Journal articles: 'Proteins'

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Boege, F. "Bence Jones-Proteine. Bence Jones Proteins." LaboratoriumsMedizin 23, no. 9 (January 1999): 477–82. http://dx.doi.org/10.1515/labm.1999.23.9.477.

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Rupal, Hemantkumar Desai, and Rao Chunduri Jayaprada. "Immuno-compatibility assessment of phytal-proteins of Zingiber zerumbet and serum gamma globulins of rheumatoid arthritis disease subjects." GSC Biological and Pharmaceutical Sciences 23, no. 1 (April 30, 2023): 168–73. https://doi.org/10.5281/zenodo.7925188.

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Phytal proteins are of great importance as they exhibit unique characteristics as immune modulators. Zingiber zerumbet family plants are used in various ways, including as food, beverages, and ornaments. The metabolites and extracts of these plants indicated an anti-viral, anti-cancer, anti-diabetic, and anti-inflammatory therapeutic characteristics features. Rheumatoid arthritis (RA) is an auto-immune condition that causes joint inflammation and malformations. The up- and down-regulation of certain rheumatoid arthritis proteins result in serious side effects. Ayurveda and other naturopathy treatments offer relief to a certain extent, while other pharmaceutical therapy is topical and temporary. The current study is aimed to comprehend the interaction of gamma-globulin proteins of RA patients with phytal proteins from leaves of the Zingiber zerumbet plant. The immunoassays, and MS orbitrap studies revealed the binding pattern and composition of the proteins. The protein- protein docking studies supported the method of binding pattern and these phytal proteins can be considered in the future for therapeutical or diagnostic purposes.

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Thorp, H. Holden. "Proteins, proteins everywhere." Science 374, no. 6574 (December 17, 2021): 1415. http://dx.doi.org/10.1126/science.abn5795.

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The first protein structures were determined by x-ray crystallography in 1957 by John C. Kendrew and Max F. Perutz. As a bioinorganic chemist, I was delighted that the structures were myoglobin and hemoglobin, both heme proteins with big, beautiful iron atoms. It must have been an extraordinary experience to stare at a physical model of the structures and see something that had previously only been imagined. Not long afterward, Christian B. Anfinsen Jr. proposed that the structure of a protein was thermodynamically stable. It seemed possible that the three-dimensional structure of a protein could be predicted based on the sequence of its amino acids. This “protein-folding problem,” as it came to be known, baffled scientists until this year, when the papers we’ve deemed the 2021 Breakthrough of the Year were published.

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Akhter, Tahmin, S. Kanamaru, and F. Arisaka. "2P043 Protein interactions among neck proteins, gp13/gp14, and the connector protein, gp15, of bacteriophage T4." Seibutsu Butsuri 45, supplement (2005): S130. http://dx.doi.org/10.2142/biophys.45.s130_3.

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Williams, R. J. P. "Synthetic Proteins: Designer proteins." Current Biology 4, no. 10 (October 1994): 942–44. http://dx.doi.org/10.1016/s0960-9822(00)00213-x.

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Töpfer-Petersen, E., D. Čechová, A. Henschen, M. Steinberger, A. E. Friess, and A. Zucker. "Cell biology of acrosomal proteins: Zellbiologie akrosomaler Proteine." Andrologia 22, S1 (April 27, 2009): 110–21. http://dx.doi.org/10.1111/j.1439-0272.1990.tb02077.x.

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Coleman, Joseph E. "Zinc Proteins: Enzymes, Storage Proteins, Transcription Factors, and Replication Proteins." Annual Review of Biochemistry 61, no. 1 (June 1992): 897–946. http://dx.doi.org/10.1146/annurev.bi.61.070192.004341.

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Paape, M., S. Nell, S. von Bargen, and J. W. Kellmann. "Identification and characterization of host proteins interacting with NSm, the Tomato spotted wilt virus movement protein." Plant Protection Science 38, SI 1 - 6th Conf EFPP 2002 (January 1, 2002): S108—S111. http://dx.doi.org/10.17221/10331-pps.

