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Relevant bibliographies by topics / Protein synthesis

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Academic literature on the topic 'Protein synthesis'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 May 2024

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Journal articles on the topic "Protein synthesis"

1

Metanis, Norman, Reem Mousa, and Post Reddy. "Chemical Protein Synthesis through Selenocysteine Chemistry." Synlett 28, no. 12 (March 21, 2017): 1389–93. http://dx.doi.org/10.1055/s-0036-1588762.

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Methods for the preparation of small-to-medium-sized proteins by chemical protein synthesis have matured in recent years and proven valuable for protein science. Thanks to the many recent discoveries and developments in the field, proteins up to 300 amino acids can now be prepared in the lab in a matter of days. This technology gives the scientists the flexibility to substitute any atom in the protein sequence; hence synthesis is not constrained to the 20 canonical amino acids. In this Synpacts article we briefly highlight the recent studies on selenocysteine chemistry in the field of chemical protein synthesis.1 Introduction2 Selenocysteine in Nature and in Folding Studies3 Selenocysteine in Protein Synthesis4 Selenocysteine in Natural Selenoproteins5 Outlook

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Franklin, James L., and Eugene M. Johnson. "Control of Neuronal Size Homeostasis by Trophic Factor–mediated Coupling of Protein Degradation to Protein Synthesis." Journal of Cell Biology 142, no. 5 (September 7, 1998): 1313–24. http://dx.doi.org/10.1083/jcb.142.5.1313.

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We demonstrate that NGF couples the rate of degradation of long-lived proteins in sympathetic neurons to the rate of protein synthesis. Inhibiting protein synthesis rate by a specific percentage caused an almost equivalent percentage reduction in the degradation rate of long-lived proteins, indicating nearly 1:1 coupling between the two processes. The rate of degradation of short-lived proteins was unaffected by suppressing protein synthesis. Included in the pool of proteins that had increased half-lives when protein synthesis was inhibited were actin and tubulin. Both of these proteins, which had half-lives of several days, exhibited no degradation over a 3-d period when protein synthesis was completely suppressed. The half-lives of seven other long-lived proteins were quantified and found to increase by 84–225% when protein synthesis was completely blocked. Degradation–synthesis coupling protected cells from protein loss during periods of decreased synthesis. The rate of protein synthesis greatly decreased and coupling between degradation and synthesis was lost after removal of NGF. Uncoupling resulted in net loss of cellular protein and somatic atrophy. We propose that coupling the rate of protein degradation to that of protein synthesis is a fundamental mechanism by which neurotrophic factors maintain homeostatic control of neuronal size and perhaps growth.

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Tang, Shao Jun, and Erin M. Schuman. "Protein synthesis in the dendrite." Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 357, no. 1420 (April 29, 2002): 521–29. http://dx.doi.org/10.1098/rstb.2001.0887.

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In neurons, many proteins that are involved in the transduction of synaptic activity and the expression of neural plasticity are specifically localized at synapses. How these proteins are targeted is not clearly understood. One mechanism is synaptic protein synthesis. According to this idea, messenger RNA (mRNA) translation from the polyribosomes that are observed at the synaptic regions provides a local source of synaptic proteins. Although an increasing number of mRNA species has been detected in the dendrite, information about the synaptic synthesis of specific proteins in a physiological context is still limited. The physiological function of synaptic synthesis of specific proteins in synaptogenesis and neural plasticity expression remains to be shown. Experiments aimed at understanding the mechanisms and functions f synaptic protein synthesis might provide important information about the molecular nature of neural plasticity.

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Kraemer, Bjoern F., Stephan Lindemann, and Andrew S. Weyrich. "Protein degradation systems in platelets." Thrombosis and Haemostasis 110, no. 11 (2013): 920–24. http://dx.doi.org/10.1160/th13-03-0183.

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SummaryProtein synthesis and degradation are essential processes that allow cells to survive and adapt to their surrounding milieu. In nucleated cells, the degradation and/or cleavage of proteins is required to eliminate aberrant proteins. Cells also degrade proteins as a mechanism for cell signalling and complex cellular functions. Although the last decade has convincingly shown that platelets synthesise proteins, the roles of protein degradation in these anucleate cytoplasts are less clear. Here we review what is known about protein degradation in platelets placing particular emphasis on the proteasome and the cysteine protease calpain.

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Ruboyianes, Mark V., Min Chen, Mathew S. Dubrava, James E. Cherwa, and Bentley A. Fane. "The Expression of N-Terminal Deletion DNA Pilot Proteins Inhibits the Early Stages of φX174 Replication." Journal of Virology 83, no. 19 (July 29, 2009): 9952–56. http://dx.doi.org/10.1128/jvi.01077-09.

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ABSTRACT The φX174 DNA pilot protein H contains four predicted C-terminal coiled-coil domains. The region of the gene encoding these structures was cloned, expressed in vivo, and found to strongly inhibit wild-type replication. DNA and protein synthesis was investigated in the absence of de novo H protein synthesis and in wild-type-infected cells expressing the inhibitory proteins (ΔH). The expression of the ΔH proteins interfered with early stages of DNA replication, which did not require de novo H protein synthesis, suggesting that the inhibitory proteins interfere with the wild-type H protein that enters the cell with the penetrating DNA. As transcription and protein synthesis are dependent on DNA replication in positive single-stranded DNA life cycles, viral protein synthesis was also reduced. However, unlike DNA synthesis, efficient viral protein synthesis required de novo H protein synthesis, a novel function for this protein. A single amino acid change in the C terminus of protein H was both necessary and sufficient to confer resistance to the inhibitory ΔH proteins, restoring both DNA and protein synthesis to wild-type levels. ΔH proteins derived from the resistant mutant did not inhibit wild-type or resistant mutant replication. The inhibitory effects of the ΔH proteins were lessened by the coexpression of the internal scaffolding protein, which may suppress H-H protein interactions. While coexpression relieved the block in DNA biosynthesis, viral protein synthesis remained suppressed. These data indicate that protein H's role in DNA replication and stimulating viral protein synthesis can be uncoupled.

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Duncan, R. F., and J. W. Hershey. "Initiation factor protein modifications and inhibition of protein synthesis." Molecular and Cellular Biology 7, no. 3 (March 1987): 1293–95. http://dx.doi.org/10.1128/mcb.7.3.1293-1295.1987.

