Journal articles: 'Proteins – Metabolism'

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Rostom, Hussam, and Brian Shine. "Basic metabolism: proteins." Surgery (Oxford) 36, no. 4 (April 2018): 153–58. http://dx.doi.org/10.1016/j.mpsur.2018.01.009.

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Shine, Brian, and Hussam Rostom. "Basic metabolism: proteins." Surgery (Oxford) 39, no. 1 (January 2021): 1–6. http://dx.doi.org/10.1016/j.mpsur.2020.11.003.

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Bidlack, Wayne R. "Proteins of Iron Metabolism." Journal of the American College of Nutrition 21, no. 3 (June 2002): 290–91. http://dx.doi.org/10.1080/07315724.2002.10719225.

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Pietrangelo, Antonello. "Proteins of iron metabolism." Gastroenterology 125, no. 6 (December 2003): 1906. http://dx.doi.org/10.1053/j.gastro.2003.08.039.

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Hamuro, Lora L., and Narendra S. Kishnani. "Metabolism of biologics: biotherapeutic proteins." Bioanalysis 4, no. 2 (January 2012): 189–95. http://dx.doi.org/10.4155/bio.11.304.

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Csaki, Lauren S., and Karen Reue. "Lipins: Multifunctional Lipid Metabolism Proteins." Annual Review of Nutrition 30, no. 1 (July 2010): 257–72. http://dx.doi.org/10.1146/annurev.nutr.012809.104729.

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Shahverdiyeva, I. J., A. H. Orujov, and U. H. Azizova. "IRON METABOLISM PROTEINS DURING PREGNANCY." Biological Markers in Fundamental and Clinical Medicine (collection of abstracts) 3, no. 1 (November 7, 2019): 90–91. http://dx.doi.org/10.29256/v.03.01.2019.escbm61.

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Christians, Uwe. "Transport Proteins and Intestinal Metabolism." Therapeutic Drug Monitoring 26, no. 2 (April 2004): 104–6. http://dx.doi.org/10.1097/00007691-200404000-00002.

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Xu, Li, Linkang Zhou, and Peng Li. "CIDE Proteins and Lipid Metabolism." Arteriosclerosis, Thrombosis, and Vascular Biology 32, no. 5 (May 2012): 1094–98. http://dx.doi.org/10.1161/atvbaha.111.241489.

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Kuhnert, Franziska, Urte Schlüter, Nicole Linka, and Marion Eisenhut. "Transport Proteins Enabling Plant Photorespiratory Metabolism." Plants 10, no. 5 (April 27, 2021): 880. http://dx.doi.org/10.3390/plants10050880.

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Photorespiration (PR) is a metabolic repair pathway that acts in oxygenic photosynthetic organisms to degrade a toxic product of oxygen fixation generated by the enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase. Within the metabolic pathway, energy is consumed and carbon dioxide released. Consequently, PR is seen as a wasteful process making it a promising target for engineering to enhance plant productivity. Transport and channel proteins connect the organelles accomplishing the PR pathway—chloroplast, peroxisome, and mitochondrion—and thus enable efficient flux of PR metabolites. Although the pathway and the enzymes catalyzing the biochemical reactions have been the focus of research for the last several decades, the knowledge about transport proteins involved in PR is still limited. This review presents a timely state of knowledge with regard to metabolite channeling in PR and the participating proteins. The significance of transporters for implementation of synthetic bypasses to PR is highlighted. As an excursion, the physiological contribution of transport proteins that are involved in C4 metabolism is discussed.

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Farid, Nagy A., Michael Masnyk, and Victor J. Wroblewski. "Pharmacokinetics and Metabolism of Therapeutic Proteins." Drug Metabolism and Pharmacokinetics 8, supplement (1993): 767–68. http://dx.doi.org/10.2133/dmpk.8.supplement_767.

