Relevant bibliographies by topics / BILIVERDINE

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  2. Dissertations / Theses
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  4. Conference papers

Academic literature on the topic 'BILIVERDINE'

Author: Grafiati
Published: 4 June 2021
Last updated: 10 February 2022

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Journal articles on the topic "BILIVERDINE"

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Wasbotten, Ingar, and Abhik Ghosh. "Biliverdine-Based Metalloradicals: Sterically Enhanced Noninnocence." Inorganic Chemistry 45, no. 13 (2006): 4914–21. http://dx.doi.org/10.1021/ic052037w.

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Steiner, Alexandre A., and Luiz G. S. Branco. "Carbon monoxide is the heme oxygenase product with a pyretic action: evidence for a cGMP signaling pathway." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 280, no. 2 (2001): R448—R457. http://dx.doi.org/10.1152/ajpregu.2001.280.2.r448.

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We have recently reported that the central heme oxygenase (HO) pathway has an important role in the genesis of lipopolysaccharide fever. However, the HO product involved, i.e., biliverdine, free iron, or carbon monoxide (CO), has not yet been identified with certainty. Therefore, in the present study, we tested the thermoregulatory effects of all HO products. Body core temperature (Tc) and gross activity of awake, freely moving rats was measured by biotelemetry. Intracerebroventricular administration of heme-lysinate (152 nmol), which induces the HO pathway, evoked a marked increase in Tc, a r
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Johnson, R. A., M. Lavesa, K. DeSeyn, M. J. Scholer, and A. Nasjletti. "Heme oxygenase substrates acutely lower blood pressure in hypertensive rats." American Journal of Physiology-Heart and Circulatory Physiology 271, no. 3 (1996): H1132—H1138. http://dx.doi.org/10.1152/ajpheart.1996.271.3.h1132.

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Heme oxygenase catalyzes the metabolism of heme to biliverdine, free iron, and carbon monoxide. The current study was designed to determine if treatment with the heme oxygenase substrates heme-L-arginate or heme-L-lysinate, to stimulate formation of heme oxygenase products, can lower blood pressure in the rat. Heme-L-arginate (45 mumol/kg ip) and heme-L-lysinate (45 mumol/kg ip) acutely lowered blood pressure in awake spontaneously hypertensive rats (SHR) by approximately 35 mmHg. For both heme oxygenase substrates, this effect was blunted by pretreatment with an inhibitor of heme oxygenase, z
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Niemevz, Fernando, and Graciela Y. Buldain. "Phenyl biliverdin isomers obtained by chemical oxidation of iron(III) complex of 5-phenyl protoporphyrin IX." Journal of Porphyrins and Phthalocyanines 08, no. 07 (2004): 989–95. http://dx.doi.org/10.1142/s1088424604000350.

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Oxidative cleavage of synthetic 5-phenyl protohemin IX in pyridine solution in the presence of ascorbic acid (coupled oxidation), followed by esterification of the products with boron trifluoride-methanol rendered mainly three isomeric biliverdins. These were identified by MS and 1D and 2D 1 H NMR as 15-phenyl biliverdin IXβ (1), 10-phenyl biliverdin IXγ (2) and 5-phenyl biliverdin IXδ (3) dimethyl esters. The fact that biliverdin IXα dimethyl ester derivative is not obtained indicates that oxidation fails to occur in the α-meso-carbon bearing the phenyl group.
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Yoshinaga, T., Y. Sudo та S. Sano. "Enzymic conversion of α-oxyprotohaem IX into biliverdin IXα by haem oxygenase". Biochemical Journal 270, № 3 (1990): 659–64. http://dx.doi.org/10.1042/bj2700659.

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Conversion of four isomers of meso-oxyprotohaem IX into the corresponding biliverdin IX was attempted with a reconstituted haem oxygenase system in the presence of NADPH-cytochrome c reductase and NADPH. Only the alpha-isomer of meso-oxyprotohaem IX was converted effectively into biliverdin IX alpha, which was further reduced to bilirubin IX alpha by biliverdin reductase. Only trace amounts of biliverdins IX beta, IX gamma and IX delta were respectively formed from the incubation mixture of the corresponding oxyprotohaemin IX isomers with the complete haem oxygenase system under the same condi
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Smith, Liam J., Seamus Browne, Adrian J. Mulholland та Timothy J. Mantle. "Computational and experimental studies on the catalytic mechanism of biliverdin-IXβ reductase". Biochemical Journal 411, № 3 (2008): 475–84. http://dx.doi.org/10.1042/bj20071495.