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To search for host proteins involved in systemic spreading of Tomato spotted wilt virus (TSWV), the virus-encoded NSm movement protein has been utilized as a bait in yeast two-hybrid interaction trap assays. J-domain chaperones from different host species and a protein denominated At-4/1 from Arabidopsis thaliana showing homologies to myosins and kinesins were identified as NSm-interacting partners. In this communication we illustrate that following TSWV infection, J-domain proteins accumulated in systemically infected leaves of A. thaliana, whereas At-4/1 was constitutively detected in leaves of A. thaliana and Nicotiana rustica.

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Lan, Nan, Hanxing Zhang, Chengcheng Hu, Wenzhao Wang, Ana M. Calvo, Steven D. Harris, She Chen, and Shaojie Li. "Coordinated and Distinct Functions of Velvet Proteins in Fusarium verticillioides." Eukaryotic Cell 13, no. 7 (May 2, 2014): 909–18. http://dx.doi.org/10.1128/ec.00022-14.

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ABSTRACTVelvet-domain-containing proteins are broadly distributed within the fungal kingdom. In the corn pathogenFusarium verticillioides, previous studies showed that the velvet proteinF. verticillioidesVE1 (FvVE1) is critical for morphological development, colony hydrophobicity, toxin production, and pathogenicity. In this study, tandem affinity purification of FvVE1 revealed that FvVE1 can form a complex with the velvet proteinsF. verticillioidesVelB (FvVelB) and FvVelC. Phenotypic characterization of gene knockout mutants showed that, as in the case of FvVE1, FvVelB regulated conidial size, hyphal hydrophobicity, fumonisin production, and oxidant resistance, while FvVelC was dispensable for these biological processes. Comparative transcriptional analysis of eight genes involved in the ROS (reactive oxygen species) removal system revealed that both FvVE1 and FvVelB positively regulated the transcription of a catalase-encoding gene,F. verticillioidesCAT2(FvCAT2). Deletion ofFvCAT2resulted in reduced oxidant resistance, providing further explanation of the regulation of oxidant resistance by velvet proteins in the fungal kingdom.

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Doolittle, Russell F. "Proteins." Scientific American 253, no. 4 (October 1985): 88–99. http://dx.doi.org/10.1038/scientificamerican1085-88.

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Deisenhofer, J. "Proteins." Current Opinion in Structural Biology 11, no. 6 (December 1, 2001): 701–2. http://dx.doi.org/10.1016/s0959-440x(01)00273-1.

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Brändén, Carl-Ivar, and Johann Deisenhofer. "Proteins." Current Opinion in Structural Biology 7, no. 6 (December 1997): 819–20. http://dx.doi.org/10.1016/s0959-440x(97)80152-2.

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Sleator, Roy D. "Proteins." Bioengineered 3, no. 2 (March 2012): 80–85. http://dx.doi.org/10.4161/bbug.18303.

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Eklund, Hans, and T. Alwyn Jones. "Proteins." Current Opinion in Structural Biology 5, no. 6 (December 1995): 719–20. http://dx.doi.org/10.1016/0959-440x(95)80002-6.

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15

Stevens, Timothy J., and Isaiah T. Arkin. "Are membrane proteins ?inside-out? proteins?" Proteins: Structure, Function, and Genetics 36, no. 1 (July 1, 1999): 135–43. http://dx.doi.org/10.1002/(sici)1097-0134(19990701)36:1<135::aid-prot11>3.0.co;2-i.

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Rukes, Verena. "Nanopore Technology: When Proteins Analyse Proteins." CHIMIA 79, no. 4 (April 30, 2025): 196–99. https://doi.org/10.2533/chimia.2025.196.

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Nanopore sensing is an emerging technology that can distinguish subtle differences in molecules and allows the observation of molecular processes. The technique has revolutionized DNA sequencing through long reads of single molecules. Following this success, nanopores are now increasingly applied to protein analysis. Proteins play central roles in cellular function and major diseases, however their analysis using established methods is complicated by the lack of protein-amplification methods. Here, two examples of nanopore-based protein analysis are described: the identification of biomarkers, and the analysis of protein function.