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Skarżyńska, Ewa, Artur Jakimiuk, Tadeusz Issat, and Barbara Lisowska-Myjak. "Meconium Proteins Involved in Iron Metabolism." International Journal of Molecular Sciences 25, no. 13 (June 25, 2024): 6948. http://dx.doi.org/10.3390/ijms25136948.

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The lack of specific biological materials and biomarkers limits our knowledge of the mechanisms underlying intrauterine regulation of iron supply to the fetus. Determining the meconium content of proteins commonly used in the laboratory to assess the transport, storage, and distribution of iron in the body may elucidate their roles in fetal development. Ferritin, transferrin, haptoglobin, ceruloplasmin, lactoferrin, myeloperoxidase (MPO), neutrophil gelatinase-associated lipocalin (NGAL), and calprotectin were determined by ELISA in meconium samples obtained from 122 neonates. There were strong correlations between the meconium concentrations of haptoglobin, transferrin, and NGAL (p < 0.05). Meconium concentrations of ferritin were several-fold higher than the concentrations of the other proteins, with the exception of calprotectin whose concentration was approximately three-fold higher than that of ferritin. Meconium ceruloplasmin concentration significantly correlated with the concentrations of MPO, NGAL, lactoferrin, and calprotectin. Correlations between the meconium concentrations of haptoglobin, transferrin, and NGAL may reflect their collaborative involvement in the storage and transport of iron in the intrauterine environment in line with their recognized biological properties. High meconium concentrations of ferritin may provide information about the demand for iron and its utilization by the fetus. The associations between ceruloplasmin and neutrophil proteins may indicate the involvement of ceruloplasmin in the regulation of neutrophil activity in the intrauterine environment.

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Samaha, Doaa, Housam H. Hamdo, Max Wilde, Kevin Prause, and Christoph Arenz. "Sphingolipid-Transporting Proteins as Cancer Therapeutic Targets." International Journal of Molecular Sciences 20, no. 14 (July 20, 2019): 3554. http://dx.doi.org/10.3390/ijms20143554.

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The understanding of the role of sphingolipid metabolism in cancer has tremendously increased in the past ten years. Many tumors are characterized by imbalances in sphingolipid metabolism. In many cases, disorders of sphingolipid metabolism are also likely to cause or at least promote cancer. In this review, sphingolipid transport proteins and the processes catalyzed by them are regarded as essential components of sphingolipid metabolism. There is much to suggest that these processes are often rate-limiting steps for metabolism of individual sphingolipid species and thus represent potential target structures for pharmaceutical anticancer research. Here, we summarize empirical and biochemical data on different proteins with key roles in sphingolipid transport and their potential role in cancer.

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Kashiwayama, Yoshinori, and Tsuneo Imanaka. "Peroxisomal ABC Proteins and Fatty Acid Metabolism." membrane 28, no. 6 (2003): 263–70. http://dx.doi.org/10.5360/membrane.28.263.

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BAAR, STELLA, and ELIZABETH TOPLEY. "Haemoglobin Metabolism and Serum Proteins Following Trauma." Acta Medica Scandinavica 153, no. 4 (April 24, 2009): 319–28. http://dx.doi.org/10.1111/j.0954-6820.1955.tb18233.x.

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Darjania, L., N. Ichise, S. Ichikawa, T. Okamoto, H. Okuyama, and G. A. Thompson. "Metabolism of glycosylphosphatidylinositol-anchored proteins in Arabidopsis." Biochemical Society Transactions 28, no. 6 (December 1, 2000): 725–27. http://dx.doi.org/10.1042/bst0280725.

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Although glycosylphosphatidylinositol (GPI)-anchored proteins have now been found in several plants, very little is known regarding their metabolism there. This report describes studies of the biosynthesis and turnover of arabinogalactan proteins, a class of abundant GPI-anchored proteins secreted by cultured Arabidopsis cells.

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Vallerie, S. N., and G. S. Hotamisligil. "The Role of JNK Proteins in Metabolism." Science Translational Medicine 2, no. 60 (December 1, 2010): 60rv5. http://dx.doi.org/10.1126/scitranslmed.3001007.