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BVR-B (biliverdin-IXβ reductase) also known as FR (flavin reductase) is a promiscuous enzyme catalysing the pyridine-nucleotide-dependent reduction of a variety of flavins, biliverdins, PQQ (pyrroloquinoline quinone) and ferric ion. Mechanistically it is a good model for BVR-A (biliverdin-IXα reductase), a potential pharmacological target for neonatal jaundice and also a potential target for adjunct therapy to maintain protective levels of biliverdin-IXα during organ transplantation. In a commentary on the structure of BVR-B it was noted that one outstanding issue remained: whether the mechani
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McDonagh, Antony F., David A. Lightner, Ari K. Kar, and Wilma S. Norona. "Hepatobiliary excretion of biliverdin isomers and C10-substituted biliverdins in Mrp2-deficient (TR−) rats." Biochemical and Biophysical Research Communications 293, no. 3 (2002): 1077–83. http://dx.doi.org/10.1016/s0006-291x(02)00325-x.

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Andresen, Jon J., Nadeem I. Shafi, William Durante, and Robert M. Bryan. "Effects of carbon monoxide and heme oxygenase inhibitors in cerebral vessels of rats and mice." American Journal of Physiology-Heart and Circulatory Physiology 291, no. 1 (2006): H223—H230. http://dx.doi.org/10.1152/ajpheart.00058.2006.

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Carbon monoxide (CO) has been postulated to be a signaling molecule in many tissues, including the vasculature. We examined vasomotor responses of adult rat and mouse cerebral arteries to both exogenously applied and endogenously produced CO. The diameter of isolated, pressurized, and perfused rat middle cerebral arteries (MCAs) was not altered by authentic CO (10−6 to 10−4 M). Mouse MCAs, however, dilated by 21 ± 10% at 10−4 M CO. Authentic nitric oxide (NO·, 10−10 to 10−7 M) dilated both rat and mouse MCAs. At 10−8 M NO·, rat vessels dilated by 84 ± 4%, and at 10−7 M NO·, mouse vessels dilat
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Itano, H. A., and T. Hirota. "A two-molecule mechanism of haem degradation." Biochemical Journal 226, no. 3 (1985): 767–71. http://dx.doi.org/10.1042/bj2260767.

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Coupled oxidation of octaethylhaemin and phenylhydrazine hydrochloride with 16,16O2 and 18,18O2 produced octaethyl[16O]verdohaemochrome and octaethyl[18O]-verdohaemochrome respectively. Reactions of these products with 16,16O2 in the presence of phenylhydrazine hydrochloride yielded octaethyl[16O, 16O]biliverdin and octaethyl[18O, 16O]biliverdin. The same reactions with 18,18O2 yielded octaethyl[16O, 18O]biliverdin and octaethyl[18O, 18O]biliverdin. Accordingly, the two oxygen atoms of biliverdin are incorporated from different O2 molecules in separate reactions, namely the formation of verdoh
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SHALLOE, Fiona, Gordon ELLIOTT, Orla ENNIS та Timothy J. MANTLE. "Evidence that biliverdin-IXβ reductase and flavin reductase are identical". Biochemical Journal 316, № 2 (1996): 385–87. http://dx.doi.org/10.1042/bj3160385.