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Anil, Kumar Tomar, Saraswat Mayank, Singh Sooch Balwinder, Singh Sarman, P. Singh Tej, and Yadav Savita. "Prediction of Heparin binding sites on Human Serum Albumin, Matrix Metalloproteinase-2 and DNA Topoisomerase1." International Journal of BioSciences and Technology (IJBST) ISSN: 0974-3987 3, no. 1 (January 31, 2010): 21–26. https://doi.org/10.5281/zenodo.1438292.

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ABSTRACT: Heparin binds a wide range of proteins of different structure as well as functions and play crucial roles in a number of biological processes. Human seminal plasma consists of many heparin binding proteins (HBPs). HBPs play crucial role in modulation of capacitation through heparin and have been correlated with fertility in many species. Very little scientific information is available about the binding modes of heparin and HBPs. There is not any well defined binding space, characterized by some consensus sequence over protein except that binding region always do consist of basic residues. Thus, we have to study each heparin-HBPs complex individually to gather information about their interactions. Here, we are reporting the results of docking studies to predict the heparin binding sites of three human seminal fluid HBPs (human serum albumin, matrix metalloproteinase-2 and DNA topoisomerase 1) using program Dock6. Our docking results show that Arg117, Arg186, Lys519 of human serum albumin, Lys531, Tyr540, Glu549, Tyr552, Tyr591, Lys596 of matrix metalloproteinase and Lys439, Lys443, Arg488, Thr585, Lys587, Thr591 of DNA topoisomerase1 make hydrogen bond contacts with heparin. The positively charged residues Arginine and Lysine play important role in their interactions. Our study may add up to better understanding of protein-heparin binding modes. Keywords: Heparin binding proteins, Molecular docking, Dock6, Protein structure http://www.ijbst.org/Home/papers-published/ijbst-2010-volume-3-issue-1

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Zarifa, Osmanli, Aliyeva Aysel, and Shahmuradov Ilham. "Isoforms of cancer-related proteins tend to destabilize the structure." Transactions of the Institute of Molecular Biology & Biotechnologies 7, no. 1 (June 25, 2023): 61–66. https://doi.org/10.5281/zenodo.8079824.

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Protein isoforms provide protein diversity through various biological mechanisms such as alternative splicing, alternative promoter usage and other mechanisms. Isoforms functions can differ depending on several factors, including their amino acid sequence and structure. Meanwhile, cancer-related protein isoforms have notable importance due to their association with the disease. Previous studies indicate that tumor suppressor protein p53 isoforms can either facilitate or inhibit tumor growth, depending on its isoform and the cellular context. However, earlier studies have mainly focused on investigating the structures of canonical proteins of cancer-related proteins, with relatively less attention given to the structural analysis of their isoforms. Determining the structure of isoforms of cancer-related proteins can be crucial for understanding the mechanisms of disease association. Changes in structure may affect the function of isoforms. Experimental studies can be expensive and time-consuming, frequently requiring significant resources to obtain accurate results. Nonetheless, recent advancements in structural biology, such as the AlphaFold tool, have provided a door of opportunity to study protein sequences deeply. Thanks to this tool, we can model highly accurate protein structures without the need for comprehensive laboratory research, allowing for more efficient and cost-effective research. Therefore, in our study, we implemented a comparative analysis of the canonical cancer-related proteins and their isoform structures made with AlphaFold to determine structural differences. Our analysis revealed that most of the isoforms of cancer-related proteins are more disordered than general protein isoforms.

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Jin, Wenzhen, and Syoji T. akada. "1P103 Asymmetry in membrane protein sequence and structure : Glycine outside rule(Membrane proteins,Oral Presentations)." Seibutsu Butsuri 47, supplement (2007): S49. http://dx.doi.org/10.2142/biophys.47.s49_2.

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20

ISOBE, TAKASHI. "Amyloid proteins and amyloidosis.2 Amyloidosis of AA proteins and AL proteins." Nihon Naika Gakkai Zasshi 82, no. 9 (1993): 1415–19. http://dx.doi.org/10.2169/naika.82.1415.

