Heme as key regulator of major mammalian cellular functions: Molecular, cellular, and pharmacological aspects

Mitochondrial control of cell death

Kroemer, G., & Reed, J. C. (2000) · Nature Medicine · doi:10.1038/74994 · Cited by 3,103

Heme oxygenase: Function, multiplicity, regulatory mechanisms, and clinical applications

Maines, M. D. (1988) · The FASEB Journal · doi:10.1096/fasebj.2.10.3290025 · Cited by 1,707

A Three-Dimensional Model of the Myoglobin Molecule Obtained by X-Ray Analysis

Kendrew, J. C., Bodo, G., Dintzis, H. M., Parrish, R. G., Wyckoff, H. W., & Phillips, D. C. (1958) · Nature · doi:10.1038/181662a0 · Cited by 1,671

The P450 Superfamily: Update on New Sequences, Gene Mapping, Accession Numbers, Early Trivial Names of Enzymes, and Nomenclature

Nelson, D. R., Kamataki, T., Waxman, D. J., Guengerich, F. P., Estabrook, R. W., Feyereisen, R., Gonzalez, F. J., Coon, M. J., GUNSALUS, I. C., Gotoh, O., et al. (1993) · DNA and Cell Biology · doi:10.1089/dna.1993.12.1 · Cited by 1,647

Microsomal Heme Oxygenase

Tenhunen, R., Marver, H. S., & Schmid, R. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63477-5 · Cited by 1,357

Structure of Myoglobin: A Three-Dimensional Fourier Synthesis at 2 Å. Resolution

Kendrew, J. C., Dickerson, R. E., Strandberg, B., Hart, R. G., Davies, D. R., Phillips, D. C., & Shore, V. C. (1960) · Nature · doi:10.1038/185422a0 · Cited by 1,351

Heme oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA radiation, hydrogen peroxide, and sodium arsenite.

Keyse, S. M., & Tyrrell, R. M. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.1.99 · Cited by 1,266

Comparison of cytochrome P450 (CYP) genes from the mouse and human genomes, including nomenclature recommendations for genes, pseudogenes and alternative-splice variants

Nelson, D. R., Zeldin, D. C., Hoffman, S. M. G., Maltais, L. J., Wain, H., & Nebert, D. W. (2003) · Pharmacogenetics · doi:10.1097/00008571-200401000-00001 · Cited by 1,044

The heme synthesis and degradation pathways: role in oxidant sensitivity

Ryter, S. W., & Tyrrell, R. M. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00223-3 · Cited by 825

Hypoxia-inducible factor-1 mediates transcriptional activation of the heme oxygenase-1 gene in response to hypoxia

Lee, P. J., Jiang, B.-H., Chin, B. Y., Iyer, N. V., Alam, J., Semenza, G. L., & Choi, A. K. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.9.5375 · Cited by 782

Insulin resistance in Alzheimer disease: Is heme oxygenase-1 an Achille's heel?

Barone, E., & Butterfield, D. A. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.02.013 · Cited by 30

The metabolism and toxicity of hemin in astrocytes

Dang, T. N. T., Bishop, G. M., Dringen, R., & Robinson, S. R. (2011) · Glia · doi:10.1002/glia.21198 · Cited by 29

Descriptive Inorganic Chemistry Researches of Metal Compounds

Akitsu, T. (2017) · InTech eBooks · doi:10.5772/65855 · Cited by 30

Assessment of the European flounder responses to chemical stress in the English Channel, considering biomarkers and life history traits

Dupuy, C., Galland, C., Pichereau, V., Sánchez, W., Riso, R. D., Labonne, M., Amara, R., Charrier, G., Fournier, M., & Laroche, J. (2014) · Marine Pollution Bulletin · doi:10.1016/j.marpolbul.2014.11.033 · Cited by 28

Inhibition of the NADPH oxidase regulates heme oxygenase 1 expression in chronic myeloid leukemia

