Relevant bibliographies by topics / Proteins. Nucleic acids

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

Academic literature on the topic 'Proteins. Nucleic acids'

Author: Grafiati
Published: 4 June 2021
Last updated: 2 February 2022

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Journal articles on the topic "Proteins. Nucleic acids"

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null. "Nod2 nucleic acids and proteins." Expert Opinion on Therapeutic Patents 13, no. 1 (2003): 111–14. http://dx.doi.org/10.1517/eotp.13.1.111.20928.

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IKEHARA, Morio. "From Nucleic Acids to Proteins." YAKUGAKU ZASSHI 111, no. 3 (1991): 170–81. http://dx.doi.org/10.1248/yakushi1947.111.3_170.

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Goodchild, John. "Antisense nucleic acids and proteins." Cell Biophysics 18, no. 3 (June 1991): 295–96. http://dx.doi.org/10.1007/bf02989820.

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Gallagher, Sean R. "Quantitation of Nucleic Acids and Proteins." Current Protocols Essential Laboratory Techniques 00, no. 1 (January 2008): 2.2.1–2.2.29. http://dx.doi.org/10.1002/9780470089941.et0202s00.

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COOPER, ALAN. "Dynamics of Proteins and Nucleic Acids." Biochemical Society Transactions 16, no. 2 (April 1, 1988): 220–21. http://dx.doi.org/10.1042/bst0160220a.

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Mccammon, J. Andrew, Stephen C. Harvey, and Peter G. Wolynes. "Dynamics of Proteins and Nucleic Acids." Physics Today 41, no. 9 (September 1988): 105–6. http://dx.doi.org/10.1063/1.2811564.

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Wüthrich, Kurt. "NMR with Proteins and Nucleic Acids." Europhysics News 17, no. 1 (1986): 11–13. http://dx.doi.org/10.1051/epn/19861701011.

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Fritzsche, H. "Dynamics of Proteins and Nucleic Acids." Journal of Electroanalytical Chemistry and Interfacial Electrochemistry 253, no. 3 (September 1988): 595–96. http://dx.doi.org/10.1016/0022-0728(88)87105-5.

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Plum, G. Eric, and Kenneth J. Breslauer. "Calorimetry of proteins and nucleic acids." Current Opinion in Structural Biology 5, no. 5 (October 1995): 682–90. http://dx.doi.org/10.1016/0959-440x(95)80062-x.

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Roberts, G. C. K. "Dynamics of proteins and nucleic acids." Trends in Biochemical Sciences 13, no. 1 (January 1988): 35–36. http://dx.doi.org/10.1016/0968-0004(88)90019-9.

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Dissertations / Theses on the topic "Proteins. Nucleic acids"

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Butler, Thomas. "Nanopore analysis of nucleic acids /." Thesis, Connect to this title online; UW restricted, 2007. http://hdl.handle.net/1773/9674.

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Horowitz, Eric D. "Intercalator-mediated assembly of nucleic acids." Diss., Georgia Institute of Technology, 2009. http://hdl.handle.net/1853/33937.

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The RNA World hypothesis suggests that RNA, or a proto-RNA, existed in an early form of life that had not yet developed the ability to synthesize protein enzymes. This hypothesis, by some interpretations, implies that nucleic acid polymers were the first polymers of life, and must have therefore spontaneously formed from simple molecular building blocks in the "prebiotic soup." Although prebiotic chemists have searched for decades for a process by which RNA can be made from plausible prebiotic reactions, numerous problems persist that stand in the way of a chemically-sound model for the spontaneous generation of an RNA World (e.g., strand-cyclization, heterogeneous backbones, non-selective ligation of activated nucleotides). The Molecular Midwife hypothesis, proposed by Hud and Anet in 2000, provides a possible solution to several problems associated with the assembly of the first nucleic acids. In this hypothesis, nucleic acid base pairs are assembled by small, planar molecules that resemble molecules which are known today to intercalate the base pairs of nucleic acid duplexes. Thus, the validity and merits of the Molecular Midwife hypothesis can be, to some extent, explored by studying the effects of intercalation on the non-covalent assembly of nucleic acids. In this thesis, I explore the role of the sugar-phosphate backbone in dictating the structure and thermodynamics of nucleic acid intercalation by using 2′,5′-linked RNA intercalation as a model system of non-natural nucleic acid intercalation. The solution structure of an intercalator-bound 2′,5′ RNA duplex reveals structural and thermodynamic aspects of intercalation that provide insight into the origin of the nearest-neighbor exclusion principle, a principle that is uniformly obeyed upon the intercalation of natural (i.e. 3′,5′-linked) RNA and DNA. I also demonstrate the ability of intercalator-mediated assembly to circumvent the strand-cyclization problem, a problem that otherwise greatly limits the polymerization of short oligonucleotides into long polymers. Together, the data presented in this thesis illustrate the important role that the nucleic acid backbone plays in governing the thermodynamics of intercalation, and provide support for the proposed role of intercalator-mediated assembly in the prebiotic formation of nucleic acids.
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Chen, Baoshan. "Encapsidation of nucleic acids by cucumovirus coat proteins /." Title page, contents and summary only, 1991. http://web4.library.adelaide.edu.au/theses/09PH/09phc5183.pdf.

