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Journal articles on the topic 'Plant proteins'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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1

Chakraborty, Biswanath. "Plant Defense Proteins." NBU Journal of Plant Sciences 2, no. 1 (2008): 1–12. http://dx.doi.org/10.55734/nbujps.2007.v02i01.001.

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Plants are compelled to withstand stresses of all kinds, be it biotic, abiotic or anthropogenic as a consequence of their immobility. The initial infection process involving adhesion/recognition events between plants and fungal pathogens is essential for the establishment of pathogenesis. The extracellular matrix (ECM) is a biologically active part of the cell surface composed of a complex mixture of macromolecules that, in addition to serving a structural function, profoundly affect the cellular physiology of the organism. During the past two decades it has become evident that the cell wall i

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2

Shewry, P. R. "Plant Storage Proteins." Biological Reviews 70, no. 3 (1995): 375–426. http://dx.doi.org/10.1111/j.1469-185x.1995.tb01195.x.

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3

Graumann, Katja, and David E. Evans. "Plant SUN domain proteins." Plant Signaling & Behavior 5, no. 2 (2010): 154–56. http://dx.doi.org/10.4161/psb.5.2.10458.

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4

Cassab, Gladys I. "PLANT CELL WALL PROTEINS." Annual Review of Plant Physiology and Plant Molecular Biology 49, no. 1 (1998): 281–309. http://dx.doi.org/10.1146/annurev.arplant.49.1.281.

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5

Vercesi, Aníbal Eugênio, Jiri Borecký, Ivan de Godoy Maia, Paulo Arruda, Iolanda Midea Cuccovia, and Hernan Chaimovich. "PLANT UNCOUPLING MITOCHONDRIAL PROTEINS." Annual Review of Plant Biology 57, no. 1 (2006): 383–404. http://dx.doi.org/10.1146/annurev.arplant.57.032905.105335.

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6

Grimes, Howard D., and R. William Breidenbach. "Plant Plasma Membrane Proteins." Plant Physiology 85, no. 4 (1987): 1048–54. http://dx.doi.org/10.1104/pp.85.4.1048.

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7

Grimes, Howard D., Raymond M. Slay, and Thomas K. Hodges. "Plant Plasma Membrane Proteins." Plant Physiology 88, no. 2 (1988): 444–49. http://dx.doi.org/10.1104/pp.88.2.444.

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8

Kandasamy, Muthugapatti K., Roger B. Deal, Elizabeth C. McKinney, and Richard B. Meagher. "Plant actin-related proteins." Trends in Plant Science 9, no. 4 (2004): 196–202. http://dx.doi.org/10.1016/j.tplants.2004.02.004.

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9

Kaas, Quentin, and David J. Craik. "NMR of plant proteins." Progress in Nuclear Magnetic Resonance Spectroscopy 71 (May 2013): 1–34. http://dx.doi.org/10.1016/j.pnmrs.2013.01.003.

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10

Deom, C. Michael, Moshe Lapidot, and Roger N. Beachy. "Plant virus movement proteins." Cell 69, no. 2 (1992): 221–24. http://dx.doi.org/10.1016/0092-8674(92)90403-y.

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11

Goodall, Greg, Jonathan Levy, Maria Mieszczak, and Witold Filipowicz. "Plant RNA-binding proteins." Molecular Biology Reports 14, no. 2-3 (1990): 137. http://dx.doi.org/10.1007/bf00360447.

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12

Urrutia, Maria E., John G. Duman, and Charles A. Knight. "Plant thermal hysteresis proteins." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1121, no. 1-2 (1992): 199–206. http://dx.doi.org/10.1016/0167-4838(92)90355-h.

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13

Kuchar, M. "Plant telomere-binding proteins." Biologia plantarum 50, no. 1 (2006): 1–7. http://dx.doi.org/10.1007/s10535-005-0067-9.

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14

Kawakami, Shigeki, and Yuichiro Watanabe. "Plant viruses. Movement proteins of plant viruses." Uirusu 49, no. 2 (1999): 107–18. http://dx.doi.org/10.2222/jsv.49.107.

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15

Curticăpean, Manuela-Claudia. "Plant Aquaporins." Acta Biologica Marisiensis 2, no. 2 (2019): 36–48. http://dx.doi.org/10.2478/abmj-2019-0009.