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Casteilla, L., M. Rigoulet, and L. Pénicaud. "Mitochondrial ROS Metabolism: Modulation by Uncoupling Proteins." IUBMB Life (International Union of Biochemistry and Molecular Biology: Life) 52, no. 3-5 (September 1, 2001): 181–88. http://dx.doi.org/10.1080/15216540152845984.

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Barthel, Andreas, Dieter Schmoll, and Terry G. Unterman. "FoxO proteins in insulin action and metabolism." Trends in Endocrinology & Metabolism 16, no. 4 (May 2005): 183–89. http://dx.doi.org/10.1016/j.tem.2005.03.010.

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Harris, Thurl E., and Brian N. Finck. "Dual function lipin proteins and glycerolipid metabolism." Trends in Endocrinology & Metabolism 22, no. 6 (June 2011): 226–33. http://dx.doi.org/10.1016/j.tem.2011.02.006.

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Londos, C., C. Sztalryd, J. T. Tansey, and A. R. Kimmel. "Role of PAT proteins in lipid metabolism." Biochimie 87, no. 1 (January 2005): 45–49. http://dx.doi.org/10.1016/j.biochi.2004.12.010.

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Rovira, Aleix Gorchs, and Alison G. Smith. "PPR proteins – orchestrators of organelle RNA metabolism." Physiologia Plantarum 166, no. 1 (April 23, 2019): 451–59. http://dx.doi.org/10.1111/ppl.12950.

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Rakhmonjonovna, Kapizova Dilafruz Rakhmonjonovna. "COMMON PATHWAYS OF PROTEIN AND AMINO ACID METABOLISM IN THE BODY." International Journal of Medical Sciences And Clinical Research 03, no. 06 (June 1, 2023): 49–52. http://dx.doi.org/10.37547/ijmscr/volume03issue06-09.

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Protein exchange is crucial for the life of the whole organism, each of its tissues and organs, some cells and subcellular components. Biochemical activity of the cell and all metabolic reactions occurring in it are related to the exchange of proteins.

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Bremer, K., K. M. Kocha, T. Snider, and C. D. Moyes. "Energy metabolism and cytochrome oxidase activity: linking metabolism to gene expression." Canadian Journal of Zoology 92, no. 7 (July 2014): 557–68. http://dx.doi.org/10.1139/cjz-2013-0267.

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Modification of mitochondrial content demands the synthesis of hundreds of proteins encoded by nuclear and mitochondrial genomes. The responsibility for coordination of this process falls to nuclear-encoded master regulators of transcription. DNA-binding proteins and coactivators integrate information from energy-sensing pathways and hormones to alter mitochondrial gene expression. In mammals, the signaling cascade for mitochondrial biogenesis can be described as follows: hormonal signals and energetic information are sensed by protein-modifying enzymes that in turn regulate the post-translational modification of transcription factors. Once activated, transcription-factor complexes form on promoter elements of many of the nuclear-encoded mitochondrial genes, recruiting proteins that remodel chromatin and initiate transcription. One master regulator in mammals, PGC-1α, is well studied because of its role in determining the metabolic phenotype of muscles, but also due to its importance in mitochondria-related metabolic diseases. However, relatively little is known about the role of this pathway in other vertebrates. These uncertainties raise broader questions about the evolutionary origins of the pathway and its role in generating the diversity in muscle metabolic phenotypes seen in nature.

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Korenevsky, A. V., A. D. Shcherbitskaia, M. E. Berezkina, K. L. Markova, E. P. Alexandrova, O. A. Balabas, S. A. Selkov, and D. I. Sokolov. "MALDI-TOF mass spectrometric protein profiling of microvesicles produced by the NK-92 natural killer cell line." Medical Immunology (Russia) 22, no. 4 (August 7, 2020): 633–46. http://dx.doi.org/10.15789/1563-0625-mms-1976.

