Results 21 to 30 of about 153,280 (319)

Endothelial TLR4 Expression Mediates Vaso-Occlusive Crisis in Sickle Cell Disease

Frontiers in Immunology, 2021
Heme, released from red blood cells in sickle cell disease (SCD), interacts with toll-like receptor 4 (TLR4) to activate NF-κB leading to the production of cytokines and adhesion molecules which promote inflammation, pain, and vaso-occlusion.
Joan D. Beckman, Fuad Abdullah, Chunsheng Chen, Rachel Kirchner, Dormarie Rivera-Rodriguez, Zachary M. Kiser, Aithanh Nguyen, Ping Zhang, Julia Nguyen, Robert P. Hebbel, John D. Belcher, Gregory M. Vercellotti   +11 more
doaj   +1 more source

Control of intracellular heme levels: Heme transporters and heme oxygenases

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2011
Heme serves as a co-factor in proteins involved in fundamental biological processes including oxidative metabolism, oxygen storage and transport, signal transduction and drug metabolism. In addition, heme is important for systemic iron homeostasis in mammals.
Anwar A. Khan, John G. Quigley
openaire   +3 more sources

Staphylococcus aureus HemX Modulates Glutamyl-tRNA Reductase Abundance To Regulate Heme Biosynthesis

mBio, 2018
Staphylococcus aureus is responsible for a significant amount of devastating disease. Its ability to colonize the host and cause infection is supported by a variety of proteins that are dependent on the cofactor heme.
Jacob E. Choby, Caroline M. Grunenwald, Arianna I. Celis, Svetlana Y. Gerdes, Jennifer L. DuBois, Eric P. Skaar   +5 more
doaj   +1 more source

Heme Oxygenase-2 Is a Hemoprotein and Binds Heme through Heme Regulatory Motifs That Are Not Involved in Heme Catalysis [PDF]

Journal of Biological Chemistry, 1997
The heme oxygenase (HO) system degrades heme to biliverdin and CO and releases chelated iron. In the primary sequence of the constitutive form, HO-2, there are three potential heme binding sites: two heme regulatory motifs (HRMs) with the absolutely conserved Cys-Pro pair, and a conserved 24-residue heme catalytic pocket with a histidine residue ...
Tian J. Huang, Mahin D. Maines, William K. McCoubrey   +2 more
openaire   +3 more sources

Endothelial Barrier Integrity Is Disrupted In Vitro by Heme and by Serum From Sickle Cell Disease Patients

Frontiers in Immunology, 2020
Free extracellular heme has been shown to activate several compartments of innate immunity, acting as a danger-associated molecular pattern (DAMP) in hemolytic diseases.
Vanessa Araujo Gomes Santaterra, Maiara Marx Luz Fiusa, Bidossessi Wilfried Hounkpe, Francine Chenou, Wouitchekpo Vincent Tonasse, Loredana Nilkenes Gomes da Costa, Loredana Nilkenes Gomes da Costa, Diego Garcia-Weber, Igor de Farias Domingos, Igor de Farias Domingos, Franciele de Lima, Ivanio Teixeira Borba-Junior, Aderson da Silva Araújo, Antonio Roberto Lucena-Araújo, Marcos André Cavalcante Bezerra, Magnun Nueldo Nunes dos Santos, Fernando Ferreira Costa, Fernando Ferreira Costa, Jaime Millán, Erich Vinicius De Paula, Erich Vinicius De Paula   +20 more
doaj   +1 more source

Heme in pathophysiology: a matter of scavenging, metabolism and trafficking across cell membranes

Frontiers in Pharmacology, 2014
Heme (iron-protoporphyrin IX) is an essential co-factor involved in multiple biological processes: oxygen transport and storage, electron transfer, drug and steroid metabolism, signal transduction, and micro RNA processing.
Deborah eChiabrando, Francesca eVinchi, Veronica eFiorito, Sonia eMercurio, Emanuela eTolosano   +4 more
doaj   +1 more source

Structure Elucidation, Total Synthesis, Antibacterial In Vivo Efficacy and Biosynthesis Proposal of Myxobacterial Corramycin**

Angewandte Chemie International Edition, Volume 61, Issue 51, December 19, 2022., 2022
Corramycin is a novel natural product produced by the myxobacterium Corallococcus coralloides. The structure, extraordinary total synthesis and biosynthesis of the antibiotic is described for the first time. Its promise as an in vivo septicemia model, the absence of cross‐resistance with commonly used antibiotic classes, and the lack of cytotoxicity ...
Cédric Couturier, Sebastian Groß, Alexander von Tesmar, Judith Hoffmann, Selina Deckarm, Anouchka Fievet, Nelly Dubarry, Thomas Taillier, Christoph Pöverlein, Heike Stump, Michael Kurz, Luigi Toti, Sabine Haag Richter, Dietmar Schummer, Philippe Sizun, Michael Hoffmann, Ram Prasad Awal, Nestor Zaburannyi, Kirsten Harmrolfs, Joachim Wink, Emilie Lessoud, Thierry Vermat, Veronique Cazals, Sandra Silve, Armin Bauer, Michael Mourez, Laurent Fraisse, Corinne Leroi‐Geissler, Astrid Rey, Stéphanie Versluys, Eric Bacqué, Rolf Müller, Stephane Renard   +32 more
wiley   +1 more source

Physical exercises for preventing injuries among adult male football players: A systematic review

Journal of Sport and Health Science, 2022
Background: Football is the most practised sport in the world and is associated with the risk of injuries in the players. Some studies have been published that identify injury prevention programs, but there is no review of the full body of evidence on ...
Jorge Pérez-Gómez, José Carmelo Adsuar, Pedro E. Alcaraz, Jorge Carlos-Vivas   +3 more
doaj  

The Role of Cytochrome P450 AbyV in the Final Stages of Abyssomicin C Biosynthesis

Angewandte Chemie International Edition, Volume 62, Issue 3, January 16, 2023., 2023
The cytochrome P450 enzyme AbyV catalyses a key epoxidation in the final stages of the biosynthesis of the spirotetronate antibiotic abyssomicin C. Combining structural and computational data with a 13C labelling strategy was found to be a powerful approach to interrogate the biotransformation and determine the precise function of the enzyme.
Andrew J. Devine, Alice E. Parnell, Catherine R. Back, Nicholas R. Lees, Samuel T. Johns, Ainul Z. Zulkepli, Rob Barringer, Katja Zorn, James E. M. Stach, Matthew P. Crump, Martin A. Hayes, Marc W. van der Kamp, Paul R. Race, Christine L. Willis   +13 more
wiley   +1 more source

Heme b (protoheme IX) is a precursor of heme a and heme d in Bacillus subtilis [PDF]

FEMS Microbiology Letters, 1993
Bacillus subtilis can synthesise cytochromes containing a-, b-, c- and d-type heme. The biosynthetic pathways of these heme prosthetic groups were investigated by using strains blocked in uroporphyrinogen III synthesis from porphobilinogen or in heme b (protoheme IX) synthesis from uroporphyrinogen III. The results strongly suggest that heme a and heme
Mats Hansson, Claes von Wachenfeldt
openaire   +3 more sources