Results 121 to 130 of about 85,477 (330)

A Prion‐Like Domain in EBV EBNA1 Promotes Phase Separation and Enables SRRM1 Splicing

open access: yesAdvanced Science, EarlyView.
This study discoveries that EBV EBNA1 behaves as a prion‐like protein, verified using cell‐based assays and the Saccharomyces cerevisiae Sup35p prion identification system. The prion‐like domain of EBNA1 drives liquid–liquid phase separation. EBNA1 interacts with the splicing factor SRSF1 to regulate the expression of the SRRM1 splicing isoforms ...
Xiaoyue Zhang   +17 more
wiley   +1 more source

Post-translational modifications of fibrinogen: implications for clotting, fibrin structure and degradation

open access: yesMolecular Biomedicine
Fibrinogen, a blood plasma protein with a key role in hemostasis and thrombosis, is highly susceptible to post-translational modifications (PTMs), that significantly influence clot formation, structure, and stability.
Francesca Nencini   +9 more
semanticscholar   +1 more source

Post-Translational Modifications in Tumor-Associated Antigens as a Platform for Novel Immuno-Oncology Therapies

open access: yesCancers, 2022
Simple Summary Tumor-associated antigens (TAAs) are antigens present in tumor cells, but are also expressed in normal cells. However, TAAs are aberrantly expressed by tumor cells, and can elicit multiple specific immune responses. One key feature of TAAs
A. Srivastava   +3 more
semanticscholar   +1 more source

The Role of Protein Post-Translational Modifications in Fruit Ripening

open access: yesHorticulturae
Fruit ripening represents a multifaceted biological process intricately controlled by an array of plant hormones, transcription factors, and epigenetic modifications.
Ting Li   +4 more
doaj   +1 more source

ProteomeScout: A repository and analysis resource for post-translational modifications and proteins [PDF]

open access: yes, 2014
ProteomeScout (https://proteomescout.wustl.edu) is a resource for the study of proteins and their post-translational modifications (PTMs) consisting of a database of PTMs, a repository for experimental data, an analysis suite for PTM experiments, and a ...
Alex S. Holehouse   +42 more
core   +3 more sources

Dynamic Arginine Methylation of YBX1 Relay Controls Its Phase Separation and Chemoradiotherapy Resistance in Rectal Cancer

open access: yesAdvanced Science, EarlyView.
Protein arginine methyltransferase 3 (PRMT3) induces the arginine methylation of Y‐box binding protein 1 (YBX1), which suppresses phase separation and is imperative for its nuclear translocation. Subsequently, lysine‐specific demethylase 4A demethylates YBX1 to unmask the R247 residue and promote its phase separation, which transcriptionally regulates ...
Yunxing Shi   +11 more
wiley   +1 more source

Post-translational modifications of Keap1: the state of the art

open access: yesFrontiers in Cell and Developmental Biology
The Keap1-Nrf2 signaling pathway plays a crucial role in cellular defense against oxidative stress-induced damage. Its activation entails the expression and transcriptional regulation of several proteins involved in detoxification and antioxidation ...
Yunjia Song   +5 more
semanticscholar   +1 more source

Integration of protein phosphorylation, acetylation, and methylation data sets to outline lung cancer signaling networks [PDF]

open access: yes, 2018
Integrated multiomics network analysis reveals signaling profiles in lung cancer.
Clark, Neil R.   +14 more
core   +1 more source

Arabidopsis TRB Proteins Form Two Closely Related Complexes to Mediate H3K4me3 Demethylation and Transcriptional Repression

open access: yesAdvanced Science, EarlyView.
This study reveals that Arabidopsis telomere repeat binding proteins (TRBs) form two closely related complexes. These complexes mediate H3K4me3 demethylation and transcriptional repression through a positive feedback loop and cooperate with PEAT and PRC2 complexes to regulate multiple histone modifications and gene expression across the genome ...
Qi Wang   +7 more
wiley   +1 more source

Substrate and Functional Diversity of Protein Lysine Post-translational Modifications

open access: yesGenomics, Proteomics & Bioinformatics
Lysine post-translational modifications (PTMs) are widespread and versatile protein PTMs that are involved in diverse biological processes by regulating the fundamental functions of histone and non-histone proteins.
Bingbing Hao   +5 more
semanticscholar   +1 more source

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