Singh, M. M., Irwin, M. E., Gao, Y. H., Ban, K., Shi, P., Arlinghaus, R. B., Amin, H. M., & Chandra, J. (2011) · Cancer · doi:10.1002/cncr.26621 · Cited by 27

Free heme is a danger signal inducing expression of proinflammatory proteins in cultured cells derived from normal rat hearts

Hao, K., Hanawa, H., Ding, L., Ota, Y., Yoshida, K., Toba, K., Ogura, M., Ito, H., Kodama, M., & Aizawa, Y. (2011) · Molecular Immunology · doi:10.1016/j.molimm.2011.02.013 · Cited by 27

Identification of rare X-linked neuroligin variants by massively parallel sequencing in males with autism spectrum disorder

Steinberg, K. M., Ramachandran, D., Patel, V. C., Shetty, A. C., Cutler, D. J., & Zwick, M. E. (2012) · Molecular Autism · doi:10.1186/2040-2392-3-8 · Cited by 30

Activation of KEAP1/NRF2 stress signaling involved in the molecular basis of hemin-induced cytotoxicity in human pro-erythroid K562 cells

Georgiou‐Siafis, S. K., & Tsiftsoglou, A. S. (2020) · Biochemical Pharmacology · doi:10.1016/j.bcp.2020.113900 · Cited by 26

Rapid and Sensitive Quantitation of Heme in Hemoglobinized Cells

Marcero, J. R., Piel, R. B., Burch, J. S., & Dailey, H. A. (2016) · BioTechniques · doi:10.2144/000114444 · Cited by 25

Ferroportin and Erythroid Cells: An Update

Cianetti, L., Gabbianelli, M., & Sposi, N. M. (2010) · Advances in Hematology · doi:10.1155/2010/404173 · Cited by 28

Cross-Talk Between Iron and Glucose Metabolism in the Establishment of Disease Tolerance

Carlos, A. R., Weis, S., & Soares, M. P. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02498 · Cited by 26

Therapeutic potential of 5-aminolevulinic acid in metabolic disorders: Current insights and future directions

Kuryata, O. V., Akimov, O. Y., Ryabushko, M. М., Kostenko, H., Kostenko, V., Mishchenko, A. V., Nazarenko, S., Solovyova, N. V., & Kostenko, V. О. (2024) · iScience · doi:10.1016/j.isci.2024.111477 · Cited by 23

Effects of dietary cyanidin-3-diglucoside-5-glucoside complexes with rutin/Mg(II) against H2O2-induced cellular oxidative stress

Xu, W., Zhang, N., Zhang, Z., & Jing, P. (2019) · Food Research International · doi:10.1016/j.foodres.2019.108591 · Cited by 23

Haptoglobin and Hemopexin in Heme Detoxification and Iron Recycling

Chiabrando, D., Vinchi, F., Fiorito, V., & Tolosano, E. (2011) · InTech eBooks · doi:10.5772/18241 · Cited by 23

Inappropriate Expression of Hepcidin by Liver Congestion Contributes to Anemia and Relative Iron Deficiency

Suzuki, T., Hanawa, H., Jiao, S., Ohno, Y., Hayashi, Y., Yoshida, K., Kashimura, T., Obata, H., & Minamino, T. (2014) · Journal of Cardiac Failure · doi:10.1016/j.cardfail.2014.01.008 · Cited by 23

Heme Sensitization to TNF-Mediated Programmed Cell Death

Gozzelino, R., & Soares, M. P. (2010) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-6612-4_22 · Cited by 23

Hypoxia inducible factor-1 modulates hemin-induced IL-8 secretion in microvascular endothelium

Natarajan, R., Fisher, B. J., & Fowler, A. A. (2007) · Microvascular Research · doi:10.1016/j.mvr.2007.01.002 · Cited by 22

New roles for GAPDH, Hsp90, and NO in regulating heme allocation and hemeprotein function in mammals

Stuehr, D. J., Dai, Y., Biswas, P., Sweeny, E. A., & Ghosh, A. (2022) · Biological Chemistry · doi:10.1515/hsz-2022-0197 · Cited by 20

5-Aminolevulinic Acid (ALA) Reduces Arsenic Toxicity Stress in Wheat (Triticum aestivum L.)