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Guo, Maolin. "Proteins and nucleic acids as targets for titanium(IV)." Thesis, University of Edinburgh, 2000. http://hdl.handle.net/1842/13967.

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TiIV compounds have pronounced anticancer, antiviral and antibacterial activities, and titanocene dichloride (TDC) is currently on phase II clinical trials as an anticancer drug. However, the biological chemistry and mechanisms of action of TiIV are poorly understood. Proteins and nucleic acids are expected to be biological targets for TiIV. Human transferrin (hTF) is a bilobal serum glycoprotein (80 kDa) which transports FeIII to cells via receptor-mediated endocytosis. A structurally similar periplasmic iron binding protein (FBP, 34 kDa) is present in some pathogenic bacteria and is required for virulence. In this thesis, the aqueous coordination chemistry of TiIV with the phenolate ligand N,N'-ethylene-bis-(o-hydroxyphenylglycine)(H4ehpg) was investigated as a model for Ti-hTF (or FBP) interactions. TiIV forms 7-coordinae monomer (rac) and dimer (meso) complexes with H4ehpg (rac + meso) with novel stereo-selectivity. 1H and 31P NMR studies show that TDC binds selectivity to H4ehpg at neutral pH, but preferentially to adenosine triphosphate (APT) at pH values below 5; TiIV transfers from TiIV-ehpg to ATP at acidic pH values. The interactions of TDC with hTF and that of Ti2-hTF with ATP have characteristics which could allow transferrin to act as a mediator for titanium delivery to tumour cells. TDC reacts rapidly with apo-hTF under extra-cellular conditions and binds in the specific FeIII sites with release of the Cp and Cl ligands. TiIV is readily released from Ti2-hTF at endosomal pH (ca 5.0) and in the presence of ATP. Ti2hTF competes effectively for cell uptake of 59Fe-hTF into BeWo cancer cells. TDC binds strongly to the phosphate group of nucleotides in aqueous solution and TiIV binds to the phosphodiester groups of nucleotides in the less polar solvent N,N-dimethylformamide. This behaviour contrasts with that of the anticancer drug cisplatin which binds mainly to N-sites of nucleobases, and may account for the intracellular localisation behaviour of TiIV drugs.
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Forties, Robert A. "Applications of statistical mechanics to nucleic acids." The Ohio State University, 2011. http://rave.ohiolink.edu/etdc/view?acc_num=osu1311022751.

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Fernández, Estrabao César. "The NMR structure of proteins, nucleic acids and their complexes /." Zürich, 1999. http://e-collection.ethbib.ethz.ch/show?type=diss&nr=13055.

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Klyashtornyy, Vladislav. "Principles of protein nucleic acid : recognition on the examples of the ribosomal protein L1 and the cold shock domain of YB-1 protein." Thesis, Evry-Val d'Essonne, 2012. http://www.theses.fr/2011EVRY0039/document.

