The DOI matches its Crossref record; 50 of the 50 references it cites were found in a registry or an index.
Iron regulates nitric oxide synthase activity by controlling nuclear transcription.
Open accessAbstract
Recently, it was reported that nitric oxide (NO) directly controls intracellular iron metabolism by activating iron regulatory protein (IRP), a cytoplasmic protein that regulates ferritin translation. To determine whether intracellular iron levels themselves affect NO synthase (NOS), we studied the effect of iron on cytokine-inducible NOS activity and mRNA expression in the murine macrophage cell line J774A.1. We show here that NOS activity is decreased by about 50% in homogenates obtained from cells treated with interferon gamma plus lipopolysaccharide (IFN-gamma/LPS) in the presence of 50 microM ferric iron [Fe(3+)] as compared with extracts from cells treated with IFN-gamma/LPS alone. Conversely, addition of the iron chelator desferrioxamine (100 microM) at the time of stimulation with IFN-gamma/LPS increases NOS activity up to 2.5-fold in J774 cells. These effects of changing the cellular iron state cannot be attributed to a general alteration of the IFN-gamma/LPS signal, since IFN-gamma/LPS-mediated major histocompatibility complex class II antigen expression is unaffected. Furthermore, neither was the intracellular availability of the NOS cofactor tetrahydrobiopterin altered by treatment with Fe(3+) or desferrioxamine, nor do these compounds interfere with the activity of the hemoprotein NOS in vitro. We demonstrate that the mRNA levels for NOS are profoundly increased by treatment with desferrioxamine and reduced by Fe(3+). The half-life of NOS mRNA appeared not to be significantly altered by administration of ferric ion, and NOS mRNA stability was only slightly prolonged by desferrioxamine treatment. Nuclear run-off experiments demonstrate that nuclear transcription of cytokine-inducible NOS mRNA is strongly increased by desferrioxamine whereas it is decreased by Fe(3+). Thus, this transcriptional response appears to account quantitatively for the changes in enzyme activity. Our results suggest the existence of a regulatory loop between iron metabolism and the NO/NOS pathway.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The cited source says what the claim attributes to it.
In the citing paper
“Thereby iron chelators antagonize a direct inhibitory effect of iron toward the expression of iNOS (Weiss et al., 1994; Melillo et al., 1997; Dlaska and Weiss, 1999).”
From Iron at the interface of immunity and infection (2014) · cites this paper as Weiss et al., 1994
In the citing paper
“Stimulation of ferroportin expression results in iron limitation to intra-macrophage bacteria and an improved control of the infection, which is also due to stimulation of MO effector functions as a consequence of intracellular iron deficiency.”
From Macrophage defense mechanisms against intracellular bacteria (2015) · cites this paper as [188]
In the citing paper
“In contrast, M1 macrophages enhance iron uptake and storage, and display an attenuated iron-release phenotype favoring intracellular iron sequestration and storage, which has been shown to enhance antimicrobial effector functions such as increased pro-inflammatory TNFα expression while suppressing expression of the anti-inflammatory cytokine, IL-10 (Weiss et al., 1994; Mulero et al., 2002; Fritsch”
From The Role of Iron Regulation in Immunometabolism and Immune-Related Disease (2019) · cites this paper as Weiss et al., 1994
In the citing paper
“Reduction in intracellular iron concentrations has been shown to promote the production of pro-inflammatory molecules such as TNF-α, IL-6, iNOS (nos2) or CCL-20 by activated macrophages (Weiss et al., 1994; Melillo et al., 1997; Ludwiczek et al., 2003; Oexle et al., 2003; Varesio et al., 2010), and these pathways are of importance for the control of intracellular pathogens like Salmonella (Andrews”
From Heme oxygenase 1 controls early innate immune response of macrophages to Salmonella Typhimurium infection: Heme oxygenase 1 expression affects Salmonella infection (2016) · cites this paper as Weiss et al., 1994
In the citing paper
“iron negatively effects the transcriptional expression of iNOS thereby building up a regulatory feedback loop linking cellular iron delivery to NO formation for host defense”
From Iron in immune cell function and host defense (2021) · cites this paper as [60]
In the citing paper
“As examples for this, iron perturbations regulate IFN-γ effector pathways by modulating ICAM-1 and HLA-DR expression on monocytes or TNFα and iNOS formation at the transcriptional level [60,141].”
