Relevant bibliographies by topics / Arginase

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Arginase'

Author: Grafiati
Published: 4 June 2021
Last updated: 25 July 2025

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Journal articles on the topic "Arginase"

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Ren, Yuanyuan, Zhuozhuo Li, Wenqing Li, et al. "Arginase: Biological and Therapeutic Implications in Diabetes Mellitus and Its Complications." Oxidative Medicine and Cellular Longevity 2022 (October 26, 2022): 1–20. http://dx.doi.org/10.1155/2022/2419412.

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Arginase is a ubiquitous enzyme in the urea cycle (UC) that hydrolyzes L-arginine to urea and L-ornithine. Two mammalian arginase isoforms, arginase1 (ARG1) and arginase2 (ARG2), play a vital role in the regulation of β-cell functions, insulin resistance (IR), and vascular complications via modulating L-arginine metabolism, nitric oxide (NO) production, and inflammatory responses as well as oxidative stress. Basic and clinical studies reveal that abnormal alterations of arginase expression and activity are strongly associated with the onset and development of diabetes mellitus (DM) and its com
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Chen, Hui, Bonnie C. McCaig, Maeli Melotto, Sheng Yang He, and Gregg A. Howe. "Regulation of Plant Arginase by Wounding, Jasmonate, and the Phytotoxin Coronatine." Journal of Biological Chemistry 279, no. 44 (2004): 45998–6007. http://dx.doi.org/10.1074/jbc.m407151200.

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In mammalian cells, induced expression of arginase in response to wound trauma and pathogen infection plays an important role in regulating the metabolism ofl-arginine to either polyamines or nitric oxide (NO). In higher plants, which also utilize arginine for the production of polyamines and NO, the potential role of arginase as a control point for arginine homeostasis has not been investigated. Here, we report the characterization of two genes (LeARG1andLeARG2) fromLycopersicon esculentum(tomato) that encode arginase. Phylogenic analysis showed that LeARG1 and -2, like all other plant argina
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Elms, Shawn, Feng Chen, Yusi Wang, et al. "Insights into the arginine paradox: evidence against the importance of subcellular location of arginase and eNOS." American Journal of Physiology-Heart and Circulatory Physiology 305, no. 5 (2013): H651—H666. http://dx.doi.org/10.1152/ajpheart.00755.2012.

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Reduced production of nitric oxide (NO) is one of the first indications of endothelial dysfunction and precedes overt cardiovascular disease. Increased expression of Arginase has been proposed as a mechanism to account for diminished NO production. Arginases consume l-arginine, the substrate for endothelial nitric oxide synthase (eNOS), and l-arginine depletion is thought to competitively reduce eNOS-derived NO. However, this simple relationship is complicated by the paradox that l-arginine concentrations in endothelial cells remain sufficiently high to support NO synthesis. One mechanism prop
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Kitowska, Kamila, Dariusz Zakrzewicz, Melanie Königshoff, et al. "Functional role and species-specific contribution of arginases in pulmonary fibrosis." American Journal of Physiology-Lung Cellular and Molecular Physiology 294, no. 1 (2008): L34—L45. http://dx.doi.org/10.1152/ajplung.00007.2007.

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Lung fibrosis is characterized by increased deposition of ECM, especially collagens, and enhanced proliferation of fibroblasts. l-arginine is a key precursor of nitric oxide, asymmetric dimethylarginine, and proline, an amino acid enriched in collagen. We hypothesized that l-arginine metabolism is altered in pulmonary fibrosis, ultimately affecting collagen synthesis. Expression analysis of key enzymes in the arginine pathway, protein arginine methyltransferases (Prmt), arginine transporters, and arginases by quantitative (q) RT-PCR and Western blot revealed significant upregulation of arginas
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Marzęta-Assas, Patrycja, Damian Jacenik, and Zbigniew Zasłona. "Pathophysiology of Arginases in Cancer and Efforts in Their Pharmacological Inhibition." International Journal of Molecular Sciences 25, no. 18 (2024): 9782. http://dx.doi.org/10.3390/ijms25189782.