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Extracellular vesicles that are shed from the plasma membrane contain a wide range of molecules, among which are proteins, lipids, nucleic acids, and sugars. The cytotoxic proteins of natural killer cells play a key role in the implementation of their cytolytic functions. One of the important steps in understanding the distant communication of cells is the determination of the proteome of microvesicles. This study was aimed at the protein profiling of the microvesicles produced by the NK-92 natural killer cell line. 986 proteins with a variety of functions were identified in the lysate of microvesicles using the MALDI-TOF mass spectrometric analysis. With automated methods of functional analysis applied, it has been shown that the largest protein groups are hypothetical proteins, proteins with unknown functions, and domains. The most representative groups are also comprised by transcription regulators; intracellular signaling proteins; RNA translation, transcription, processing, and utilization regulators; receptors; protein processing and proteolysis regulators; amino acid metabolism enzymes, as well as transport proteins and transport regulators. Minor functional groups are represented by vitamins and mineral metabolism enzymes, membrane and microdomain-forming proteins, hormones, hemostatic regulators, regulators of sensory systems, specific mitochondrial and Golgi apparatus proteins, and extracellular signaling proteins. An intermediate position is occupied by various functional groups, including cytoskeleton and motor proteins; proteins of centrioles; ion channels and their regulators; proteins of the ubiquitin-proteasome pathway of protein degradation; lipid, steroid, and fatty acid metabolism enzymes; nucleic acid base and carbohydrate metabolism enzymes, as well as energy metabolism enzymes and other proteins involved in intermediate metabolism; proteins of the immune response and inflammation; antigens and histocompatibility proteins; cytokines and growth factors; regulators of apoptosis, autophagy, endocytosis, and exocytosis; regulators of the cell cycle and division; regulators of proliferation, cell differentiation, and morphogenesis; regulators of cell adhesion and matrix metabolism; nuclear transport proteins; transposition proteins; DNA replication and repair proteins, as well as inactive proteins. The data obtained expand the existing knowledge of the distant communication of cells and indicate new mechanisms of interaction between natural killer and target cells.

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Samardzic, Kate, and Kenneth J. Rodgers. "Oxidised protein metabolism: recent insights." Biological Chemistry 398, no. 11 (October 26, 2017): 1165–75. http://dx.doi.org/10.1515/hsz-2017-0124.

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Abstract The ‘oxygen paradox’ arises from the fact that oxygen, the molecule that aerobic life depends on, threatens its very existence. An oxygen-rich environment provided life on Earth with more efficient bioenergetics and, with it, the challenge of having to deal with a host of oxygen-derived reactive species capable of damaging proteins and other crucial cellular components. In this minireview, we explore recent insights into the metabolism of proteins that have been reversibly or irreversibly damaged by oxygen-derived species. We discuss recent data on the important roles played by the proteasomal and lysosomal systems in the proteolytic degradation of oxidatively damaged proteins and the effects of oxidative damage on the function of the proteolytic pathways themselves. Mitochondria are central to oxygen utilisation in the cell, and their ability to handle oxygen-derived radicals is an important and still emerging area of research. Current knowledge of the proteolytic machinery in the mitochondria, including the ATP-dependent AAA+ proteases and mitochondrial-derived vesicles, is also highlighted in the review. Significant progress is still being made in regard to understanding the mechanisms underlying the detection and degradation of oxidised proteins and how proteolytic pathways interact with each other. Finally, we highlight a few unanswered questions such as the possibility of oxidised amino acids released from oxidised proteins by proteolysis being re-utilised in protein synthesis thus establishing a vicious cycle of oxidation in cells.

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Valle-Mendiola, Arturo, and Isabel Soto-Cruz. "Energy Metabolism in Cancer: The Roles of STAT3 and STAT5 in the Regulation of Metabolism-Related Genes." Cancers 12, no. 1 (January 3, 2020): 124. http://dx.doi.org/10.3390/cancers12010124.

