Relevant bibliographies by topics / Proteins

Academic literature on the topic 'Proteins'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 June 2024

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Contents

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

Journal articles on the topic "Proteins":

1

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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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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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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You might also be interested in the extended bibliographies on the topic 'Proteins' for particular source types:
Journal articles Dissertations / Theses Books

Dissertations / Theses on the topic "Proteins":

1

Gill, Katrina Louise. "Protein-protein interactions in membrane proteins." Thesis, University of Newcastle Upon Tyne, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.400016.

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Stylianou, Julianna. "Protein-protein interaction of HSV-1 tegument proteins." Thesis, Imperial College London, 2013. http://hdl.handle.net/10044/1/24663.

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Herpes simplex virus type 1 virions contain a proteinaceous layer between the nucleocapsid and the virus envelope termed the tegument. The mechanism underlying tegumentation remains largely undefined for all herpesviruses, as does the role of many tegument proteins in virus replication. The networks of protein interactions involved in virus assembly have been largely explored and although large-scale studies have been carried out using yeast two hybrid analyses of herpesvirus protein interactions, few of the identified networks have been validated in infected cells. Here, the molecular interactions that occur between the major tegument proteins VP22, VP16 and VP13/14 and a range of glycoproteins and tegument proteins were defined in detail. Two alternative studies were performed from infected cells, however one based on the purification of GFP-tagged proteins and their protein partners proved more successful. These studies validated previous findings and also identified VP13/14, UL21, UL16 and vhs as novel binding partners of VP22, and VP22, UL21, UL16 and vhs as novel binding partners of VP13/14. Thus, these results have led to the identification of two discrete tegument protein complexes in the infected cell: VP22-VP16-VP13/14-vhs and VP22-VP13/14-UL21-UL16. To investigate the nature of the VP22-VP16-VP13/14-vhs complex in more detail, a number of techniques were used and showed that VP22 and VP13/14 both bind directly to the C-terminus of VP16, but were unable to interact with each other. As anticipated from other studies on transfected cell extracts, vhs was shown to be incorporated into this complex by virtue of its direct binding to VP16 during infection, and did not have the capacity to interact directly with VP22. This work has established a defined network of protein-protein interactions encompassing over one third of tegument proteins, and will improve our understanding of the wider protein interaction networks that lead to the assembly of the herpesvirus tegument.
3

Pateman, Cassandra Sophie Catherine. "RGS proteins and G protein signalling." Thesis, University of Warwick, 2002. http://wrap.warwick.ac.uk/2367/.

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The work within this thesis is concerned with the creation of a temperature-sensitive Schizosaccharomyces pombe marker protein, and the regulation of the pheromone communication system of Sz. pombe reporter strains by RGS proteins. There are a limited number of marker proteins available for use in the genetic manipulation of Sz. pombe, and the generation of a temperature-sensitive Ura4p was envisaged to expand the scope of carrying out sequential gene disruptions in the fission yeast. PCR-based mutagenesis was used to introduce mutations in the ura4 cassette, and a leucine to proline mutation identified at residue 261 in the ura4 open reading frame conferred a temperature-sensitive requirement for uracil. To demonstrate the use of the Ura4sp marker in gene disruption, the Sz. pombe irpl gene was disrupted with the ura4u cassette, and subsequently, the prkl gene was disrupted with the wild-type ura4 cassette. RGS proteins are a recently discovered family of proteins that negatively regulate G protein-coupled signalling pathways. This thesis describes the ability of mammalian RGS proteins to regulate the pheromone communication system of Sz. pombe reporter strains. Human RGS 1 and human RGS4 displayed the greatest ability to negatively regulate the Sz. pombe pheromone signalling pathway when expressed from multicopy expression vectors. Human RGS2, human RGS3, human RGS9-2 and murine RGS2 displayed lesser, varying abilities. Expression of human RGS 1 from single copy reduced signalling at low pheromone concentrations. Expression of human RGS4 from single copy was incapable of reducing pheromone-independent and pheromone-dependent signalling. This thesis also describes the search for gain-of-function RGS proteins. Two potential gain-of-function szRgslp mutants were previously identified, and these mutants were recreated. The two mutations identified (histidine to arginine at szRgslp residue 171 and valine to isoleucine at szRgslp residue 305) conferred gain-of-function szRgslp phenotypes in an sxa2:: ura4 reporter strain. Hydroxylamine treatment of the human RGS4 open reading frame resulted in the identification of a potential gain-of-function RGS4 mutant. The lysine to arginine mutation at huRGS4p residue 20 conferred a gain-of-function huRGS4p phenotype in an sxa2:: ura4 reporter strain.
4

Nauli, Sehat. "Folding kinetics and redesign of Peptostreptococcal protein L and G /." Thesis, Connect to this title online; UW restricted, 2003. http://hdl.handle.net/1773/9237.