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Arginases are key enzymes that hydrolyze L-arginine to urea and L-ornithine in the urea cycle. The two arginase isoforms, arginase 1 (ARG1) and arginase 2 (ARG2), regulate the proliferation of cancer cells, migration, and apoptosis; affect immunosuppression; and promote the synthesis of polyamines, leading to the development of cancer. Arginases also compete with nitric oxide synthase (NOS) for L-arginine, and their participation has also been confirmed in cardiovascular diseases, stroke, and inflammation. Due to the fact that arginases play a crucial role in the development of various types o
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Dzikowska, A., J. P. Le Caer, P. Jonczyk, and P. Wëgleński. "Purification of arginase from Aspergillus nidulans." Acta Biochimica Polonica 41, no. 4 (1994): 467–71. http://dx.doi.org/10.18388/abp.1994_4700.

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Arginase (EC 3.5.3.1) of Aspergillus nidulans, the enzyme which enables the fungus to use arginine as the sole nitrogen source was purified to homogeneity. Molecular mass of the purified arginase subunit is 40 kDa and is similar to that reported for the Neurospora crassa (38.3 kDa) and Saccharomyces cerevisiae (39 kDa) enzymes. The native molecular mass of arginase is 125 kDa. The subunit/native molecular mass ratio suggests a trimeric form of the protein. The arginase protein was cleaved and partially sequenced. Two out of the six polypeptides sequenced show a high degree of homology to conse
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Belik, Jaques, Darakhshanda Shehnaz, Jingyi Pan, and Hartmut Grasemann. "Developmental changes in arginase expression and activity in the lung." American Journal of Physiology-Lung Cellular and Molecular Physiology 294, no. 3 (2008): L498—L504. http://dx.doi.org/10.1152/ajplung.00242.2007.

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Arginases compete with nitric oxide (NO) synthases for l-arginine as common substrate. Pulmonary vascular and airway diseases in which arginase activity is increased are associated with decreased NO production and reduced smooth muscle relaxation. The developmental patterns of arginase activity and type I and II isoforms expression in the lung have not been previously evaluated. Hypothesizing that lung arginase activity is developmentally regulated and highest in the fetus, we measured the expression of both arginase isoforms and total arginase activity in fetal, newborn, and adult rat lung, p
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Gao, Kai, Sergey Lunev, Mariska P. M. van den Berg, et al. "A synthetic peptide as an allosteric inhibitor of human arginase I and II." Molecular Biology Reports 48, no. 2 (2021): 1959–66. http://dx.doi.org/10.1007/s11033-021-06176-5.

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AbstractArginine metabolism mediated by arginases plays a critical role in cell and tissue function. The arginine hydrolysis is deeply involved in the urea cycle, which helps the kidney excrete ammonia from blood. Upregulation of arginases affects microenvironment stability due to the presence of excess urea in blood. To regulate the arginase activities properly, a synthetic peptide based on the structure of human arginase I was designed and assessed. Preliminary data shows it inhibits human arginase I and II with an IC50 of 2.4 ± 0.3 and 1.8 ± 0.1 mmol, respectively. Our kinetic analysis indi
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Ide, Alejandra Arteaga, Victor M. Hernández, Liliana Medina-Aparicio, et al. "Genetic regulation, biochemical properties and physiological importance of arginase from Sinorhizobium meliloti." Microbiology 166, no. 5 (2020): 484–97. http://dx.doi.org/10.1099/mic.0.000909.

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In bacteria, l-arginine is a precursor of various metabolites and can serve as a source of carbon and/or nitrogen. Arginine catabolism by arginase, which hydrolyzes arginine to l-ornithine and urea, is common in nature but has not been studied in symbiotic nitrogen-fixing rhizobia. The genome of the alfalfa microsymbiont Sinorhizobium meliloti 1021 has two genes annotated as arginases, argI1 (smc03091) and argI2 (sma1711). Biochemical assays with purified ArgI1 and ArgI2 (as 6His-Sumo-tagged proteins) showed that only ArgI1 had detectable arginase activity. A 1021 argI1 null mutant lacked argi
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Orellana, María-Soledad, Gonzalo A. Jaña, Maximiliano Figueroa, et al. "New Insights into the Determinants of Specificity in Human Type I Arginase: Generation of a Mutant That Is Only Active with Agmatine as Substrate." International Journal of Molecular Sciences 23, no. 12 (2022): 6438. http://dx.doi.org/10.3390/ijms23126438.