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A central characteristic of many types of cancer is altered energy metabolism processes such as enhanced glucose uptake and glycolysis and decreased oxidative metabolism. The regulation of energy metabolism is an elaborate process involving regulatory proteins such as HIF (pro-metastatic protein), which reduces oxidative metabolism, and some other proteins such as tumour suppressors that promote oxidative phosphorylation. In recent years, it has been demonstrated that signal transducer and activator of transcription (STAT) proteins play a pivotal role in metabolism regulation. STAT3 and STAT5 are essential regulators of cytokine- or growth factor-induced cell survival and proliferation, as well as the crosstalk between STAT signalling and oxidative metabolism. Several reports suggest that the constitutive activation of STAT proteins promotes glycolysis through the transcriptional activation of hypoxia-inducible factors and therefore, the alteration of mitochondrial activity. It seems that STAT proteins function as an integrative centre for different growth and survival signals for energy and respiratory metabolism. This review summarises the functions of STAT3 and STAT5 in the regulation of some metabolism-related genes and the importance of oxygen in the tumour microenvironment to regulate cell metabolism, particularly in the metabolic pathways that are involved in energy production in cancer cells.

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Yan, Xue, Aurélie Budin-Verneuil, Yanick Auffray, and Vianney Pichereau. "Proteome phenotyping of ΔrelA mutants in Enterococcus faecalis V583." Canadian Journal of Microbiology 60, no. 8 (August 2014): 525–31. http://dx.doi.org/10.1139/cjm-2014-0254.

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The (p)ppGpp synthetase RelA contributes to stress adaptation and virulence in Enterococcus faecalis V583. A 2-dimensional electrophoresis proteomic analysis of 2 relA mutants, i.e., ΔrelA carrying a complete deletion of the relA gene, and ΔrelAsp that is deleted from only its 3′ extremity, showed that 31 proteins were deregulated in 1 or both of these mutants. Mass spectrometry identification of these proteins showed that 10 are related to translation, including 5 ribosomal proteins, 3 proteins involved in translation elongation, and 2 proteins in tRNA synthesis; 14 proteins are involved in diverse metabolisms and biosynthesis (8 in sugar and energy metabolisms, 2 in fatty acid biosynthesis, 2 in amino acid biosynthesis, and 2 in nucleotide metabolism). Five proteins were relevant to the adaptation to different environmental stresses, i.e., SodA and a Dps family protein, 2 cold-shock domain proteins, and Ef1744, which is a general stress protein that plays an important role in the response to ethanol stress. The potential role of these proteins in the development of stress phenotypes associated with these mutations is discussed.

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Napoli, Joseph L. "Retinoid binding-proteins redirect retinoid metabolism: biosynthesis and metabolism of retinoic acid." Seminars in Cell & Developmental Biology 8, no. 4 (August 1997): 403–15. http://dx.doi.org/10.1006/scdb.1997.0164.

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Teerlink, Tom. "ADMA metabolism and clearance." Vascular Medicine 10, no. 2_suppl (May 2005): S73—S81. http://dx.doi.org/10.1191/1358863x05vm597oa.

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The plasma concentration of asymmetric dimethylarginine (ADMA), an endogenous inhibitor of nitric oxide synthase, is the resultant of many processes at cellular and organ levels. Post-translational methylation of arginine residues of proteins plays a crucial role in the regulation of their functions, which include processes such as transcription, translation and RNA splicing. Because protein methylation is irreversible, the methylation signal can be turned off only by proteolysis of the entire protein. Consequently, most methylated proteins have high turnover rates. Free ADMA, which is formed during proteolysis, is actively degraded by the intracellular enzyme dimethylarginine dimethylaminohydrolase (DDAH). Some ADMA escapes degradation and leaves the cell via cationic amino acid transporters. These transporters also mediate uptake of ADMA by neighboring cells or distant organs, thereby facilitating active interorgan transport. Clearance of ADMA from the plasma occurs in small part by urinary excretion, but the bulk of ADMA is degraded by intracellular DDAH, after uptake from the circulation. This review discusses the various processes involved in ADMA metabolism: protein methylation, proteolysis of methylated proteins, metabolism by DDAH, and interorgan transport. In addition, the role of the kidney and the liver in the clearance of ADMA is highlighted.

