Results 71 to 80 of about 28,838 (280)

Regulation of SUMO Modification [PDF]

, 2007
The small ubiquitin related modifier SUMO is a posttranslational modifier that functions in a wide range of cellular processes like intracellular transport, cell cycle regulation, DNA repair and regulation of transcription.
Knipscheer, P.M. (Puck Maria)
core   +1 more source

Posttranslational modifications of proteins in the pathobiology of medically relevant fungi [PDF]

, 2012
Peer reviewedPublisher ...
Brown, Alistair J P, Leach, Michelle D
core   +2 more sources

Hyperandrogenemia Induces Trophoblast Ferroptosis and Early Pregnancy Loss in Patients With PCOS via CMA‐Dependent FTH1 Degradation

Advanced Science, EarlyView.
In PCOS patients with hyperandrogenemia, decreased ferritin heavy chain 1 (FTH1) causes Fe2⁺ overload and ferroptosis in trophoblasts. Androgens induce FTH1 protein degradation via AR‐LAMP2A‐mediated chaperone‐mediated autophagy pathway, leading to placental development disruption and early pregnancy loss. Metformin mitigates androgen‐induced placental
Hanjing Zhou, Weijie Yang, Na Liu, Qing Liu, Jiamin Jin, Chenqiong Zhao, Xiaoying Jin, Miao Gui, Haiyan Zhu, Songying Zhang, Yinli Zhang   +10 more
wiley   +1 more source

The impact of dysregulation SUMOylation on prostate cancer

Journal of Translational Medicine
Prostate cancer (PCa) remains one of the most common malignancies in men, with its development and progression being governed by complex molecular pathways.
Kailang Li, Haifeng Wang, Bitao Jiang, Xiaofeng Jin   +3 more
doaj   +1 more source

Emerging roles of the SUMO pathway in mitosis

Cell Division, 2008
SUMO proteins are small ubiquitin-like modifiers found in all eukaryotes that become covalently conjugated to other cellular proteins. The SUMO conjugation pathway is biochemically similar to ubiquitin conjugation, although the enzymes within the pathway
Dasso Mary
doaj   +1 more source

Structural basis for the RING catalyzed synthesis of K63 linked ubiquitin chains [PDF]

, 2015
This work was supported by grants from Cancer Research UK (C434/A13067), the Wellcome Trust (098391/Z/12/Z) and Biotechnology and Biological Sciences Research Council (BB/J016004/1).The RING E3 ligase catalysed formation of lysine 63 linked ubiquitin ...
A Plechanovová, A Plechanovová, A Rojas-Fernandez, AA Yunus, AJ McCoy, Anna Plechanovová, AP VanDemark, CE Berndsen, CE Berndsen, CM Guzzo, D Reverter, DC Scott, E Krissinel, Ellis G Jaffray, Emma Branigan, G Winter, GN Murshudov, H Dou, James H Naismith, JN Pruneda, L Chang, L Spyracopoulos, M Scheffner, M Zhang, MB Metzger, MD Winn, MH Tatham, MH Tatham, MJ Eddins, MJ Lewis, P Emsley, P Evans, PY Wu, R Vyas, RM Hofmann, Ronald T Hay, S McKenna, S McKenna, TF Moraes, VB Chen, W Kabsch, Y Galanty, Y Yin   +42 more
core   +4 more sources

Protein Language Model‐Guided Engineering of a 2,3‐Butanediol Dehydrogenase for the Enantioselective Synthesis of Cyclic α‐Hydroxy Ketones

Advanced Science, EarlyView.
A (2R,3R)‐butanediol dehydrogenase from Bacillus subtilis (BsBDH) is engineered for the enantioselective synthesis of 2‐hydroxycyclohexanone. A PASS computational design strategy is proposed to enhance the thermostability of BsBDH. Moreover, ESM‐1v combined with ISM is utilized for enhancing and inverting its stereoselectivity.
Haote Ding, Ling Jiang, Yijia Song, Zhongji Pu, Lirong Yang, Haoran Yu   +5 more
wiley   +1 more source

Targeting the Membrane‐Embedded Rhomboid Protease GlpG: A Multimodal Strategy for Inhibitor Discovery and Mechanistic Insight

Angewandte Chemie, EarlyView.
Created in BioRender. Bohg, C. (2026) https://BioRender.Com/ vi9hi4f. Rhomboid proteases are a mechanistically unique and evolutionarily conserved protein family. Despite their pharmacological relevance, the development of selective inhibitors has lagged behind that of soluble proteases.
Claudia Bohg, Yurii Dubanych, Spyridon Kosteletos, Taoran Xiao, Martin Neuenschwander, Tillmann Utesch, Michael Lisurek, Carl Öster, Andreas Oder, Carola Seyffarth, Kathrin Bach, Denise‐Liù Gracias Leone, František Filandr, Marc Wegert, Sascha Lange, Henry Sawczyc, Jens Peter von Kries, Christian P. R. Hackenberger, Edgar Specker, Han Sun, Kvido Stříšovský, Adam Lange   +21 more
wiley   +2 more sources

SUMO chain-induced dimerization activates RNF4 [PDF]

, 2014
Dimeric RING E3 ligases interact with protein substrates and conformationally restrain the ubiquitin-E2-conjugating enzyme thioester complex such that it is primed for catalysis.
Alejandro Rojas-Fernandez, Anna Plechanovová, Brzovic, Buchwald, Budhidarmo, Calderon-Villalobos, de Bie, Deshaies, Desterro, Desterro, Dou, Dou, Dueber, Ellis Jaffray, Feltham, Galanty, Geiss-Friedlander, Geoffroy, Geoffroy, Goddard, Goddard, Golebiowski, Guzzo, Haas, Hattersley, Hay, Hecker, Hickey, Johnson, Kang, Kravtsova-Ivantsiv, Lallemand-Breitenbach, Liew, Linke, Mace, Martin, Melchior, Michael H. Tatham, Mu, Mukhopadhyay, Mukhopadhyay, Neil Hattersley, Perry, Plechanovová, Plechanovová, Pruneda, Rodriguez, Ronald T. Hay, Saitoh, Sampson, Scheffner, Schermelleh, Shen, Song, Spencer, Sun, Tatham, Tatham, Tatham, Tatham, Vyas, Wenzel, Yin, Yin, Zhang   +64 more
core   +3 more sources

Cinnamic‐Hydroxamic‐Acid Derivatives Exhibit Antibiotic, Anti‐Biofilm, and Supercoiling Relaxation Properties by Targeting Bacterial Nucleoid‐Associated Protein HU

Advanced Science, EarlyView.
Cinnamic‐hydroxamic‐acid derivatives (CHADs) are identified as novel inhibitors of the bacterial nucleoid‐associated protein HU, exhibiting potent antibacterial, anti‐biofilm (both inhibition and eradication), and DNA relaxation (anti‐supercoiling) activities. Moreover, CHADs demonstrate strong synergistic effects with multiple antibiotics.
Huan Chen, Yingqi Xu, Zhaoping Xiong, Hongliang Wang, Xin Wang, Yue Kang, Zhonglin Wang, Xiaoyan Zeng, Yahui Liu, Yehuan Zheng, Wei Chen, Mengzhe Li, Zhenyue Hu, Chi Xu, Yue Wu, Yawen Wang, Zuyi Yuan, Shuai Yuan, Huadong Liu, Steve Matthews, Nan Qiao, Yan Li, Bing Liu   +22 more
wiley   +1 more source