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Abstract This mini-review briefly presents the main types of plant aquaporins, highlighting their importance for different plant species and for plant cellular functions. Aquaporins (AQPs), families of water channel proteins (WCPs) are transmembrane proteins that are present in prokaryotes, animals, plants, and humans. The plant aquaporins are part of the Major Intrinsic Proteins (MIPs) family which resides in the following plant organs: roots, stems, leaves, flowers, fruits, and seeds. According to the sub-cellular localization, to their sequence homologies and to their phylogenetic distribut

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16

Lawit, Shai J., Heidi M. Wych, Deping Xu, Suman Kundu, and Dwight T. Tomes. "Maize DELLA Proteins dwarf plant8 and dwarf plant9 as Modulators of Plant Development." Plant and Cell Physiology 51, no. 11 (2010): 1854–68. http://dx.doi.org/10.1093/pcp/pcq153.

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17

BURNS, ROBERT A. "Protease Inhibitors in Processed Plant Foods." Journal of Food Protection 50, no. 2 (1987): 161–66. http://dx.doi.org/10.4315/0362-028x-50.2.161.

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Plants contain a wide variety of protein protease inhibitors. However, most is known about the serine protease (trypsin and chymotrypsin) inhibitors found in legumes, particularly soybeans. These inhibitors in unheated legume protein (a) impair the protein's nutritional quality, (b) induce pancreatic hyper-trophy in some but not all experimental animals, (c) enhance the action of chemical pancreatic carcinogens in Wistar rats but not hamsters or mice, (d) are reported to be carcinogenic to the pancreas of Wistar rats and (e) inhibit certain experimental tumors in rats, mice and hamsters. The p

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18

Marangon, Matteo, Simone Vincenzi, and Andrea Curioni. "Wine Fining with Plant Proteins." Molecules 24, no. 11 (2019): 2186. http://dx.doi.org/10.3390/molecules24112186.

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Fining treatments involve the addition of a substance or a mixture to wine, and are generally carried out in order to clarify, stabilize or modify the wine’s organoleptic characteristics. Usually these fining agents will bind the target compound(s) to form insoluble aggregates that are subsequently removed from the wine. The main reasons to perform wine fining treatments are to carry out wine clarification, stabilization and to remove phenolic compounds imparting unwanted sensory characteristics on the wine, which is an operation that often relies on the use of animal proteins, such as casein,

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19

Ma, Kai Kai, Maija Greis, Jiakai Lu, Alissa A. Nolden, David Julian McClements, and Amanda J. Kinchla. "Functional Performance of Plant Proteins." Foods 11, no. 4 (2022): 594. http://dx.doi.org/10.3390/foods11040594.

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Increasingly, consumers are moving towards a more plant-based diet. However, some consumers are avoiding common plant proteins such as soy and gluten due to their potential allergenicity. Therefore, alternative protein sources are being explored as functional ingredients in foods, including pea, chickpea, and other legume proteins. The factors affecting the functional performance of plant proteins are outlined, including cultivars, genotypes, extraction and drying methods, protein level, and preparation methods (commercial versus laboratory). Current methods to characterize protein functionali

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20

Barbosa, Mayck Silva, Bruna da Silva Souza, Ana Clara Silva Sales, et al. "Antifungal Proteins from Plant Latex." Current Protein & Peptide Science 21, no. 5 (2020): 497–506. http://dx.doi.org/10.2174/1389203720666191119101756.

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Latex, a milky fluid found in several plants, is widely used for many purposes, and its proteins have been investigated by researchers. Many studies have shown that latex produced by some plant species is a natural source of biologically active compounds, and many of the hydrolytic enzymes are related to health benefits. Research on the characterization and industrial and pharmaceutical utility of latex has progressed in recent years. Latex proteins are associated with plants’ defense mechanisms, against attacks by fungi. In this respect, there are several biotechnological applications of anti

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21

Evrard, Jean-Luc, Laurent Pieuchot, Jan W. Vos, Isabelle Vernos, and Anne-Catherine Schmit. "Plant TPX2 and related proteins." Plant Signaling & Behavior 4, no. 1 (2009): 69–72. http://dx.doi.org/10.4161/psb.4.1.7409.

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22

Talalaev, O. S. "Plant small heat shock proteins." Biopolymers and Cell 21, no. 5 (2005): 392–99. http://dx.doi.org/10.7124/bc.000701.

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23

Thakur, Nitasha, and Neelam Sharma. "Plant Lectin as defense proteins." Biotech Today : An International Journal of Biological Sciences 5, no. 1 (2015): 25. http://dx.doi.org/10.5958/2322-0996.2015.00004.6.

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24

Moffatt, Barbara, Vanya Ewart, and Ann Eastman. "Cold comfort: plant antifreeze proteins." Physiologia Plantarum 126, no. 1 (2006): 5–16. http://dx.doi.org/10.1111/j.1399-3054.2006.00618.x.