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The protein covalent modification state of eucaryotic initiation factors eIF-2 and eIF-4B in HeLa cells was examined after they were exposed to a variety of conditions or treatments that regulate protein synthesis. A few factors (e.g., variant pH and sodium fluoride) altered the phosphorylation state of the initiation factor proteins, but the majority (hypertonic medium, ethanol, dimethyl sulfoxide sodium selenite, sodium azide, and colchicine) had no effect on either protein. While initiation factor phosphorylation may regulate protein synthesis in response to many physiological situations, other pathways can regulate protein synthesis under nonphysiological circumstances.

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Duncan, R. F., and J. W. Hershey. "Initiation factor protein modifications and inhibition of protein synthesis." Molecular and Cellular Biology 7, no. 3 (March 1987): 1293–95. http://dx.doi.org/10.1128/mcb.7.3.1293.

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The protein covalent modification state of eucaryotic initiation factors eIF-2 and eIF-4B in HeLa cells was examined after they were exposed to a variety of conditions or treatments that regulate protein synthesis. A few factors (e.g., variant pH and sodium fluoride) altered the phosphorylation state of the initiation factor proteins, but the majority (hypertonic medium, ethanol, dimethyl sulfoxide sodium selenite, sodium azide, and colchicine) had no effect on either protein. While initiation factor phosphorylation may regulate protein synthesis in response to many physiological situations, other pathways can regulate protein synthesis under nonphysiological circumstances.

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Stephens, Samuel B., and Christopher V. Nicchitta. "Divergent Regulation of Protein Synthesis in the Cytosol and Endoplasmic Reticulum Compartments of Mammalian Cells." Molecular Biology of the Cell 19, no. 2 (February 2008): 623–32. http://dx.doi.org/10.1091/mbc.e07-07-0677.

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In eukaryotic cells, mRNAs encoding signal sequence-bearing proteins undergo translation-dependent trafficking to the endoplasmic reticulum (ER), thereby restricting secretory and integral membrane protein synthesis to the ER compartment. However, recent studies demonstrating that mRNAs encoding cytosolic/nucleoplasmic proteins are represented on ER-bound polyribosomes suggest a global role for the ER in cellular protein synthesis. Here, we examined the steady-state protein synthesis rates and compartmental distribution of newly synthesized proteins in the cytosol and ER compartments. We report that ER protein synthesis rates exceed cytosolic protein synthesis rates by 2.5- to 4-fold; yet, completed proteins accumulate to similar levels in the two compartments. These data suggest that a significant fraction of cytosolic proteins undergo synthesis on ER-bound ribosomes. The compartmental differences in steady-state protein synthesis rates correlated with a divergent regulation of the tRNA aminoacylation/deacylation cycle. In the cytosol, two pathways were observed to compete for aminoacyl-tRNAs—protein synthesis and aminoacyl-tRNA hydrolysis—whereas on the ER tRNA deacylation is tightly coupled to protein synthesis. These findings identify a role for the ER in global protein synthesis, and they suggest models where compartmentalization of the tRNA acylation/deacylation cycle contributes to the regulation of global protein synthesis rates.

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N. Marinov, Marin. "SYNTHESIS OF SOME NON-PROTEIN AMINO ACIDS DERIVED FROM SPIROHYDANTOINS." Journal Scientific and Applied Research 10, no. 1 (November 11, 2016): 39–46. http://dx.doi.org/10.46687/jsar.v10i1.204.

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This article presents a synthesis of non-protein amino acids derived from 6- and 8- substituted cyclohexanespiro-5-hydantoins, spiro(adamantane-2',4'-imidazolidine)- 2,5-dione and 3',4'-dihydro-2H,2'H,5H-spiro[imidazolidine-4,1'-naphthalene]-2,5-dione. The target compounds were prepared by an alkaline hydrolysis of the corresponding spirohydantoins with barium hydroxide. The products obtained were characterized by physicochemical parameters, IR , 1H and 13C NMR spectral data.

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Estrada, Andrea Lee, William Max Hudson, Paul Y. Kim, Claire Marie Stewart, Frederick F. Peelor, Yuren Wei, Dong Wang, Karyn L. Hamilton, Benjamin F. Miller, and Michael J. Pagliassotti. "Short-term changes in diet composition do not affect in vivo hepatic protein synthesis in rats." American Journal of Physiology-Endocrinology and Metabolism 314, no. 3 (March 1, 2018): E241—E250. http://dx.doi.org/10.1152/ajpendo.00209.2017.

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Protein synthesis is critical to protein homeostasis (proteostasis), and modifications in protein synthesis influence lifespan and the development of comorbidities associated with obesity. In the present study, we examined the acute response of liver protein synthesis to either high-fat or high-sucrose diets in order to elucidate nutrient-mediated regulation of hepatic protein synthesis in the absence of body fat accumulation. Total and endoplasmic reticulum-associated protein syntheses were assessed by use of the stable isotope, deuterium oxide (2H2O), in rats provided a control diet or diets enriched in polyunsaturated fat, saturated fat, or sucrose for 2, 4, or 7 days. The three experimental diets increased hepatic triglycerides 46–91% on day 7 and fasting insulin levels 83–117% on day 7, but did not result in differences in body weight when compared with control ( n = 6/diet/time). The fraction of newly synthesized proteins in total liver lysates and microsomes was not significantly different among dietary groups ( n = 3/diet/time). To determine whether the experimental diets provoked a transcriptional response to enhance the capacity for protein synthesis, we also measured a panel of genes linked to amino acid transport, synthesis, and processing. There were no significant differences in any of the genes measured among groups. Therefore, dietary treatments that have been linked to impaired proteostasis and that promote hepatic steatosis and insulin resistance, did not result in significant changes in total or ER-associated protein synthesis in the liver over a 7-day period.

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Dissertations / Theses on the topic "Protein synthesis"

1

Baas, Tracey Lynn. "The design, synthesis, and characterization of template assembled synthetic proteins /." Thesis, Connect to this title online; UW restricted, 2000. http://hdl.handle.net/1773/11561.

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Robertson, Nicola. "Protein synthesis." Thesis, University of Edinburgh, 1996. http://hdl.handle.net/1842/14314.

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Reyes, Samuel Onofre J. "Expanding beta-turn analogs for mimicking protein-protein hot spots." Thesis, [College Station, Tex. : Texas A&M University, 2006. http://hdl.handle.net/1969.1/ETD-TAMU-1748.

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Hassan, Hani Mutlak Abdullah. "Chemical Synthesis of Protein Ligands." Thesis, University of Manchester, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.501975.