From Iron in immune cell function and host defense (2021) · cites this paper as [60]
In the citing paper
“On one hand, macrophage iron overload is associated with the inhibition of IFN-γ-driven antimicrobial immune effector pathways such as nitric oxide synthase 2 (Nos2) expression, resulting in impaired control of intracellular microbes (Weiss et al., 1994; Mencacci et al., 1997; Oexle et al., 2003).”
From Genetic and Dietary Iron Overload Differentially Affect the Course of Salmonella Typhimurium Infection (2017) · cites this paper as Weiss et al., 1994
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Bradford, M. M. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90527-3 · Cited by 255,302
Single-Step Method of RNA Isolation by Acid Guanidinium Thiocyanate–Phenol–Chloroform Extraction
Chomczynski, P., & Sacchi, N. (1987) · Analytical Biochemistry · doi:10.1006/abio.1987.9999 · Cited by 65,515
A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity
Feinberg, A. P., & Vogelstein, B. (1983) · Analytical Biochemistry · doi:10.1016/0003-2697(83)90418-9 · Cited by 24,512
Analysis of nitrate, nitrite, and [15N]nitrate in biological fluids
Green, L. C., Wagner, D. A., Glogowski, J. A., Skipper, P. L., Wishnok, J. S., & Tannenbaum, S. R. (1982) · Analytical Biochemistry · doi:10.1016/0003-2697(82)90118-x · Cited by 12,061
The L-Arginine-Nitric Oxide Pathway
Epstein, F. H., Moncada, S., & Higgs, A. (1993) · New England Journal of Medicine · doi:10.1056/nejm199312303292706 · Cited by 6,678
Nitric oxide as a secretory product of mammalian cells
Nathan, C. (1992) · The FASEB Journal · doi:10.1096/fasebj.6.12.1381691 · Cited by 4,350
Nitric oxide: A cytotoxic activated macrophage effector molecule
Hibbs, J. B., Taintor, R. R., Vavrin, Z., & Rachlin, E. M. (1988) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(88)80015-9 · Cited by 2,030
Cloning and Characterization of Inducible Nitric Oxide Synthase from Mouse Macrophages
Xie, Q. W., Cho, H. J., Calaycay, J. R., Mumford, R. A., Swiderek, K. M., Lee, T. D., Ding, A. H., Troso, T., & Nathan, C. (1992) · Science · doi:10.1126/science.1373522 · Cited by 1,888
Nitric oxide mediates glutamate-linked enhancement of cGMP levels in the cerebellum.
Bredt, D. S., & Snyder, S. H. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.22.9030 · Cited by 1,849
Cleveland, D. W., Lopata, M. A., MacDonald, R. J., Cowan, N. J., Rutter, W. J., & Kirschner, M. W. (1980) · Cell · doi:10.1016/0092-8674(80)90238-x · Cited by 1,835
Flagged first, then by citations
Cited by
Sorted by citations
Items 301–400 of 411
Molecular Biology and Molecular Genetics of Nitric Oxide Synthase Genes
Nadaud, S., & Soubrier, F. (1996) · Clinical and Experimental Hypertension · doi:10.3109/10641969609081761 · Cited by 14
Effect of nitric oxide on iron‐mediated cytotoxicity in primary cultured renal proximal tubules
Wu, Z., & Qiu, L. (2001) · Cell Biochemistry and Function · doi:10.1002/cbf.921 · Cited by 13
Castration differentially regulates nitric oxide synthase in the hypothalamus and pituitary
Shi, Q., LaPaglia, N., Emanuele, N., & Emanuele, M. A. (1998) · Endocrine Research · doi:10.3109/07435809809031867 · Cited by 13
Leplingard, A., Brung-Lefebvre, M., Guédon, C., Savoye, G., Déchelotte, P., Lemoine, F., Lebreton, J.-P., & Lerebours, É. (2001) · The American Journal of Gastroenterology · doi:10.1016/s0002-9270(01)02511-4 · Cited by 13