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Cette thèse est une étude structurale sur l’interaction entre 2 protéines modèles et des acides nucléiques : la protéine L1 (navette ribosome/ARN messagers) et le sous domaine CSD de YB-1, protéine régulatrice de la transcription et traduction. Deux méthodes sont utilisées : i) diffraction des RX par des cristaux de complexes L1:ARN ribosomal ou messager et ii) modélisation et dynamique moléculaire pour l’interaction CSD avec des homo-ribo- ou homo-deoxyribo-nucléotides simple brin. Les méthodes sont décrites avec leurs forces et limites. Les résultats sur L1-rARN/ARN éclairent les mécanismes de régulation de la traduction en montrant des différences d’affinité pour l’ARN des sous domaines I et II de L1. L’analyse de mutants de L1 dans le site de liaison à l’ARN du sous domaine I éclairent la nature des liaisons non covalentes sous tendant l’affinité de ce sous domaine pour l’ARN et souligne l’importance de la structure de L1, de sa « complémentarité » avec l’ARN et de liaisons hydrogènes non accessibles au solvant. Les travaux de modélisation et de dynamique moléculaire sur l’interaction CSD:acides nucléiques montrent que la séquence nucléotidique module l’affinité de ce complexe, l’oligonucléotide de type oligoG donnant le complexe le plus stable suivi des séquences de type oligoU et oligoA puis des oligoT et oligoC. L’orientation du brin d’ARN par rapport au CSD impacte aussi la stabilité du complexe. Une analyse des surfaces d’interaction et de la nature des liaisons intermoléculaires, montre que des principes similaires guident l’interaction L1:ARN et CSD:acides nucléiques : géométrie complémentaire des partenaires et liaisons hydrogène protégées du solvant
This thesis is a structural study on the interaction between two model proteins and nucleic acids: the L1 protein (shuttle ribosome/mRNA) and the CSD subdomain of YB-1, a protein that regulates transcription and translation. Two methods are used: i) X-ray diffraction by crystals of L1:ribosomal or messenger RNA complexes and ii) molecular modeling and dynamics for the CSD interaction with homo-ribo or homo-deoxyribo- single-stranded nucleotide. The methods are described with their strengths and limitations. Results on L1-rARN/ARN enlighten the mechanisms regulating translation by showing differences in affinity for RNA of the subdomains I and II of L1. Analyses of L1 mutants in the RNA binding site from the subdomain I illuminate the nature of non-covalent bonds subtending the affinity of this subdomain for RNA and stress the importance of the structure of L1, its "complementarity" with RNA and of hydrogen bonds not accessible to the solvent. Molecular modeling and dynamics of the CSD:nucleic acids interaction shows that the nucleotide sequence modulates the affinity of the complex, oligoG giving the most stable complex followed by oligoU and then oligoA or oligoT and oligoC. The orientation of the RNA strand relative to the CSD also impacts the stability of the complex. An analysis of the interaction surfaces and of the nature of intermolecular bonds, shows that similar principles guide the L1: RNA and CSD: nucleic acids interactions, i.e. a complementary geometry between partners and presence of hydrogen bonds protected from the solvent
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Kalafut, Bennett Samuel. "Optical Tweezers studies of Nucleic Acids and their Interaction with Proteins." Diss., The University of Arizona, 2011. http://hdl.handle.net/10150/202969.