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Bland, Lorraine. "Methodology for chemical protein synthesis." Thesis, University of Edinburgh, 2001. http://hdl.handle.net/1842/12014.

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A number of groups have been investigated as potential protecting groups for the thiol functionality of cysteine residues during Solid Phase Peptide Synthesis. Of these the 4-picolyl system has been found to be successful. A short, efficient synthesis to the protected amino acid and mild cleavage conditions have been developed. This protected amino acid has been applied in the synthesis of a number of interesting cysteine-containing peptide targets. Deglycosylated human erythropoietin (dhEPO) has been synthesised by SPPS, employing the picolyl group for cysteine protection. Purification of this material has been achieved by gel filtration. The synthetic material has been characterised by amino acid analysis, SDS-PAGE, iso-electric focusing and N-terminal sequencing. Attempts have been made to synthesise deglycosylated human erythropoietin via a fragment coupling technique. All fragments were successfully synthesised and purified and model ligation studies carried out.

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Gordon, Carolyn Alexandra. "Investigations in chemical protein synthesis." Thesis, University of Edinburgh, 2001. http://hdl.handle.net/1842/14919.

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The chemical synthesis of the 184aa anti-angiogenic peptide, endostatin, was undertaken. Preparation via the stepwise of two large fragments approximately 90aa in length was attempted but was unsuccessful. A method that would allow the efficient, sequential coupling of several small fragments was required. To this end, the segment coupling of minimally protected fragments via transfer active ester condensation (TAEC), a technique recently developed within this research group, was investigated. The fragments for synthesis were provisionally selected based on hydrophobicity and potential coupling sites. These peptide fragments were then optimised for stepwise solid phase peptide synthesis (SPPS), using the Fmoc strategy. Peptides containing two types of C-terminal functionality - hydrazides and semicarbazides - were prepared. An alternative strategy for the synthesis of the Wang resin-based hydrazide linker, first proposed by Wang and Merrifield in 1969, was developed to facilitate this process. Peptide fragments of up to 20aa in length were successfully coupled using TAEC. A novel approach to the protection of arginine side chains was also investigated. This target was based on the dibenzocycloheptenyl system, a species which was originally deigned for use as a linker in the preparation of peptide amides. Recent work by Noda involved a derivative of this linker, which has proven to be significantly more acid labile than current arginine protection. Concurrent work on an improved design led to an alternative system - the dimethoxy-suberyl compound - being proposed. The synthesis of the target molecule was achieved in seven steps; key steps involved a Perkin reaction and an intramolecular Friedel Krafts acylation. Coupling to arginine was undertaken but proved unsuccessful.

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Dorywalska, Magdalena. "Conformational dynamics of protein synthesis /." May be available electronically:, 2007. http://proquest.umi.com/login?COPT=REJTPTU1MTUmSU5UPTAmVkVSPTI=&clientId=12498.

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Badger, David B. "Design and Synthesis of Protein-Protein Interaction Inhibitor Scaffolds." Scholar Commons, 2012. http://scholarcommons.usf.edu/etd/3964.

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Many currently relevant diseases such as cancer arise from altered biological pathways that rely on protein-protein interactions. The proteins involved in these interactions contain certain functional domains that are responsible for the protein's biological activities. These domains consist of secondary structural elements such as α-helices and Β-sheets which are at the heart of the protein's biological activity. Therefore, designing drugs that inhibit protein-protein interactions by binding to these key secondary structural elements should provide an effective treatment for many diseases. Presented in this dissertation are the designs, syntheses, and biological evaluations for both novel α-helix and novel Β-sheet mimics. The α-helix mimics were designed to inhibit the interactions between the tumor suppressor protein p53 and its inhibitor protein, MDM2. We also targeted the interactions between the Bak/Bcl-xL proteins. Using the knowledge gained from Hamilton's 1,4-terphenylene scaffold, we designed our inhibitors to be non-peptidic small molecule α-helix mimics. These molecules were designed to bind to the NH2-terminal domain of MDM2 protein thus preventing it from binding to the p53 protein thereby allowing p53 to induce apoptosis. The α-helix mimetic scaffold is designed around a central functionalized pyridazine ring while maintaining the appropriate distances between the ith, ith+4, and ith+7 positions of a natural alpha helix. The Β-sheet mimics were designed as inhibitors for the integrin mediated extracellular matrix cell adhesion found in Multiple Myeloma. We have designed, synthesized, and incorporated novel Β-turns to induce the formation of Β-hairpins as well as to cyclize the peptides in order to increase their binding affinities and reduce proteolytic cleavage. Given that many protein-protein interactions occur through hydrophobic interactions; our primary Β-turn promoter was designed with the ability to alter the Β-hairpin's hydrophobicity depending on the sulfonyl group used in the turn. The synthesis of several different sulfonyl chlorides for use in our Β-turn promoter is included in this section. We have also provided a detailed structural analysis and characterization of these new cyclic peptides via NMR and CD spectrometry. Using standard 2D NMR methods, we have elucidated the 3D conformation of several peptides in solution. We have also studied the structure activity relationships (SAR) for these cyclic peptides and then correlated these results with those obtained from the NMR studies.

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Blum, Janna Karen. "Broadening the enyzme-catalyzed synthesis of semi-synthetic antibiotics." Diss., Georgia Institute of Technology, 2011. http://hdl.handle.net/1853/39528.

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An alpha-amino ester hydrolase (AEH) applicable to synthesis of semi-synthetic antibiotics was cloned from the genomic DNA of Xanthomonas campestris pv. campestris sp. strain ATCC 33913. AEHs catalyze the synthesis and hydrolysis of alpha-amino beta-lactam antibiotics. The enzyme was characterized for thermodynamic and kinetic parameters. The enzyme shows optimal ampicillin hydrolytic activity at 25C and pH 6.8. The AEH enzymes have been shown to have excellent synthetic capability. Additionally, we demonstrated the first fully aqueous enzymatic one-pot synthesis of ampicillin direct from the natural product penicillin G eliminating the isolation of the intermediate 6-APA. Lastly, to improve the thermostability of the AEH a modified structure-guided consensus model of seven homologous enzymes was generated along with analysis of the B-factors from the available crystal structures of the known AEH from Xanthomonas citri. Our best variant, which is a quadruple mutant, E143H/A275P/N186D/V622I, which has a T_50_30, the temperature at which the half-life is 30 minutes, of 34C and 1.3-fold activity compared to wild-type. Overall, we have successfully improved the understanding of the AEH class of enzymes and applied a novel cascade application, demonstrating AEHs unique applicability in the synthesis of beta-lactam antibiotics. The improved thermostability will further improve the industrial relevance of AEHs.