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21

Martínez-Navarro, Angélica Concepción, Alejandra Chamorro-Flores, Grissel Vázquez-Bustos, Selma Ríos-Meléndez, Miguel Ángel Villalobos-López, Omar Pantoja, and Analilia Arroyo-Becerra. "Tráfico vesicular, un viaje épico de las proteínas hacia la membrana." Alianzas y Tendencias BUAP 7, no. 28 (November 14, 2022): 1–38. https://doi.org/10.5281/zenodo.7238038.

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RESUMEN La comunicación en las células eucariontes depende de un complejo sistema de membranas y varios mecanismos de tráfico intracelular en respuesta a señales externas e internas para controlar las respuestas fisiológicas. Las proteínas recién sintetizadas se envían a sus destinos celulares a través de dos tipos de procesos, uno basado en el péptido señal y el otro basado en el tráfico vesicular. El transporte de proteínas a través de vesículas ocurre en la vía secretora y la vía endocítica. El sistema de endomembranas funciona como una vía por la cual las vesículas se movilizan para llegar a su destino. Esta revisión brinda una descripción general de los mecanismos involucrados en el tráfico vesicular, incluidas las principales proteínas para la formación, división y fusión de vesículas, con énfasis general en las cubiertas de vesículas, proteínas SNARE, proteínas adaptadoras y receptores de selección de carga. Además, se dan a conocer ejemplos de defectos y enfermedades causadas por la inadecuada movilización de las proteínas en diferentes organismos con énfasis en humanos, lo que evidencia la importancia del tráfico vesicular. Finalmente se plantea un panorama de lo que falta por conocer y el potencial aporte del estudio de organismos adaptados a ambientes extremos.   ABSTRACT Communication in eukaryotic cells depends on a complex membrane system and several intracellular trafficking mechanisms in response to external and internal cues to control physiological responses. Newly synthesized proteins are delivered to their cellular destinations through two types of processes, one based on signal peptide, and the other, based on vesicular trafficking. Transport of proteins through vesicles occurs along the secretory pathway and endocytic pathway. The endomembrane system functions as a track by which the vesicles are mobilized to reach their destination. This review gives an overview of mechanisms involved in vesicular trafficking including the main proteins for vesicle formation, cleavage, and fusion with overall emphasis on vesicle coats, SNARE proteins, adaptor proteins and cargo selection receptors. Additionally, examples of defects and diseases caused by the inadequate mobilization of proteins in different organisms, with emphasis on humans, are disclosed, which shows the importance of vesicular traffic. Finally, an overview of what remains to be known and the potential contribution of the study of organisms adapted to extreme environments is given.

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Bilyk, Olena, Tetyana Vasylchenko, Oksana Kochubei-Lytvynenko, Yulia Bondarenko, and Volodymyr Piddubnyi. "STUDYING THE EFFECT OF MILK PROCESSING PRODUCTS ON THE STRUCTURAL-MECHANICAL PROPERTIES OF WHEAT FLOUR DOUGH." EUREKA: Life Sciences, no. 1 (February 3, 2021): 44–52. https://doi.org/10.21303/2504-5695.2021.001642.

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Dry whey enriched with magnesium and manganese (DW) that contains protein in the amount of 13 %, and a whey protein concentrate (WPC) with a protein content of 65 %, have been chosen as functional bases in the production of complex baking improvers with a targeted effect. When developing a composition of the complex improver, the rational dosage of DW is 2 % by weight of flour, and that of WPC – 3 % by weight of flour. Adding DW and WPC during the kneading of wheat flour dough predetermines a decrease in its gluten content, by 4 % and 6.1 %, respectively, after 20 minutes of the dough rest, and by 7.5 and 10.7 % after two hours of the dough fermentation. This is due to the introduction of lactic acid with milk processing products, which peptizes proteins resulting in that the gluten proteins are partially converted into water-soluble ones. If DW and WPC are included in the dough formulation, there is an increase in the total amount of proteins in it, as well as a change in their fractional composition: the mass fraction of water-soluble and intermediate fractions of proteins increases while the amount of gluten proteins decreases. That confirms a decrease in the amount of gluten washed out from the dough with the addition of DW and WPC. Increasing the mass fraction of water-soluble proteins contributes to the intensification of the fermentation process through the additional nutrition of microflora with nitrogenous substances and an increase in the content of free water in the dough, which predetermines its thinning. It was established that despite the high water absorption capacity of DW and WPC, the water-absorbing ability of the dough that contains them decreases compared to control by 8.4 and 10.7 %, respectively. Studying the dough at the farinograph has shown that in the case of using DW, its stability is somewhat prolonged while in the case of WPC introduction the dough stability is extended by almost 10 minutes, which leads to prolonging the dough kneading. Along with this, in the case of using WPC, there is a rapid descent of the farinogram curve, which could lead to a strong weakening of the dough during fermentation and rest, even though that the thinning after 12 minutes is lower than that of control