Nanke, Y., Kotake, S., Yonemoto, K., Saito, S., Tomatsu, T., & Kamatani, N. (2002) · Annals of the Rheumatic Diseases · doi:10.1136/ard.62.1.82 · Cited by 13
Brittenham, G. M., Weiß, G., Brissot, P., Lainé, F., Guillygomarc’h, A., Guyader, D., Moirand, R., & Deugnier, Y. (2000) · Hematology · doi:10.1182/asheducation.v2000.1.39.39 · Cited by 13
Iron and the Reticuloendothelial System
Weiß, G. (2011) · Humana Press eBooks · doi:10.1007/978-1-60327-485-2_11 · Cited by 13
Growth Enhancement by Intramuscular Injection of Elemental Iron Nano- and Microparticles
Sizova, E. A., Yausheva, Е., Kosyan, D., & Miroshnikov, S. (2015) · Modern Applied Science · doi:10.5539/mas.v9n10p17 · Cited by 12
Batista, L. F. S., Torrecilha, R. B. P., da Silva, R. B., Utsunomiya, Y. T., Silva, T. B. F., Tomokane, T. Y., Pacheco, A. D., Bosco, A. M., Paulan, S. D. C., Rossi, C. N., et al. (2020) · Veterinary Parasitology · doi:10.1016/j.vetpar.2020.109276 · Cited by 12
Choi, E., Lee, S., Oh, H., Kim, Y., Choi, E., Kim, S., Kim, S.-W., Choi, S. C., & Jun, C. (2006) · Life Sciences · doi:10.1016/j.lfs.2006.09.044 · Cited by 12
Characterization of the Murine Nramp1 Promoter
Bowen, H., Lapham, A. S., Phillips, E. S., Yeung, I., Alter-Koltunoff, M., Levi, B.-Z., Perry, V. H., Mann, D. A., & Barton, C. H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304301200 · Cited by 13
Leyshon, B. J., Ji, P., Caputo, M. P., Matt, S. M., & Johnson, R. W. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2018.03150 · Cited by 10
Adam, I., Ehassan, E. M., Mohmmed, A. A., Salih, M. M., & Elbashir, M. I. (2012) · Pathogens and Global Health · doi:10.1179/2047773212y.0000000011 · Cited by 11
Interactions Between Gasotransmitters
Carson, R. J., Seyffarth, G., Mian, R., & Maddock, H. L. (2004) · Humana Press eBooks · doi:10.1007/978-1-59259-806-9_2 · Cited by 12
Kobak, K. A., Franczuk, P., SCHUBERT, J., Dzięgała, M., Kasztura, M., Tkaczyszyn, M., Drozd, M., Kosiorek, A., Kiczak, L., Bania, J., et al. (2021) · Cells · doi:10.3390/cells10040818 · Cited by 11
Roberts, S. A., Brabin, L., Tinto, H., Gies, S., Diallo, S., & Brabin, B. J. (2021) · BMC Public Health · doi:10.1186/s12889-021-11819-0 · Cited by 12
Marzban, A., Akbarzadeh, A., Ardestani, M. S., Ardestani, F., & Akbari, M. (2017) · The Canadian Journal of Chemical Engineering · doi:10.1002/cjce.23048 · Cited by 11
Requirement for multiple activation signals by anti-inflammatory feedback in macrophages
Ray, J. C. J., & Kirschner, D. E. (2006) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2005.11.037 · Cited by 11
Saleppico, S., Boelaert, J. R., Salè, F. O., Mazzolla, R., Morucci, P., Bistoni, F., & Blasi, E. (1999) · Journal of Neuroimmunology · doi:10.1016/s0165-5728(98)00206-9 · Cited by 11
Effects of the Ferritin Open Reading Frame on Translational Induction by iron
Mascotti, D. P., Goessling, L. S., Rup, D., & Thach, R. E. (1996) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(08)60191-9 · Cited by 11
Inducible enzymes with special reference to COX-2 in inflammation and apoptosis
Willoughby, D. A., Tomlinson, A., Gilroy, D. W., & Willis, D. (1996) · Springer eBooks · doi:10.1007/978-94-010-9029-2_4 · Cited by 11
Patidar, A., Malhotra, H., Chaudhary, S., Kumar, M., Dilawari, R., Chaubey, G., Dhiman, A., Modanwal, R., Talukdar, S., Raje, C., et al. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-04110-3 · Cited by 9
Methodologies and tools to shed light on erythrophagocytosis