Elsheery, N. I., Helaly, M. N., El-Hefnawy, S., Elhamahmy, M. M., Abdelrazik, E., Sardarov, Y. B., Ahmad, P., Živčák, M., Brestič, M., & Allakhverdiev, S. I. (2022) · Journal of Plant Growth Regulation · doi:10.1007/s00344-022-10791-2 · Cited by 21

A Correlation Between Diet and Longevity Characterization by Means of Element Profiles in Healthy People over 80 Years from a Chinese Longevous Region

Cai, D., Li, D., Zhao, S., Dou, X., Fang, W., Huang, G., Zhao, M., & Li, Q. (2015) · Biological Trace Element Research · doi:10.1007/s12011-015-0233-7 · Cited by 21

New light on the anti-colitic actions of therapeutic aminosalicylates: the role of heme oxygenase

Whittle, B. J. R., & Varga, C. (2010) · Pharmacological Reports · doi:10.1016/s1734-1140(10)70312-1 · Cited by 21

Alas1 is essential for neutrophil maturation in zebrafish

Lian, J., Chen, J., Wang, K., Zhao, L., Meng, P., Yang, L., Wei, J., Ma, N., Xu, J., Zhang, W., et al. (2018) · Haematologica · doi:10.3324/haematol.2018.194316 · Cited by 20

Complementation studies of the A rabidopsis fc1 mutant substantiate essential functions of ferrochelatase 1 during embryogenesis and salt stress

Fan, T., Roling, L., Meiers, A., Brings, L., Ortega‐Rodés, P., Hedtke, B., & Grimm, B. (2018) · Plant Cell & Environment · doi:10.1111/pce.13448 · Cited by 21

Down-regulation of aminolevulinate synthase, the rate-limiting enzyme for heme biosynthesis in Alzheimer's disease

Dwyer, B. E., Smith, M. A., Richardson, S. L., Perry, G. L., & Zhu, X. (2009) · Neuroscience Letters · doi:10.1016/j.neulet.2009.05.058 · Cited by 22

Disruption of heme-peptide covalent cross-linking in mammalian peroxidases by hypochlorous acid

Abu‐Soud, H. M., Maitra, D., Shaeib, F., Khan, S., Byun, J., Abdulhamid, I. B., Yang, Z., Saed, G. M., Diamond, M. P., Andreana, P. R., et al. (2014) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2014.06.018 · Cited by 20

Effects of rutin on the redox reactions of hemoglobin

Lu, N., Ding, Y., Yang, Z., & Gao, P. (2016) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2016.04.066 · Cited by 20

Transgenic Tobacco Lines Expressing Sense or AntisenseFERROCHELATASE 1RNA Show Modified Ferrochelatase Activity in Roots and Provide Experimental Evidence for Dual Localization of Ferrochelatase 1

Hey, D., Ortega‐Rodés, P., Fan, T., Schnurrer, F., Brings, L., Hedtke, B., & Grimm, B. (2016) · Plant and Cell Physiology · doi:10.1093/pcp/pcw171 · Cited by 20

Effects of 5-Aminolevulinic Acid on Gene Expression, Immunity, and ATP Levels in Pacific White Shrimp, Litopenaeus vannamei

Pedrosa‐Gerasmio, I. R., Tanaka, T., Sumi, A., Kondo, H., & Hırono, I. (2018) · Marine Biotechnology · doi:10.1007/s10126-018-9852-2 · Cited by 20

A scavenger receptor B (CD36)-like protein is a potential mediator of intestinal heme absorption in the hematophagous ectoparasite Lepeophtheirus salmonis

Heggland, E. I., Eichner, C., Støve, S. I., Martı́nez, A., Nilsen, F., & Dondrup, M. (2019) · Scientific Reports · doi:10.1038/s41598-019-40590-x · Cited by 20