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Wadahama, Hiroyuki. "Identification and Characterization of Soybean Protein Disulfide Isomerase Family Proteins as Functional Proteins for Folding of Seed-storage Proteins." Kyoto University, 2010. http://hdl.handle.net/2433/120458.

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Kyoto University (京都大学)
0048
新制・課程博士
博士(農学)
甲第15414号
農博第1799号
新制||農||978(附属図書館)
学位論文||H22||N4513(農学部図書室)
27892
京都大学大学院農学研究科食品生物科学専攻
(主査)教授 河田 照雄, 教授 村田 幸作, 教授 井上 國世
学位規則第4条第1項該当
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Sakhawalkar, Neha. "Hub Proteins, Paralogs, and Unknown Proteins in Bacterial Interaction Networks." VCU Scholars Compass, 2017. http://scholarscompass.vcu.edu/etd/4730.

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Proteins are the functional units of cells. However, a major portion of the proteome does not have a known functional annotation. This dissertation explores protein -protein interactions, involving these uncharacterized or unknown function proteins. Initially, protein – protein interactions were tested and analyzed for paralogous proteins in Escherichia coli. To expand this concept further and to get an overview, protein – protein interactions were analyzed using ‘comparative interactomics’ for four pathogenic bacterial species including Escherichia coli, Yersinia pestis, Vibrio cholerae and Staphylococcus aureus. This approach was used to study unknown function protein pairs as well as to focus on uncharacterized hub proteins. The dissertation aims at using protein – protein interactions along with other research data about proteins as a possible approach to narrow down on functions of proteins.
7

Nguyen, Giang Huong. "A functional analysis of the human LPA₁G protein coupled receptor." Thesis, Available online, Georgia Institute of Technology, 2004:, 2004. http://etd.gatech.edu/theses/available/etd-06072004-131304/unrestricted/nguyen%5Fgiang%5Fh%5F200405%5Fms.pdf.

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Ndabambi, Nonkululeko. "Recombinant expression of the pRb- and p53-interacting domains from the human RBBP6 protein for in vitro binding studies." Thesis, University of the Western Cape, 2004. http://etd.uwc.ac.za/index.php?module=etd&amp.

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The aim of this thesis was to produce DNA expression constructs and use them to investigate the feasibility of recombinantly expression proteins for future interaction studies between human RBBP6 and p53 and pRb proteins.
9

Baisden, Joseph M. "AFAP-110 is a cSrc activator." Morgantown, W. Va. : [West Virginia University Libraries], 2003. http://etd.wvu.edu/templates/showETD.cfm?recnum=2766.

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Thesis (Ph. D.)--West Virginia University, 2003.
Title from document title page. Document formatted into pages; contains v, 149 p. : ill. (some col.). Vita. Includes abstract. Includes bibliographical references.
10

Filipponi, Luisa. "New micropatterning techniques for the spatial addressable immobilization of proteins." Australian Digital Thesis Program, 2006. http://adt.lib.swin.edu.au/public/adt-VSWT20060905.113858/index.html.

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Thesis (PhD) - Swinburne University of Technology, Industrial Research Institute Swinburne - 2006.
A thesis submitted in fulfilment of the requirements for the degree of Doctor of Philosophy, Industrial Research Institute Swinburne, Swinburne University of Technology - 2006. Typescript. Includes bibliographical references (p. 184-197).
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Books on the topic "Proteins":

1

B, Biswas B., and Roy Siddhartha, eds. Proteins: Structure, function, and engineering. New York: Plenum, 1995.

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Ki͡aĭvi͡ari͡aĭnen, A. I. Solvent-dependent flexibility of proteins and principles of their function. Dordrecht: D. Reidel, 1985.

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Robson, Barry. Introductionto proteins and protein engineering. Amsterdam: Elsevier, 1988.

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Siddhartha, Roy, and Biswas B. B, eds. Subcellular biochemistry. New York: Plenum, 1995.

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Walsh, Christopher. Posttranslational modification of proteins: Expanding nature's inventory. Englewood, Colo: Roberts and Co. Publishers, 2006.

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Rotheim, Philip. Bioengineered protein drugs: Antibodies, blood proteins. Norwalk, CT: Business Communications Co., 1995.

