoS Genetics, 2022
The sumoylation (SUMO) pathway is involved in a variety of processes during C. elegans development, such as gonadal and vulval fate specification, cell cycle progression and maintenance of chromosome structure.
Aleksandra Fergin, Gabriel Boesch, Nadja R Greter, Simon Berger, Alex Hajnal   +4 more
doaj   +1 more source

Atomic structures of TDP-43 LCD segments and insights into reversible or pathogenic aggregation. [PDF]

, 2018
The normally soluble TAR DNA-binding protein 43 (TDP-43) is found aggregated both in reversible stress granules and in irreversible pathogenic amyloid. In TDP-43, the low-complexity domain (LCD) is believed to be involved in both types of aggregation. To
A Jain, A Molliex, A Patel, A Saini, A Soragni, AE Conicella, AF Harrison, AJ McCoy, AK Chen, AK Walker, AWP Fitzpatrick, C Amador-Ortiz, C Colombrita, C Lagier-Tourenne, C Schwab, C Yang, C-H Chiang, CK Chang, CM Dewey, Collaborative Computational Project, Number 4., D Shi, DA Bosco, David R. Boyer, David S. Eisenberg, DS Eisenberg, DT Murray, Duilio Cascio, E Bentmann, E Buratti, E Kabashi, EB Lee, Elizabeth L. Guenther, EM Marcotte, F Meersman, GM Sheldrick, GN Murshudov, GS Pesiridis, H Nakashima-Yasuda, Hamilton Trinh, HB Schmidt, HJ Dyson, HJ Kim, HY Zoghbi, J Hattne, JA Rodriguez, Jiahui Lu, JJ Wiltzius, Jose A. Rodriguez, JP Ling, JR Wheeler, L Goldschmidt, L Lim, LC Reineke, LL Jiang, LL Jiang, LM Igaz, M Budini, M Cushman, M Hasegawa, M Kato, M Mompeán, M Neumann, M Xu, MA Gitcho, Masato Kato, MC Lawrence, MD Winn, Michael P. Hughes, Michael R. Sawaya, MP Hughes, MR Sawaya, N Gilks, N Kedersha, P Emsley, P Hackman, P-N Cheng, PD Adams, PJ Lukavsky, PM Seidler, PS Estes, Qin Cao, RA Fuentealba, S Higashi, S Xiang, SC Ling, TM Franzmann, TPJ Knowles, W Guo, W Kabsch, W Kabsch, Y Dang, Y Lin, Z Otwinowski, ZM March   +93 more
core   +1 more source

The Polycomb Protein Pc2 Is a SUMO E3 [PDF]

Cell, 2003
Polycomb group (PcG) proteins form large multimeric complexes (PcG bodies) which are involved in the stable repression of gene expression. The human PcG protein, Pc2, has been shown to recruit the transcriptional corepressor, CtBP, to PcG bodies. We show that CtBP is sumoylated at a single lysine.
Kagey, Michael H, Melhuish, Tiffany A, Wotton, David   +2 more
openaire   +2 more sources