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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.
Nawas, Mariam T., Evan J. Walker, Megan B. Richie, Andrew A. White, and Gerald Hsu. "A Protean Protein." Journal of Hospital Medicine 14, no. 2 (February 2019): 117–22. http://dx.doi.org/10.12788/jhm.3102.
Busler, Valerie J., Victor J. Torres, Mark S. McClain, Oscar Tirado, David B. Friedman, and Timothy L. Cover. "Protein-Protein Interactions among Helicobacter pylori Cag Proteins." Journal of Bacteriology 188, no. 13 (July 1, 2006): 4787–800. http://dx.doi.org/10.1128/jb.00066-06.
ABSTRACT Many Helicobacter pylori isolates contain a 40-kb region of chromosomal DNA known as the cag pathogenicity island (PAI). The risk for development of gastric cancer or peptic ulcer disease is higher among humans infected with cag PAI-positive H. pylori strains than among those infected with cag PAI-negative strains. The cag PAI encodes a type IV secretion system that translocates CagA into gastric epithelial cells. To identify Cag proteins that are expressed by H. pylori during growth in vitro, we compared the proteomes of a wild-type H. pylori strain and an isogenic cag PAI deletion mutant using two-dimensional difference gel electrophoresis (2D-DIGE) in multiple pH ranges. Seven Cag proteins were identified by this approach. We then used a yeast two-hybrid system to detect potential protein-protein interactions among 14 Cag proteins. One heterotypic interaction (CagY/7 with CagX/8) and two homotypic interactions (involving H. pylori VirB11/ATPase and Cag5) were similar to interactions previously reported to occur among homologous components of the Agrobacterium tumefaciens type IV secretion system. Other interactions involved Cag proteins that do not have known homologues in other bacterial species. Biochemical analysis confirmed selected interactions involving five of the proteins that were identified by 2D-DIGE. Protein-protein interactions among Cag proteins are likely to have an important role in the assembly of the H. pylori type IV secretion apparatus.
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Kim, J., K. Harter, and A. Theologis. "Protein-protein interactions among the Aux/IAA proteins." Proceedings of the National Academy of Sciences 94, no. 22 (October 28, 1997): 11786–91. http://dx.doi.org/10.1073/pnas.94.22.11786.
Liu, Jun O. "Recruitment of proteins to modulate protein-protein interactions." Chemistry & Biology 6, no. 8 (August 1999): R213—R215. http://dx.doi.org/10.1016/s1074-5521(99)80080-5.
Lin, Hening, and Virginia W. Cornish. "In Vivo Protein-Protein Interaction Assays: Beyond Proteins." Angewandte Chemie International Edition 40, no. 5 (March 2, 2001): 871–75. http://dx.doi.org/10.1002/1521-3773(20010302)40:5<871::aid-anie871>3.0.co;2-s.
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.
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.
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Folkman, Lukas. "Predicting Stability and Functional Changes Induced by Protein Mutations with a Machine Learning Approach." Thesis, Griffith University, 2015. http://hdl.handle.net/10072/367589.
Proteins form a group of one of the most vital macromolecules in living organisms. Yet, even a single mutation in a protein sequence may result in significant changes in protein stability, structure, and thus in protein function as well. Therefore, reliable prediction of stability changes induced by protein mutations is an important aspect of computational protein design, which can aid novel medical and technological discoveries. Also, many mutations have a functional impact which may lead to a disease. Therefore, a key component of personalised medicine is to fully annotate human genetic variations among different individuals. Obviously, it would be infeasible to examine the impact of each possible variant experimentally. Instead, computational methods are needed for a quick and large-scale annotation of genetic variants.
In this thesis, we proposed machine learning methods for predicting stability changes induced by single amino acid substitutions and for detecting disease-causing frameshifting indels (genetic variants caused by short insertions and deletions in the DNA sequence) and nonsense mutations (single nucleotide variants which truncate the protein sequence). The proposed methods can predict the effects of these mutations without the knowledge of the protein structure, which make them applicable universally to all proteins encoded in the human genome. Thesis (PhD Doctorate) Doctor of Philosophy (PhD) School of Information and Communication Technology Science, Environment, Engineering and Technology Full Text
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Li, Wei. "Protein-protein interaction specificity of immunity proteins for DNase colicins." Thesis, University of East Anglia, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.302033.