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Mechanics and biological function of nucleic acids are intimately coupled. The DNA double helix must be opened to allow base pairing of RNA during transcription; RNA must bend and fold in its many cellular functions. Presented in this dissertation are two investigations of mechanical deformations of nucleic acids, conducted with optical tweezers.In the introduction, the mechanical properties of DNA and RNA and their relevance to their cellular functions are introduced, to give the reader context for the results presented in the Chapters 2 and 3. This is followed by an introduction to the theory of semiflexible polymer elasticity. The optical tweezers instruments used in conducting these investigations are then presented, along with calibration procedures and a short introduction to optical trapping physics.Chapter 2 presents an investigation of the effect of downstream DNA tension on initiation by T7 RNA polymerase. A hidden Markov model is fit to force-dependent lifetimes obtained from optical tweezers experiments, allowing us to identify which steps in initiation are force-dependent and estimate rates and transition state distances. We find that 1-2 pN of tension is sufficient to turn o gene expression by causing transcription bubble collapse and destabilizing the bound state. Our force-dependence scheme and estimated transition distances provide independent supportfor the \scrunching" model of initiation.The effects of cation binding and screening on single-stranded helix formation in poly(A) RNA are presented in Chapter 3. Magnesium and calcium bind to poly(A), stabilize the helix, and change its mechanical properties. A new model of helix-coil transitions is presented and used to estimate energetics and mechanical properties.Chapter 4 presents the first fully objective algorithm for use in analyzing the noisy staircaselike data that is often produced by single-molecule fluorescence experiments. A test based on the SIC (BIC) statistic is used in conjunction with a progressive step-placement scheme to locate changepoints (steps) in noisy data. Its performance is compared to other step detection algorithms in use by biophysicists by repeating tests performed in a recent review.Experimental protocols and computer codes used in these investigations are presentedin detail in the appendices.
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Furman, Jennifer Lynn. "IN VITRO AND IN VIVO DETECTION OF NUCLEIC ACIDS AND PROTEINS USING SPLIT-PROTEIN REASSEMBLY." Diss., The University of Arizona, 2010. http://hdl.handle.net/10150/195828.

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The ability to directly monitor the presence of specific proteins or nucleic acids in a variety of in vitro and in vivo contexts has great utility for understanding biology as well as for the development of diagnostic agents. Herein I describe several methodologies, utilizing split-protein reassembly, which provides potentially general strategies for sequence-specific detection of DNA and RNA sequences as well as poly(ADP-ribose). I also provide a new split-protein approach for the direct detection of native proteins, such as the cancer marker HER2.The green fluorescent protein (GFP) provides a convenient sensor for reporting on a variety of cellular events. A series of spectroscopically distinct GFP variants was developed for sequence-specifically reporting on DNA. Each of these variants was demonstrated to provide a sensitive readout for the presence of a particular DNA sequence. Furthermore, utilizing a method of mixed split-protein complementation, I was able to simultaneously report on the presence of two distinct DNA sequences in the same solution.To provide a general solution for reporting on the presence of particular RNA sequences, a method was developed that utilized elements from a hybridization-based detection strategy coupled with split-protein reassembly. Specifically, DNA guide sequences complementary to an intended target were attached to hairpin sites that served as binding sites for high-affinity zinc fingers. Localization of the zinc fingers allowed for reassembly of the attached split enzyme, providing a sensitive readout for the presence of potentially any RNA sequence of interest. This methodology was applied to the detection of mRNA encoding VEGF, hDM2, and HER2, each of which may be overexpressed in cancer.A method was established for reporting on the presence of modifications to DNA and proteins that are elicited in response to DNA damage. Specifically, sensors were designed, which incorporated endogenous damage-recognition domains, to report on the global presence of particular DNA modifications, including the formation of 8-oxoguanine and pyrimidine dimers. Furthermore, to provide a technique for monitoring the general accrual of DNA damage and to interrogate the DNA damage response in cells, a sensor was developed which reported on the accrual of a posttranslational protein modification, poly(ADP-ribosyl)ation.Finally, I describe advances toward the adaptation of our protein-based biosensors for use in living cells, utilizing both GFP-based approaches for live cell imaging as well as luminescent-based strategies for reporting on proteins and nucleic acids following cell lysis.
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Pérez, González Daniel Cibrán. "Single-molecule studies of nucleic acid folding and nucleic acid-protein interactions." Thesis, University of St Andrews, 2017. http://hdl.handle.net/10023/12039.

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Nucleic acids and proteins, some of the building blocks of life, are not static structures but highly dynamic entities that need to interact with one another to meet cellular demands. The work presented in this thesis focuses on the application of highly sensitive fluorescence methods, both at ensemble and single-molecule level, to determine the dynamics and structure of specific biomolecular interactions with nanometer resolution and in temporal scales from nanoseconds to minutes, which includes most biologically relevant processes. The main aims of my PhD can be classified in three areas: i) exploring new fluorescent sensors with increased specificity for certain nucleic acid structures; ii) understanding how some of these nucleic acids sense the presence of small molecules in the cellular environment and trigger gene regulation by altering their structure; and iii) understanding how certain molecular machines, such as helicase proteins, are able to unwind the DNA double helix by using chemical energy in the form of ATP hydrolysis.
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Books on the topic "Proteins. Nucleic acids"

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NMR of proteins and nucleic acids. New York: Wiley, 1986.