Mechanism‐Guided Design and Synthesis of a Mitochondria‐Targeting Artemisinin Analogue with Enhanced Anticancer Activity

Zhang, C., Wang, J., Zhang, J., Lee, Y. M., Feng, G., Lim, T. K., Shen, H., Lin, Q., & Liu, B. (2016) · Angewandte Chemie · doi:10.1002/ange.201607303 · Cited by 19

Nrf2/HO-1 blocks TXNIP/NLRP3 interaction via elimination of ROS in oxygen-glucose deprivation-induced neuronal necroptosis

Liu, Z., Cheng, P., Feng, T., Xie, Z., Yang, M., Chen, Z., Hu, S., Han, D. K., & Chen, W. (2023) · Brain Research · doi:10.1016/j.brainres.2023.148482 · Cited by 20

Dual role of the active-center cysteine in human peroxiredoxin 1: Peroxidase activity and heme binding

Watanabe, Y., Ishimori, K., & Uchida, T. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.01.034 · Cited by 22

Influence of a Short-Term Iron-Deficient Diet on Hepatic Gene Expression Profiles in Rats

Kamei, A., Watanabe, Y. S., Kondo, K., Okada, S., Shinozaki, F., Ishijima, T., Nakai, Y., Kondo, T., Arai, S., & Abe, K. (2013) · PLoS ONE · doi:10.1371/journal.pone.0065732 · Cited by 19

The Potential Role of Cell Penetrating Peptides in the Intracellular Delivery of Proteins for Therapy of Erythroid Related Disorders

Papadopoulou, L. C., & Tsiftsoglou, A. S. (2013) · Pharmaceuticals · doi:10.3390/ph6010032 · Cited by 20

Blood cell oxidative stress precedes hemolysis in whole blood–liver slice co-cultures of rat, dog, and human tissues

Vickers, A. E. M., Sinclair, J. R., Fisher, R. L., Morris, S. R., & Way, W. G. (2010) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2010.01.017 · Cited by 18

Hemin inhibits cyclin D1 and IGF-1 expression via STAT5b under hypoxia in ERα-negative MDA-MB 231 breast cancer cells

Yang (2010) · International Journal of Oncology · doi:10.3892/ijo_00000608 · Cited by 17

Heme oxygenase/carbon monoxide in the female reproductive system: an overlooked signalling pathway.

Němeček, D., Dvořáková, M., & Sedmı́ková, M. (2017) · PubMed Central · Cited by 18

A compound-specific isotope method for measuring the stable nitrogen isotopic composition of tetrapyrroles

Chikaraishi, Y., Kashiyama, Y., Ogawa, N. O., Kitazato, H., Satoh, M., Nomoto, S., & Ohkouchi, N. (2007) · Organic Geochemistry · doi:10.1016/j.orggeochem.2007.08.010 · Cited by 18

Hemes in Biology

de Montellano, P. R. O. (2008) · Wiley Encyclopedia of Chemical Biology · doi:10.1002/9780470048672.wecb221 · Cited by 18

Heme biosensor-guided in vivo pathway optimization and directed evolution for efficient biosynthesis of heme

Zhang, J., Li, Q., Wang, Q., Zhao, J., Zhu, Y., Su, T., Qi, Q., & Wang, Q. (2023) · Biotechnology for Biofuels and Bioproducts · doi:10.1186/s13068-023-02285-4 · Cited by 17

Physiological stress-induced corticosterone increases heme uptake via KLF4-HCP1 signaling pathway in hippocampus neurons

Li, H., Zhang, C., Shen, H., Shen, Z., Wu, L., Mo, F., & Li, M. (2017) · Scientific Reports · doi:10.1038/s41598-017-06058-6 · Cited by 17

Hemin accumulation and identification of a heme‐binding protein clan in K562 cells by proteomic and computational analysis

Tsolaki, V. C., Georgiou‐Siafis, S. K., Tsamadou, A. I., Tsiftsoglou, S. A., Samiotaki, M. K., Panayotou, G., & Tsiftsoglou, A. S. (2021) · Journal of Cellular Physiology · doi:10.1002/jcp.30595 · Cited by 16