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Ferris, Douglas K. "Protein phosphatases and protein kinases in dictyostelium." Diss., Virginia Polytechnic Institute and State University, 1986. http://hdl.handle.net/10919/50017.

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In the present work, the chromatographic behavior and partial characterization of 5 protein phosphatases, 6 paranitrophenyl phosphate (pnpp) phosphatases and 2 protein kinases from Dictyostelium are described. .Two of the protein phosphatases are shown to have subunit structures. All of the protein phosphatase activities described were able to dephosphorylate sites on proteins that had previously been phosphorylated by the cAMP-dependent protein kinase. Therefore it may be that these phosphatases function in vivo to antagonize the action of the cAMP-dependent protein kinase. Various pnpp phosphatase activities, varying in size, cation requirements and pH optima are described. Since many pnpp phosphatases also function with protein substrates it is possible that these activities represent protein phosphatases that function with phosphoproteins that have not been tested. Evidence for the existence of protein kinase C in Dictyostelium is presented. A histone protein kinase was found in Dictyostelium extracts that eluted from DE52 cellulose at the same salt concentration that rabbit brain protein kinase C did. In addition in one experiment clear dependency on calcium and phospholipids is shown. The purification to homogeneity, and characterization of a low molecular weight autophosphorylating protein kinase, pp20, is described. This protein kinase is a major phosphorylated protein and in addition represents at least 0.03% of the total cellular protein. The autophosphorylation reaction can be inhibited by EDTA but not by EGTA. Following inhibition by EDTA, autophosphorylation can be reactivated by the addition of Mn²⁺, Mg²⁺, or Ca²⁺. Western blotting evidence is presented that shows cross reactivity of pp20 and an 85 KDa protein that may possess casein kinase activity.
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Books on the topic "Protein synthesis"

1

Martin, Robin. Protein Synthesis. New Jersey: Humana Press, 1998. http://dx.doi.org/10.1385/089603397x.

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E, Esterhouse Toma, and Petrinos Lado B, eds. Protein biosynthesis. New York: Nova Science, 2008.

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Li, Xuechen, ed. Chemical Protein Synthesis. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2489-0.

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1958-, Martin Robin, ed. Protein synthesis: Methods and protocols. Totowa, N.J: Humana Press, 1998.

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Alexandrov, Kirill, and Wayne A. Johnston, eds. Cell-Free Protein Synthesis. Totowa, NJ: Humana Press, 2014. http://dx.doi.org/10.1007/978-1-62703-782-2.

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Bermek, Engin, ed. Mechanisms of Protein Synthesis. Berlin, Heidelberg: Springer Berlin Heidelberg, 1985. http://dx.doi.org/10.1007/978-3-642-69912-2.

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H, Nierhaus Knud, and Wilson Daniel N, eds. Protein synthesis and ribosome structure: Translating the genome. Weinheim: Wiley-VCH, 2004.

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Giovanni, Cesareni, ed. Modular protein domains. Weinheim: Wiley-VCH, 2005.

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L, Hatfield Dolph, Lee Byeong J, and Pirtle Robert M, eds. Transfer RNA in protein synthesis. Boca Raton: CRC Press, 1992.

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A, Wallace Carmichael J., ed. Protein engineering by semisynthesis. Boca Raton, Fla: CRC Press, 2000.

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Book chapters on the topic "Protein synthesis"

1

Giudice, Giovanni. "Protein Synthesis." In The Sea Urchin Embryo, 123–44. Berlin, Heidelberg: Springer Berlin Heidelberg, 1986. http://dx.doi.org/10.1007/978-3-642-70431-4_6.

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Webster, George C. "Protein synthesis." In Drosophila as a Model Organism for Ageing Studies, 119–28. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4899-2683-8_9.

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Thiriet, Marc. "Protein Synthesis." In Biomathematical and Biomechanical Modeling of the Circulatory and Ventilatory Systems, 215–84. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-9758-6_6.

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Stauffer, Sarah, Aaron Gardner, Dewi Ayu Kencana Ungu, Ainara López-Córdoba, and Matthias Heim. "Protein Synthesis." In Labster Virtual Lab Experiments: Basic Biology, 57–77. Berlin, Heidelberg: Springer Berlin Heidelberg, 2018. http://dx.doi.org/10.1007/978-3-662-57996-1_5.

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Baker, Julien S., Fergal Grace, Lon Kilgore, David J. Smith, Stephen R. Norris, Andrew W. Gardner, Robert Ringseis, et al. "Protein Synthesis." In Encyclopedia of Exercise Medicine in Health and Disease, 732. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-540-29807-6_2922.

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Wu, Guoyao. "Protein Synthesis." In Amino Acids, 407–59. 2nd ed. Boca Raton: CRC Press, 2021. http://dx.doi.org/10.1201/9781003092742-8.

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Chaudhary, Govind R., Anjali Singh, and Akanksha Pandey. "Protein Synthesis." In Encyclopedia of Sexual Psychology and Behavior, 1–7. Cham: Springer International Publishing, 2023. http://dx.doi.org/10.1007/978-3-031-08956-5_95-1.

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Anandabaskar, Nishanthi. "Protein Synthesis Inhibitors." In Introduction to Basics of Pharmacology and Toxicology, 835–68. Singapore: Springer Singapore, 2021. http://dx.doi.org/10.1007/978-981-33-6009-9_55.

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Machova, Zuzana, and Annette G. Beck-Sickinger. "Expressed Protein Ligation for Protein Semisynthesis and Engineering." In Peptide Synthesis and Applications, 105–30. Totowa, NJ: Humana Press, 2005. http://dx.doi.org/10.1385/1-59259-877-3:105.

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Sánchez-Navarro, Macarena, and Benjamin G. Davis. "SUGAR-PROTEIN HYBRIDS FOR BIOMEDICAL APPLICATIONS." In Glycochemical Synthesis, 509–34. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2016. http://dx.doi.org/10.1002/9781119006435.ch19.

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Conference papers on the topic "Protein synthesis"

1

Terwilliger, Thomas C., and Joel Berendzen. "Protein Crystallography: From X-ray diffraction spots to a three-dimensional image." In Signal Recovery and Synthesis. Washington, D.C.: Optica Publishing Group, 1998. http://dx.doi.org/10.1364/srs.1998.swa.1.