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C, Harvey Stephen, ed. Dynamics of proteins and nucleic acids. Cambridge: Cambridge University Press, 1988.

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Nannipieri, Paolo, and Kornelia Smalla, eds. Nucleic Acids and Proteins in Soil. Berlin, Heidelberg: Springer Berlin Heidelberg, 2006. http://dx.doi.org/10.1007/3-540-29449-x.

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C, Harvey Stephen, ed. Dynamics of proteins and nucleic acids. Cambridge [Cambridgeshire]: Cambridge University Press, 1987.

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1953-, Budowle Bruce, ed. Gel electrophoresis of proteins and nucleic acids: Selected techniques. Berlin: W. de Gruyter, 1994.

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International Symposium on Structure and Dynamics of Nucleic Acids, Proteins, and Membranes (1986 Riva, Italy). Structure and dynamics of nucleic acids, proteins, and membranes. New York: Plenum Press, 1986.

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Clementi, Enrico, and Steven Chin, eds. Structure and Dynamics of Nucleic Acids, Proteins, and Membranes. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-5308-9.

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Dahlem Workshop on Simplicity and Complexity in Proteins and Nucleic Acids (83rd 1998 Berlin, Germany). Simplicity and complexity in proteins and nucleic acids: Report of the 83rd Dahlem Workshop on Simplicity and Complexity in Proteins and Nucleic Acids, Berlin, May 17-22, 1998. Berlin: Dahlem University Press, 1999.

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Spada, Stefania. Directory of approved biopharmaceutical products. Boca Raton: CRC Press, 2005.

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1939-, Sarma Ramaswamy H., and Sarma M. H. 1940-, eds. Structure & function: Proceedings of the Seventh Conversation in the Discipline Biomolecular Stereodynamics held at the State University of New York at Albany, June 18-22, 1991. Schenectady, NY, USA: Adenine Press, 1992.

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Book chapters on the topic "Proteins. Nucleic acids"

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Frauenfelder, Hans. "Nucleic Acids." In The Physics of Proteins, 37–46. New York, NY: Springer New York, 2010. http://dx.doi.org/10.1007/978-1-4419-1044-8_5.

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Urich, Klaus. "Nucleic Acids and Nuclear Proteins." In Comparative Animal Biochemistry, 9–69. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-662-06303-3_2.

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Hyman, Bradley C. "Nucleic Acids and Proteins." In Introduction to Bioinformatics, 5–23. Totowa, NJ: Humana Press, 2003. http://dx.doi.org/10.1007/978-1-59259-335-4_1.

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Higgs, Paul G., and Teresa K. Attwood. "Nucleic Acids, Proteins, and Amino Acids." In Bioinformatics and Molecular Evolution, 12–36. Malden, MA USA: Blackwell Publishing Ltd., 2013. http://dx.doi.org/10.1002/9781118697078.ch2.

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Vollhardt, Peter, and Neil Schore. "Amino Acids, Peptides, Proteins, and Nucleic Acids." In Organic Chemistry, 2013–111. New York: Macmillan Learning, 2014. http://dx.doi.org/10.1007/978-1-319-19197-9_26.

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Durzan, D. J. "Amino Acids, Proteins, Enzymes, and Nucleic Acids." In Natural Products of Woody Plants, 179–200. Berlin, Heidelberg: Springer Berlin Heidelberg, 1989. http://dx.doi.org/10.1007/978-3-642-74075-6_6.

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Price, C. M. "Telomere-Binding Proteins of Ciliated Protozoa." In Nucleic Acids and Molecular Biology, 299–307. Berlin, Heidelberg: Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-79488-9_15.

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Pankratz, M. J., M. Hoch, M. Rothe, U. Nauber, N. Gerwin, G. Brönner, K. Goerlich, and H. Jäckle. "DNA-Binding Proteins in Drosophila Development." In Nucleic Acids and Molecular Biology, 185–204. Berlin, Heidelberg: Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-84150-7_12.

