Press Release – Large-scale analysis of protein arginine methylation by mass spectrometry

The article by Dr. Tiziana Bonaldi et al. is published in Current Protein & Peptide Science, 2020

Methylation (namely addition of a methyl group) of arginine amino acid residues of proteins is a post-translational modification (PTM) catalyzed by a family of nine enzymes called Protein Arginine Methyl-Transferases (PRMTs).

PRMTs have been gaining increasing attention in the scientific landscape due their role in several essential physiological processes and implication in various diseases, including cancer and neurological disorders; loss of PRMT1 is lethal at the early developmental stages, while overexpression is frequently observed in different tumor types and correlates with poor patient prognosis, suggesting that inhibition of PRMTs may represent an effective therapeutic approach in oncology. Moreover, PTM levels are deregulated in different tumor types, and both local and global changes in PTM of the DNA-associated proteins – the histones – are linked to Amyotrophic Lateral Sclerosis. Due to the large body of scientific evidence indicating their role in cell pathophysiology, several PRMT inhibitors have been designed and developed as a potential new class of drugs. For instance, a potent, reversible type I PRMT inhibitor has been shown to have anti-tumor effects in human cancer models and some of the molecular candidates have entered clinical trials for solid tumors and lymphomas.

“Although it was first described in 1968,” says Dr Tiziana Bonaldi, Group Leader at the European Institute of Oncology, “for almost 30 years, very little was known about the extent of protein arginine methylation, its effect on protein activity, and its biological role. The first PRMT, capable of catalyzing arginine methylation, was discovered in 1996 and, since then, nine proteins exerting the same functions have been discovered. However, inefficient analytical approaches have largely limited a comprehensive understanding of their biological function. Quantitative Mass spectrometry has emerged as the ideal analytical strategy to study the extent of protein arginine-methylation in model systems and identify PRMT targets, thus contributing substantial knowledge in this field.”

In their article published in Current Protein & Peptide Science, Dr. Bonaldi and co-workers offer an overview on state-of-the-art arginine methyl-proteomics, describing the innovations that led – from the description by Mathias Mann’s group of the first high-quality methyl-proteome in 2004 – to the latest studies that profile protein-methylation events occurring on hundreds of cellular proteins. Throughout this review, the authors describe the implementations both in the biochemical methods and in the computational methods for Mass spectrometry data analysis or the identification of sites of arginine methylation, discussing the pros and cons of the most common strategies employed.

Furthermore, relevant issues related to protein-arginine methylation analysis that are still under development are also discussed, such as the discrimination of symmetric and asymmetric arginine-di-methylation from Mass spectrometry fragmentation spectra. “These two modifications have identical mass, yet they are catalyzed by different PRMTs and have substantially different biological outcomes,” explains Bonaldi; “Indeed, even though, for instance, both have a role in regulation of transcription, while asymmetric di-methylation is activating, symmetric di-methylation is repressive. Therefore, being able to distinguish between the two processes is crucial.”

Finally, major emphasis is devoted to the heavy methyl SILAC strategy, a variation of the more conventional SILAC (Stable Isotope Labelling with Amino acids in Cell culture). “The heavy methyl SILAC strategy was designed to increase the confidence of in vivo arginine methyl-peptides identification by Mass spectrometry,” – continues Bonaldi – “and the use will be facilitated by the recent development of ad hoc algorithms tailored for processing of heavy methyl SILAC datasets, such as MethylQuant and hmSEEKER.”

Importantly, the authors conclude that optimization of the currently available analytical approaches and their systematic application will play a key role in the future research on the involvement of protein methylation in biological processes, providing critical insights in the related cellular biology processes and likely offering potential novel targets to be exploited in a clinical context. Read the full Press Release to find out more: https://www.eurekalert.org/pub_releases/2020-05/bsp-lao052220.php

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To get the full-text article, please visit the following link: http://www.eurekaselect.com/181344/article

Wishing you a very Happy Birthday | Prof. Ben M. Dunn

 

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Prof. Ben M. Dunn

Editor in Chief: Current Protein & Peptide Science

 

Department of Biochemistry and Molecular Biology University of Florida
College of Medicine, P.O. Box 100245, Gainesville
Florida, FL 32610-0245
USA

New Issue :: Current Protein & Peptide Science (Volume: 19, Issue: 11)

 

Current Protein & Peptide Science publishes review articles on specific aspects involving proteins, peptides, and interactions between the enzymes, the binding interactions of hormones and their receptors; the properties of transcription factors and other molecules that regulate gene expression; the reactions leading to the immune response; the process of signal transduction; the structure and function of proteins involved in the cytoskeleton and molecular motors; the properties of membrane channels and transporters; and the generation and storage of metabolic energy. In addition, reviews of experimental studies of protein folding and design are given special emphasis.