Turpin, C., Meilhac, O., Bourdon, E., Canonne‐Hergaux, F., & Rondeau, P. (2022) · Biochimie · doi:10.1016/j.biochi.2022.07.017 · Cited by 10
Makene, V. W., Tijani, J. O., Petrik, L. F., & Pool, E. J. (2016) · Environmental Monitoring and Assessment · doi:10.1007/s10661-016-5441-x · Cited by 10
Nairz, M., Metzendorf, C., Spasić, M. V., Mitterstiller, A., Schroll, A., Haschka, D., Hoffmann, A., von Raffay, L., Sparla, R., Huck, C. W., et al. (2020) · Haematologica · doi:10.3324/haematol.2019.241745 · Cited by 11
Nitrite/Nitrate Responses to Endotoxin in Calves*
Hüsler, B. R., & Blum, J. W. (2001) · Zentralblatt für Veterinärmedizin Reihe A · doi:10.1046/j.1439-0442.2001.00380.x · Cited by 10
Efficacy and Safety of Intravenous Iron Therapy for HCV-Positive Haemodialysis Patients
Kahraman, S., Yılmaz, R., Gençtoy, G., Arıcı, M., Altun, B., Erdem, Y., Yasavul, Ü., & Turgan, Ç. (2005) · Nephron Clinical Practice · doi:10.1159/000085052 · Cited by 10
Hasegawa, T., Sorensen, L. K., Ooi, H., & Marshall, B. C. (1999) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.21.2.3445 · Cited by 10
Effects of Different Doses of Excessive Iron in Diets on Oxidative Stress in Immune Organs of Sheep
Liu, X., Zhao, J., Zhang, L., Lu, J., Lv, X., Liu, C., & Gao, X. (2020) · Biological Trace Element Research · doi:10.1007/s12011-019-02006-9 · Cited by 9
Choi, J., Lee, J., Lee, J.-H., Kim, S., Kim, J., & Kim, S. (2013) · Nitric Oxide · doi:10.1016/j.niox.2013.05.003 · Cited by 8
Hepcidin mediated iron homoeostasis as immune regulator in visceral leishmaniasis patients
Singh, B., Singh, S. S., & Sundar, S. (2018) · Parasite Immunology · doi:10.1111/pim.12601 · Cited by 8
Georgalas, I., Makris, G., Papaconstantinou, D., Petrou, P., Chalkiadaki, E., Droutsas, K. D., Andreanos, K. D., & Kanakis, M. G. (2019) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.19-27291 · Cited by 8
Piepoli, A. L., Salvatore, G. D., Lemoli, M., Benedictis, L. D., Mitolo‐Chieppa, D., & Salvia, M. A. D. (2008) · Neurogastroenterology & Motility · doi:10.1111/j.1365-2982.2008.01193.x · Cited by 8
Short term protective effects of iron in a murine model of ischemia/reperfusion
Metzler, B., Jehle, J., Theurl, I., Ludwiczek, S., Obrist, P., Pachinger, O. M., & Weiß, G. (2006) · BioMetals · doi:10.1007/s10534-006-9034-y · Cited by 8
Nishiya, K., Wang, H., Tahara, K., & Hashimoto, K. (2002) · Annals of the Rheumatic Diseases · doi:10.1136/ard.62.1.89 · Cited by 8
Association of Serum Hepcidin With Preeclampsia: A Systematic Review and Meta-Analysis
Bandyopadhyay, A., Ahamed, F., Palepu, S., Ghosh, T. K., & Yadav, V. (2022) · Cureus · doi:10.7759/cureus.26699 · Cited by 9
Delayed Hyperresistance of Endothelial Cells to Photodynamic Inactivation After Contact with Hemin
Lin, F., Bertling, C. J., Geiger, P. G., & Girotti, A. W. (1998) · Photochemistry and Photobiology · doi:10.1111/j.1751-1097.1998.tb02491.x · Cited by 7
Regulation of Mammalian Iron Metabolism: Current State and Need for Further Knowledge
Goldenberg, H., & Poňka, P. (1997) · Critical Reviews in Clinical Laboratory Sciences · doi:10.3109/10408369709006425 · Cited by 8
Inducible enzymes in inflammation: advances, interactions and conflicts
Tomlinson, A., & Willoughby, D. A. (1999) · Birkhäuser Basel eBooks · doi:10.1007/978-3-0348-8747-2_9 · Cited by 7
Toxicity of the iron siderophore mycobactin J in mouse macrophages: Evidence for a hypoxia response
McQueen, C. F., & Groves, J. T. (2021) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2021.111669 · Cited by 6