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Keller, Rob C. A. "Identification of Possible Lipid Binding Regions in Food Proteins and Peptides and Additional In Silico Analysis." Food Biophysics 13, no. 2 (March 7, 2018): 139–46. https://doi.org/10.1007/s11483-018-9519-6.

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The results of the search for potential helical lipid binding regions in a number of well-known food proteins is described. All selected food proteins have either well-described or strong indications of protein-lipid interaction features. The results are obtained with the aid of a number of selected bioinformatics tools. The identified potential lipid binding regions either correspond nicely with regions demonstrated experimentally or can be identified as novel lipid binding regions. The results are discussed in relation to earlier found experimental results and if relevant are discussed in mechanistic terms as well. A possible general use of the approach as used in this study is discussed as well. The in this study described approach can be used as a tool to come to a more focused approach for further research of yet unknown proteins. It is also possible to use this approach for more directed research when it comes to for example rational functional design of proteins for particular desired features like the emulsifying or foaming ability of the protein of interest.

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Jeffery, Constance J. "An introduction to protein moonlighting." Biochemical Society Transactions 42, no. 6 (November 17, 2014): 1679–83. http://dx.doi.org/10.1042/bst20140226.

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Moonlighting proteins comprise a class of multifunctional proteins in which a single polypeptide chain performs multiple physiologically relevant biochemical or biophysical functions. Almost 300 proteins have been found to moonlight. The known examples of moonlighting proteins include diverse types of proteins, including receptors, enzymes, transcription factors, adhesins and scaffolds, and different combinations of functions are observed. Moonlighting proteins are expressed throughout the evolutionary tree and function in many different biochemical pathways. Some moonlighting proteins can perform both functions simultaneously, but for others, the protein's function changes in response to changes in the environment. The diverse examples of moonlighting proteins already identified, and the potential benefits moonlighting proteins might provide to the organism, such as through coordinating cellular activities, suggest that many more moonlighting proteins are likely to be found. Continuing studies of the structures and functions of moonlighting proteins will aid in predicting the functions of proteins identified through genome sequencing projects, in interpreting results from proteomics experiments, in understanding how different biochemical pathways interact in systems biology, in annotating protein sequence and structure databases, in studies of protein evolution and in the design of proteins with novel functions.

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Jeffery, Constance J. "Moonlighting proteins: old proteins learning new tricks." Trends in Genetics 19, no. 8 (August 2003): 415–17. http://dx.doi.org/10.1016/s0168-9525(03)00167-7.

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Smith, Valerie J., and Elisabeth A. Dyrynda. "Antimicrobial proteins: From old proteins, new tricks." Molecular Immunology 68, no. 2 (December 2015): 383–98. http://dx.doi.org/10.1016/j.molimm.2015.08.009.

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TSUGITA, AKIRA. "Ultramicroanalysis of proteins. 1. Purification of proteins." Kagaku To Seibutsu 26, no. 5 (1988): 330–37. http://dx.doi.org/10.1271/kagakutoseibutsu1962.26.330.

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Serdyuk, I. N. "Structured proteins and proteins with intrinsic disorder." Molecular Biology 41, no. 2 (April 2007): 262–77. http://dx.doi.org/10.1134/s0026893307020082.

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Xu, Shengnan, and Hai-Yu Hu. "Fluorogen-activating proteins: beyond classical fluorescent proteins." Acta Pharmaceutica Sinica B 8, no. 3 (May 2018): 339–48. http://dx.doi.org/10.1016/j.apsb.2018.02.001.