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Proteins are remarkable molecular machines that are essential for life. They can do many things ranging from the precise control of blood clotting to synthesizing complex organic compounds. Pictures of protein molecules are in high demand in biotechnology because they are important for applications such as drug discovery and for engineering enzymes for commercial use.

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Grothe, Rob. "Adaptive Protein Structure Refinement Using Diffraction Data." In Signal Recovery and Synthesis. Washington, D.C.: Optica Publishing Group, 1998. http://dx.doi.org/10.1364/srs.1998.swa.2.

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X-ray crystallography remains the primary technique for discovering the arrangement of a protein’s atoms in space. If this arrangement is given by a vector of atom positions r = (r 1 ,r 2 ,…,r N ), then the resulting structure factor F(r)(S) in direction S is given by where F a ( i ) is the atomic scattering function of a(i) ∈ {“Carbon", “Nitrogen", “Hydrogen",…}, the atom type of the ith atom. F a ( i ) is the Fourier transform of ρ a (i), the spherical electron density for an atom of type a(i) placed at the origin.

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Jackson, C. W., N. K. Hutson, and S. A. Steward. "CHANGES IN PROTEIN SYNTHESIS PROFILES OF MEGAKARYOCYTES (MK) DURING MATURATION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643545.

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Several key differentiation events occur within the recognizable MK compartment; however, little is known about the macromolecular changes responsible for these events. In this study, protein synthesis profiles of morphologically immature and mature guinea pig MK populations have been analyzed by twodimensional gel electrophoresis after in vivo labeling with 35S-methionine. MK were enriched by a bovine plasma aggregation enrichment procedure (Blood 69:173, 1987) and then fractionated into immature and mature populations based on differences in their respective buoyant densities (Brit. J. Haematol. 64:33, 1986). With this protocol, immature and mature MK populations were obtained in which MK constituted 95% of the cell mass. Ninety percent of the MK in the immature population had basophilic, immature morphology while ≥90% of those in the mature population had acidophilic, mature staining characteristics after Wright's staining. Protease inhibitors were used throughout the isolation procedure. The cells were solubilized and proteins subjected to two-dimensional electrophoresis according to O'Farrell (J. Biol. Chem. 250:4007, 1975). To examine basic proteins, proteins were electrophoresed in the first dimension under nonequilibrium conditions in a pH gradient as described by O'Farrell et al. (Cell 12:1133, 1977). Analyses of fluorograms revealed both qualitative and quantitative differences in synthesis profiles between these two MK populations. Among acidic proteins whose synthesis was readily detected in immature but not mature MK were ones whose MW and pi were respectively: 120K, 6.4; 7OK, 5.9; 70K, 6.9; 65K, 6.8; 55K, 6.2; 55K, 6.0; 53K, 5.8; 53K, 6.5; 52K, 6.7; 50K, 6.8; 41K, 5.5 and 33K, 6.7. Acidic and neutral proteins prominently synthesized in mature but not immature MK were found at MW and PI of: 110K, 5.7; 110K, 5.8 and 80K, 7.2. Basic proteins prominently synthesized in immature but not mature MK were found at MWs of: 110K; 70K; 52K; 48K; 39K and 18K. Basic proteins actively synthesized by mature but not immature MK had MWs of: 83K; 43K and 17K. These findings demonstrate that differences in protein synthesis patterns can be readily detected between immature and mature MK and provide baseline data with which to explore the role of these proteins in MK differentiation

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Mei, Qian, Carl K. Fredrickson, Andrew Simon, and Z. Hugh Fan. "Fabricating a Plastic Microfluidic Device for Protein Synthesis." In ASME 2006 International Mechanical Engineering Congress and Exposition. ASMEDC, 2006. http://dx.doi.org/10.1115/imece2006-14122.

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We developed an array device consisting of miniaturized wells and a mechanism of fluid manipulation for cell-free protein synthesis. The array offers high-throughput protein production, matching the format of gene discovery. Each unit in the array is for synthesis of one individual protein and it consists of a tray chamber and a well chamber. The tray chamber is for in vitro protein synthesis reaction, while the well functions as a nutrient reservoir. The tray and well are separated by a dialysis membrane, which is glued to the bottom of the tray. The connection between the tray and the well provides a means to supply nutrients and remove the reaction byproducts. The device was demonstrated by synthesis of green fluorescent protein (GFP). The effectiveness of the device design on the protein production yield has been studied. The resultant advantages due to miniaturization include rapid analysis, less consumption of samples and reagents, and the decrease in the cost of protein synthesis.

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Hojo, Hironobu, Fumika Nakatani, and Isao Suetake. "Chemical Synthesis of Palmitoylated Histone Protein." In 36th European Peptide Symposium. The European Peptide Society, 2022. http://dx.doi.org/10.17952/36eps.2022.269.

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Hojo, Hironobu, Fumika Nakatani, and Isao Suetake. "Chemical Synthesis of Palmitoylated Histone Protein." In 36th European Peptide Symposium. The European Peptide Society, 2022. http://dx.doi.org/10.17952/36eps/36eps.2022.269.

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Nawroth, Peter P., Jerry Brett, Susan Steinberg, Charles T. Esmon, and David M. Stern. "ENDOTHELIUM AND PROTEIN S: SYNTHESIS, RELEASE AND REGULATION OF ANTICOAGULANT ACTIVITY." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642962.