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Huang, Weiwei, Fei Gao, Yuting Zhang, Tianhui Chen, and Chen Xu. "Lipid Droplet-Associated Proteins in Cardiomyopathy." Annals of Nutrition and Metabolism 78, no. 1 (December 2, 2021): 1–13. http://dx.doi.org/10.1159/000520122.

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Background: The heart requires a high rate of fatty-acid oxidation (FAO) to meet its energy needs. Neutral lipids are the main source of energy for the heart and are stored in lipid droplets (LDs), which are cytosolic organelles that primarily serve to store neutral lipids and regulate cellular lipid metabolism. LD-associated proteins (LDAPs) are proteins either located on the surface of the LDs or reside in the cytosol and contribute to lipid metabolism. Therefore, abnormal cardiac lipid accumulation or FAO can alter the redox state of the heart, resulting in cardiomyopathy, a group of diseases that negatively affect the myocardial function, thereby leading to heart failure and even cardiac death. Summary: LDs, along with LDAPs, are pivotal for modulating heart lipid homeostasis. The proper cardiac development and the maintenance of its normal function depend largely on lipid homeostasis regulated by LDs and LDAPs. Overexpression or deletion of specific LDAPs can trigger myocardial dysfunction and may contribute to the development of cardiomyopathy. Extensive connections and interactions may also exist between LDAPs. Key Message: In this review, the various mechanisms involved in LDAP-mediated regulation of lipid metabolism, the association between cardiac development and lipid metabolism, as well as the role of LDAPs in cardiomyopathy progression are discussed.

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Coomes, Eric, Edwin S. L. Chan, and Allison B. Reiss. "Methotrexate in Atherogenesis and Cholesterol Metabolism." Cholesterol 2011 (February 22, 2011): 1–8. http://dx.doi.org/10.1155/2011/503028.

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Methotrexate is a disease-modifying antirheumatic drug commonly used to treat inflammatory conditions such as rheumatoid arthritis which itself is linked to increased cardiovascular risk. Treatments that target inflammation may also impact the cardiovascular system. While methotrexate improves cardiovascular risk, inhibition of the cyclooxygenase (COX)-2 enzyme promotes atherosclerosis. These opposing cardiovascular influences may arise from differing effects on the expression of proteins involved in cholesterol homeostasis. These proteins, ATP-binding cassette transporter (ABC) A1 and cholesterol 27-hydroxylase, facilitate cellular cholesterol efflux and defend against cholesterol overload. Methotrexate upregulates expression of cholesterol 27-hydroxylase and ABCA1 via adenosine release, while COX-2 inhibition downregulates these proteins. Adenosine, acting through the A2A and A3 receptors, may upregulate proteins involved in reverse cholesterol transport by cAMP-PKA-CREB activation and STAT inhibition, respectively. Elucidating underlying cardiovascular mechanisms of these drugs provides a framework for developing novel cardioprotective anti-inflammatory medications, such as selective A2A receptor agonists.

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Zeng, Li, Nian Chen, Junlin Liao, Xu Shen, Shenghua Song, and Feng Wang. "Metabolic Analysis of Potential Key Genes Associated with Systemic Lupus Erythematosus Using Liquid Chromatography-Mass Spectrometry." Computational and Mathematical Methods in Medicine 2021 (October 4, 2021): 1–17. http://dx.doi.org/10.1155/2021/5799348.