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A search of the database shows that human biliverdin-IXβ reductase and flavin reductase are identical. We have isolated flavin reductase from bovine erythrocytes and show that the activity co-elutes with biliverdin-IXβ reductase. Preparations of the enzyme that are electrophoretically homogeneous exhibit both flavin reductase and biliverdin-IXβ reductase activities; however, they are not capable of catalysing the reduction of biliverdin-IXα. Although there is little obvious sequence identity between biliverdin-IXα reductase (BVR-A) and biliverdin-IXβ reductase (BVR-B), they do show weak immuno
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Dissertations / Theses on the topic "BILIVERDINE"

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Peixoto, Mauricio Cupello. "Análise e identificação de produtos do catabolismo de heme nas formas epimastigotas de Trypanosoma cruzi." Universidade do Estado do Rio de Janeiro, 2014. http://www.bdtd.uerj.br/tde_busca/arquivo.php?codArquivo=8257.

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O Trypanosoma cruzi, agente etiológico da doença de Chagas, possui um ciclo de vida complexo, deve lidar com diversas condições do ambiente e depende dos hospedeiros para suprir suas necessidades nutricionais. Uma delas é a necessidade de captar a molécula de heme (Fe-protoporfirina IX) que será utilizada como fator de crescimento. Os mecanismos envolvendo o metabolismo de heme são cruciais para a sobrevivência do T. cruzi pois o parasito não possui várias enzimas de biossíntese dessa porfirina e o heme livre pode apresentar citotoxicidade para célula. Na tentativa de perseguir o destino final
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Almeida, Fahyme Costa da Silva. "Fatores de Plasmodium falciparum envolvidos na fosforilação de eIF2α em resposta a melatonina." Universidade de São Paulo, 2016. http://www.teses.usp.br/teses/disponiveis/42/42135/tde-17082016-154439/.

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A malária é causada por parasitas Plasmodium falciparum, e embora vários aspectos ainda sejam desconhecidos, é sabido que a regulação do ciclo intraeritrocítico é crítica para a compreensão do ciclo celular e patogênese. A melatonina modula o ciclo de P. falciparum promovendo a sincronização, mas, o mecanismo de transdução de sinal é parcialmente caracterizado, envolvendo variações citosólicas de cálcio, AMPc e ativação da PKA. Modificações pós-traducionais participam na via de sinalização, e diversas proteínas quinase podem estar envolvidas na sinalização por melatonina. eIF2α fosforila
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Santos, Eduardo Alves dos. "Papel do IP3 na transdução de sinal e função da heme oxigenase em Plasmodium falciparum." Universidade de São Paulo, 2013. http://www.teses.usp.br/teses/disponiveis/42/42135/tde-20032014-174955/.

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Demonstramos que o P. falciparum dentro do eritrócito é capaz de usar a via de sinalização celular dependente do inositol trifosfato (IP3). Investigamos os estoques de Ca2+ intracelular sensíveis ao IP3 neste parasita e a sensibilidade ao IP3 em diferentes estágios no ciclo intraeritrocítico. Demonstramos que o hormônio melatonina é capaz de aumentar a concentração de IP3 neste parasita. Com o uso de uma coluna de afinidade ao IP3 tentamos encontrar proteínas candidatas ao receptor de IP3 em P. falciparum. Este trabalho também estuda a enzima heme oxigenade de P. falciparum (PfHO). Testamos a
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Gomes, Antoniella Souza. "Efeito protetor da via hemeoxigenase 1/ biliverdina/ CO em modelos de lesões gástricas em camundongos : papel da guanilato ciclase solúvel (GCS) e DA no sintase (NOS)." reponame:Repositório Institucional da UFC, 2009. http://www.repositorio.ufc.br/handle/riufc/2680.

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GOMES, Antoniella Souza. Efeito protetor da via hemeoxigenase 1/Biliverdina/CO em modelos de lesões gástricas em camundongos : papel da guanilato ciclase solúvel (GCS) e da sintase (NOS). 2009. 200 f. Tese (Doutorado em Farmacologia) - Universidade Federal do Ceará. Faculdade de Medicina, Fortaleza, 2009.<br>Submitted by denise santos (denise.santos@ufc.br) on 2012-05-24T14:19:46Z No. of bitstreams: 1 2009_tese_asgomes.pdf: 2256560 bytes, checksum: 9d8cc277feea50867d84d91dacad0870 (MD5)<br>Approved for entry into archive by Eliene Nascimento(elienegvn@hotmail.com) on 2012-05-30T14:16:19Z (GMT)
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Russell, Malcolm Peter. "Resonance raman spectroscopic studies of bilirubin and biliverdin." Thesis, University of York, 1993. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.358273.

