Results 61 to 70 of about 11,485 (176)
Nutrient limitation restricts bacterial growth in privileged sites such as the middle ear. Transient heme-iron restriction of nontypeable Haemophilus influenzae (NTHI), the major causative agent of chronic and recurrent otitis media (OM), promotes new ...
Rachael L. Hardison +8 more
doaj +1 more source
One ring to bring them all and in the darkness bind them: The trafficking of heme without deliverers
Heme, as a hydrophobic iron-containing organic ring, is lipid soluble and can interact with biological membranes. The very same properties of heme that nature exploits to support life also renders heme potentially cytotoxic. In order to utilize heme, while also mitigating its toxicity, cells are challenged to tightly control the concentration and ...
Ian G, Chambers +3 more
openaire +2 more sources
Ultrasound‐responsive nanoplatforms reprogram the tumor immune microenvironment by targeting tumor cells, immune cells, and non‐immune stromal cells to enhance the efficacy of cancer immunotherapy. Abstract Cancer immunotherapy represents a significant advancement in cancer treatment by enhancing the specific recognition and elimination of cancer cells.
Shilong Zhao +4 more
wiley +1 more source
ABSTRACT Heat stress (HS) is an increasing threat to male reproductive health, disrupting spermatogenesis through complex and interdependent cellular responses within the seminiferous epithelium. Although excessive reactive oxygen species (ROS) production is a hallmark of HS, ROS also act as central regulators of cell fate decisions beyond their role ...
Ribrio Ivan Tavares Pereira Batista
wiley +1 more source
A proteomic investigation of forebrain regeneration in the leopard gecko (Eublepharis macularius)
Our investigation reveals ontogenetic, injury‐ and regeneration‐associated proteomic changes in the leopard gecko forebrain. Abstract Background The ability to replace lost or damaged neurons following an injury is termed reactive neurogenesis. Although reactive neurogenesis has been reported in several lizard species, the molecular mechanisms ...
Alexandra I. Noble +2 more
wiley +1 more source
T47D Cells Expressing Myeloperoxidase Are Able to Process, Traffic and Store the Mature Protein in Lysosomes: Studies in T47D Cells Reveal a Role for Cys319 in MPO Biosynthesis that Precedes Its Known Role in Inter-Molecular Disulfide Bond Formation. [PDF]
Among the human heme-peroxidase family, myeloperoxidase (MPO) has a unique disulfide-linked oligomeric structure resulting from multi-step processing of the pro-protein monomer (proMPO) after it exits the endoplasmic reticulum (ER).
Richard P Laura +3 more
doaj +1 more source
In this review, we critically summarized the application of natural polysaccharides (NPs) for the treatment of IBD. This approach combines, in a unique way (right), the basic structure–activity relationships of NPs from different origins (left) with their multipronged mode of action, which involves modulation of the gut microbiota and other ...
Felix Danso +3 more
wiley +1 more source
This study generates a comprehensive Ebola virus (EBOV)‐human protein–protein interactome, comprising 1728 core high‐confidence interactions. Further interactome analysis revealed the potential association of EBOV glycoprotein (GP) with the host factor TM9SF2. Subsequent mechanistic investigations confirmed that TM9SF2 functions as an attachment factor
Limin Shang +16 more
wiley +1 more source
Mitochondrial-nuclear heme trafficking is regulated by GTPases that control mitochondrial dynamics [PDF]
Abstract Heme is an essential cofactor and signaling molecule. All heme-dependent processes require that heme is trafficked from its site of synthesis in the mitochondria to hemoproteins in virtually every subcellular compartment. However, the mechanisms governing the mobilization of heme out of the mitochondria, and the spatio-temporal
Martinez-Guzman, Osiris +5 more
openaire +1 more source
Visualizing mitochondrial heme flow through GAPDH in living cells and its regulation by NO
Iron protoporphyrin IX (heme) is a redox-active cofactor that is bound in mammalian cells by GAPDH and allocated by a process influenced by physiologic levels of NO.
Pranjal Biswas +6 more
doaj +1 more source