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Robson, Barry. Introduction to proteins and protein engineering. Amsterdam: Elsevier, 1988.

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Robson, Barry. Introduction to proteins and protein engineering. Amsterdam: Elsevier, 1986.

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Robson, Barry. Introduction to proteins and protein engineering. Amsterdam: Elsevier, 1986.

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B, Vallee Richard, ed. Structural and contractile proteins. Orlando: Academic Press, 1986.

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Book chapters on the topic "Proteins":

1

Kurochkina, Natalya. "Proteins and Protein Structure." In Protein Structure and Modeling, 1–52. Singapore: Springer Singapore, 2019. http://dx.doi.org/10.1007/978-981-13-6601-7_1.

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Buntru, Matthias, Simon Vogel, Ricarda Finnern, and Stefan Schillberg. "Plant-Based Cell-Free Transcription and Translation of Recombinant Proteins." In Recombinant Proteins in Plants, 113–24. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2241-4_8.

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AbstractPlant cell-free lysates contain all the cellular components of the protein biosynthesis machinery, providing an alternative to intact plant cells, tissues, and whole plants for the production of recombinant proteins. Cell-free lysates achieve rapid protein production (within hours or days) and allow the synthesis of proteins that are cytotoxic or unstable in living cells. The open nature of cell-free lysates and their homogeneous and reproducible performance is ideal for protein production, especially for screening applications, allowing the direct addition of nucleic acid templates encoding proteins of interest, as well as other components such as enzyme substrates, chaperones, artificial amino acids, or labeling molecules. Here we describe procedures for the production of recombinant proteins in the ALiCE (Almost Living Cell-free Expression) system, a lysate derived from tobacco cell suspension cultures that can be used to manufacture protein products for molecular and biochemical analysis as well as applications in the pharmaceutical industry.
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Wüthrich, Kurt. "NMR structures of proteins: Improved precision through stereospecific resonance assignments." In Proteins, 3–10. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-010-9063-6_1.

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Garbow, Joel R., and Charles A. McWherter. "The determination of carbon-to-nitrogen distances in melanostatin using 13C, 15N-REDOR NMR spectroscopy." In Proteins, 74–78. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-010-9063-6_10.

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Balasubramaniam, A., S. G. Huang, S. Sheriff, M. Prabhakaran, and V. Renugopalakrishnan. "Solution conformation of neuropeptide Y: 2D NMR and molecular dynamics studies." In Proteins, 79–81. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-010-9063-6_11.

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Deber, Charles M., Guang-Yi Xu, and Barbara J. Sorrell. "Proline residues in bacteriorhodopsin: Conformation and temperature dependence." In Proteins, 82–86. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-010-9063-6_12.

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Shukla, D. R., and Sudha Mahajan. "A magnetic resonance study of solution conformation of Substance P and its N-terminal fragment." In Proteins, 87–95. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-010-9063-6_13.

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Sasidhar, Y. U., M. M. Dhingra, and Anil Saran. "Solution conformation of dermorphin in DMSO: 2D NMR studies." In Proteins, 96–104. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-010-9063-6_14.

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Mosberg, Henry I., and Katarzyna Sobczyk-Kojiro. "An 1H NMR study of HTyr-d-Cys-Phe-d-PenOH (JOM-13), a highly selective ligand for the δ opioid receptor." In Proteins, 105–9. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-010-9063-6_15.

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Havel, Timothy F. "The precision of protein structures determined from NMR data: Reality or illusion?" In Proteins, 110–15. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-010-9063-6_16.

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Conference papers on the topic "Proteins":

1

Kemp, Regina, Kevin Fraser, Kyoko Fujita, Douglas MacFarlane, and Gloria Elliott. "Biocompatible Ionic Liquids: A New Approach for Stabilizing Proteins in Liquid Formulation." In ASME 2008 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2008. http://dx.doi.org/10.1115/sbc2008-192986.

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The stabilization of proteins is a priority for several important fields, most notably the pharmaceutical industry. Protein-based therapeutic drugs have demonstrated significant efficacy in controlling and curing disease. Unlike traditional small molecule-based drug therapies, a major hurdle in the development of protein drugs is the challenge of maintaining the protein in the folded state throughout processing and also during storage at the end point-of-use. When a protein is taken from its native environment, it is often unstable and unfolds. Because the protein’s 3-dimensional structure is responsible for its functional activity, much work has been dedicated to finding excipients that will stabilize proteins outside of their native environment.
2

Munch, Katharina, Claire Berton-Carabin, Karin Schroen, and Simeon Stoyanov. "Plant protein-stabilized emulsions: Implications of protein and non-protein components for lipid oxidation." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/zznf4565.