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25

Aguilera-Alvarado, G. Paulina, and Sobeida Sï¿½nchez-Nieto. "Plant Hexokinases are Multifaceted Proteins." Plant and Cell Physiology 58, no. 7 (2017): 1151–60. http://dx.doi.org/10.1093/pcp/pcx062.

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26

Helm, Ricki M. "Allergy to Plant Seed Proteins." Journal of New Seeds 3, no. 3 (2001): 37–60. http://dx.doi.org/10.1300/j153v03n03_02.

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27

Day, Peter R. "The biology of plant proteins." Critical Reviews in Food Science and Nutrition 36, sup001 (1996): 39–47. http://dx.doi.org/10.1080/10408399609527758.

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28

Hwang, Hee-Youn, and Seong-Hee Bhoo. "Photoperiodic Proteins in Plant Cells." Journal of Applied Biological Chemistry 53, no. 3 (2010): 121–25. http://dx.doi.org/10.3839/jabc.2010.023.

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29

Peumans, W. J., and EJM Van Damme. "Lectins as Plant Defense Proteins." Plant Physiology 109, no. 2 (1995): 347–52. http://dx.doi.org/10.1104/pp.109.2.347.

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30

Parate, Vishal R., and Ritika P. Chaudhari. "Study on Plant Based Proteins." International Journal of Innovations in Engineering and Science 9, no. 4 (2024): 110–15. http://dx.doi.org/10.46335/ijies.2024.9.4.21.

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31

Bouché, Nicolas, Ayelet Yellin, Wayne A. Snedden, and Hillel Fromm. "PLANT-SPECIFIC CALMODULIN-BINDING PROTEINS." Annual Review of Plant Biology 56, no. 1 (2005): 435–66. http://dx.doi.org/10.1146/annurev.arplant.56.032604.144224.

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32

Prescott, Andrea. "Plant proteins — an engineer's perspective." Trends in Biotechnology 11, no. 2 (1993): 69–70. http://dx.doi.org/10.1016/0167-7799(93)90126-t.

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33

Jervis, L., and W. S. Pierpoint. "Purification technologies for plant proteins." Journal of Biotechnology 11, no. 2-3 (1989): 161–98. http://dx.doi.org/10.1016/0168-1656(89)90117-x.

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34

Van Engelen, F. "Extracellular proteins in plant embryogenesis." Trends in Genetics 8, no. 1 (1992): 66–70. http://dx.doi.org/10.1016/0168-9525(92)90046-7.

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35

Van Engelen, Fred A., and Sacco C. De Vries. "Extracellular proteins in plant embryogenesis." Trends in Genetics 8, no. 2 (1992): 66–70. http://dx.doi.org/10.1016/0168-9525(92)90352-5.

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36

Y. I. Takinami, Patricia. "Radiation, Plant Proteins and Sustainability." American Journal of Biological and Environmental Statistics 2, no. 4 (2016): 28. http://dx.doi.org/10.11648/j.ajbes.20160204.11.

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37

Hanke, G., C. Bowsher, M. N. Jones, I. Tetlow, and M. Emes. "Proteoliposomes and plant transport proteins." Journal of Experimental Botany 50, no. 341 (1999): 1715–26. http://dx.doi.org/10.1093/jxb/50.341.1715.

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38

Moriyasu, Y., and M. Tazawa. "Plant vacuole degrades exogenous proteins." Protoplasma 130, no. 2-3 (1986): 214–15. http://dx.doi.org/10.1007/bf01276604.

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39

Ahsan, Nagib, Rashaun S. Wilson, and Jay J. Thelen. "Absolute Quantitation of Plant Proteins." Current Protocols in Plant Biology 3, no. 1 (2018): 1–13. http://dx.doi.org/10.1002/cppb.20064.

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40

Reddy, Narendra, and Yiqi Yang. "Thermoplastic films from plant proteins." Journal of Applied Polymer Science 130, no. 2 (2013): 729–38. http://dx.doi.org/10.1002/app.39481.

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41

Jacques, Silke, Bart Ghesquière, Frank Van Breusegem, and Kris Gevaert. "Plant proteins under oxidative attack." PROTEOMICS 13, no. 6 (2013): 932–40. http://dx.doi.org/10.1002/pmic.201200237.

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42

Kreuger, Marc, and Gerrit-Jan van Holst. "Arabinogalactan proteins and plant differentiation." Plant Molecular Biology 30, no. 6 (1996): 1077–86. http://dx.doi.org/10.1007/bf00019543.