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Марьянович, Александр Тимурович, and Дмитрий Юрьевич Кормилец. "SARS CoV-2 PROTEINS AND HUMAN PROTEINS." Russian Biomedical Research 9, no. 1 (May 22, 2024): 48–58. http://dx.doi.org/10.56871/rbr.2024.11.95.006.

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Белки SARS CoV-2 представляют собой молекулы с массой от нескольких десятков до нескольких тысяч аминокислотных остатков. Существуют структурные и неструктурные белки. К первым относятся шиповый гликопротеин, или S-белок (S), малый мембранный оболочечный белок (E), мембранный белок (M) и нуклеопротеин или нуклеокапсид (N). Вторая группа состоит из 16 неструктурных белков (Nsp1-16, включая полипротеины репликазы RPP 1a и 1ab) и 10 вспомогательных факторов или белков открытой рамки считывания (ORF3a, 3b, 6, 7a, 7b, 8, 9b, 9c, 10 и 14). Белки S, E и M, расположенные снаружи и в мембране вириона, участвуют в контакте вириона с клеткой и проникновении в нее. Другие белки участвуют в захвате внутриклеточных механизмов и их использовании в собственных интересах вируса. Большинство этих белков содержат многочисленные мотивы, гомологичные человеческим белкам, в том числе таким важным, как интерлейкин-7. Возможно, эта гомология является важным фактором, позволяющим «обмануть» иммунную систему на начальных стадиях инфекции и спровоцировать аутоиммунный ответ впоследствии. Гомология белков SARS CoV-2, с одной стороны, и белков вкусовых и обонятельных рецепторов — с другой, возможно, объясняетпричины нарушения восприятия вкусовых и обонятельных раздражителей, характерного для COVID-инфекции. SARS CoV-2 proteins are molecules with a mass of several tens to several thousand amino acid residues. There are structural and nonstructural proteins. The former include Spike glycoprotein (S), small membrane envelope protein (E), membrane protein (M), and nucleoprotein or nucleocapsid (N). The second group consists of 16 nonstructural proteins (Nsp1-16, including replicase&nbsp; polyproteins RPP 1a and 1ab) and 10 accessory factors or open reading frame proteins (ORF3a, 3b, 6, 7a, 7b, 8, 9b, 9c, 10 and 14). Proteins S, E and M, located outside and in the membrane of a virion, are involved in the contact of the virion with a cell and penetration into it. Other proteins are involved in the hijacking of intracellular mechanisms and their use in the virus’s own interests. Most of these proteins contain numerous motifs that are homologous to human proteins including such important ones as Interleukin-7. Perhaps this homology is an important factor in deceiving the immune system at the initial stages of infection and provoking an autoimmune response later. The homology of SARS CoV-2 proteins on the one hand and taste and olfactory receptor proteins on the other hand may possibly explain the causes of the impaired perception of taste and olfactory stimuli characteristic of COVID infection.

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Pillai, Harikrishna, Harikumar, S. Harikumar, S, Pramod kumar, R. Pramod kumar, R, and Anuraj, K. S. Anuraj, K.S. "Dna Mimicry by Proteins." International Journal of Scientific Research 3, no. 8 (June 1, 2012): 471–72. http://dx.doi.org/10.15373/22778179/august2014/150.

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Littler, Dene R., Stephen J. Harrop, Sophia C. Goodchild, Juanita M. Phang, Andrew V. Mynott, Lele Jiang, Stella M. Valenzuela, et al. "The enigma of the CLIC proteins: Ion channels, redox proteins, enzymes, scaffolding proteins?" FEBS Letters 584, no. 10 (January 18, 2010): 2093–101. http://dx.doi.org/10.1016/j.febslet.2010.01.027.

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Ro`zieva, Nazira Yodgorovna, and Baxriddin Baxtiyorovich Xudoyberdiyev. "THE IMPORTANCE OF PEDAGOGICAL DIAGNOSIS IN PRESCHOOL EDUCATIONAL ORGANIZATIONS." Eurasian Journal of Academic Research 1, no. 2 (May 31, 2021): 843–44. https://doi.org/10.5281/zenodo.4898809.