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Arginase catalyzes the hydrolysis of L-arginine into L-ornithine and urea. This enzyme has several analogies with agmatinase, which catalyzes the hydrolysis of agmatine into putrescine and urea. However, this contrasts with the highlighted specificity that each one presents for their respective substrate. A comparison of available crystal structures for arginases reveals an important difference in the extension of two loops located in the entrance of the active site. The first, denominated loop A (I129-L140) contains the residues that interact with the alpha carboxyl group or arginine of argin
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Dissertations / Theses on the topic "Arginase"

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Cloke, Thomas Edward. "Immunoregulation by arginase mediated L-arginine metabolism in HIV seropositive patients." Thesis, Imperial College London, 2011. http://hdl.handle.net/10044/1/7105.

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Infection with HIV results in a chronic infection that progressively impairs the immune system. Although depletion of CD4+ T cells is frequently used to explain the deterioration in immune function, the combination of the chronicity of infection and progressive loss of CD4+ T cells are not sufficient to fully account for the immune dysregulation that occurs during the progression to AIDS. Arginase-induced L-arginine deprivation is emerging as a key mechanism for the downregulation of immune responses. In this thesis it is shown that PBMC arginase activity increases with disease severity in HIV
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King, Janice Elizabeth. "The role of arginine and arginase in Pinus taeda L. early seedling growth." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1998. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp02/NQ34789.pdf.

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Pethe, Stéphanie. "L'arginase : mise au point d'inhibiteurs et études des couples arginase-inhibiteurs par spectroscopies RX et RPE." Paris 5, 2003. http://www.theses.fr/2003PA05P609.

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Les arginases catalysent la réaction d'hydrolyse de l'arginine en ornithine et urée. Outre leur rôle au niveau du cycle de l'urée, les arginases jouent un rôle de régulation dans la production de nombreux intermédiaires biologiques clés (polyamines, NO ). Il a été montré que les NO synthases métabolisent l'arginine en citrulline et NO, médiateur fondamental de l'organisme. Les deux enzymes peuvent donc être en compétition pour l'appropriation de leur substrat. Nous avons montré que les sels de fluorure ont un effet inhibiteur sur l'activité et avons découvert un nouveau substrat : le NIO. Nous
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Silva, Maria Fernanda Laranjeira da. "Relação entre a localização celular da enzima arginase de Leishmania (Leishmania) amazonensis e seu papel na infecção de macrófagos murinos." Universidade de São Paulo, 2010. http://www.teses.usp.br/teses/disponiveis/41/41135/tde-21072010-135930/.

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Nos hospedeiros mamíferos, os parasitas do gênero Leishmania vivem nos macrófagos se evadindo de mecanismos microbicidas dessas células, tais como a produção de óxido nítrico (NO). A produção de NO pela enzima óxido nítrico sintase induzida (iNOS) nos macrófagos requer L-arginina como substrato, o mesmo aminoácido utilizado pela arginase para produzir ornitina e uréia. Logo, a arginase pode atuar na sobrevivência de Leishmania no hospedeiro competindo com a iNOS, reduzindo a produção de NO, além de seu papel na via de poliaminas, essencial para a replicação dessas células. Com isso, o objetivo
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Ocampos, Maristela. "A study of arginase in fission yeast." Thesis, University of Cambridge, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.388437.

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Dumont, Julie. "Recherche de facteurs de prédisposition génétique aux maladies cardio-vasculaires : études d'association de polymorphismes affectant les gènes du métabolisme de la L-arginine et de la L-ornithine." Lille 2, 2006. http://www.theses.fr/2006LIL2S063.