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The use of plant proteins to stabilize oil-in-water (O/W) emulsions has been an increasing trend lately. The complexity of the available plant protein ingredients, along with the proteins’ physicochemical properties, require advanced processing that typically leads to substantial concentrations of non-protein components in the final isolates or concentrates. It is known that those components, such as polyphenols, phytic acid or phospholipids, can have a strong influence on the oxidative stability of emulsions. Thus, to understand the oxidative stability of plant protein-stabilized emulsions, the influence of the non-protein components also needs to be considered. Many food emulsions, such as mayonnaise or infant formula, are stabilized by not only proteins, but also phospholipids. Such an interfacial protein-phospholipid combination can also be found in oleosomes, natural lipid droplets which show a high oxidative stability. This stability has been attributed to their interfacial architecture in which oleosins and phospholipids form a tight physical barrier against pro-oxidant species. However, while the antioxidant properties of proteins are widely reported, the contribution of phospholipids to lipid oxidation in plant protein-based emulsions remains underexplored. In this work, we investigated how mixed interfacial plant proteins and phospholipids may be rationally used to control the oxidative stability of O/W emulsions. The interfacial composition was modulated by varying the ratio between pea proteins and sunflower phosphatidylcholine (PC) while keeping the total concentration of pea proteins constant. Increasing the phospholipid-to-protein ratio led to a monotonic decrease in the concentration of proteins and an increase of phospholipids at the interface, while the oxidative stability of those O/W emulsions changed in a non-monotonic pattern. The results were put in perspective by embedding them in a context of reviewing the potential implications of typical components in plant protein ingredients on lipid oxidation.
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Lamsal, Buddhi, and Bibek Byanju. "Processing opportunities and challenges for plant-based proteins." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/cjmp7212.

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With demand for nutritious and functional protein-rich ingredients rising, there are opportunities to acquire protein from new/ emerging sources, as well as from coproducts of agro-food industry. Some of these sources include plants/ seeds and oilseeds, microalgae, fungi, cell/ microbial, and insect protein; however, each of these may have their own unique challenges in terms of extraction, nutritional profile, bioactivity, techno-functional properties, safety, allergenicity as well as in food and feed applications. Some of the challenges for plant/seed proteins are that they have relatively lower extraction yields and relatively inferior functional/ nutritional aspects, including off-flavor and digestibility. Protein quality in defatted meals is also impacted by harsh oil removal process, which is further exacerbated by the downstream protein extraction and isolation conditions (pH, ionic strength, temperature etc.) resulting in protein denaturation, aggregation, and potential loss of functionality. Also, plant proteins have other issues such as off-flavors, astringency/ taste, allergenicity, and antinutritional factors that reduce mineral bioavailability and protein absorption. Various food processing techniques can be used to reduce/ remove these aspects of protein ingredients; fermentation, germination, heating, enzymatic, or acidic treatment, membrane separation etc. have been employed to improve protein purity and quality. The choice of processing technology, even for oil removal from oilseed, impacts protein extraction and quality. For example, protein recovered from meal/ fibers of aqueous oil extraction were of better quality than from desolventized meals. Emerging physical and biochemical processes, such as high-power sonication, extrusion, high-pressure processing, microwave, pulsed electric field, enzymatic pretreatment (pectinase, proteinase, carbohydrase), and fermentation are reported to increase protein extraction efficiency, removing/ reducing allergenicity, and modify functional characteristics. This presentation will discuss such processing challenges and opportunities for plant-based proteins for extraction and downstream isolation, as well as their impact on important functional characteristics.
4

Hu, Jing, and Yihang Du. "Predicting Moonlighting Proteins from Protein Sequence." In 14th International Conference on Bioinformatics Models, Methods and Algorithms. SCITEPRESS - Science and Technology Publications, 2023. http://dx.doi.org/10.5220/0011782300003414.

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Zhou, Hualu, Giang Vu, and David J. McClements. "Rubisco Proteins as Plant-based Alternatives to Egg White Proteins: Characterization of Thermal Gelation Properties." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/vamx3998.

