RNA-binding proteins (RBPs) play crucial roles in almost all aspects of cellular biology. RBP binding at specific target sites impacts expression of functionally coordinated sets of mRNAs and involves combinatorial and dynamic interactions with other RBPs. The complexity and principles of these regulatory networks are only beginning to be understood. In recent years, transcriptome-wide experimental and computational methods to study RBPs and their interactions with RNA provided new insights into their function. Here, we review the approaches used in examining RBPs and their networks and the concepts that have been developed. We emphasize studies focusing on RBP-RNA interactions and higher-order RBP coregulation and describe approaches that integrate multiple types of transcriptome-wide data to form a global picture of these regulatory pathways.
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http://dx.doi.org/10.1016/j.tibs.2020.03.005 | DOI Listing |
Arch Dermatol Res
January 2025
Department of Dermatology, Medical Research and Clinical Studies Institute, National Research Centre, Giza, Egypt.
Acne vulgaris is a common and challenging condition to treat. To assess the effect of botulinum toxin type A (BTX-A) in the treatment of mild to moderate acne vulgaris. This study included 30 patients with mild to moderate acne vulgaris treated with intradermal injections of diluted BTX-A (microbotox) on the cheek in a regular grid pattern using very small droplets (microbotox).
View Article and Find Full Text PDFNaunyn Schmiedebergs Arch Pharmacol
January 2025
Department of Biochemistry, Faculty of Pharmacy, Badr University in Cairo (BUC), Badr City, , 11829, Cairo, Egypt.
Globally, the incidence and death rates associated with cancer persist in rising, despite considerable advancements in cancer therapy. Although some malignancies are manageable by a mix of chemotherapy, surgery, radiation, and targeted therapy, most malignant tumors either exhibit poor responsiveness to early identification or endure post-treatment survival. The prognosis for prostate cancer (PCa) is unfavorable since it is a perilous and lethal malignancy.
View Article and Find Full Text PDFCurr Microbiol
January 2025
Molecular Biology Laboratory, Department of Microbiology, Science Campus, Alagappa University, Karaikudi, Tamil Nadu, 630003, India.
Antimicrobial resistance (AMR) is an escalating global health concern that results in approximately 700,000 deaths annually owing to drug-resistant infections. It compromises the effectiveness of conventional antibiotics, as well as fundamental medical procedures, such as surgery and cancer treatment. Phytochemicals, natural plant constituents, and biogenic nanoparticles synthesized through biological processes are pharmacological alternatives for supplementing or replacing traditional antibiotics.
View Article and Find Full Text PDFAnal Chem
January 2025
State Key Laboratory of Geological Processes and Mineral Resources, China University of Geosciences, Wuhan 430074, PR China.
The elemental imaging of laser ablation inductively coupled plasma mass spectrometry (LA-ICP-MS) provides spatial information on elements and therefore can further investigate the growth or evolution processes of an analyte. However, the accurate determination of spatial information is limited by the decoupling between the elemental distribution and mass spectrometry signals. This phenomenon, which is more distinct when high-diffusion ablation cells are used, arises from the overlap of ablation and the transport dispersion of aerosols.
View Article and Find Full Text PDFLett Appl Microbiol
January 2025
Clinical Laboratory, Huzhou Central Hospital, Affiliated Central Hospital of Huzhou University, Fifth School of Clinical Medicine of Zhejiang Chinese Medical University.
MRSA's resistance poses a global health challenge. This study investigates lysine succinylation in MRSA using proteomics and bioinformatics approaches to uncover metabolic and virulence mechanisms, with the goal of identifying novel therapeutic targets. Mass spectrometry and bioinformatics analyses mapped the MRSA succinylome, identifying 8 048 succinylation sites on 1 210 proteins.
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