Wang, Chu. "Improved conformational sampling for protein-protein docking /." Thesis, Connect to this title online; UW restricted, 2007. http://hdl.handle.net/1773/9194.
Sarkar, Mohosin M. "Engineering Proteins with GFP: Study of Protein-Protein Interactions In vivo, Protein Expression and Solubility." The Ohio State University, 2009. http://rave.ohiolink.edu/etdc/view?acc_num=osu1261418776.
Xu, Ping. "Sensing and analyzing unfolded protein response during heterologous protein production :." Access to citation, abstract and download form provided by ProQuest Information and Learning Company; downloadable PDF file, 205 p, 2008. http://proquest.umi.com/pqdweb?did=1555621341&sid=2&Fmt=2&clientId=8331&RQT=309&VName=PQD.
Flöck, Dagmar. "Protein-protein docking and Brownian dynamics simulation of electron transfer proteins." [S.l. : s.n.], 2003. http://deposit.ddb.de/cgi-bin/dokserv?idn=969418736.
Warkentin, Peter H., Ingemar Lundström, and Pentti Tengvall. "Protein—Protein Interactions Affecting Proteins at Surfaces." In ACS Symposium Series, 163–80. Washington, DC: American Chemical Society, 1995. http://dx.doi.org/10.1021/bk-1995-0602.ch012.
Martin, Shawn, W. Michael Brown, and Jean-Loup Faulon. "Using Product Kernels to Predict Protein Interactions." In Protein – Protein Interaction, 215–45. Berlin, Heidelberg: Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/10_2007_084.
Pitre, Sylvain, Md Alamgir, James R. Green, Michel Dumontier, Frank Dehne, and Ashkan Golshani. "Computational Methods For Predicting Protein–Protein Interactions." In Protein – Protein Interaction, 247–67. Berlin, Heidelberg: Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/10_2007_089.
Chan, Catherine S., Tara M. L. Winstone, and Raymond J. Turner. "Investigating Protein–Protein Interactions by Far-Westerns." In Protein – Protein Interaction, 195–214. Berlin, Heidelberg: Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/10_2007_090.
Abu-Farha, Mohamed, Fred Elisma, and Daniel Figeys. "Identification of Protein–Protein Interactions by Mass Spectrometry Coupled Techniques." In Protein – Protein Interaction, 67–80. Berlin, Heidelberg: Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/10_2007_091.
Guan, Hongtao, and Endre Kiss-Toth. "Advanced Technologies for Studies on Protein Interactomes." In Protein – Protein Interaction, 1–24. Berlin, Heidelberg: Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/10_2007_092.
Shin, Sung-Young, Sang-Mok Choo, Sun-Hee Woo, and Kwang-Hyun Cho. "Cardiac Systems Biology and Parameter Sensitivity Analysis: Intracellular Ca2+ Regulatory Mechanisms in Mouse Ventricular Myocytes." In Protein – Protein Interaction, 25–45. Berlin, Heidelberg: Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/10_2007_093.
Beutling, Ulrike, Kai Städing, Theresia Stradal, and Ronald Frank. "Large-Scale Analysis of Protein–Protein Interactions Using Cellulose-Bound Peptide Arrays." In Protein – Protein Interaction, 115–52. Berlin, Heidelberg: Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/10_2008_096.
Zhu, Yonggang, and Barbara E. Power. "Lab-on-a-chip in Vitro Compartmentalization Technologies for Protein Studies." In Protein – Protein Interaction, 81–114. Berlin, Heidelberg: Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/10_2008_098.
Korf, Ulrike, Frauke Henjes, Christian Schmidt, Achim Tresch, Heiko Mannsperger, Christian Löbke, Tim Beissbarth, and Annemarie Poustka. "Antibody Microarrays as an Experimental Platform for the Analysis of Signal Transduction Networks." In Protein – Protein Interaction, 153–75. Berlin, Heidelberg: Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/10_2008_101.
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.