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The biological mechanism underlying the pathogenesis of systemic lupus erythematosus (SLE) remains unclear. In this study, we found 21 proteins upregulated and 38 proteins downregulated by SLE relative to normal protein metabolism in our samples using liquid chromatography-mass spectrometry. By PPI network analysis, we identified 9 key proteins of SLE, including AHSG, VWF, IGF1, ORM2, ORM1, SERPINA1, IGF2, IGFBP3, and LEP. In addition, we identified 4569 differentially expressed metabolites in SLE sera, including 1145 reduced metabolites and 3424 induced metabolites. Bioinformatics analysis showed that protein alterations in SLE were associated with modulation of multiple immune pathways, TP53 signaling, and AMPK signaling. In addition, we found altered metabolites associated with valine, leucine, and isoleucine biosynthesis; one carbon pool by folate; tyrosine metabolism; arginine and proline metabolism; glycine, serine, and threonine metabolism; limonene and pinene degradation; tryptophan metabolism; caffeine metabolism; vitamin B6 metabolism. We also constructed differently expressed protein-metabolite network to reveal the interaction among differently expressed proteins and metabolites in SLE. A total of 481 proteins and 327 metabolites were included in this network. Although the role of altered metabolites and proteins in the diagnosis and therapy of SLE needs to be further investigated, the present study may provide new insights into the role of metabolites in SLE.

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Kersten, S. "Regulation of lipid metabolism via angiopoietin-like proteins." Biochemical Society Transactions 33, no. 5 (October 26, 2005): 1059–62. http://dx.doi.org/10.1042/bst0331059.

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Regulation of mammalian energy metabolism is an intricate process involving numerous hormones, transcription factors and signal transduction cascades. Much of the regulation occurs via secreted factors that relay information from one organ to another. One group of secreted factors that recently emerged as having a major impact on lipid and possibly glucose metabolism are the ANGPTLs (angiopoietin-like proteins). This includes ANGPTL3, ANGPTL4/FIAF (fasting-induced adipose factor), and ANGPTL6/AGF (angiopoietin-related growth factor). Although the receptors for these proteins have yet to be identified, it is nevertheless increasingly clear that these proteins have important effects on plasma triacylglycerol clearance, adipose tissue lipolysis, and adiposity. This review summarizes contemporary data on ANGPTLs with emphasis on the connection with energy metabolism.

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Kersten, S. "Regulation of lipid metabolism via angiopoietin-like proteins." Biochemical Society Transactions 33, no. 5 (October 1, 2005): 1059. http://dx.doi.org/10.1042/bst20051059.

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SILVER, DAVID L., XIAN-CHENG JIANG, TAKESHI ARAI, CAN BRUCE, and ALAN R. TALL. "Receptors and Lipid Transfer Proteins in HDL Metabolism." Annals of the New York Academy of Sciences 902, no. 1 (January 25, 2006): 103–12. http://dx.doi.org/10.1111/j.1749-6632.2000.tb06305.x.

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Dijk, Wieneke, and Sander Kersten. "Regulation of lipid metabolism by angiopoietin-like proteins." Current Opinion in Lipidology 27, no. 3 (June 2016): 249–56. http://dx.doi.org/10.1097/mol.0000000000000290.

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Silve, Caroline. "DMP1 and phosphate metabolism – matrix proteins go systemic." BoneKEy-Osteovision 3, no. 12 (December 2006): 30–35. http://dx.doi.org/10.1138/20060241.

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Knutson, Mitchell D. "Steap Proteins: Implications for Iron and Copper Metabolism." Nutrition Reviews 65, no. 7 (June 28, 2008): 335–40. http://dx.doi.org/10.1111/j.1753-4887.2007.tb00311.x.

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Lim, Sangbin, Joshua B. Phillips, Luciana Madeira da Silva, Ming Zhou, Oystein Fodstad, Laurie B. Owen, and Ming Tan. "Interplay between Immune Checkpoint Proteins and Cellular Metabolism." Cancer Research 77, no. 6 (February 28, 2017): 1245–49. http://dx.doi.org/10.1158/0008-5472.can-16-1647.

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Knutson,, Mitchell D. "Steap Proteins: Implications for Iron and Copper Metabolism." Nutrition Reviews 65, no. 7 (July 1, 2007): 335–40. http://dx.doi.org/10.1301/nr.2007.jul.335340.