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Coulthurst, Sandra Jane. "A spectroscopic study of bilirubin and biliverdin and their complexes with proteins." Thesis, University of York, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.323607.

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Rodrigues, Pedro Mendes de Azambuja. "Heme oxigenase-1 como um alvo terapêutico na sepse o papel da biliverdina." reponame:Repositório Institucional da FIOCRUZ, 2007. https://www.arca.fiocruz.br/handle/icict/12864.

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Made available in DSpace on 2016-02-26T13:34:40Z (GMT). No. of bitstreams: 2 pedro_rodrigues_ioc_dout_2007.pdf: 495339 bytes, checksum: 0791930416bc740981dac64b0ead8959 (MD5) license.txt: 1748 bytes, checksum: 8a4605be74aa9ea9d79846c1fba20a33 (MD5) Previous issue date: 2016-01-13<br>Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Rio de Janeiro, RJ, Brasil<br>A heme oxigenase-1 (HO-1), uma enzima induzida sob diversas condições de estresse celular, cataboliza o heme em monóxido de carbono (CO), biliverdina (convertida posteriormente a bilirrubina) e ferro livre. A deficiência dessa enzima
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Kawasaki, Yukie. "Scalable Bio-Production of High Value Products in Bacteria." DigitalCommons@USU, 2015. https://digitalcommons.usu.edu/etd/4609.

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Biliverdin IXα is a green bile pigment produced by enzymatic cleavage of a tetrapyrrole ring of heme by heme oxygenase. While biliverdin IXα is emerging as an effective cytoprotectant, the conventional method for producing biliverdin IXα by chemical conversion of animal bile is not suitable for large scale production. A novel scalable production method was pursued via bacterial fermentation. Recombinant Escherichia coli strains were obtained by sequence optimization and plasmid transformation of a cyanobacterial heme oxygenase gene. Further strain development was done by plasmid overexpression
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Clark, William D. "The isolation, identification and exploration of the biophysiological significance of plasma biliverdin in the ballan wrasse (Labrus bergylta)." Thesis, University of Stirling, 2016. http://hdl.handle.net/1893/25380.

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Labrus bergylta (ballan wrasse) have recently emerged as a key resource to aquaculture through proven efficacy in controlling infestations of sea lice (Leclercq et al., 2014a). However, due to complex ecology, and a complete lack of sexual dimorphism gender identification endures as a key restriction to optimising broodstock management therefore male selection and establishing optimal sex ratios is difficult (Talbot et al., 2012). L. bergylta, are noted to demonstrate unusually coloured plasma ranging in hue from green to blue with the haem catabolite biliverdin established as the causal pigme
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Aga, Rubina Gul. "Studies of the Chemistry of S-Nitrosothiols and the Interactions of Biliverdin and Bilirubin with Selected Reactive Nitrogen Compounds." Thesis, King's College London (University of London), 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.487754.

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S-nitrosothiols undergo homolytic decomposition in aqueous solution to release NO and are also able to transfer the NO+ group to other thiolates to generate Snitrosothiols, which may undergo more facile homolysis. These reactions are probably of some significance in intracellular processes, while the use of S-nitrosothiols as sources of NO is well known, although the possibility of transnitrosation has not always been considered. However, it is possible that some of the biochemistry of Snitrosothiols takes place in cell walls and that their lipophilicity is an important factor in controlling r
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Book chapters on the topic "BILIVERDINE"

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Gressner, A. M., and O. A. Gressner. "Biliverdin." In Springer Reference Medizin. Springer Berlin Heidelberg, 2019. http://dx.doi.org/10.1007/978-3-662-48986-4_561.

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Gressner, A. M., and O. A. Gressner. "Biliverdin." In Lexikon der Medizinischen Laboratoriumsdiagnostik. Springer Berlin Heidelberg, 2017. http://dx.doi.org/10.1007/978-3-662-49054-9_561-1.

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Schomburg, Dietmar, Margit Salzmann, and Dörte Stephan. "Biliverdin reductase." In Enzyme Handbook. Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-58051-2_97.