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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Chu, Benjamin, Dean Ho, Hyeseung Lee, Karen Kuo, and Carlo Montemagno. "Protein-Functionalized Proton Exchange Membranes." In ASME 2004 3rd Integrated Nanosystems Conference. ASMEDC, 2004. http://dx.doi.org/10.1115/nano2004-46018.
Protein-functionalized biomimetic membranes, based upon a triblock copolymer simulating a natural lipid bilayer in a single chain, serves as a core technology for applications in bioenergetics. Monolayers of block copolymer, which simulates the hydrophilic-hydrophobic-hydrophilic chain of a natural cell membrane, can be formed by Langmuir-Blodgett (LB) deposition and provides a favorable environment for protein refolding. Large-scale membrane formation is achieved using LB deposition on a variety of substrates, such as gold, quartz, silicon, and Nafion®. We have successfully inserted membrane proteins, such as the light-activated proton pump, bacteriorhodopsin (BR) and the pH/voltage-gateable porin, Outermembrane Protein F (OmpF), into large-area LB monolayers. We have also established sustained protein functionality in films through the measurement of light-activated proton transport.
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Wang, Jianxin, Wei Peng, Yingjiao Chen, Yu Lu, and Yi Pan. "Identifying essential proteins based on protein domains in protein-protein interaction networks." In 2013 IEEE International Conference on Bioinformatics and Biomedicine (BIBM). IEEE, 2013. http://dx.doi.org/10.1109/bibm.2013.6732476.
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.
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.
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Cotton, Therese M., Bernard Rospendowski, Vicki Schlegel, Robert A. Uphaus, Danli L. Wang, Lars Eng, and Marion T. Stankovich. "Spectroscopy of proteins on surfaces: implications for protein orientation and protein-protein interactions." In Moscow - DL tentative, edited by Sergei A. Akhmanov and Marina Y. Poroshina. SPIE, 1991. http://dx.doi.org/10.1117/12.57297.
Walker, F. J. "REGULATION OF THE ANTICOAGULANT ACTIVITY OF ACTIVATED PROTEIN C BY PROTEIN S AND PROTEIN S BINDING PROTEIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642964.
Protein S is a vitamin K-dependent protein that acts as a cofactor for the anticoagulant activity of activated protein C both in the proteolytic inactivation of factor V and VIII. Protein S is a single chain protein with a molecular weight of approximately 62 kDa. When the molecular weight of protein S in plasma was determined it was found to be much larger than the single chain protein. The molecular weight of functional protein S when measured by sedimentation equilibrium with the air-driven ultracentrifuge was observed to be between 115 and 130 kDa. In high salt or in the presence of copper ions this was observed to be reduced to approximately 62 kDa. Frontal analysis of plasma indicated that the functional protein by exist in as many as three molecular weight foras. Gel filtration of radiolabeled protein S also indicates heterogeneity in the molecular weight. In order to isolate the binding protein, bovine plasma was fractionated first on a column of immobilized iminodiacetic acid that had been equilibrated with copper ions. The proteins that eluted in the 0.6 M NaCl wash were passed over a column of protein S immobilized on agarose beads. A single protein was observed to elute from the protein S agarose at high salt. Fractionation of human plasma indicated the presence of several proteins. One major component isolated was C4-binding protein. A second major component has also been isolated that appears to correspond to protein S-binding protein that has been isolated from bovine plasma. When added to plasma depleted of both protein S and the binding protein, the binding protein was observed to enhance the anticoagulant activity of activated protein C only in the presence of protein S. Protein S-binding protein was also observed to enhance the rate of factor Va inactivation by activated protein C and protein S.
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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.
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.
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Bakar, Sakhinah Abu, Javid Taheri, and Albert Y. Zomaya. "Identifying Hub Proteins and Their Essentiality from Protein-protein Interaction Network." In Bioengineering (BIBE). IEEE, 2011. http://dx.doi.org/10.1109/bibe.2011.67.
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.
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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Comp, P. C., and C. T. Esmon. "Defects in the protein C pathway." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643715.