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The protein C-protein S pathway is closely linked to the vessel wall. In terms of protein C, endothelium has been shown to provide the receptor thrombomodulin, which promotes thrombin-mediated formation of activated protein C. Optimal anticoagulant function of activated protein C requires protein S and a cellular surface. Recent studies have indicated that endothelium can facilitate assembly of the activated protein C-protein S complex and that bovine endothelium expresses specific binding site(s) for protein S which promote its anticoagulant function. Expression of protein S binding sites is subject to down-regulation by Tumor Necrosis Factor (TNF) . Exposure of cultured bovine endothelium to TNF results in decreased 125I-protein s binding and attenuated rates of Factor Va inactivation after 2 hrs followed by negligible 125I-protein S binding and Factor Va inactivation by 10 hrs. These changes persist for over 48 hrs, in contrast to the more transient rise in endothelial cell tissue factor induced by TNF which returns to baseline by 24 hrs.In addition to providing binding sites for protein S, endothelium constitutively synthesizes and releases this vitamin K-dependent anticoagulant cofactor. Release of protein S is blocked by addition of warfarin, indicating that y-carboxylation facilitates the release of intracellular protein S. Morphologic studies, at the level of electron microscope, have shown protein S antigen to be present in cisternae of rough endoplasmic reticulum, the trans face of the golgi and a population of intracellular vesicles which appear to be distributed at the cellular periphery. By immunofluorescence, the distribution of protein S is distinct from that of von Willebrand Factor. The intracellular vesicles containing protein S constitute a storage pool potentially available for rapid release. Treatment of endothelium with norepinephrine results in release of protein S over the next 20 min. Release is half-maximal at a norepinephrine concentration of about 0.1 uM and is not observed with the biologically inactive entantiomer (+) norepinephrine. Norepinephrine-induced release of intracellular protein S can be blocked by prazosine (10-7 7 M), but not by propranolol (10-6 M) or yohimbine (10-5 M). These data are consistent with release of protein S being a receptor-mediated process dependent on an endothelial cell alpha 1 adrenergic receptor. Blockade of norepinephrine-induced release of protein S by pertussis toxin treatment of endothelium further defines the intracellular pathway of protein S and implicates regulatory G proteins in the stimulus-response coupling. Electron microscopic studies have shown that following exposure of endothelium to norepinephrine the intracellular vesicles containing protein S undergo exocytosis at the plasma membrane. These data define a new relationship between the autonomic nervous system and the coagulation mechanism.Protein S is clearly an endothelial cell-associated anticoagulant protein. A specific binding site on the endothelial cell surface can regulate its anticoagulant function on the vessel wall. Endothelial cell synthesis and release of protein S defines a new level of participation of endothelium in the protein C-protein S pathway.

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Sana, Barindra, Marcia Calista, and Sierin Lim. "Protein cage assisted metal-protein nanocomposite synthesis: Optimization of loading conditions." In INTERNATIONAL CONFERENCE ON NANOTECHNOLOGY - RESEARCH AND COMMERCIALIZATION 2011: (ICONT 2011). AIP, 2012. http://dx.doi.org/10.1063/1.4769136.

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Gaivoronskaya, Irina, and Valenitna Kolpakova. "MATHEMATICAL MODELS FOR THE SYNTHESIS OF PLANT-BASED COMPOSITIONS WITH IMPROVED AMINO ACID COMPOSITION." In GEOLINKS Conference Proceedings. Saima Consult Ltd, 2021. http://dx.doi.org/10.32008/geolinks2021/b1/v3/12.

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The aim of the work was to optimize the process of obtaining multicomponent protein compositions with high biological value and higher functional properties than the original vegetable protein products. Was realized studies to obtain biocomposites on the base of pea protein-oat protein and pea protein-rice protein. Developed composites were enriched with all limited amino acids. For each of the essential amino acids, the amino acid score was 100% and higher. Protein products used in these compositions are not in major allergen list, which allows to use these compositions in allergen-free products and specialized nutrition. To determine biosynthesis parameters for compositions from pea protein and various protein concentrates with the use of transglutaminase enzyme, was studied effect of concentration and exposition time on the amount of amino nitrogen released during the reaction. Decreasing of amino nitrogen in the medium indicated the occurrence of a protein synthesis reaction with the formation of new covalent bonds. Were determined optimal parameters of reaction: the hydromodule, the exposure time, the concentration of EP of the preparation, were obtained mathematical models. Studies on the functional properties of composites, the physicochemical properties of the proteins that make up their composition, and structural features will make it possible to determine the uses in the manufacture of food products based on their ability to bind fat, water, form foam, gels, and etc.

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Waart, P. v. d., K. T. Preissner, U. Delvos, and G. Müller-Berghaus. "SIMULTANEOUS PRODUCTION OF ENDOTHELIAL CELL-DERIVED PROTEIN S AND FACTOR V, AND INACTIVATION OF FACTOR Va AT THE ENDOTHELIAL CELL SURFACE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644737.

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Several proteins synthesized and expressed by endothelial cells are involved in the regulation of coagulation. The synthesis and expression of factor V and protein S has been demonstrated in independent studies. The present work evaluates the simultaneous synthesis and expression of bovine factor V and protein S and the effect of endothelial protein S on the inactivation of endothelial factor Va by activated protein C. The accumulation of both proteins in conditioned medium was detected by SDS-PAGE followed by immunoblotting, and their activities were tested by functional assays. The synthesis of protein S and factor V per 105 cells over 24 h amounted up to 2 ng protein S and 440 ng factor V, respectively. The addition of thrombin did not increase the yield of synthesized cofactors. Thrombin did neither proteolyse protein S on endothelial cells nor in a purified system in the presence of thrombomodulin and calcium ions. Factor V was secreted partly in its activated form as evidenced by the appearance of active intermediates with M = 220,000-280,000 on immunoblots as well as by only a three-Fold further activation of factor V/Va following addition of thrombin. The rate constant for the inactivation of factor Va by activated protein C was only two-fold higher for factor Va derived from cells cultured in the presence of vitamin K as compared in the presence of warfarin. For the inactivation of comparable factor Va concentrations in conditioned medium a 10-fold higher and on endothelial cells a 40-fold higher concentration of activated protein C was required to obtain similar inactivation rates of factor Va as compared to a purified system. These results suggest that resting endothelial cells contain a factor V activator, and that a regulatory mechanism is operative on the endothelial cell surface that suppresses the inactivation potential of activated protein C/ protein S.

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Reports on the topic "Protein synthesis"

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McGuire, Mark A., Amichai Arieli, Israel Bruckental, and Dale E. Bauman. Increasing Mammary Protein Synthesis through Endocrine and Nutritional Signals. United States Department of Agriculture, January 2001. http://dx.doi.org/10.32747/2001.7574338.bard.