Iron status and oxidative stress in the aged rabbit heart

Lapenna, D., Ciofani, G., Pierdomenico, S. D., Giamberardino, M. A., & Porreca, E. (2017) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2017.11.016 · Cited by 17

Tyrosine can protect against oxidative stress through ferryl hemoglobin reduction

Lu, N., He, Y., Chen, C., Tian, R., Xiao, Q., & Peng, Y. (2014) · Toxicology in Vitro · doi:10.1016/j.tiv.2014.03.014 · Cited by 17

Protective effects of 5-aminolevulinic acid against toxicity induced by alpha-cypermethrin to the liver-gut-microbiota axis in zebrafish

Cheng, Y., Zhang, J., Gao, F., Xu, Y. B., & Wang, C. (2022) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2022.113422 · Cited by 16

Heme Binding to Porphobilinogen Deaminase from Vibrio cholerae Decelerates the Formation of 1-Hydroxymethylbilane

Uchida, T., Funamizu, T., Chen, M., Tanaka, Y., & Ishimori, K. (2018) · ACS Chemical Biology · doi:10.1021/acschembio.7b00934 · Cited by 16

Disruption of the dimerization interface of the sensing domain in the dimeric heme-based oxygen sensor AfGcHK abolishes bacterial signal transduction

Skálová, T., Lengálová, A., Dohnálek, J., Harlos, K., Mihalčin, P., Kolenko, P., Stráňava, M., Bláha, J., Shimizu, T., & Martínková, M. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.011574 · Cited by 16

Glutathione–Hemin/Hematin Adduct Formation to Disintegrate Cytotoxic Oxidant Hemin/Hematin in Human K562 Cells and Red Blood Cells’ Hemolysates: Impact of Glutathione on the Hemolytic Disorders and Homeostasis

Georgiou‐Siafis, S. K., Samiotaki, M. K., Demopoulos, V. J., Panayotou, G., & Tsiftsoglou, A. S. (2022) · Antioxidants · doi:10.3390/antiox11101959 · Cited by 15

Molecular Structures and Solvation of Free Monomeric and Dimeric Ferriheme in Aqueous Solution: Insights from Molecular Dynamics Simulations and Extended X-ray Absorption Fine Structure Spectroscopy

Kuter, D., Streltsov, V. A., Davydova, N., Venter, G. A., Naidoo, K. J., & Egan, T. J. (2014) · Inorganic Chemistry · doi:10.1021/ic500454d · Cited by 16

Heme Oxygenase-1 Attenuates Contact Hypersensitivity Induced by 2,4-Dinitrofluorobenzene in Mice

Pae, H., Ha, Y., Chai, K., & Chung, H. (2008) · Immunopharmacology and Immunotoxicology · doi:10.1080/08923970801946824 · Cited by 16

Shapes and Patterns of Heme-Binding Motifs in Mammalian Heme-Binding Proteins

Rathod, D., Vaidya, S. M., Hopp, M.-T., Kühl, T., & Imhof, D. (2023) · Biomolecules · doi:10.3390/biom13071031 · Cited by 18

Proteomic analysis of haem-binding protein from Arabidopsis thaliana and Cyanidioschyzon merolae

Shimizu, T., Yasuda, R., Mukai, Y., Tanoue, R., Shimada, T., Imamura, S., Tanaka, K., Watanabe, S., & Masuda, T. (2020) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2019.0488 · Cited by 15

Relationship between reactive oxygen species and heme metabolism during the differentiation of Neuro2a cells

Shinjyo, N., & Kita, K. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.04.071 · Cited by 15

Formation of novel N-acetylcysteine-hemin adducts abrogates hemin-induced cytotoxicity and suppresses the NRF2-driven stress response in human pro-erythroid K562 cells

Georgiou‐Siafis, S. K., Samiotaki, M. K., Demopoulos, V. J., Panayotou, G., & Tsiftsoglou, A. S. (2020) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2020.173077 · Cited by 15