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43

Bardani, Eirini, Paraskevi Kallemi, Martha Tselika, Konstantina Katsarou, and Kriton Kalantidis. "Spotlight on Plant Bromodomain Proteins." Biology 12, no. 8 (2023): 1076. http://dx.doi.org/10.3390/biology12081076.

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Bromodomain-containing proteins (BRD-proteins) are the “readers” of histone lysine acetylation, translating chromatin state into gene expression. They act alone or as components of larger complexes and exhibit diverse functions to regulate gene expression; they participate in chromatin remodeling complexes, mediate histone modifications, serve as scaffolds to recruit transcriptional regulators or act themselves as transcriptional co-activators or repressors. Human BRD-proteins have been extensively studied and have gained interest as potential drug targets for various diseases, whereas in plan

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44

Kader, Jean-Claude. "Lipid-transfer proteins: a puzzling family of plant proteins." Trends in Plant Science 2, no. 2 (1997): 66–70. http://dx.doi.org/10.1016/s1360-1385(97)82565-4.

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45

Watanabe, Yuichiro. "Special issue: Plant viruses. Movement proteins of plant viruses." Uirusu 44, no. 1 (1994): 11–17. http://dx.doi.org/10.2222/jsv.44.11.

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46

Kerksick, Chad M., Andrew Jagim, Anthony Hagele, and Ralf Jäger. "Plant Proteins and Exercise: What Role Can Plant Proteins Have in Promoting Adaptations to Exercise?" Nutrients 13, no. 6 (2021): 1962. http://dx.doi.org/10.3390/nu13061962.

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Adequate dietary protein is important for many aspects of health with current evidence suggesting that exercising individuals need greater amounts of protein. When assessing protein quality, animal sources of protein routinely rank amongst the highest in quality, largely due to the higher levels of essential amino acids they possess in addition to exhibiting more favorable levels of digestibility and absorption patterns of the amino acids. In recent years, the inclusion of plant protein sources in the diet has grown and evidence continues to accumulate on the comparison of various plant protei

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47

İsmail, Karakaş. "Plants That Can be Used as Plant-Based Edible Vaccines; Current Situation and Recent Developments." Virology & Immunology Journal 6, no. 3 (2022): 1–10. http://dx.doi.org/10.23880/vij-16000302.

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Among the purposes of genetic engineering technology applications in plants, improving product quality, increasing resistance to harmful organisms and improving agronomic properties, the most important one is the production of drugs, hormones and vaccines for humans and animals (for example, the use of potatoes in cholera vaccines). Today, the use of plants as bioreactors to obtain recombinant proteins from plants has been further developed and accelerated thanks to the developments in plant genetics, molecular biology and biotechnology. Appearing as a concept about a decade ago, plant bioreac

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48

Narváez-Barragán, Delia A., Omar E. Tovar-Herrera, Lorenzo Segovia, Mario Serrano, and Claudia Martinez-Anaya. "Expansin-related proteins: biology, microbe–plant interactions and associated plant-defense responses." Microbiology 166, no. 11 (2020): 1007–18. http://dx.doi.org/10.1099/mic.0.000984.

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Expansins, cerato-platanins and swollenins (which we will henceforth refer to as expansin-related proteins) are a group of microbial proteins involved in microbe-plant interactions. Although they share very low sequence similarity, some of their composing domains are near-identical at the structural level. Expansin-related proteins have their target in the plant cell wall, in which they act through a non-enzymatic, but still uncharacterized, mechanism. In most cases, mutagenesis of expansin-related genes affects plant colonization or plant pathogenesis of different bacterial and fungal species

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49

Maulik, A., A. I. Sarkar, S. Devi, and S. Basu. "Polygalacturonase-inhibiting proteins - leucine-rich repeat proteins in plant defence." Plant Biology 14 (November 1, 2011): 22–30. http://dx.doi.org/10.1111/j.1438-8677.2011.00501.x.

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50

Butkovic, Anamarija, Valerian V. Dolja, Eugene V. Koonin, and Mart Krupovic. "Plant virus movement proteins originated from jelly-roll capsid proteins." PLOS Biology 21, no. 6 (2023): e3002157. http://dx.doi.org/10.1371/journal.pbio.3002157.

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Numerous, diverse plant viruses encode movement proteins (MPs) that aid the virus movement through plasmodesmata, the plant intercellular channels. MPs are essential for virus spread and propagation in distal tissues, and several unrelated MPs have been identified. The 30K superfamily of MPs (named after the molecular mass of tobacco mosaic virus (TMV) MP, the classical model of plant virology) is the largest and most diverse MP variety, represented in 16 virus families, but its evolutionary origin remained obscure. Here, we show that the core structural domain of the 30K MPs is homologous to

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