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L'épidémiologie génétique a permis des avancées significatives dans la compréhension des mécanismes physiopathologiques impliqués dans la survenue des maladies cardio-vasculaires. De nombreux travaux ont notamment souligné la place déterminante du gène codant la NO synthase endothéliale (NOS3) dans la physiologie artérielle et l'impact de mutations du gène NOS3 sur le risque cardio-vasculaire. La NO synthase endothéliale synthétise le monoxyde d'azote à partir de la L-arginine. Or, cet acide aminé est également le précurseur métabolique de composés comme l'urée, la L-ornithine, la L-proline ou
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Pereira, Alexandre Lustosa. "Terapia periodontal não-cirúrgica: avaliação de eficiência por parâmetros clínicos microbianos e salivares." Universidade de Taubaté, 2009. http://www.bdtd.unitau.br/tedesimplificado/tde_busca/arquivo.php?codArquivo=439.

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Hipótese do estudo: O presente estudo parte do pressuposto de que a terapia periodontal não cirúrgica é eficaz no tratamento da doença periodontal. Objetivos: este estudo de intervenção avaliou a eficácia dos procedimentos de raspagem e aplainamento radicular utilizando como ferramenta de validação parâmetros clínicos, microbianos e salivares em indivíduos diagnosticados com gengivite e periodontite comparando-os a controles saudáveis. Método: Foram alocados no presente estudo 89 indivíduos assim caracterizados: 31 periodontalmente saudáveis (K), 27 com gengivite (G) e 31 com periodontite crôn
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Schick, Martin Alexander. "Expression der Arginase Isoformen in Fibroblasten während der Wundheilung." [S.l. : s.n.], 2007.

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BRANLY, NATHALIE. "Le deficit en arginase ou hyperargininemie : revue de la litterature a propos d'un nouveau cas." Nice, 1991. http://www.theses.fr/1991NICE6519.

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Moreira, Gabriel Sassarão Alves. "Identificação e expressão gênica das enzimas arginase 1, arginase 2, e citocinas pró-inflamatórias em Pseudoplatystoma corruscans e Pseudoplatystoma reticulatum, imunizados com Ichthyophthirius multifiliis." Universidade de São Paulo, 2017. http://www.teses.usp.br/teses/disponiveis/74/74131/tde-23112017-145109/.

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O protozoário ciliado Ichthyophthirius multifiliis causador da doença dos pontos brancos em muitas espécies de peixes de água doce destaca-se como um importante patógeno por ser responsável por grandes perdas para a indústria de pescados mundial. Duas espécies de peixes de grande importância para a economia no Brasil foram selecionadas para este estudo, o pintado (Pseudoplatystoma corruscans (Spix & Agassiz, 1829) e a cachara (Pseudoplatystoma reticulatum (Eigenmann & Eigenmann, 1889). Com o objetivo de avaliar a resposta imune destes peixes frente ao parasita, inicialmente, o protozoário I. m
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Books on the topic "Arginase"

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Callery, Elizabeth Mary. Developmental regulation of the urea-cycle enzyme, arginase, in the direct-developing frog, eleutherodactylus coqui. National Library of Canada, 1994.

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Jacobs, Nathan L., and Nathan L. Jacobs. Arginine amino acid. Nova Science Publishers, 2011.

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Jacobs, Nathan L. Arginine amino acid. Nova Science Publishers, 2011.

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Patel, Vinood B., Victor R. Preedy, and Rajkumar Rajendram, eds. L-Arginine in Clinical Nutrition. Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-26009-9.

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Floderus, Eugenie. Aminopeptidases and arginine catabolism in oral streptococci. Karolinska Institute, Dept. of Oral Microbiology], 1990.

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Floderus, Eugenie. Aminopeptidases and arginine catabolism in oral straptococci. Kongl. Carolinska Medico Chirurgiska Institutet, 1990.

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Robinson, Tristan Mark. Aspects of creatine and arginine supplementation on metabolism in humans. typescript, 1999.

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Warne, Justin Mark. Arginine vasotocin's role in the adaptive osmoregulatory physiology of euryhaline fish. University of Manchester, 1994.

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C, Merrell Woodson, and Thornton James 1952-, eds. The arginine solution: The first guide to America's new cardio-enhancing supplement. Warner Books, 1999.

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Lühnenschloss, Anne. Immunzytochemische Studien zur Ontogenese von MSEL- und VLDV-Neurophysin, Arginin-Vasotocin, Mesotocin und ACTH im Gehirn des Haushuhnes (Gallus gallus domesticus). A. Lühnenschloss, 1988.