Examining Hemin and its Derivatives: Induction of Heme-Oxygenase-1 Activity and Oxidative Stress in Breast Cancer Cells through Collaborative Experimental Analysis and Molecular Dynamics Simulations

Alsharabasy, A. M., Lagarias, P. I., Papavasileiou, K. D., Afantitis, A., Farràs, P., Glynn, S. A., & Pandit, A. S. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c00989 · Cited by 14

Dietary 5-aminolevulinic acid enhances adenosine triphosphate production, ecdysis and immune response in Pacific white shrimp, Litopenaeus vannamei (Boone)

Pedrosa‐Gerasmio, I. R., Kondo, H., & Hırono, I. (2019) · Aquaculture Research · doi:10.1111/are.13987 · Cited by 14

Reduced Iron Stores and Its Effect on Vasovagal Syncope (Simple Faint)

Stewart, J. M. (2008) · The Journal of Pediatrics · doi:10.1016/j.jpeds.2008.03.010 · Cited by 14

The dual effects of nitrite on hemoglobin-dependent redox reactions

Lu, N., Chen, C., He, Y., Tian, R., Xiao, Q., & Peng, Y. (2014) · Nitric Oxide · doi:10.1016/j.niox.2014.04.010 · Cited by 13

Genetic screens reveal CCDC115 as a modulator of erythroid iron and heme trafficking

Sobh, A., Loguinov, A. V., Zhou, J., Jenkitkasemwong, S., Zeidan, R. S., Ahmadie, N. E., Tagmount, A., Knutson, M. D., Fraenkel, P. G., & Vulpe, C. D. (2020) · American Journal of Hematology · doi:10.1002/ajh.25899 · Cited by 13

The Iron Chaperone Protein CyaY from Vibrio cholerae Is a Heme-Binding Protein

Uchida, T., Kobayashi, N., Muneta, S., & Ishimori, K. (2017) · Biochemistry · doi:10.1021/acs.biochem.6b01304 · Cited by 13

Pharmacophore Modeling, Synthesis, Scaffold Hopping and Biological β- Hematin Inhibition Interaction Studies for Anti-malaria Compounds

Fayyazi, N., Esmaeili, S., Taheri, S., Ribeiro, F. F., Scotti, L., Scotti, L., Ghasemi, J. B., Saghaei, L., & Fassihi, A. (2019) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026619666191116160326 · Cited by 13

Cardiac repolarization changes in the children with breath-holding spells.

Amoozgar, H., Saleh, F., Farhani, N., Rafiei, M., Inaloo, S., & Asadi‐Pooya, A. A. (2013) · Europe PMC (PubMed Central) · Cited by 13

Heme-Regulated eIF2α Kinase Plays a Crucial Role in Protecting Erythroid Cells against Pb-Induced Hemolytic Stress

Wang, X., Wang, L., & Liu, S. (2015) · Chemical Research in Toxicology · doi:10.1021/tx500422q · Cited by 12

The interaction between desferrioxamine and hemin: A potential toxicological implication

Lu, N., Yi, L., Deng, Q., Li, J., Gao, Z., & Li, H. (2012) · Toxicology in Vitro · doi:10.1016/j.tiv.2012.03.006 · Cited by 12

Unsaturated Glycerophospholipids Mediate Heme Crystallization: Biological Implications for Hemozoin Formation in the Kissing Bug Rhodnius prolixus

Stiebler, R., Majerowicz, D., Knudsen, J., Gondim, K. C., Wright, D. W., Egan, T. J., & de Oliveira, M. F. (2014) · PLoS ONE · doi:10.1371/journal.pone.0088976 · Cited by 12

Ferriheme catalyzes nitric oxide reaction with glutathione to form S-nitrosoglutathione: A novel mechanism for formation of S-nitrosothiols

Nagababu, E. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.09.015 · Cited by 12

Heme-binding to the nuclear receptor retinoid X receptor α (RXRα) leads to the inhibition of the transcriptional activity