Genetic Iron Overload Hampers Development of Cutaneous Leishmaniasis in Mice
Charlebois, E., Li, Y., Wagner, V., Pantopoulos, K., & Olivier, M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24021669 · Cited by 6
Haptoglobin phenotypes and iron status in children living in a malaria endemic area of Kenyan coast
Nyakeriga, A. M., & Troye‐Blomberg, M. (2013) · Acta Tropica · doi:10.1016/j.actatropica.2013.02.004 · Cited by 6
Tian, P.-W., Wang, Y., Yc, S., Chen, L., Wan, C., Liao, Z.-L., & Wen, F.-Q. (2014) · PubMed · Cited by 6
Nifedipine Potentiates Susceptibility of Salmonella Typhimurium to Different Classes of Antibiotics
Haschka, D., Grander, M., Eibensteiner, J., Dichtl, S., Koppelstätter, S., & Weiß, G. (2021) · Antibiotics · doi:10.3390/antibiotics10101200 · Cited by 5
Testa, U. (2001) · CRC Press eBooks · doi:10.1201/b14262-9 · Cited by 4
Enzymatic Targets of Nitric Oxide as Detected by EPR Spectroscopy within Mammal Cells
Henry, Y. A., Ducastel, B., & Guissani, A. (1997) · Springer eBooks · doi:10.1007/978-1-4613-1185-0_11 · Cited by 5
Effect of nitric oxide donor on viability of human leukemic cells upon arginine deprivation
Chen, O. I., Lyniv, L., Igumentseva, N. I., Barska, M., Sybirna, N. O., & Stasyk, O. V. (2011) · Studia Biologica · doi:10.30970/sbi.0502.155 · Cited by 5
Henry, Y. (1997) · Springer eBooks · doi:10.1007/978-1-4613-1185-0_7 · Cited by 5
The Iron Responsive Element (IRE), the Iron Regulatory Protein (IRP), and Cytosolic Aconitase
Eisenstein, R. S., Kennedy, M. C., & Beinert, H. (1998) · Springer eBooks · doi:10.1007/978-1-4615-5993-1_7 · Cited by 5
Richardson, D. R., Dickson, L., & Baker, E. (1996) · In Vitro Cellular & Developmental Biology - Animal · doi:10.1007/bf02723052 · Cited by 4
Belosevic, M., Haddad, G., Walsh, J. G., Grayfer, L., Katzenback, B. A., Hanington, P. C., Neumann, N. F., & Stafford, J. L. (2009) · Science Publishers eBooks · doi:10.1201/b10188-6 · Cited by 4
Bhalla, P., Singh, N. P., & Ravi, K. (2011) · Journal of the Renin-Angiotensin-Aldosterone System · doi:10.1177/1470320311399604 · Cited by 4
Wang, B.-S., Lin, J., & Lin‐Shiau, S. (1999) · Biochemical Pharmacology · doi:10.1016/s0006-2952(99)00047-7 · Cited by 4
Innate immunity of fish: antimicrobial responses of fish macrophages.
Belosevic, M., Haddad, G., Walsh, J. G., Grayfer, L., Katzenback, B. A., Hanington, P. C., Neumann, N. F., Stafford, J. L., Zaccone, G., Meseguer, J., et al. (2008) · Cited by 4
Weiler, S., & Nairz, M. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.627223 · Cited by 4
Weiß, G. (2004) · Humana Press eBooks · doi:10.1007/978-1-59259-652-2_11 · Cited by 4
Richardson, D. R. (2007) · Elsevier eBooks · doi:10.1016/b978-044452236-8/50004-6 · Cited by 3
Tahara, K., Nishiya, K., Hisakawa, N., Wang, H., & Hashimoto, K. (2003) · Immunological Investigations · doi:10.1081/imm-120025103 · Cited by 3
Qi, J., Liang, Y., Yu, D., Li, W., Long, F., Yuan, M., Lou, Z., Liu, C., Wang, G., Wu, B., et al. (2026) · Journal of Animal Science and Biotechnology/Journal of animal science and biotechnology · doi:10.1186/s40104-026-01356-4 · Cited by 2
Ołdakowska, A. K., Kamiński, K. A., & Ptaszyńska‐Kopczyńska, K. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27052333 · Cited by 2
EPR Detection of Nitrosylated Compounds : Introduction with some Historical Background
Henry, Y. A., & Guissani, A. (1998) · Springer eBooks · doi:10.1007/978-1-4615-5081-5_1 · Cited by 2