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Book chapters on the topic "Arginase"

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Schomburg, Dietmar, and Margit Salzmann. "Arginase." In Enzyme Handbook 4. Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-84437-9_180.

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Schomburg, Dietmar, and Margit Salzmann. "D-Arginase." In Enzyme Handbook 4. Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-84437-9_189.

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Indika, Neluwa-Liyanage R., Udara D. Senarathne, and Andreas Schulze. "Arginase Deficiency." In Genetic Syndromes. Springer International Publishing, 2023. http://dx.doi.org/10.1007/978-3-319-66816-1_1328-1.

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da Silva, Maria Fernanda Laranjeira, and Lucile Maria Floeter-Winter. "Arginase in Leishmania." In Subcellular Biochemistry. Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-7305-9_4.

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Russo, Nino, Monica Leopoldini, and Marirosa Toscano. "Manganese-Containing Arginase - Computational Studies." In Encyclopedia of Biophysics. Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-16712-6_598.

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Lu, Min, Rachel L. Palte, Scott N. Mlynarski, and Jason D. Shields. "ARGINASE INHIBITORS FOR IMMUNO-ONCOLOGY." In 2022 Medicinal Chemistry Reviews. MEDI, Inc. Published by American Chemical Society., 2022. http://dx.doi.org/10.1021/mc-2022-vol57.ch10.

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Wheatley, Denys N., Ruth Philip, and Elaine Campbell. "Arginine deprivation and tumour cell death: Arginase and its inhibition." In Guanidino Compounds in Biology and Medicine. Springer US, 2003. http://dx.doi.org/10.1007/978-1-4615-0247-0_26.

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Scharnagl, Hubert, Winfried März, Markus Böhm, et al. "Argininosuccinic Acid Lyase and Arginase Deficiency." In Encyclopedia of Molecular Mechanisms of Disease. Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-29676-8_8814.

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Dave, Kashyap, Manmeet Ahuja, T. N. Jayashri, Rekha Bisht Sirola, Khyati Dave, and Narayan S. Punekar. "Arginase (agaA) as a Fungal Transformation Marker." In Fungal Biology. Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-10503-1_12.

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Ogino, Keiki, and Kei Takemoto. "Serum l-Arginase in Healthy Subjects and Nitric Oxide." In L-Arginine in Clinical Nutrition. Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-26009-9_14.

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Conference papers on the topic "Arginase"

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Xu, W., K. Asosingh, A. J. Janocha, et al. "Arginine Metabolism Changes Hypoxia Responses in Mice Deficient for Arginase-2 (ARG2)." In American Thoracic Society 2023 International Conference, May 19-24, 2023 - Washington, DC. American Thoracic Society, 2023. http://dx.doi.org/10.1164/ajrccm-conference.2023.207.1_meetingabstracts.a6119.

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ahmad, Tanveer. "L-ARGININE IN ARGINASE-NOS PARADOX AND NITROSATIVE STREES IN MURINE MODEL OF ASTHMA." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a5590.

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Asosingh, K., K. Weiss, M. Frimel, et al. "Regulation of Airway Inflammation by Arginine Metabolic Pathways for Nitric Oxide Synthesis and Mitochondrial Arginase." In American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a2960.

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Thompson, M., S. Hamrick, K. Lee, et al. "Targeting BDNF/arginase Pathways in Airway Remodeling." In American Thoracic Society 2024 International Conference, May 17-22, 2024 - San Diego, CA. American Thoracic Society, 2024. http://dx.doi.org/10.1164/ajrccm-conference.2024.209.1_meetingabstracts.a7178.

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Brunner, Julia S., Melanie Hofmann, Victoria Saferding, et al. "02.28 The role of arginase I in osteoclasts." In 37th European Workshop for Rheumatology Research 2–4 March 2017 Athens, Greece. BMJ Publishing Group Ltd and European League Against Rheumatism, 2017. http://dx.doi.org/10.1136/annrheumdis-2016-211050.28.