Gotoh, S., Ohgari, Y., Nakamura, T., Osumi, T., & Taketani, S. (2008) · Gene · doi:10.1016/j.gene.2008.07.006 · Cited by 12

The brain heme oxygenase/biliverdin reductase system as a target in drug research and development

Mancuso, C. (2022) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2022.2052848 · Cited by 11

Hemin Improves Insulin Sensitivity and Lipid Metabolism in Cultured Hepatocytes and Mice Fed a High-Fat Diet

Luan, Y., Zhang, F., Cheng, Y., Liu, J., Huang, R., Yan, M., Wang, Y., He, Z., Lai, H., Wang, H. J., et al. (2017) · Nutrients · doi:10.3390/nu9080805 · Cited by 11

HEME: a neglected player in nociception?

Chiabrando, D., Fiorito, V., Petrillo, S., Bertino, F., & Tolosano, E. (2021) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2021.01.011 · Cited by 11

Managing GSH elevation and hypoxia to overcome resistance of cancer therapies using functionalized nanocarriers

Dabbour, N. M., Salama, A. M., Donia, T., Al-Deeb, R. T., Elghane, A. M. A., Badry, K. H., & Loutfy, S. A. (2021) · Journal of Drug Delivery Science and Technology · doi:10.1016/j.jddst.2021.103022 · Cited by 11

Highly fluorescent CdTe nanocrystals: Synthesis, characterization, property, mechanism, and application as a sensor for biomolecule analysis

Yao, J., Yang, M., & Duan, Y. (2014) · Journal of materials research/Pratt's guide to venture capital sources · doi:10.1557/jmr.2014.25 · Cited by 11

Systemic messenger RNA replacement therapy is effective in a novel clinically relevant model of acute intermittent porphyria developed in non-human primates

Córdoba, K. M., Jericó, D., Jiang, L., Collantes, M., Alegre, M., García-Ruiz, L., Manzanilla, O., Sampedro, A., Herranz, J. M., Insausti, I., et al. (2024) · Gut · doi:10.1136/gutjnl-2024-332619 · Cited by 10

Decoding the prospective of metal complexes in anti-cancer therapeutics by targeting of G-quadruplex DNA

Pramanik, P., & Bhattacharya, S. (2025) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2025.112947 · Cited by 10

Metal-organic framework material-derived Fe-Si micro-nuclei drive a robust anammox process via multiple pathways: “Shelter” provision, “barrier” reinforcement, and biological “inducer” modulation

Wang, P., Wu, B., Lü, B., & Chai, X. (2025) · Water Research · doi:10.1016/j.watres.2025.123906 · Cited by 10

Intracellular hemin is a potent inhibitor of the voltage-gated potassium channel Kv10.1

Sahoo, N., Yang, K., Coburger, I., Bernert, A., Swain, S. M., Geßner, G., Kappl, R., Kühl, T., Imhof, D., Hoshi, T., et al. (2022) · Scientific Reports · doi:10.1038/s41598-022-18975-2 · Cited by 10

Multilevel assessment of carbamazepine effects: An integrative approach using zebrafish early-life stages

da Silva, M. L., Andrade, T. S., Villacis, R. A. R., Sousa-Moura, D., Domingues, I., Lisboa, C. A., Camargo, N. S., Pic‐Taylor, A., Oliveira, R., & Grisólia, C. K. (2024) · Chemosphere · doi:10.1016/j.chemosphere.2024.141772 · Cited by 10

Substituent effects of iron porphyrins: Structural, kinetic, and theoretical studies

Lu, X., Ma, J., Sun, R., Nan, M., Meng, F., Du, J., Wang, X., & Shang, H. (2010) · Electrochimica Acta · doi:10.1016/j.electacta.2010.08.088 · Cited by 10

The Heme Metabolite Carbon Monoxide Facilitates KSHV Infection by Inhibiting TLR4 Signaling in Endothelial Cells

Botto, S., Gustin, J. K., & Moses, A. V. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.00568 · Cited by 10

Crosstalk between Erythropoiesis and Iron Metabolism

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