There are many different types of RNA modifications, which are essential for numerous biological processes. Knowledge about the occurrence sites of RNA modifications in its sequence is a key for in-depth understanding of their biological functions and mechanism. Unfortunately, it is both time-consuming and laborious to determine these sites purely by experiments alone. Although some computational methods were developed in this regard, each one could only be used to deal with some type of modification individually. To our knowledge, no method has thus far been developed that can identify the occurrence sites for several different types of RNA modifications with one seamless package or platform. To address such a challenge, a novel platform called "iRNA-PseColl" has been developed. It was formed by incorporating both the individual and collective features of the sequence elements into the general pseudo K-tuple nucleotide composition (PseKNC) of RNA via the chemicophysical properties and density distribution of its constituent nucleotides. Rigorous cross-validations have indicated that the anticipated success rates achieved by the proposed platform are quite high. To maximize the convenience for most experimental biologists, the platform's web-server has been provided at http://lin.uestc.edu.cn/server/iRNA-PseColl along with a step-by-step user guide that will allow users to easily achieve their desired results without the need to go through the mathematical details involved in this paper.
Download full-text PDF |
Source |
---|---|
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5415964 | PMC |
http://dx.doi.org/10.1016/j.omtn.2017.03.006 | DOI Listing |
Background: TAR-DNA-binding protein 43 (TDP43), is a pathologic marker in neurodegenerative diseases including frontotemporal lobar degeneration and amyotrophic lateral sclerosis. The aggregation of TDP-43, a crucial RNA-binding protein, is a consequence of post-translational modifications (PTMs) that disrupt its normal function. PTMs such as phosphorylation and ubiquitination contribute to the aberrant accumulation of TDP-43 aggregates, leading to neurodegenerative disorders like amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD).
View Article and Find Full Text PDFInt J Med Sci
January 2025
Department of Cardiology, The Second Xiangya Hospital, Central South University, Changsha 410011, Hunan Province, People's Republic of China.
Elevated lipoprotein(a) [Lp(a)] levels are increasingly recognized as a significant risk factor for cardiovascular diseases and may also contribute to atrial fibrillation (AF). This review investigated the indirect mechanisms through which Lp(a) may influence AF, including proatherogenic, prothrombotic, and proinflammatory pathways. Traditional lipid-lowering therapies, such as lifestyle modifications and statins, have limited effects on Lp(a) levels.
View Article and Find Full Text PDFResearch (Wash D C)
January 2025
Cancer Institute, Xuzhou Medical University, Xuzhou, Jiangsu, China.
Numerous diseases have been connected to protein arginine methylations mediated by protein arginine methyltransferase 5 (PRMT5). Clinical investigations of the PRMT5-specific inhibitor GSK3326595 are currently being conducted, and the results are promising for preventing cancers. However, the detailed mechanism of PRMT5 promoting colorectal cancer (CRC) malignant progression remains unclear.
View Article and Find Full Text PDFJ Gerontol A Biol Sci Med Sci
January 2025
BIO@SNS, Scuola Normale Superiore, Piazza dei Cavalieri,7, Pisa, 56126, Italy.
The African turquoise killifish Nothobranchius furzeri represents an emerging short-lived model for aging research. Captive strains of this species are characterized by large differences in lifespan. To identify the gene expression correlates of this lifespan differences, we analyzed a public transcriptomic dataset consisting of four different tissues in addition to embryos.
View Article and Find Full Text PDFNat Chem Biol
January 2025
Institute of Organic Chemistry, Julius-Maximilians-Universität Würzburg, Würzburg, Germany.
Ribozymes that catalyze site-specific RNA modification have recently gained increasing interest for their ability to mimic methyltransferase enzymes and for their application to install molecular tags. Recently, we reported SAMURI as a site-specific alkyltransferase ribozyme using S-adenosylmethionine (SAM) or a stabilized analog to transfer a methyl or propargyl group to N of an adenosine. Here, we report the crystal structures of SAMURI in the postcatalytic state.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!