 

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Articles from the journal Current Protein & Peptide Science Volume 19, Issue 11:

 

For details on the articles, please visit this link ::  https://bit.ly/2Ob67Tp

EDITOR’S CHOICE ARTICLE – Central Role of Transforming Growth Factor Type Beta 1 in Skeletal Muscle Dysfunctions: An Update on Therapeutic Strategies

Journal Name: Current Protein & Peptide Science

Author(s): Johanna Abrigo, Felipe Simon, Daniel Cabrera, Gonzalo Cordova, Capucine Trollet, Claudio Cabello-Verrugio*.

Graphical Abstract:

 

Abstract:

Among the soluble factors that regulate skeletal muscle function, Transforming Growth Factor type Beta 1 (TGF-β1) is one of the most studied. This factor inhibits myogenesis and regeneration by regulating the activity and function of satellite cells (SCs). Indeed, TGF-β has a central role in muscle pathologies in which there is development of fibrosis and/or atrophy of skeletal muscle. Thus, in this review we present the critical and recent antecedents regarding the mechanisms and cellular targets involved in the effects of TGF-β1 in the muscle, in pathological processes such as the inhibition of regeneration, fibrosis and atrophy. In addition, an update on the development of new strategies with therapeutic potential to inhibit the deleterious actions of TGF-β in skeletal muscle is discussed.

For more details, please visit: http://www.eurekaselect.com/157258/article

EDITOR’S CHOICE ARTICLE – Current Concepts and Perspectives on Connexin43: A Mini Review

Journal Name: Current Protein & Peptide Science

Author(s): Qingwei Zhang, Xiao Bai, Yang Liu, Kai Wang, Baozhong Shen*, Xilin Sun*

 

 

 

Graphical Abstract:

 

Abstract:

Connexins are a family of gap junction proteins widely distributed in human organs and tissues. Gap junctions are organized systems of intercellular protein channels that allow the exchange of ions, chemical signals, and energy substrates between two adjacent cells. Connexin43 (Cx43) is the most abundant isoform of connexins in the heart which play an important role in myocardium disease. Numerous studies have shown that Cx43 was involved in tumor migration and invasion by mediating gap junctions between tumor cells and normal cells. Changes in the expression and distribution of Cx43 contribute to heart disease and cancer. This review discusses current knowledge on the functional and structural abnormalities in Cx43 associated with heart disease and cancer, aiming to highlight the importance of this connexin as an emerging therapeutic target. Here, the current knowledge on the pharmacology of Gap Junction Channels and Hemichannels were also summarized. Finally, we propose that these knowledges can be exploited to identify new diagnostic and effective therapeutic approaches for ischemic heart disease and cancer.

 

Fore more details, please visit: http://www.eurekaselect.com/163614/article

AIMS & SCOPE – Current Protein & Peptide Science.

Aims & Scope:

Current Protein & Peptide Science publishes review articles on specific aspects involving proteins, peptides, and interactions between the enzymes, the binding interactions of hormones and their receptors; the properties of transcription factors and other molecules that regulate gene expression; the reactions leading to the immune response; the process of signal transduction; the structure and function of proteins involved in the cytoskeleton and molecular motors; the properties of membrane channels and transporters; and the generation and storage of metabolic energy. In addition, reviews of experimental studies of protein folding and design are given special emphasis. Manuscripts submitted to Current Protein and Peptide Science should cover a field by discussing research from the leading laboratories in a field and should pose questions for future studies. Original papers, research articles and letter articles/short communications are not considered for publication in Current Protein & Peptide Science.

 

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FOR DETAILS, PLEASE VISIT: https://benthamscience.com/journals/current-protein-and-peptide-science/aims-scope/#top

MOST ACCESSED ARTICLE – Natural Product Inhibitors of Topoisomerases: Review and Docking Study

Journal Name: Current Protein & Peptide Science

Author(s): Luciana Scotti*, Francisco Jaime Bezerra Mendonca, Frederico Favaro Ribeiro,Josean Fechine Tavares, Marcelo Sobral da Silva, Jose Maria Barbosa Filho, Marcus Tullius Scotti.