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Parrow, Nermi L., and Robert E. Fleming. "Bone Morphogenetic Proteins as Regulators of Iron Metabolism." Annual Review of Nutrition 34, no. 1 (July 17, 2014): 77–94. http://dx.doi.org/10.1146/annurev-nutr-071813-105646.

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Gella, F. Javier, Francisco Palomo, and Jorge Beleta. "Purification of Several Proteins Involved in Glycogen Metabolism." Enzyme 39, no. 3 (1988): 167–73. http://dx.doi.org/10.1159/000469113.

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Clemmons, David R. "Role of IGF Binding Proteins in Regulating Metabolism." Trends in Endocrinology & Metabolism 27, no. 6 (June 2016): 375–91. http://dx.doi.org/10.1016/j.tem.2016.03.019.

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A. Wilson, Michael, Chenyu Wei, and Andrew Pohorille. "Towards Co-Evolution of Membrane Proteins and Metabolism." Origins of Life and Evolution of Biospheres 44, no. 4 (December 2014): 357–61. http://dx.doi.org/10.1007/s11084-014-9393-2.

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Mattijssen, Frits, and Sander Kersten. "Regulation of triglyceride metabolism by Angiopoietin-like proteins." Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1821, no. 5 (May 2012): 782–89. http://dx.doi.org/10.1016/j.bbalip.2011.10.010.

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Palida, F. A., and M. J. Ettinger. "Identification of proteins involved in intracellular copper metabolism." Journal of Biological Chemistry 266, no. 7 (March 1991): 4586–92. http://dx.doi.org/10.1016/s0021-9258(20)64363-0.

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El Khoury, Dalia, and G. Harvey Anderson. "Recent advances in dietary proteins and lipid metabolism." Current Opinion in Lipidology 24, no. 3 (June 2013): 207–13. http://dx.doi.org/10.1097/mol.0b013e3283613bb7.

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Doedt, Thomas, Shankarling Krishnamurthy, Dirk P. Bockmühl, Bernd Tebarth, Christian Stempel, Claire L. Russell, Alistair J. P. Brown, and Joachim F. Ernst. "APSES Proteins Regulate Morphogenesis and Metabolism inCandida albicans." Molecular Biology of the Cell 15, no. 7 (July 2004): 3167–80. http://dx.doi.org/10.1091/mbc.e03-11-0782.

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Abstract:

Fungal APSES proteins regulate morphogenetic processes, including filamentation and differentiation. The human fungal pathogen Candida albicans contains two APSES proteins: the regulator Efg1p and its homologue Efh1p, described here. Overexpression of EFG1 or EFH1 led to similar phenotypes, including pseudohypha formation and opaque-white switching. An efh1 deletion generated no phenotype under most conditions but caused hyperfilamentation in an efg1 background under embedded or hypoxic conditions. This suggests cooperation of these APSES proteins in the suppression of an alternative morphogenetic signaling pathway. Genome-wide transcriptional profiling revealed that EFG1 and EFH1 regulate partially overlapping sets of genes associated with filament formation. Unexpectedly, Efg1p not only regulates genes involved in morphogenesis but also strongly influences the expression of metabolic genes, inducing glycolytic genes and repressing genes essential for oxidative metabolism. Using one- and two-hybrid assays, we further demonstrate that Efg1p is a repressor, whereas Efh1p is an activator of gene expression. Overall, the results suggest that Efh1p supports the regulatory functions of the primary regulator, Efg1p, and indicate a dual role for these APSES proteins in the regulation of fungal morphogenesis and metabolism.

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Cameron, Elizabeth A., Mallory A. Maynard, Christopher J. Smith, Thomas J. Smith, Nicole M. Koropatkin, and Eric C. Martens. "Multidomain Carbohydrate-binding Proteins Involved inBacteroides thetaiotaomicronStarch Metabolism." Journal of Biological Chemistry 287, no. 41 (August 21, 2012): 34614–25. http://dx.doi.org/10.1074/jbc.m112.397380.

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Journal articles on the topic 'Proteins – Metabolism'

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