Possible Pivotal Role of Latent Chronic T. gondii Infection in the Pathogenesis of Atherosclerosis
PRANDOTA, J. (2017) · Journal of Cardiology and Therapy · doi:10.17554/j.issn.2309-6861.2017.04.130 · Cited by 2
Chemistry and Biology of Nitric Oxide
Komarov, A. M. (2003) · Biological magnetic resonance · doi:10.1007/978-1-4615-0061-2_13 · Cited by 2
Enzymology of Nitric Oxide Biosynthesis
Hemmens, B., & Mayer, B. (2002) · Springer eBooks · doi:10.1007/0-306-46816-6_4 · Cited by 2
Krzystek‐Korpacka, M., Korpacki, A., Wąsowicz, A., & Neubauer, K. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27188359 · Cited by 1
Involvement of Peroxynitrite in NO Donor-Induced HO-1 Expression in Rat Articular Chondrocytes
Song, J.-D., Kim, K.-M., Kim, J. M., Yoo, Y.-H., & Park, Y.-C. (2011) · Journal of Life Science · doi:10.5352/jls.2011.21.4.486 · Cited by 1
Linkage of Pteridine Metabolism to Iron Homeostasis
Weiß, G. (2004) · Pteridines · doi:10.1515/pteridines.2004.15.3.120 · Cited by 1
Xin, P. (2011) · African Journal of Microbiology Research · doi:10.5897/ajmr11.549 · Cited by 1
Landeros-Sánchez, B., Gutierrez-Pabello, J. A., Basulto, G. E. M., Evangelista, T. B. R., Aparicio, E. D., & Hori-Oshima, S. (2016) · Veterinaria México OA · doi:10.21753/vmoa.3.1.361 · Cited by 1
Chattopadhya, D., & Verghese, A. (2018) · Journal of Biosciences and Medicines · doi:10.4236/jbm.2018.64001 · Cited by 1
Raj, N. L. S., Sharma, U. A., Devi, M. L. R., Purushothama, S. M., Manjunath, S., & Shashidhar, H. (2020) · Biomedicine · doi:10.51248/.v39i2.194 · Cited by 1
Iron and Nitric Oxide in Anemia of Chronic Disease (ACD)
Stephen, O., Sulaiman, F. A., & Akanji, M. A. (2012) · InTech eBooks · doi:10.5772/28612 · Cited by 1
Kezele, T. G. (2018) · Healthy ageing and longevity · doi:10.1007/978-3-030-03742-0_1 · Cited by 1
Thomas, L., & Thomas, C. (2017) · Journal of Laboratory Medicine · doi:10.1515/labmed-2017-0083 · Cited by 1
Regulation of iron metabolism in higher eukaryotes: iron–sulfur centers as genetic switches
Pantopoulos, K., & Hentze, M. W. (1999) · Wiley eBooks · doi:10.1002/9783527613700.ch08 · Cited by 1
Self-citationBiological markers in children with iron deficiency
Dastgheyb, S., Gordeuk, V. R., & Kasvosve, I. (2007) · Digital Howard (Howard University) · Cited by 1
Nitric Oxide Does Not Contribute to Inflammation-Induced Hypoferremia in Humans
Kemna, E., Pickkers, P., Tjalsma, H., & Swinkels, D. W. (2007) · Acta Haematologica · doi:10.1159/000108583 · Cited by 1
Control of tuberculosis in India
Mohapatra, P. R. (2003) · The Lancet · doi:10.1016/s0140-6736(03)14528-x · Cited by 1
Etiology of Metabolic Changes in Severe Plasmodium falciparum Malaria
Eisenhut, M. (2015) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiv084 · Cited by 1
Regulation and Role of Heme Oxygenase-1 in Glomerulonephritis
Datta, P. K., & Lianos, E. A. (2002) · Springer eBooks · doi:10.1007/978-1-4615-0741-3_21 · Cited by 1
Nitric Oxide in Human Physiology
Mohammed, M. K., & Zuckerbraun, B. S. (2022) · Wiley eBooks · doi:10.1002/9781119783435.ch8 · Cited by 1
Post-Transcriptional Regulation of Iron Metabolism
Hentze, M. W. (1996) · Springer eBooks · doi:10.1007/978-3-642-61180-3_10
Self-citationHeme Oxygenase and Acute Lung Injury: The Functional Significance of Heme Oxygenase Induction
Lamb, N. J., Quinlan, G. J., & Evans, T. W. (1999) · Yearbook of intensive care and emergency medicine · doi:10.1007/978-3-662-13453-5_35