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RuBisCO proteins can be isolated from abundant and sustainable plant sources, such as duckweed (e.g., Lemnoideae). These plant-based globular proteins are capable of irreversibly unfolding and forming gels when heated, which means they may be able to mimic some of the functional attributes exhibited by animal globular proteins. In this study, we examined the ability of RuBisCo proteins to mimic the initial rheology and thermal gelation properties of egg white, which the aim of developing plant-based egg analogs. The impact of protein concentration (10-15% w/w), pH (7 to 9), and calcium concentration (0 to 50 mM CaCl2) on the properties of the egg white analogs was examined. The appearance (colorimetry), thermal denaturation (differential scanning calorimetry), thermal gelation (dynamic shear rheology), and texture profiles (compression testing) were measured. RuBisCO-based egg white analogs could be successfully produced at 10% protein content and pH 8 in the absence of salt. These RuBisCO protein solutions had similar apparent viscosity-shear rate profiles, shear modulus-temperature profiles, gelling temperatures, and final gel strengths as egg white. However, there were some differences. RuBisCO protein gels were slightly darker than egg white, which was attributed to the presence of some phenolic impurities. RuBisCo protein exhibited a single thermal transition temperature (~ 66 ℃) whereas egg white exhibited two (~66 and ~81 ℃). RuBisCo protein gels were more brittle but less chewy and resilient than egg white gels. This study provides valuable insights into the potential of RuBisCo protein for formulating plant-based egg white analogs, which may help improve the sustainability of the modern food supply.
6

Samarawickrama, O., R. Jayatillake, and D. Amaratunga. "Identifying Proteins Associated with Disease Severity." In SLIIT INTERNATIONAL CONFERENCE ON ADVANCEMENTS IN SCIENCES AND HUMANITIES [SICASH]. Faculty of Humanities and Sciences, SLIIT, 2022. http://dx.doi.org/10.54389/eegc3170.

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Proteomic studies or studies of protein expression levels are growing swiftly with the steady improvement in technology and knowledge on understanding various anomalies affecting humans. Since differentially expressed proteins have an influence on overall cell functionality, this improves discrimination between healthy and diseased states. Identifying prime proteins offers prospective insights for developing optimized and targeted treatment methods. This research involves analyzing data from an early-stage study whose main purpose was to identify differentially expressed proteins. The presence of 3 progressively serious states of disease (healthy to mild to severe) escalates the importance of this study because there is not much research literature that considers ordinal outcomes in studies of this nature. The analysis can be segregated into 2 stages, univariate and multiprotein analysis. Approach of the univariate analysis was to implement continuation ratio model considering one protein at a time to pick those that exhibits potential ordinality. Penalized continuation ratio model using lasso regularization incorporated with bootstrapping proteins was performed as the next stage to identify protein combinationsthat perform well together. Compound results of the univariate and multi-protein analysis identified 20 most dominant proteins that have the capability to discriminate between the disease states in an ordinal manner satisfactorily. Keywords: Proteomic studies; Ordinal nature; Trend tests; Lasso regularization; Bootstrapping
7

Luo, Fei, Ondrej Halgas, Pratish Gawand, and Sagar Lahiri. "Animal-free protein production using precision fermentation." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/ntka8679.

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The $1.4 trillion animal industry could not sustainably scale further to feed the next billion population, as it is resource intensive, and heavy in greenhouse gas emission. The recent plant-based food movement has provided solution for more sustainable protein sources. However, the plant-based food sector faces challenges in reaching parity in texture, sensory experience (mouthfeel) and nutritional value as animal products, limiting their potential of reaching beyond the vegan and flexitarian consumers. The technical challenge behind this problem is that proteins from plants have intrinsically different amino acid compositions and structures from animal proteins, making it challenging to emulate the properties of animal products using plant-proteins alone. There is a clear and underserved need for novel protein ingredients that can complement plant-based protein ingredients to achieve parity of animal products. Fermentation is considered the third pillar of alternative protein revolution. At Liven, we focus our efforts on developing precision fermentation technology to produce functional protein ingredients that are natural replica of animal proteins. Using engineering biology, we transforms microorganisms with genes that are responsible for producing animal proteins such as collagen and gelatin. The transformed microorganisms are cultivated in fermenters to produce proteins from plant-based raw-materials. Since the protein produced are have identical amino acid sequences and structure as proteins that would be derived from animals, they provide the desired texture and sensory characteristics currently missing in plant-based formulations. For instance, our animal-free gelatin provides the functionality of thermally reversible gel. As our protein ingredients provides functionality and nutrition value of animal proteins, these ingredients could complement plant-based protein ingredients to deliver alt-protein food formulations more accurately emulate animal products, expand the market acceptance of alt-protein foods to mass consumers.
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Swasti, Olivia, Alhadi Bustamam, Dian Lestari, and Wibowo Mangunwardoyo. "Biclustering protein interactions between HIV-1 proteins and humans proteins using LCM-MBC algorithm." In PROCEEDINGS OF THE SYMPOSIUM ON BIOMATHEMATICS (SYMOMATH) 2018. Author(s), 2019. http://dx.doi.org/10.1063/1.5094279.

