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Decoding Post-Translational Modification Crosstalk With Proteomics.

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TLDR
In this paper, the authors provide an overview of the basic modes of PTM crosstalk, the proteomic methods to elucidate PTM co-stalk and approaches that can inform about the functional consequences.
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This article is published in Molecular & Cellular Proteomics.The article was published on 2021-01-01 and is currently open access. It has received 65 citations till now. The article focuses on the topics: Crosstalk (biology).

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Journal ArticleDOI

Deciphering combinatorial post-translational modifications by top-down mass spectrometry.

TL;DR: Top-down analysis of intact proteins, termed the top-down approach, offers the potential to map protein sequences and localize multiple PTMs on each protein, providing the most comprehensive cataloging of proteoforms as discussed by the authors .
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FAIMS Enhances the Detection of PTM Crosstalk Sites

TL;DR: An enrichment-free, label-free proteomics method that utilizes high-field asymmetric ion mobility spectrometry (FAIMS) to enhance the detection of PTM crosstalk and envisage LC-FAIMs-MS/MS to play an important role in expanding the repertoire of multi-PTM identifications.
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The evolution of post-translational modifications.

TL;DR: In this paper , the authors review advances made in the past two years towards understanding the evolution of PTMs and their associated enzymes, and the true fraction of PTM sites that are functional and thus subject to selection remains an open question.
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Proximity-Dependent Biotinylation Approaches to Explore the Dynamic Compartmentalized Proteome

TL;DR: Progress made in this field is discussed and how proximity-dependent biotinylation strategies could elucidate the contributions of PTMs, such as phosphorylation, to the compartmentalization of proteins.
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Trans-anethole ameliorates lipopolysaccharide-induced acute liver inflammation in broilers via inhibiting NF-κB signaling pathway

TL;DR: In this article , the authors investigated the effect of trans-anethole (TA) on liver inflammation in broilers by determining the levels of inflammatory mediators in serum and liver, relative mRNA expression and protein expression of inflammatory genes in NF-κB signaling pathway.
References
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Journal ArticleDOI

The Protein Kinase Complement of the Human Genome

TL;DR: The protein kinase complement of the human genome is catalogued using public and proprietary genomic, complementary DNA, and expressed sequence tag sequences to provide a starting point for comprehensive analysis of protein phosphorylation in normal and disease states and a detailed view of the current state of human genome analysis through a focus on one large gene family.
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PEST sequences and regulation by proteolysis

TL;DR: Recent experimental support for the hypothesis that polypeptide sequences enriched in proline, glutamic acid, serine, and threonine target proteins for rapid destruction is provided with a number of papers providing strong evidence that PEST regions serve as proteolytic signals.
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PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse

TL;DR: PhosphoSitePlus as discussed by the authors is an open, comprehensive, manually curated and interactive resource for studying experimentally observed post-translational modifications, primarily of human and mouse proteins.
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Protein posttranslational modifications: the chemistry of proteome diversifications.

TL;DR: An understanding of the scope and pattern of the many posttranslational modifications in eukaryotic cells provides insight into the function and dynamics of proteome compositions.
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Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution

TL;DR: It is proposed that the regulation of protein function by phosphorylation often depends on simple nonspecific mechanisms that disrupt or enhance protein-protein interactions and the gain or loss of phosphorylated sites in rapidly evolving regions could facilitate the evolution of kinase-signaling circuits.
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