Results 71 to 80 of about 11,782 (206)

Metal‐dependent regulated cell death: Molecular architecture and translational frontiers

iMeta, EarlyView.
Intracellular metal dyshomeostasis orchestrates distinct regulated cell death programs, including iron‐driven ferroptosis, copper‐mediated cuproptosis, calcicoptosis, newly designated zincoptosis, mnoptosis, and coptosis. This review systematically delineates their molecular architectures—spanning from Sorafenib‐induced lipid peroxidation and ...
Haoliang Hu, Zhe Chen, Yaqi Li, Jiayi Peng, Jiangang Cao, Hong Zhou, Mengqi Wang, Yuejia Du, Hailin Wu, Huiqin Zhao, Shifang Huang, Dianmei Yu, Meiqing Liu, Olga V. Shevchenko, Natalia Yu. Matveeva, Yiyuan Yang, Kerui Huang, Deguan Lv, Junxia Min, Linxi Chen, Fudi Wang   +20 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]

PLoS ONE, 2016
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, David Dong, Wanda F Reynolds, Richard A Maki   +3 more
doaj   +1 more source

Binuclear Copper‐Dependent Oxidative Enzymes Involved in Fungal Natural Product Modifications

Journal of the Chinese Chemical Society, EarlyView.
This article summarizes recent biochemical characterizations of a new enzyme family named by the authors as binuclear copper‐dependent oxidative enzymes (BiNCOs). Found in fungal natural product biosynthesis, BiNCOs catalyze diverse CH functionalization reactions, including C(sp3)H halogenation, C(sp3)H hydroxylation, C(sp3)O macrocyclization, and ...
Chen‐Yu Chiang, Masao Ohashi, Yi Tang
wiley   +1 more source

Characterization of the novel Maurer's clefts protein MAHRP1 in "Plasmodium falciparum" [PDF]

, 2007
Plasmodium falciparum causes the worst form of human malaria and is responsible for 1-2 million deaths annually. A vaccine is not available and resistance to drugs is widespread.
Spycher, Anna Cornelia
core   +1 more source

Proteomic and Metabolomic Profiling Reveal Mitochondrial Transplantation–Mediated Reprogramming in Gastric Cancer Cells

The Kaohsiung Journal of Medical Sciences, EarlyView.
ABSTRACT Mitochondria provide multiple functions for cellular physiology. Transplantation of mitochondria isolated from gastric epithelial cells GES‐1 reducing the malignancy of gastric cancer cells AGS was previously reported. To elucidate the underlying mechanisms, TMT‐based proteomic analysis coupling ingenuity pathway software prediction revealed ...
Ping‐Chen Chen, Chen‐Kai Liu, Ching‐Chung Tsai, Erna Sulistyowati, Fu‐An Li, Chung‐Jung Liu, Deng‐Chyang Wu, Shih‐Hsuan Chou, Fu‐Chen Kuo, Bin Huang   +9 more
wiley   +1 more source

Heme Uptake and Metabolism in Bacteria [PDF]

, 2012
All but a few bacterial species have an absolute need for heme, and most are able to synthesize it via a pathway that is highly conserved among all life domains. Because heme is a rich source for iron, many pathogenic bacteria have also evolved processes
Mario Rivera, Rivera, Mario, Benson, David R., David R. Benson   +3 more
core   +1 more source

Mitochondrial-nuclear heme trafficking is regulated by GTPases that control mitochondrial dynamics [PDF]

, 2019
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, Dietz, Jonathan V., Bohovych, Iryna, Medlock, Amy E., Khalimonchuk, Oleh, Reddi, Amit R.   +5 more
openaire   +1 more source

Visualizing mitochondrial heme flow through GAPDH in living cells and its regulation by NO

Redox Biology
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, Joseph Palazzo, Simon Schlanger, Dhanya Thamaraparambil Jayaram, Sidra Islam, Richard C. Page, Dennis J. Stuehr   +6 more
doaj   +1 more source

Heme Oxygenase-1: A Critical Link between Iron Metabolism, Erythropoiesis, and Development

Advances in Hematology, 2011
The first mature cells to arise in the developing mammalian embryo belong to the erythroid lineage. This highlights the immediacy of the need for red blood cells during embryogenesis and for survival.
Stuart T. Fraser, Robyn G. Midwinter, Birgit S. Berger, Roland Stocker   +3 more
doaj   +1 more source

Widespread Distribution and Functional Specificity of the Copper Importer CcoA: Distinct Cu Uptake Routes for Bacterial Cytochrome c Oxidases

mBio, 2018
Cytochrome c oxidases are members of the heme-copper oxidase superfamily. These enzymes have different subunits, cofactors, and primary electron acceptors, yet they all contain identical heme-copper (CuB) binuclear centers within their catalytic subunits.
Bahia Khalfaoui-Hassani, Hongjiang Wu, Crysten E. Blaby-Haas, Yang Zhang, Federica Sandri, Andreia F. Verissimo, Hans-Georg Koch, Fevzi Daldal   +7 more
doaj   +1 more source