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Sodnomov, T. C., and I. A. Kutyrev. "STUDY ON POTENTIAL IMMUNOREGULATORY PROTEINS IN THE EXCRETORY-SECRETORY PRODUCTS OF CESTODES." In THEORY AND PRACTICE OF PARASITIC DISEASE CONTROL. VNIIP – FSC VIEV, 2024. http://dx.doi.org/10.31016/978-5-6050437-8-2.2024.25.388-393.

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This article studied excretory-secretory products of parasitic flatworms aimed at searching for potential immunoregulatory proteins. Immunoregulatory proteins are poorly studied at the moment. Recent years have showed increased interest in identifying immunoregulatory molecules produced by parasitic worms. Potential immunoregulatory proteins will make a significant contribution to the development of medicine and biotechnology and will make it possible to effectively treat allergic and other autoimmune diseases. The study used methods of bioinformatics, proteomics, and transcriptomics. Potential immunoregulatory proteins were identified in the Ligula interrupta secretome proteins and listed. Each protein was analyzed for possible immunoregulatory functions in the parasite-host system. Based on identification data of SEP proteins using parasite transcriptomes, annotation of secretome proteins (SEP) was made in the NCBI and Swissprot international databases. A table was compiled with identified potential immunoregulatory proteins. A functional analysis of each protein was performed. Protein functions were determined based on analysis of scientific articles, patents and publications. By comparing different proteins, it is possible to identify those that are similar in domain structure, phylogeny, and description. The discovered potential immunoregulatory proteins will make a significant contribution to the development of medicine and biotechnology and will make it possible to effectively treat allergic and other autoimmune diseases.
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Tirtom, Sena, and Aslı Akpınar. "Dairy Protein vs. Plant Protein and Their Consumer Perception." In 7th International Students Science Congress. Izmir International guest Students Association, 2023. http://dx.doi.org/10.52460/issc.2023.026.

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Proteins are crucial macronutrient for human health. Animal, dairy, and some plant proteins are considered high-quality proteins that provide health and metabolic benefits based on the digestible levels of essential amino acids they contain. Animal protein is rich in many essential amino acids, but excessive animal protein intake greatly increases fat intake. Therefore, due to the improvement in people's living standards and increase in protein intake, the animal protein supply is not sufficient to meet the increasing demand of people. Technologically, milk proteins are the most important component of milk due to their unique properties that allow milk to be converted into a wide range of products such as cheese or yoghurt quite easily. It is widely accepted that dairy products are excellent sources of highly digestible essential amino acids. Nowadays, plant protein is preferred because has advantages such as it is an abundant source, cheap, easy to obtain, preferred by special consumer groups such as vegan/vegetarian, does not contain cholesterol and preventing diseases. In the last decades, the increasing interest of both producers and consumers in plant proteins and the decrease in animal protein intake and inclination to plant protein intake with the innovations in the markets emphasize the importance of these alternative sources. In this review, information is given about the importance of milk proteins and plant proteins and the role they play in consumer preference is mentioned.

Reports on the topic "Proteins":

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Herman, Eliot D., Gad Galili, and Alan Bennett. Recognition and Disposal of Misfolded Seed Proteins. United States Department of Agriculture, August 1994. http://dx.doi.org/10.32747/1994.7568791.bard.

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This project was directed at determining mechanisms involved in storage of intrinsic and foreign storage proteins in seeds. Seeds constitute the majority of direct and indirect food. Understanding how seeds store proteins is important to design approaches to improve the quality of seed proteins through biotechnology. In the Israeli part of this project we have conducted investigations to elucidate the mechanisms involved in assembling wheat storage proteins into ER-derived protein bodies. The results obtained have shown how domains of storage protein molecules are critical in the assembly of protein bodies. In the US side of this project the fate of foreign and engineered proteins expressed in seeds has been investigated. Engineering seed proteins offers the prospect of improving the quality of crops. Many foreign proteins are unstable when expressed in transgenic seeds. The results obtained have demonstrated that sequestering foreign proteins in the ER or ER-derived protein bodies stabilizes the proteins permitting their accumulation. The collaboration conducted in this project has advanced the understanding how protein bodies are assembled and the potential to use the ER and protein bodies to store engineered proteins that can enhance the composition of seeds.
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Matthews, Lisa, Guanming Wu, Robin Haw, Timothy Brunson, Nasim Sanati, Solomon Shorser, Deidre Beavers, Patrick Conley, Lincoln Stein, and Peter D'Eustachio. Illuminating Dark Proteins using Reactome Pathways. Reactome, October 2022. http://dx.doi.org/10.3180/poster/20221027matthews.

