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Flipped binding modes for the same agonist in closely related neuropeptide-gated ion channels.
Biophys J
January 2025
Michael Sars Centre, University of Bergen, Norway. Electronic address:
Neuropeptides are inter-cellular signaling molecules occurring throughout animals. Most neuropeptides bind and activate G-protein coupled receptors, but some also activate ionotropic receptors (or "ligand-gated ion channels"). This is exemplified by the tetra-peptide H-Phe-Met-Arg-Phe-NH (FMRFa), which activates mollusc and annelid FMRFa-gated sodium channels (FaNaCs) from the trimeric degenerin/epithelial sodium channel superfamily.
View Article and Find Full Text PDFExploring the structure and nucleic acid interactions of the Leishmania sp. telomerase reverse transcriptase N-terminal region.
Arch Biochem Biophys
February 2025
Department of Chemical and Biological Sciences, Biosciences Institute, São Paulo State University (UNESP), Botucatu, SP, Brazil.
Leishmaniasis is a neglected tropical disease caused by protozoans of the Leishmania genus, against which no effective treatment or control is available. Like other eukaryotes, parasite telomeres are maintained by telomerase, a ribonucleoprotein complex vital for genome stability. Its protein component, TERT (telomerase reverse transcriptase), presents four structural and functional domains, with the TEN (Telomerase N-terminal) and TRBD (Telomerase RNA-binding) located at its N-terminal.
View Article and Find Full Text PDFSynthesis of Temporin-SHa Retro Analogs with Lysine Addition/Substitution and Antibiotic Conjugation to Enhance Antibacterial, Antifungal, and Anticancer Activities.
Antibiotics (Basel)
December 2024
Third World Center for Science and Technology, International Center for Chemical and Biological Sciences, University of Karachi, Karachi 75270, Pakistan.
In the face of rising the threat of resistant pathogens, antimicrobial peptides (AMPs) offer a viable alternative to the current challenge due to their broad-spectrum activity. This study focuses on enhancing the efficacy of temporin-SHa derived NST-2 peptide (), which is known for its antimicrobial and anticancer activities. We synthesized new analogs of using three strategies, i.
View Article and Find Full Text PDFInstallation of an Indole on the BRCA1 Disordered Domain Using Triazine Chemistry.
Biomolecules
December 2024
Department of Chemistry & Biochemistry, Texas Christian University, Fort Worth, TX 76129, USA.
The functionalization of protein sidechains with highly water-soluble chlorotriazines (or derivatives thereof) using nucleophilic aromatic substitution reactions has been commonly employed to install various functional groups, including poly(ethylene glycol) tags or fluorogenic labels. Here, a poorly soluble dichlorotriazine with an appended indole is shown to react with a construct containing the disordered domain of BRCA1. Subsequently, this construct can undergo proteolytic cleavage to remove the SUMO-tag: the -terminal poly(His) tag is still effective for purification.
View Article and Find Full Text PDFStructure/function of ATP sulfurylase domain of human 3'-phosphoadenosine 5'-phosphosulfate synthase (hPAPSS).
Biochem Biophys Rep
March 2025
College of Biomedical Sciences, Larkin University, Miami, FL, 33169, USA.
Article Synopsis
- PAPS is synthesized in two steps: first, ATP sulfurylase converts ATP into APS, then APS-kinase phosphorylates APS to produce PAPS.
- Mutations in the hPAPSS isoform1, particularly in histidine residues, disrupt the function of ATP sulfurylase without affecting APS-kinase.
- The N-K mutant exhibited improved catalytic efficiency for ATP and sulfate, indicating how specific residues can enhance enzyme activity and the importance of inter-domain interactions in the overall structure and function of hPAPSS1.
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