 

 

Graphical Abstract:

 

Abstract:

Since ancient times, natural products have been used in treating various diseases effectively and safely. Nowadays, these natural compounds are submitted to sophisticated methodologies from isolation, computing, analytical, and even serving as pharmacophore suggestions for synthesis. The substances extracted from marine species, plants, and microorganisms present activities beneficial to our health, including protection against malignant tumors. The topoisomerase enzymes play an important role in DNA metabolism, and searching for enzyme inhibitors is an important target in the search for new anticancer drugs. This review discusses this problem, reporting research involving alkaloids, terpenes, flavonoids, xanthones, coumarins, acetogenins, and in addition, includes a docking study with our Brazilian diterpenes to topoisomerases I and II. The better compound, the trachylobane 1, forms one hydrogen bond when submitted to docking with Topo I (with the ASP533 residue) and two with residues in Topo II (THR213 and TYR188). The difference observed in the energy of formation can be attributed to hydrogen-bond interactions.

The difference observed in the energy of formation can be attributed to hydrogen-bond interactions.

 

READ MORE HERE: http://www.eurekaselect.com/149155

OPEN ACCESS ARTICLE – Viscosity Control of Protein Solution by Small Solutes: A Review

Journal Name: Current Protein & Peptide Science

Author(s): Taehun Hong, Kazuki Iwashita, Kentaro Shiraki*.

 

 

 

Graphical Abstract:

 

 

Abstract:

Viscosity of protein solution is one of the most troublesome issues for the high-concentration formulation of protein drugs. In this review, we summarize the practical methods that suppress the viscosity of protein solution using small molecular additives. The small amount of salts decreases the viscosity that results from electrostatic repulsion and attraction. The chaotrope suppresses the hydrophobic attraction and cluster formation, which can lower the solution viscosity. Arginine hydrochloride (ArgHCl) also suppresses the solution viscosity due to the hydrophobic and aromatic interactions between protein molecules. The small molecular additives are the simplest resolution of the high viscosity of protein solution as well as understanding of the primary cause in complex phenomena of protein interactions.

 

 

READ MORE HERE: http://www.eurekaselect.com/158257 

New Issue :: Current Protein & Peptide Science (Volume: 19, Issue: 9)

Current Protein & Peptide Science publishes review articles on specific aspects involving proteins, peptides, and interactions between the enzymes, the binding interactions of hormones and their receptors; the properties of transcription factors and other molecules that regulate gene expression; the reactions leading to the immune response; the process of signal transduction; the structure and function of proteins involved in the cytoskeleton and molecular motors; the properties of membrane channels and transporters; and the generation and storage of metabolic energy. In addition, reviews of experimental studies of protein folding and design are given special emphasis. Manuscripts submitted to Current Protein and Peptide Science should cover a field by discussing research from the leading laboratories in a field and should pose questions for future studies. Original papers, research articles and letter articles/short communications are not considered for publication in Current Protein & Peptide Science.

 

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Articles from the journal Current Protein & Peptide Science Volume 19, Issue 9:

 

For details on the articles, please visit this link ::  https://bit.ly/2NWoSpR

 

PRESS RELEASE: BENTHAM SCIENCE JOURNALS – IMPACT FACTORS 2018

News release date: July 11, 2018

 

The latest edition of Journal Citation Reports® 2018 has been recently published, and according to the report, 41 Bentham Science Publishers (BSP) journals have received Impact Factor ratings. Current Neuropharmacology has continued to top the list with the highest impact factor among all Bentham Science Journals. Current Molecular Pharmacology has also joined the BSP High Impact Journals list with its first JCR Impact Factor rating of 2.481.

 

Here are the top 10 high impact factor journals published by Bentham Science:

  1. Current Neuropharmacology
    Impact Factor: 4.068
  2. Current Medicinal Chemistry
    Impact Factor: 3.469
  3. Current Topics in Medicinal Chemistry
    Impact Factor: 3.374
  4. Current Alzheimer Research
    Impact Factor: 3.289
  5. Current Drug Targets
    Impact Factor: 3.112
  6. Current Pharmaceutical Design
    Impact Factor: 2.757
  7. Current Protein & Peptide Science
    Impact Factor: 2.696
  8. Current Drug Metabolism
    Impact Factor: 2.655
  9. Mini-Reviews in Medicinal Chemistry
    Impact Factor: 2.645
  10. Medicinal Chemistry
    Impact Factor: 2.631

 

Journal Citation Reports (JCR) is an annual publication by Clarivate Analytics. JCR has been integrated with the Web of Science and is accessible from the Web of Science-Core Collections. Its purpose is to offer a systematic means to critically evaluate the world’s leading journals, with quantifiable, statistical information based on citation data.

Bentham Science publishes over 100 print & online scholarly subscription journals and books. Learn more about Bentham Science here.

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