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Diseases are often the consequence of proteins or protein complexes that are non-functional or that function improperly. An active area of research has focused on the identification of molecules that can interact with defective proteins and restore their function. While 22% percent of human proteins are estimated to be druggable, less than fifteen percent are targeted by FDA-approved drugs, and the vast majority of untargeted proteins are understudied or so-called "dark" proteins. Elucidation of the function of these dark proteins, particularly those in commonly drug-targeted protein families, may offer therapeutic opportunities for many diseases. Reactome is the most comprehensive, open-access pathway knowledgebase covering 2585 pathways and including 14246 reactions, 11088 proteins, 13984 complexes, and 1093 drugs. Placing dark proteins in the context of Reactome pathways provides a framework of reference for these proteins facilitating the generation of hypotheses for experimental biologists to develop targeted experiments, unravel the potential functions of these proteins, and then design drugs to manipulate them. To this end, we have trained a random forest with 106 protein/gene pairwise features collected from multiple resources to predict functional interactions between dark proteins and proteins annotated in Reactome and then developed three scores to measure the interactions between dark proteins and Reactome pathways based on enrichment analysis and fuzzy logic simulations. Literature evidence via manual checking and systematic NLP-based analysis support predicted interacting pathways for dark proteins. To visualize dark proteins in the context of Reactome pathways, we have also developed a new website, idg.reactome.org, by extending the Reactome web application with new features illustrating these proteins together with tissue-specific protein and gene expression levels and drug interactions.
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Martin, Shawn Bryan, Kenneth L. Sale, Jean-Loup Michel Faulon, and Diana C. Roe. Developing algorithms for predicting protein-protein interactions of homology modeled proteins. Office of Scientific and Technical Information (OSTI), January 2006. http://dx.doi.org/10.2172/883467.

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Barakat, Dr Shima, Dr Samuel Short, Dr Bernhard Strauss, and Dr Pantea Lotfian. https://www.food.gov.uk/research/research-projects/alternative-proteins-for-human-consumption. Food Standards Agency, June 2022. http://dx.doi.org/10.46756/sci.fsa.wdu243.

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The UK is seeing growing interest in alternative protein sources to traditional animal-based proteins such as beef, lamb, pork, poultry, fish, eggs, and dairy. There is already an extensive market in alternative protein materials, however, technological advances combined with the pressure for more sustainable sources of protein has led to an acceleration of innovation and product development and the introduction of a large amount of new alternative protein ingredients and products to the market. These have the potential to dramatically impact on the UK food system. This report is a combination of desk research, based on thorough review of the academic and non-academic literature and of the alternative proteins start-up scene, and presents an analysis of the emerging market for alternative proteins, the potential implications and the potential policy responses that the FSA might need to consider. Four main categories of alternative proteins are presented and reviewed in this report: Plant-based meat substitutes Novel protein sources Proteins and biomass biosynthesised by microorganisms Cultured meat
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Chen, Junjie. Cellular Proteins Interacting with the Tumor Suppressor Protein p53. Fort Belvoir, VA: Defense Technical Information Center, August 1996. http://dx.doi.org/10.21236/ada316821.

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Chen, Junjie, and Anindya Dutta. Cellular Proteins Interacting with the Tumor Suppressor Protein p53. Fort Belvoir, VA: Defense Technical Information Center, August 1997. http://dx.doi.org/10.21236/ada333509.

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Chen, Junjie. Cellular Proteins Interacting with the Tumor Suppressor Protein p53. Fort Belvoir, VA: Defense Technical Information Center, July 1995. http://dx.doi.org/10.21236/ada305736.

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Banai, Menachem, and Gary Splitter. Molecular Characterization and Function of Brucella Immunodominant Proteins. United States Department of Agriculture, July 1993. http://dx.doi.org/10.32747/1993.7568100.bard.

