Abnormal atrial depolarization, characterized by P waves > or =110 ms on the electrocardiogram, can manifest as partial or advanced interatrial block (IAB). Advanced IAB, denoted by biphasic P waves in leads II, II and aVF, is considered to confer increased severity in interatrial conduction delay, and is now perceived to be a result of continued deterioration in interatrial impulse propagation between the atria. While progression from partial to advanced IAB has been described, the converse, resolution of advanced IAB, which has often been touted as 'complete block' to its partial, 'incomplete' type, i.e. the occurrence of intermittent advanced IAB, has escaped observations so far. We present the first known report of such a scenario.
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http://dx.doi.org/10.1159/000109409 | DOI Listing |
BMC Genomics
January 2025
Centre for Environmental Health, Hasselt University, Hasselt, Belgium.
Background: Telomere length is an important indicator of biological age and a complex multi-factor trait. To date, the telomere interactome for comprehending the high-dimensional biological aspects linked to telomere regulation during childhood remains unexplored. Here we describe the multi-omics signatures associated with childhood telomere length.
View Article and Find Full Text PDFPharmaceuticals (Basel)
January 2025
Department of Pharmacy Practice, Faculty of Pharmacy, Bahauddin Zakariya University, Multan 60800, Pakistan.
Glimepiride (GLM), a commonly used sulphonylurea drug for the management of type 2 diabetes mellitus (T2DM), has been the subject of numerous studies exploring its kinetic behaviors. However, a comprehensive evaluation that synthesizes all available pharmacokinetic (PK) data across diverse populations remains limited. This systematic review aims to provide detailed knowledge about the pharmacokinetics (PK), the associated pharmacodynamics (PD), and the drug interactions of GLM, which can be used to assess key parameters and identify factors influencing variability across diverse populations and clinical settings.
View Article and Find Full Text PDFVaccines (Basel)
January 2025
Leiden University Center for Infectious Diseases, Leiden University Medical Center, 2333 ZA Leiden, The Netherlands.
Background: Shigella infections remain endemic in places with poor sanitation and are a leading cause of diarrheal mortality globally, as well as a major contributor to gut enteropathy and stunting. There are currently no licensed vaccines for shigellosis but it has been estimated that an effective vaccine could avert 590,000 deaths over a 20-year period. A challenge to effective Shigella vaccine development has been the low immunogenicity and protective efficacy of candidate Shigella vaccines in infants and young children.
View Article and Find Full Text PDFProtein Sci
February 2025
Department of Biotechnology and Bioengineering, Sandia National Laboratories, Livermore, California, USA.
Engineered monoclonal antibodies have proven to be highly effective therapeutics in recent viral outbreaks. However, despite technical advancements, an ability to rapidly adapt or increase antibody affinity and by extension, therapeutic efficacy, has yet to be fully realized. We endeavored to stand-up such a pipeline using molecular modeling combined with experimental library screening to increase the affinity of F5, a monoclonal antibody with potent neutralizing activity against Venezuelan Equine Encephalitis Virus (VEEV), to recombinant VEEV (IAB) E1E2 antigen.
View Article and Find Full Text PDFAdv Sci (Weinh)
January 2025
Univ. Grenoble Alpes, Inserm, CNRS, Institute for Advanced Biosciences (IAB), Grenoble, 38000, France.
The fungal Bromodomain and Extra-Terminal (BET) protein Bdf1 is a potential antifungal target against invasive fungal infections. However, the need to selectively inhibit both Bdf1 bromodomains (BDs) over human orthologs and the lack of molecular tools to assess on-target antifungal efficacy hamper efforts to develop Bdf1 BD inhibitors as antifungal therapeutics. This study reports a phenyltriazine compound that inhibits both Bdf1 BDs from the human fungal pathogen Candida glabrata with selectivity over the orthologous BDs from the human BET protein Brd4.
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