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In this paper, proteins perform different functions in many more processes than other compounds in the cell, and the functions performed by proteins are unique to protein molecules and are largely unrepeatable. The most important functions are catalytic, transport, protection, contraction, structure, hormonal and nutritional functions.

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Ro`zieva, Nazira Yodgorovna, and Baxriddin Baxtiyorovich Xudoyberdiyev. "THE IMPORTANCE OF PEDAGOGICAL DIAGNOSIS IN PRESCHOOL EDUCATIONAL ORGANIZATIONS." Eurasian Journal of Academic Research 1, no. 2 (May 31, 2021): 976–80. https://doi.org/10.5281/zenodo.4902822.

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In this paper, proteins perform different functions in many more processes than other compounds in the cell, and the functions performed by proteins are unique to protein molecules and are largely unrepeatable. The most important functions are catalytic, transport, protection, contraction, structure, hormonal and nutritional functions.

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Chakraborty, Asit Kumar. "Multi-Alignment Comparison of Coronavirus Non-Structural Proteins Nsp13- Nsp16 with Ribosomal Proteins and other DNA/RNA Modifying Enzymes Suggested their Roles in the Regulation of Host Protein Synthesis." International Journal of Clinical & Medical Informatics 3, no. 1 (June 1, 2020): 7–19. http://dx.doi.org/10.46619/ijcmi.2020.1024.

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Hung, Kuo-Wei, Chun-Chia Cheng, Yi-Chao Lin, Tsan-Hung Yu, Pei-Ju Fan, Chi-Fon Chang, Shih-Feng Tsai, and Tai-Huang Huang. "2P089 NMR Studies of Virulence-associated Proteins and Small Conserved Hypothetical Proteins in Klebsiella Pneumoniae(30. Protein function (II),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)." Seibutsu Butsuri 46, supplement2 (2006): S318. http://dx.doi.org/10.2142/biophys.46.s318_1.

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Borgese, N., S. Brambillasca, P. Soffientini, M. Yabal, and M. Makarow. "Biogenesis of tail-anchored proteins." Biochemical Society Transactions 31, no. 6 (December 1, 2003): 1238–42. http://dx.doi.org/10.1042/bst0311238.

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A group of integral membrane proteins, known as C-tail anchored, is defined by the presence of a cytosolic N-terminal domain that is anchored to the phospholipid bilayer by a single segment of hydrophobic amino acids close to the C-terminus. The mode of insertion into membranes of these proteins, many of which play key roles in fundamental intracellular processes, is obligatorily post-translational, is highly specific and may be subject to regulatory processes that modulate the protein's function. Recent work has demonstrated that tail-anchored proteins translocate their C-termini across the endoplasmic reticulum membrane by a mechanism different from that used for Sec61-dependent post-translational signal-peptide-driven translocation. Here we summarize recent results on the insertion of tail-anchored proteins and discuss possible mechanisms that could be involved.

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Ma, Yingxuan, and Kim Johnson. "Arabinogalactan-proteins." WikiJournal of Science 4, no. 1 (2021): 2. http://dx.doi.org/10.15347/wjs/2021.002.

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Arabinogalactan-proteins (AGPs) are highly glycosylated proteins (glycoproteins) found in the cell walls of plants. AGPs account for only a small portion of the cell wall, usually no more than 1% of dry mass of the primary wall. AGPs are members of the hydroxyproline-rich glycoprotein (HRGP) superfamily that represent a large and diverse group of glycosylated wall proteins. AGPs have attracted considerable attention due to their highly complex structures and potential roles in signalling. In addition, they have industrial and health applications due to their chemical/physical properties (water-holding, adhesion and emulsification). Glycosylation can account for more than 90% of the total mass. AGPs have been reported in a wide range of higher plants in seeds, roots, stems, leaves and inflorescences. They have also been reported in secretions of cell culture medium of root, leaf, endosperm and embryo tissues, and some exudate producing cell types such as stylar canal cells are capable of producing lavish amounts of AGPs.