Activated protein C functions as an anticoagulant by enzymatically degrading factors Va and Villa in the clotting cascade. Protein C may be converted to its enzymatically active form bythrombin. The rate at which thrombin cleavage of the zymogen occurs is greatly enhanced when thrombin is bound to an endothelial cell receptor protein, thrombomodulin. Activated proteinC has a relatively long half-life in vivo and the formation of activated protein C in response to low level thrombin infusion suggests that the protein C system may provide a feedback mechanism to limit blood clotting. Clinical support for such a physiologic role for activated protein C includes an increased incidence of thrombophlebitis and pulmonary emboli in heterozygous deficient individuals, and severe, often fatal, cutaneous thrombosis in homozygous deficient newborns. A third thrombotic condition associated with protein C deficiency is coumarin induced skin (tissue) necrosis. This localized skin necrosis occurs shortly after the initiation of coumarin therapy and is hypothesized to bedue to the rapid disappearance of protein C activity in the plasma beforean adequate intensity of anticoagulation is achieved. Recent estimates of heterozygous protein C deficiency range as high as 1 in 300 individuals in the general population. Since coumarin compounds are in routine clinical use throughout the world and skin necrosis remains a relatively rare clinical finding, this suggests that factors other than protein C deficiency alone may be involved in the pathogenesis of the skin necrosis.The anticoagulant properties of activated protein C are greatly enhanced by another vitamin K-dependent plasma protein, protein S. Protein S functions by increasing the affinity of activated protein C for cell surfaces.Protein S is found in two forms in plasma: free and in complex with C4b-binding protein, "an inhibitor of the complement system. Free protein S is functionally active and the complexed protein S is not active. Individuals congenitally deficient in protein S ae subject to recurrent thromboembolicevents. At least two classes of protin S deficiency occur.Some patienshavedecreased levels of protein S antigen and reduced protein S functional activity. A second group of deficient individuals have normal levels of protein S antigen but most or all their protein S is complexed to C4b-binding protein and they have little or no functional protein S activity. Such a protein S distribution could result from abnormal forms of protein S or C4b-binding protein or some other abnormal plasma or cellular component. Patients with functionally inactive forms of protein S have yet to be identified. Identification of protein S deficient individuals is complicated by thepossible effect of sex hormones on plasma protein S levels. Total protein S antigen is reduced during pregnancyand during oral contraceptive administration. This finding is of practicalclinical importance since the decrease in protein S which occurs during pregnancy may be an added risk factor for congenitally protein S deficient women and may explain why some proteinS deficient women experience their first episode of thrombosis during pregnancy.In addition to having anticoagulant properties, activated protein C enhances fibrinolysis, at least in part,by inhibiting the inhibitor of tissueplasminogen activator. This profibrinolytic effect is enhanced by protein S and cell surfaces. This protection of plasminogen activator activity suggests that the combination of tissue plasminogen activator and activated protein C may be useful in the treatment of coronary artery thrombi. Tissueplasminogen activator would promote clot lysis while activated protein C protected the plasminogen activatorfrom inhibition and also prevented further clot deposition. There is no evidence at present that fibrinolytic activity is reduced in protein C deficient individuals. The possible clinical relevance of this aspect of protein Cfunction in the predisposition of protein C deficient individuals to thrombosis remains to be defined.
Reports on the topic "Protein":
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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.
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.
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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Noy, A., T. Sulchek, and R. Friddle. Direct Probing of Protein-Protein Interactions. Office of Scientific and Technical Information (OSTI), March 2005. http://dx.doi.org/10.2172/15015174.
Blackwell, T. K. C-Myc Protein-Protein and Protein-DNA Interactions: Targets for Therapeutic Intervention. Fort Belvoir, VA: Defense Technical Information Center, September 1998. http://dx.doi.org/10.21236/ada371161.
Blackwell, T. K. C-Myc Protein-Protein and Protein-DNA Interactions: Targets for Therapeutic Intervention. Fort Belvoir, VA: Defense Technical Information Center, September 1997. http://dx.doi.org/10.21236/ada344737.
Blackwell, T. K. C-MYC Protein-Protein and Protein-DNA Interactions: Targets for Therapeutic Intervention. Fort Belvoir, VA: Defense Technical Information Center, September 1999. http://dx.doi.org/10.21236/ada381686.
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.
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.
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.
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.
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
