Specific binding sites for the thyroid hormones have been demonstrated in the liver nuclear matrix, a structural framework of the nucleus. When labelled 3,5,3'-tri-iodo-L-thyronine ([125I]T3) is injected into rats, 5% of the total nucleus bound T3 is bound to the matrix after 1 hour. However, when either isolated nuclei or isolated nuclear matrices were incubated with [125I]T3 in vitro, a 3- to 7-fold greater number of specific T3 binding sites were revealed in the nuclear matrix. The properties of the matrix-associated thyroid hormone binding sites were investigated in vitro. These binding sites showed limited capacity and high affinity for T3; the equilibrium association constant (Ka) was 1,3 x 10(9) M-1 and the binding capacity was 20,2 fmol T3 per 100 microgram matrix protein.
Download full-text PDF |
Source |
|---|
Publication Analysis
Top Keywords
Similar Publications
Hsa_circ_0001304 promotes vascular neointimal hyperplasia accompanied by autophagy activation.
Commun Biol
January 2025
Department of Biochemistry and Molecular Biology, Key Laboratory of Neural and Vascular Biology, Ministry of Education, Hebei Key Laboratory of Forensic Medicine, Hebei Medical University, Shijiazhuang, 050017, China.
Aberrant autophagy in vascular smooth muscle cells (VSMCs) is associated with the progression of vascular remodeling diseases caused by neointimal hyperplasia. Platelet-derived growth factor-BB (PDGF-BB)-induced vascular remodeling is accompanied by autophagy activation, however, the involvement of circular RNAs (circRNAs) remains unclear. Here, we show the role of PDGF-BB-regulated hsa_circ_0001304 (circ-1304) in neointimal hyperplasia and its potential involvement in VSMC autophagy, while also elucidating the potential mechanisms.
View Article and Find Full Text PDFThe mycobacterial ABC transporter IrtAB employs a membrane-facing crevice for siderophore-mediated iron uptake.
Nat Commun
January 2025
Institute of Medical Microbiology, University of Zurich, Zurich, Switzerland.
The mycobacterial ABC transporter IrtAB features an ABC exporter fold, yet it imports iron-charged siderophores called mycobactins. Here, we present extensive cryo-EM analyses and DEER measurements, revealing that IrtAB alternates between an inward-facing and an outward-occluded conformation, but does not sample an outward-facing conformation. When IrtAB is locked in its outward-occluded conformation in nanodiscs, mycobactin is bound in the middle of the lipid bilayer at a membrane-facing crevice opening at the heterodimeric interface.
View Article and Find Full Text PDFThe Rbfox1/LASR complex controls alternative pre-mRNA splicing by recognition of multipart RNA regulatory modules.
Genes Dev
January 2025
Molecular Biology Institute, University of California, Los Angeles, Los Angeles, California 90095, USA;
The Rbfox proteins regulate alternative pre-mRNA splicing by binding to the RNA element GCAUG. In the nucleus, most of Rbfox is bound to the large assembly of splicing regulators (LASR), a complex of RNA-binding proteins that recognize additional RNA motifs. However, it remains unclear how the different subunits of the Rbfox/LASR complex act together to bind RNA and regulate splicing.
View Article and Find Full Text PDFTPepRet: a deep learning model for characterizing T cell receptors-antigen binding patterns.
Bioinformatics
January 2025
School of Computer Science and engineering, Central South University, Changsha, 410083, China.
Motivation: T-cell receptors (TCRs) elicit and mediate the adaptive immune response by recognizing antigenic peptides, a process pivotal for cancer immunotherapy, vaccine design, and autoimmune disease management. Understanding the intricate binding patterns between TCRs and peptides is critical for advancing these clinical applications. While several computational tools have been developed, they neglect the directional semantics inherent in sequence data, which are essential for accurately characterizing TCR-peptide interactions.
View Article and Find Full Text PDFSensitive detection and propagation of brain-derived tau assemblies in HEK293 based wild-type tau seeding assays.
J Biol Chem
January 2025
UK Dementia Research Institute at the University of Cambridge, Department of Clinical Neurosciences, Hills Road, Cambridge, CB2 0AH, United Kingdom. Electronic address:
The assembly of tau into filaments defines tauopathies, a group of neurodegenerative diseases including Alzheimer's disease (AD), Pick's disease (PiD), corticobasal degeneration (CBD) and progressive supranuclear palsy (PSP). The seeded aggregation of tau has been modelled in cell culture using pro-aggregant modifications such as truncation of N- and C-termini and point-mutations within the microtubule-binding repeat domain. This limits the applicability of research findings to sporadic disease, where aggregates contain wild-type, full-length tau.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!