Chlosta, S. (2008) · Universitätsbibliothek der FU Berlin Hochschulschriftenstelle u. Dokumentenserver · doi:10.17169/refubium-18022
O papel das mutações do gene HFE e da sobrecarga de ferro na evolução da hepatite crônica pelo VHC
da Silva, A. L. B. (2009) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/d.5.2009.tde-08122009-181724
Histochemical Analysis of Heme Degradation Enzymes
Ewing, J. F. (1999) · Current Protocols in Toxicology · doi:10.1002/0471140856.tx0905s02
Review on Iron, Immunity and Intensive Care
van Eijk, L. T., Swinkels, D. W., & Pickkers, P. (2014) · Springer eBooks · doi:10.1007/978-3-319-03746-2_2
The role of iron in rheumatoid arthritis
Al-Qenaei, A. (2008) · The University of Bath Online Publications Store (The University of Bath)
Crosstalk Between Iron Homeostasis And Nitric Oxide Signalling: Impact On Cancer Cell Viability
Ariffin, M. (2012) · Otago University Research Archive (University of Otago)
Post-Transcriptional Regulation of Gene Expression by Iron
Hentze, M. W. (1995) · Birkhäuser Boston eBooks · doi:10.1007/978-1-4684-6840-3_8
Self-citationHara, E., Takahashi, K., Fujita, H., & Shibahara, S. (1998) · Springer eBooks · doi:10.1007/978-4-431-68476-3_41
[Sudden cardiac death in mitral valve prolapse syndrome?].
Penning, R. (1990) · PubMed
Jung, M., Shu, Z.-J., Beger, H. G., & Nussler, A. K. (1997) · Springer eBooks · doi:10.1007/978-3-642-60717-2_124
Connor, J. R., Cheepsunthorn, P., & Zhang, X. (2004) · CRC Press eBooks · doi:10.1201/9781420039740.ch23
Iron inhibits replication of infectious hepatitis C virus in permissive Huh7.5.1 cells
Davis, L., Mortimer, S., & Lynn, B. C. D. (2010)
An atypical case of Stanford type‐A chronic aortic dissection managed conservatively
Maffè, S., Nicali, R., Dellavesa, P., Paffoni, P., Bergamasco, L., & Parravicini, U. (2019) · Echocardiography · doi:10.1111/echo.14493
In Silico Identification of L. Donovani Excretory-secretory Proteins Interacting with Human SLC11 A1
Singh, N. K., Singh, S., & Rawat, A. K. (2020) · Journal of scientific research · doi:10.37398/jsr.2020.640119
Wick, M. W., Pinggera, W., & Lehmann, P. (2002) · Springer eBooks · doi:10.1007/978-3-7091-6143-2_12
Metadata
- Authors
- Weiss, G., Werner-Felmayer, G., Werner, E. R., Grünewald, K., Wachter, H., & Hentze, M. W.
- Affiliations
- Universität Innsbruck (AT)
- Department of Internal Medicine, University of Innsbruck, Austria.
- Venue
- The Journal of experimental medicine
- Publisher
- Rockefeller University Press
- Published
- 1994-09-01
- Volume
- 180
- Issue
- 3
- Pages
- 969-976
- ISSN
- 0022-1007 (ISSN-L)
- 1540-9538
- PMC
- PMC2191642
- OpenAlex
- W1976665224
- Cited by
- 412
- References
- 50
- Citations by year
- 2026: 4 · 2024: 6 · 2023: 6 · 2022: 6 · 2021: 11 · 2020: 14 · 2019: 6 · 2018: 14 · 2017: 8 · 2016: 8 · 2015: 10 · 2014: 11 · 2013: 13 · 2012: 9
- FWCI
- 12.22
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Experimental Medicine (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
- Keywords
- nitric oxide synthase, iron metabolism, deferoxamine, iron(III), macrophages, interferon-gamma, lipopolysaccharide, tetrahydrobiopterin, iron regulatory proteins, MHC class II expression
- MeSH terms
- Amino Acid Oxidoreductases, Animals, Cell Nucleus, Cells, Cultured, Deferoxamine, Half-Life, Interferon-gamma, Iron, Macrophages, Nitric Oxide, RNA, Messenger, Transcription, Genetic, Gene Expression Regulation, Enzymologic, Nitric Oxide Synthase, Mice
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