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Objectives To determine endocrine factors that regulate the partitioning of amino acids by the mammary gland. To evaluate dietary flow and supply of energy and amino acids and their effects on milk protein synthesis and endocrine status. To use primary cultures of cow mammary epithelial cells to examine the role of specific factors on the rates and pattern of milk protein synthesis. Milk protein is an increasingly valuable component of milk but little is known regarding the specific hormonal and nutritional factors controlling milk protein synthesis. The research conducted for this project has determined that milk protein synthesis has the potential to be enhanced much greater than previously believed. Increases of over 25% in milk protein percent and yield were detected in studies utilizing abomasal infusion of casein and a hyperinsulinemic-euglycemic clamp. Thus, it appears that insulin, either directly or indirectly, can elicit a substantial increase in milk protein synthesis if additional amino acids are supplied. For additional amino acids, casein provided the best response even though substantial decreases in branched chain amino acids occur when the insulin clamp is utilized. Branched chain amino acids alone are incapable of supporting the enhanced milk protein output. The mammary gland can vary both blood flow and extraction efficiency of amino acids to support protein synthesis. A mammary culture system was used to demonstrate specific endocrine effects on milk protein synthesis. Insulin-like growth factor-I when substituted for insulin was able to enhance casein and a-lactalbumin mRNA. This suggests that insulin is a indirect regulator of milk protein synthesis working through the IGF system to control mammary production of casein and a-lactalbumin. Principal component analysis determined that carbohydrate had the greatest effect on milk protein yield with protein supply only having minor effects. Work in cattle determined that the site of digestion of starch did not affect milk composition alone but the degradability of starch and protein in the rumen can interact to alter milk yield. Cows fed diets with a high degree of rumen undegradability failed to specifically enhance milk protein but produced greater milk yield with similar composition. The mammary gland has an amazing ability to produce protein of great value. Research conducted here has demonstrated the unprecedented potential of the metabolic machinery in the mammary gland. Insulin, probably signaling the mammary gland through the IGF system is a key regulator that must be combined with adequate nutrition in order for maximum response.

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Karen S. Browning. Protein Synthesis Initiation Factors: Phosphorylation and Regulation. Office of Scientific and Technical Information (OSTI), June 2009. http://dx.doi.org/10.2172/956983.

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Barash, Itamar, and Robert E. Rhoads. Translational Mechanisms that Govern Milk Protein Levels and Composition. United States Department of Agriculture, November 2004. http://dx.doi.org/10.32747/2004.7586474.bard.

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Original objectives: The long term objective of the project is to achieve higher content of protein in the milk of ruminants by modulating the translational machinery in the mammary gland. The first specific aim of the BARD proposal was to characterize responsiveness of various experimental systems to combination of lactogenic hormones and amino acids with particular emphasis on discrimination between the control of total protein synthesis and milk protein synthesis. Based on the results, we planned to proceed by characterizing the stage of protein synthesis in which the stimulation by lactogenic hormones and amino acid occur and finally we proposed to identify which components of the translation machinery are modified. Background to the topic: Milk protein is the most valuable component in milk, both for direct human consumption and for manufacturing cheese and other protein-based products. Attempts to augment protein content by the traditional methods of genetic selection and improved nutritional regimes have failed. The proposal was based on recent results suggesting that the limiting factor for augmenting protein synthesis in the bovine mammary gland is the efficiency of converting amino acids to milk proteins. Major conclusions, solutions, achievements: Insulin and prolactin synergistically stimulate â-casein mRNA translation by cytoplasmatic polyadenylation. The interaction between insulin and prolactin was demonstrated two decades ago as crucial for milk-protein synthesis, but the molecular mechanisms involved were not elucidated. We found in differentiated CID 9 mouse mammary epithelial cells line that insulin and prolactin synergistically increases the rate of milk protein mRNA translation. We focused on â-casein, the major milk protein, and found that the increase in â-casein mRNA translation was reflected in a shift to larger polysomes, indicating an effect on translational initiation. Inhibitors of the PI3K, mTOR, and MAPK pathways blocked insulin-stimulated total protein and â-casein synthesis but not the synergistic stimulation. Conversely, cordycepin, a polyadenylation inhibitor, abolished synergistic stimulation of protein synthesis without affecting insulin-stimulated translation. The poly(A) tract of â-casein mRNA progressively increased over 30 min of treatment with insulin plus prolactin. The 3’-untranslated region of â-casein mRNA was found to contain a cytoplasmic polyadenylation element (CPE), and in reporter constructs, this was sufficient for the translational enhancement and mRNA-specific polyadenylation. Furthermore, insulin and prolactin stimulated phosphorylation of cytoplasmic polyadenylation element binding protein (CPEB) but did not increase cytoplasmic polyadenylation.

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Barash, Itamar, and Robert Rhoads. Translational Mechanisms Governing Milk Protein Levels and Composition. United States Department of Agriculture, 2006. http://dx.doi.org/10.32747/2006.7696526.bard.

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Original objectives: The long-term goal of the research is to achieve higher protein content in the milk of ruminants by modulating the translational apparatus of the mammary gland genetically, nutritionally, or pharmacologically. The short-term objectives are to obtain a better understanding of 1) the role of amino acids (AA) as regulators of translation in bovine and mouse mammary epithelial cells and 2) the mechanism responsible for the synergistic enhancement of milk-protein mRNA polyadenylation by insulin and prolactin. Background of the topic: In many cell types and tissues, individual AA affect a signaling pathway which parallels the insulin pathway to modulate rates and levels of protein synthesis. Diverse nutritional and hormonal conditions are funneled to mTOR, a multidomain serine/threonine kinase that regulates a number of components in the initiation and elongation stages of translation. The mechanism by which AA signal mTOR is largely unknown. During the current grant period, we have studied the effect of essential AA on mechanisms involved in protein synthesis in differentiated mammary epithelial cells cultured under lactogenic conditions. We also studied lactogenic hormone regulation of milk protein synthesis in differentiated mammary epithelial cells. In the first BARD grant (2000-03), we discovered a novel mechanism for mRNA-specific hormone-regulated translation, namely, that the combination of insulin plus prolactin causes cytoplasmic polyadenylation of milk protein mRNAs, which leads to their efficient translation. In the current BARD grant, we have pursued the signaling pathways of this novel hormone action. Major conclusions/solutions/achievements: The positive and negative signaling from AA to the mTOR pathway, combined with modulation of insulin sensitization, mediates the synthesis rates of total and specific milk proteins in mammary epithelial cells. The current in vitro study revealed cryptic negative effects of Lys, His, and Thr on cellular mechanisms regulating translation initiation and protein synthesis in mammary epithelial cells that could not be detected by conventional in vivo analyses. We also showed that a signaling pathway involving Jak2 and Stat5, previously shown to lead from the prolactin receptor to transcription of milk protein genes, is also used for cytoplasmic polyadenylation of milk protein mRNAs, thereby stabilizing these mRNAs and activating them for translation. Implications: In vivo, plasma AA levels are affected by nutritional and hormonal effects as well as by conditions of exercise and stress. The amplitude in plasma AA levels resembles that applied in the current in vitro study. Thus, by changing plasma AA levels in the epithelial cell microenvironment or by sensitizing the mTOR pathway to their presence, it should be possible to modulate the rate of milk protein synthesis. Furthermore, knowledge that phosphorylation of Stat5 is required for enhanced milk protein synthesis in response to lactogenic opens the possibility for pharmacologic approaches to increase the phosphorylation of Stat5 and, thereby, milk protein production.

