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Articoli di riviste sul tema "Proteins"

Autore: Grafiati

Pubblicato: 4 giugno 2021

Ultima modifica: 25 luglio 2025

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1

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

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2

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 (2023): 168–73. https://doi.org/10.5281/zenodo.7925188.

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Abstract (sommario):

Phytal proteins are of great importance as they exhibit unique characteristics as immune modulators. <em>Zingiber zerumbet</em> 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 o

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3

Thorp, H. Holden. "Proteins, proteins everywhere." Science 374, no. 6574 (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 co

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4

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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5

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

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6

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 (2009): 110–21. http://dx.doi.org/10.1111/j.1439-0272.1990.tb02077.x.

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7

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

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8

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 (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

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9

Lan, Nan, Hanxing Zhang, Chengcheng Hu, et al. "Coordinated and Distinct Functions of Velvet Proteins in Fusarium verticillioides." Eukaryotic Cell 13, no. 7 (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

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10

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

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11

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

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12

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

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13

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

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14

Eklund, Hans, and T. Alwyn Jones. "Proteins." Current Opinion in Structural Biology 5, no. 6 (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 (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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16

Rukes, Verena. "Nanopore Technology: When Proteins Analyse Proteins." CHIMIA 79, no. 4 (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,

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17

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 (2010): 21–26. https://doi.org/10.5281/zenodo.1438292.

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<strong>ABSTRACT:</strong> 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 cons

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18

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 (2023): 61–66. https://doi.org/10.5281/zenodo.8079824.

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<strong>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

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19

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, et al. "Tráfico vesicular, un viaje épico de las proteínas hacia la membrana." Alianzas y Tendencias BUAP 7, no. 28 (2022): 1–38. https://doi.org/10.5281/zenodo.7238038.

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<strong>RESUMEN</strong> 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 se

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22

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, an

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23

Jeffery, Constance J. "An introduction to protein moonlighting." Biochemical Society Transactions 42, no. 6 (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 per

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24

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 (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 me

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25

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

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26

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

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27

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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28

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

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29

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

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30

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

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Abstract (sommario):

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,

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31

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 (2012): 471–72. http://dx.doi.org/10.15373/22778179/august2014/150.

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32

Littler, Dene R., Stephen J. Harrop, Sophia C. Goodchild, et al. "The enigma of the CLIC proteins: Ion channels, redox proteins, enzymes, scaffolding proteins?" FEBS Letters 584, no. 10 (2010): 2093–101. http://dx.doi.org/10.1016/j.febslet.2010.01.027.

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33

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 (2021): 843–44. https://doi.org/10.5281/zenodo.4898809.

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<em>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.</em>

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34

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 (2021): 976–80. https://doi.org/10.5281/zenodo.4902822.

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Abstract (sommario):

<em>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.</em>

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35

Borgese, N., S. Brambillasca, P. Soffientini, M. Yabal, and M. Makarow. "Biogenesis of tail-anchored proteins." Biochemical Society Transactions 31, no. 6 (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 e

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36

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 (2020): 7–19. http://dx.doi.org/10.46619/ijcmi.2020.1024.

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37

Hung, Kuo-Wei, Chun-Chia Cheng, Yi-Chao Lin, et al. "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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38

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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Abstract (sommario):

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

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39

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

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40

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

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41

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

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42

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

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43

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

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44

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

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Abstract (sommario):

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 prote

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45

Mudgil, Yashwanti, and Alan M. Jones. "NDR proteins." Plant Signaling & Behavior 5, no. 8 (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 (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 (2017): 400–401. http://dx.doi.org/10.6026/97320630013400.

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48

Glomset, John A., Michael H. Gelb, and Christopher C. Farnsworth. "Geranylgeranylated proteins." Biochemical Society Transactions 20, no. 2 (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 (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 (2012): 196–201. http://dx.doi.org/10.4161/worm.20466.

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