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The BARD project was a continuation of a previous BARD funded research project. It was aimed at characterization of the 12kDa immunodominant protein and subsequently the cloning and expression of the gene in E. coli. Additional immunodominant proteins were sought among genomic B. abortus expression library clones using T-lymphocyte proliferation assay as a screening method. The 12kDa protein was identified as the L7/L12 ribosomal protein demonstrating in the first time the role a structural protein may play in the development of the host's immunity against the organism. The gene was cloned from B. abortus (USA) and B. melitensis (Israel) showing identity of the oligonucleotide sequence between the two species. Further subcloning allowed expression of the protein in E. coli. While the native protein was shown to have DTH antigenicity its recombinant analog lacked this activity. In contrast the two proteins elicited lymphocyte proliferation in experimental murine brucellosis. CD4+ cells of the Th1 subset predominantly responded to this protein demonstrating the development of protective immunity (g-IFN, and IL-2) in the host. Similar results were obtained with bovine Brucella primed lymphocytes. UvrA, GroE1 and GroEs were additional Brucella immunodominant proteins that demonstrated MHC class II antigenicity. The role cytotoxic cells are playing in the clearance of brucella cells was shown using knock out mice defective either in their CD4+ or CD8+ cells. CD4+ defective mice were able to clear brucella as fast as did normal mice. In contrast mice which were defective in their CD8+ cells could not clear the organisms effectively proving the importance of this subtype cell line in development of protective immunity. The understanding of the host's immune response and the expansion of the panel of Brucella immunodominant proteins opened new avenues in vaccine design. It is now feasible to selectively use immunodominant proteins either as subunit vaccine to fortify immunity of older animals or as diagnostic reagents for the serological survaillance.
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Bercovier, Herve, Raul Barletta, and Shlomo Sela. Characterization and Immunogenicity of Mycobacterium paratuberculosis Secreted and Cellular Proteins. United States Department of Agriculture, January 1996. http://dx.doi.org/10.32747/1996.7573078.bard.

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Our long-term goal is to develop an efficient acellular vaccine against paratuberculosis based on protein antigen(s). A prerequisite to achieve this goal is to analyze and characterize Mycobacterium paratuberculosis (Mpt) secreted and cellular proteins eliciting a protective immune response. In the context of this general objective, we proposed to identify, clone, produce, and characterize: the Mpt 85B antigen and other Mpt immunoreactive secreted proteins, the Mpt L7/L12 ribosomal protein and other immunoreactive cellular proteins, Mpt protein determinants involved in invasion of epithelial cells, and Mpt protein antigens specifically expressed in macrophages. Paratuberculosis is still a very serious problem in Israel and in the USA. In the USA, a recent survey evaluated that 21.6% of the dairy herd were infected with Mpt resulting in 200-250 million dollars in annual losses. Very little is known on the virulence factors and on protective antigens of Mpt. At present, the only means of controlling this disease are culling or vaccination. The current vaccines do not allow a clear differentiation between infected and vaccinated animals. Our long-term goal is to develop an efficient acellular paratuberculosis vaccine based on Mpt protein antigen(s) compatible with diagnostic tests. To achieve this goal it is necessary to analyze and characterize secreted and cellular proteins candidate for such a vaccine. Representative Mpt libraries (shuttle plasmid and phage) were constructed and used to study Mpt genes and gene products described below and will be made available to other research groups. In addition, two approaches were performed which did not yield the expected results. Mav or Mpt DNA genes that confer upon Msg or E. coli the ability to invade and/or survive within HEp-2 cells were not identified. Likewise, we were unable to characterize the 34-39 kDa induced secreted proteins induced by stress factors due to technical difficulties inherent to the complexity of the media needed to support substantial M. pt growth. We identified, isolated, sequenced five Mpt proteins and expressed four of them as recombinant proteins that allowed the study of their immunological properties in sensitized mice. The AphC protein, found to be up regulated by low iron environment, and the SOD protein are both involved in protecting mycobacteria against damage and killing by reactive oxygen (Sod) and nitrogen (AhpC) intermediates, the main bactericidal mechanisms of phagocytic cells. SOD and L7/L12 ribosomal proteins are structural proteins constitutively expressed. 85B and CFP20 are both secreted proteins. SOD, L7/L12, 85B and CFP20 were shown to induce a Th1 response in immunized mice whereas AphC was shown by others to have a similar activity. These proteins did not interfere with the DTH reaction of naturally infected cows. Cellular immunity provides protection in mycobacterial infections, therefore molecules inducing cellular immunity and preferentially a Th1 pathway will be the best candidate for the development of an acellular vaccine. The proteins characterized in this grant that induce a cell-mediated immunity and seem compatible with diagnostic tests, are good candidates for the construction of a future acellular vaccine.
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Yazdidoust, Ladan. Defining Protein Interactions: Ankle Link Proteins of Stereocilia in Hair Cells. Portland State University Library, January 2016. http://dx.doi.org/10.15760/honors.276.

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