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Löer, Birgit, and Michael Hoch. "Wech proteins." Cell Adhesion & Migration 2, no. 3 (July 2008): 177–79. http://dx.doi.org/10.4161/cam.2.3.6579.

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Yarotskyy, Viktor, and Robert T. Dirksen. "RGK proteins." Channels 8, no. 4 (July 2014): 286–87. http://dx.doi.org/10.4161/chan.29982.

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Flannery, Maura C. "Designing Proteins." American Biology Teacher 48, no. 2 (February 1, 1986): 112–14. http://dx.doi.org/10.2307/4448220.

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Guo, Shiny Shengzhen, and Reinhard Fässler. "KANK proteins." Current Biology 32, no. 19 (October 2022): R990—R992. http://dx.doi.org/10.1016/j.cub.2022.08.073.

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GÖKSEL, Şeyma, and Mustafa AKÇELİK. "Autotransporter Proteins." Uluslararası Muhendislik Arastirma ve Gelistirme Dergisi 13, no. 3 (December 31, 2021): 49–57. http://dx.doi.org/10.29137/umagd.1037361.

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Danilova, Lubov A. "Glycated proteins." Pediatrician (St. Petersburg) 10, no. 5 (January 28, 2020): 79–86. http://dx.doi.org/10.17816/ped10579-86.

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Glycation is a biological reaction that occurs in all proteins. Thisreaction proceeds more slowly in healthy subjects and more rapidly in patients suffering from a hyperglycemia. Glycated proteins cannot fulfill their functions that could lead to metabolic disorders. The process of glycation leads to building of advanced glycation end-products (AGEs). Thestructureof AGEs has not been fully researched yet. Glycated proteins have diagnostic meaning in different health conditions and not only in patients with diabetes mellitus. Determination of glycated proteins level (hemoglobin and plasma proteins) in diagnostics of diabetes mellitus and the effectiveness of its treatment; measurements of glycated proteins could be used as a predictor of different illnesses and their complications. Glycated hemoglobin was researched in children with diabetes mellitus of different severity. It has been shown that the level of glycated proteins does not always correlate with blood sugar level. Results of glycated proteins measurements in patients with thyroid disorders shows that the glycation takes place not only in patients with diabetes mellitus, but also with other illnesses without hyperglycemia. Our research in patients with diabetes mellitus has shown that the measured level of glycated proteins and plasma proteins could be more significant in the course of disease than the level of blood sugar. Compensation of diabetes mellitus in children in regard of the blood sugar level does not always correlate with the level of glycated proteins. This assumption could lead to the conclusion that only the combination of measurements like blood sugar, glycated hemoglobin and glycated proteins could give a full picture of disease compensation.

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Mudgil, Yashwanti, and Alan M. Jones. "NDR proteins." Plant Signaling & Behavior 5, no. 8 (August 2010): 1017–18. http://dx.doi.org/10.4161/psb.5.8.12290.

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Thomas, Clément, Céline Hoffmann, Sabrina Gatti, and André Steinmetz. "LIM Proteins." Plant Signaling & Behavior 2, no. 2 (March 2007): 99–100. http://dx.doi.org/10.4161/psb.2.2.3614.

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Roterman, Irena, Mateusz Banach, and Leszek Konieczny. "Antifreeze proteins." Bioinformation 13, no. 12 (December 31, 2017): 400–401. http://dx.doi.org/10.6026/97320630013400.

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Glomset, John A., Michael H. Gelb, and Christopher C. Farnsworth. "Geranylgeranylated proteins." Biochemical Society Transactions 20, no. 2 (May 1, 1992): 479–84. http://dx.doi.org/10.1042/bst0200479.

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DECLERCQ, JEROEN, KAREN HENSEN, WIM J. VAN DE VEN, and MARCELA CHAVEZ. "PLAG Proteins." Annals of the New York Academy of Sciences 1010, no. 1 (December 2003): 264–65. http://dx.doi.org/10.1196/annals.1299.045.

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Anderson, Alexandra, and Rachel McMullan. "G-proteins." Worm 1, no. 4 (October 2012): 196–201. http://dx.doi.org/10.4161/worm.20466.

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Journal articles on the topic 'Proteins'

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