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Brunner, JS, M. Hofmann, V. Saferding, et al. "P113 Arginase I and the metabolic control of osteoclastogenesis." In 38th European Workshop for Rheumatology Research, 22–24 February 2018, Geneva, Switzerland. BMJ Publishing Group Ltd and European League Against Rheumatism, 2018. http://dx.doi.org/10.1136/annrheumdis-2018-ewrr2018.128.

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Petersen, Bodil, Cornelius J. Busch, Kenneth D. Bloch, and Warren M. Zapol. "Arginase Inhibition Restores Hypoxic Pulmonary Vasoconstriction In Endotoxemic Mice." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a4830.

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Choy, Chi Tung, Hio Teng Cheong, Kin Pong U, Chi Hang Wong, and Herbert Ho Fung Loong. "Abstract 5512: Preclinical evaluation of the recombinant human arginase PEG-BCT-100 leading to arginine deprivation in sarcomas." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-5512.

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Carretta, Marco, Marion Chapellier, Ines Lecoq, et al. "1335 Arginase-1 vaccine promotes T cell immunity against arginase-1+cells, controls tumor growth via immune modulation of tumor microenvironment." In SITC 38th Annual Meeting (SITC 2023) Abstracts. BMJ Publishing Group Ltd, 2023. http://dx.doi.org/10.1136/jitc-2023-sitc2023.1335.

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Zeki, AA, JM Bratt, and NJ Kenyon. "Simvastatin Inhibits Pulmonary Arginase-1 Protein Expression in Allergic Asthma." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a5452.

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Reports on the topic "Arginase"

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Grody, Wayne W. Arginase: A Novel Proliferative Determinant in Prostate Cancer. Defense Technical Information Center, 2005. http://dx.doi.org/10.21236/ada443025.

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Grody, Wayne W. Arginase: A Novel Proliferative Determinant in Prostate Cancer. Defense Technical Information Center, 2006. http://dx.doi.org/10.21236/ada455780.

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Grody, Wayne W. Arginase: A Novel Proliferative Determinant in Prostate Cancer. Defense Technical Information Center, 2004. http://dx.doi.org/10.21236/ada427919.

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O'Malley, Karen. Characteristics of Arginase from the Terebellid Polychaete Pista Pacifica Berkeley. Portland State University Library, 2000. http://dx.doi.org/10.15760/etd.1659.

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Spek, J. W. Standardized ileal digestible arginine requirement for broilers. Wageningen Livestock Research, 2018. http://dx.doi.org/10.18174/455518.

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Soler, Germán. Arginasa, un enzima clave en el destino de la respuesta inmune. Sociedad Española de Bioquímica y Biología Molecular (SEBBM), 2015. http://dx.doi.org/10.18567/sebbmdiv_rpc.2015.01.1.

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Pohlschroder Mechthild. Haloarchaeal Protein Translocation via the Twin Arginine Translocation Pathway. Office of Scientific and Technical Information (OSTI), 2009. http://dx.doi.org/10.2172/946802.

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Theg, Steven. Mechanism of Protein Transport on the Twin Arginine Translocation Pathway. Office of Scientific and Technical Information (OSTI), 2018. http://dx.doi.org/10.2172/1633086.

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Yibchok-anun, Sirintorn, and Wara Panichkriangkrai. The role of arginine vasopressin in diabetes-associated glucagons secretion. Chulalongkorn University, 2002. https://doi.org/10.58837/chula.res.2002.63.

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Abstract:
The purpose of this study was to investigate the role of arginine-vasopressin (AVP) on glucagons secretion in both normal and diabetic rats. Diabetes was induced by intraperitoneal administration of alloxan HCI(200 mg/kg). Both glucagon and AVP were determined in the effluent of the perfused pancreas using radioimmunoassay. Diabetic rats had higher baseline glucagons concentrations than normal rats. AVP (1 pmol/L) failed to change glucagons secretion in normal rats, but significantly increased glucagons secretion in diabetic rats. AVP (10-100 pmol/L) increased glucagons secretion from both nor
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Kim, Randle. The Role of Autophagy with Arginine Deiminase as a Novel Prostate Cancer Therapy. Defense Technical Information Center, 2009. http://dx.doi.org/10.21236/ada510982.

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