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Yoshii, Akira, and Martha Constantine-Patton. Studying Protein Synthesis-Dependent Synaptic Changes in Tuberous Sclerosis. Fort Belvoir, VA: Defense Technical Information Center, April 2013. http://dx.doi.org/10.21236/ada582389.

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Varga, Gabriella A., Amichai Arieli, Lawrence D. Muller, Haim Tagari, Israel Bruckental, and Yair Aharoni. Effect of Rumen Available Protein, Amimo Acids and Carbohydrates on Microbial Protein Synthesis, Amino Acid Flow and Performance of High Yielding Cows. United States Department of Agriculture, August 1993. http://dx.doi.org/10.32747/1993.7568103.bard.

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The effect of rumen available protein amino acids and carbohydrates on microbial protein synthesis, amino acid flow and performance of high yielding dairy cows was studied. A significant relationship between the effective degradabilities of OM in feedstuffs and the in vivo ruminal OM degradation of diets of dairy cows was found. The in situ method enabled the prediction of ruminal nutrients degradability response to processing of energy and nitragenous supplements. The AA profile of the rumen undegradable protein was modified by the processing method. In a continuous culture study total N and postruminal AA flows, and bacterial efficiency, is maximal at rumen degradable levels of 65% of the CP. Responses to rumen degradable non carbohydrate (NSC) were linear up to at least 27% of DM. Higher CP flow in the abomasum was found for cows fed high ruminally degradable OM and low ruminally degradable CP diet. It appeared that in dairy cows diets, the ratio of rumen degradable OM to rumenally degradable CP should be at least 5:1 in order to maximize postruminal CP flow. The efficiency of microbial CP synthesis was higher for diets supplemented with 33% of rumen undegradable protein, with greater amounts of bacterial AA reaching the abomasum. Increase in ruminal carbohydrate availability by using high moisture corn increased proportions of propionate, postruminal nutrients flow, postruminal starch digestibility, ruminal availability of NSC, uptake of energy substrates by the mammory gland. These modifications resulted with improvement in the utilization of nonessential AA for milk protein synthesis, in higher milk protein yield. Higher postruminal NSC digestibility and higher efficiency of milk protein production were recorded in cows fed extruded corn. Increasing feeding frequency increased flow of N from the rumen to the blood, reduced diurnal variation in ruminal and ammonia, and of plasma urea and improved postruminal NSC and CIP digestibility and total tract digestibilities. Milk and constituent yield increased with more frequent feeding. In a study performed in a commercial dairy herd, changes in energy and nitrogenous substrates level suggested that increasing feeding frequency may improve dietary nitrogen utilization and may shift metabolism toward more glucogenesis. It was concluded that efficiency of milk protein yield in high producing cows might be improved by an optimization of ruminal and post-ruminal supplies of energy and nitrogenous substrates. Such an optimization can be achieved by processing of energy and nitrogenous feedstuffs, and by increasing feeding frequency. In situ data may provide means for elucidation of the optimal processing conditions.

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Grafi, Gideon, and Brian Larkins. Endoreduplication in Maize Endosperm: An Approach for Increasing Crop Productivity. United States Department of Agriculture, September 2000. http://dx.doi.org/10.32747/2000.7575285.bard.

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The focus of this research project is to investigate the role of endoreduplication in maize endosperm development and the extent to which this process contributes to high levels of starch and storage protein synthesis. Although endoreduplication has been widely observed in many cells and tissues, especially those with high levels of metabolic activity, the molecular mechanisms through which the cell cycle is altered to produce consecutive cycles of S-phase without an intervening M-phase are unknown. Our previous research has shown that changes in the expression of several cell cycle regulatory genes coincide with the onset of endoreduplication. During this process, there is a sharp reduction in the activity of the mitotic cyclin-dependent kinase (CDK) and activation of the S-phase CDK. It appears the M-phase CDK is stable, but its activity is blocked by a proteinaceous inhibitor. Coincidentally, the S-phase checkpoint protein, retinoblastoma (ZmRb), becomes phosphorylated, presumably releasing an E2F-type transcriptional regulator which promotes the expression of genes responsible for DNA synthesis. To investigate the role of these cell cycle proteins in endoreduplication, we have created transgenic maize plants that express various genes in an endosperm-specific manner using a storage protein (g-zein) promoter. During the first year of the grant, we constructed point mutations of the maize M-phase kinase, p34cdc2. One alteration replaced aspartic acid at position 146 with asparagine (p3630-CdcD146N), while another changed threonine 161 to alanine (p3630-CdcT161A). These mutations abolish the activity of the CDK. We hypothesized that expression of the mutant forms of p34cdc2 in endoreduplicating endosperm, compared to a control p34cdc2, would lead to extra cycles of DNA synthesis. We also fused the gene encoding the regulatory subunit of the M- phase kinase, cyclin B, under the g-zein promoter. Normally, cyclin B is expected to be destroyed prior to the onset of endoreduplication. By producing high levels of this protein in developing endosperm, we hypothesized that the M-phase would be extended, potentially reducing the number of cycles of endoreduplication. Finally, we genetically engineered the wheat dwarf virus RepA protein for endosperm-specific expression. RepA binds to the maize retinoblastoma protein and presumably releases E2F-like transcription factors that activate DNA synthesis. We anticipated that inactivation of ZmRb by RepA would lead to additional cycles of DNA synthesis.

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Nilsson, Emil. Synthesis of Sulfamoyl??Aminoacyl Adenylate Analogs for use in Protein?RNA Structure Determination. Portland State University Library, May 2013. http://dx.doi.org/10.15760/honors.28.

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Weiser, Douglas C. The Role of GADD34 (Growth Arrest and DNA Damage-Inducible Protein) in Regulating Apoptosis, Proliferation, and Protein Synthesis in Human Breast Cancer Cells. Fort Belvoir, VA: Defense Technical Information Center, July 2004. http://dx.doi.org/10.21236/ada427916.

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Weiser, Douglas C. The Role of GADD34 (Growth Arrest and DNA Damage-Inducible Protein) in Regulating Apoptosis, Proliferation, and Protein Synthesis in Human Breast Cancer Cells. Fort Belvoir, VA: Defense Technical Information Center, July 2003. http://dx.doi.org/10.21236/ada418759.

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