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Kamp, Marc Willem. "Biliverdin IX-Beta Reductase: Computational Studies." In Encyclopedia of Biophysics. Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-16712-6_252.

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Overhaus, M., B. A. Moore, B. A. Flynn, and A. J. Bauer. "Biliverdin schützt die intestinale Integrität in der Sepsis." In Deutsche Gesellschaft für Chirurgie. Springer Berlin Heidelberg, 2004. http://dx.doi.org/10.1007/978-3-642-18547-2_86.

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Berberat, P. O., Y. I. A-Rahim, K. Yamashita, et al. "Heme Oxygenase-1 (HO-1) generiertes Biliverdin schützt vor Kolitis." In Deutsche Gesellschaft für Chirurgie. Springer Berlin Heidelberg, 2003. http://dx.doi.org/10.1007/978-3-642-19024-7_53.

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Berberat, P. O., K. Yamashita, Y. I. A-Rahim, et al. "Heme Oxygenase-1 (HO-1) generiertes Biliverdin schützt vor Kolitis." In Zurück in die Zukunft. Springer Berlin Heidelberg, 2003. http://dx.doi.org/10.1007/978-3-642-55611-1_429.

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Tamulis, A., J. Tamuliene, V. Tamulis, and A. Graja. "Quantum Mechanical Design of Elements of Molecular Quantum Computers Based on Biliverdin and Aza-Fullerene Compounds." In Low-Dimensional Systems: Theory, Preparation, and Some Applications. Springer Netherlands, 2003. http://dx.doi.org/10.1007/978-94-010-0143-4_21.

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"Biliverdin Reductase." In Encyclopedia of Biophysics. Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-16712-6_100098.

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Thompson, Richard. "Jaundice." In Oxford Textbook of Medicine. Oxford University Press, 2010. http://dx.doi.org/10.1093/med/9780199204854.003.1520_update_002.

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All haem molecules are degraded in macrophages by haem oxygenase to biliverdin, and thence by biliverdin reductase to bilirubin, which is selectively removed by hepatocytes from sinusoidal blood and then conjugated, mainly by one of the two specific isoforms of the microsomal enzyme UDP-glucuronyl (glucuronate-glucuronosyl) transferase, chiefly with two glucuronic acid moieties. Conjugated bilirubin is excreted into the bile by the anionic conjugate transporter protein (MRP2), but in many liver diseases it refluxes back into blood and—since it is water soluble and less firmly bound to albumin than unconjugated bilirubin—about 1% is filtered across the glomerular membrane and darkens the urine (choluria). In the distal intestine conjugated bilirubin is deconjugated and reduced to a series of uro- and stercobilinogens that give the normal colour to faeces. Some colourless urobilinogen is normally absorbed from the colon and undergoes an enterohepatic circulation, with a small amount being excreted in urine. If this biliary excretion is impaired in liver disease, or increased in haemolysis, then excess urobilinogen is excreted in urine, where it is easily detected by routine clinical ‘stix’....
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Conference papers on the topic "BILIVERDINE"

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Huang, Chin-Jie, Cheng-Ham Wu, and Tzu-Ming Liu. "Multiphoton fluorescence spectra and lifetimes of biliverdins and their protein-associated complex." In SPIE BiOS, edited by Samuel Achilefu and Ramesh Raghavachari. SPIE, 2012. http://dx.doi.org/10.1117/12.907725.

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Zagorec-Marks, Wyatt, J. Weber, and Leah Dodson. "SOLVATOCHROMIC BEHAVIOR OF THE ANIONIC BIOCHROMOPHORE BILIVERDIN INVESTIGATED USING A CRYOGENIC ION TRAP." In 74th International Symposium on Molecular Spectroscopy. University of Illinois at Urbana-Champaign, 2019. http://dx.doi.org/10.15278/isms.2019.wf10.

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Zheng, Jun, Danish A. Nagda, Shayanne A. Lajud, et al. "Abstract 2263: Biliverdin inhibits head and neck cancer cell growth via activation of retinoblastoma signaling pathway." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-2263.

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