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Lehming, N., J. Sartorius, B. Kisters-Woike, B. von Wilcken-Bergmann, and B. Müller-Hill. "Rules for Protein DNA Recognition for a Family of Helix-Turn-Helix Proteins." In Nucleic Acids and Molecular Biology, 114–25. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-84292-4_8.

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Ferré-D’Amaré, A. R., and S. K. Burley. "DNA Recognition by Helix-Loop-Helix Proteins." In Nucleic Acids and Molecular Biology, 285–98. Berlin, Heidelberg: Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-79488-9_14.

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Conference papers on the topic "Proteins. Nucleic acids"

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Ross, J. B. Alexander, Carol A. Hasselbacher, Elena Rusinova, D. F. Senear, and William R. Laws. "Pseudointrinsic probes for generating spectrally enhanced proteins and nucleic acids." In Photonics West '95, edited by Gerald E. Cohn, Jeremy M. Lerner, Kevin J. Liddane, Alexander Scheeline, and Steven A. Soper. SPIE, 1995. http://dx.doi.org/10.1117/12.206034.

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ADAMCZYK, MACIEJ, PHILLIP G. MATTINGLY, JEFFREY A. MOORE, and SUSHIL D. REGE. "THIOL-SPECIFIC ACRIDINIUM REAGENTS FOR LABELING PROTEINS AND NUCLEIC ACIDS." In Proceedings of the 11th International Symposium. WORLD SCIENTIFIC, 2001. http://dx.doi.org/10.1142/9789812811158_0082.

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Vrabel, Milan, Emine Kaya, and Thomas Carell. "Incorporation of unnatural amino acids into proteins for click chemistry." In XVth Symposium on Chemistry of Nucleic Acid Components. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 2011. http://dx.doi.org/10.1135/css201112487.

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Larabell, Carolyn A. "Localization of proteins and nucleic acids using soft x-ray microscopy." In Sixth international conference on x-ray microscopy (XRM99). AIP, 2000. http://dx.doi.org/10.1063/1.1291126.

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Olive, Mike, Amy Geschwender, Huaxian Chen, Marjeta Urh, Margaret Esser, and Yonghong Zhang. "Application of infrared fluorescent technology for the analysis of proteins and nucleic acids." In International Symposium on Biomedical Optics, edited by Darryl J. Bornhop, David A. Dunn, Raymond P. Mariella, Jr., Catherine J. Murphy, Dan V. Nicolau, Shuming Nie, Michelle Palmer, and Ramesh Raghavachari. SPIE, 2002. http://dx.doi.org/10.1117/12.472079.

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Lisdat, F., M. Riedel, and F. Heinrich. "BS4.2 - Label-free detection of nucleic acids and proteins using impedance spectroscopy and surface plasmon resonance." In 17th International Meeting on Chemical Sensors - IMCS 2018. AMA Service GmbH, Von-Münchhausen-Str. 49, 31515 Wunstorf, Germany, 2018. http://dx.doi.org/10.5162/imcs2018/bs4.2.

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Lewis, Jean M., David Searson, Alfred Kinana, Heath Balcer, Debrah Thompson, David Bodkin, Juan P. Hinestrosa, and Rajaram Krishnan. "Abstract 3978: Direct analysis of exosome-bound proteins and nucleic acids using the ExoVerita™ Flex platform." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-3978.

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Lewis, Jean M., David Searson, Alfred Kinana, Heath Balcer, Debrah Thompson, David Bodkin, Juan P. Hinestrosa, and Rajaram Krishnan. "Abstract 3978: Direct analysis of exosome-bound proteins and nucleic acids using the ExoVerita™ Flex platform." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-3978.

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Beechem, Joseph, Liz Manrao, Marty Ross, Gokhan Demirkan, Brian Filanoski, Brian Birditt, Celine Ngouenet, et al. "Abstract A013: Biomarker development for cancer immuno-oncology/immunotherapy: Simultaneous digital counting of nucleic acids and proteins at 800-plex." In Abstracts: CRI-CIMT-EATI-AACR Inaugural International Cancer Immunotherapy Conference: Translating Science into Survival; September 16-19, 2015; New York, NY. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/2326-6074.cricimteatiaacr15-a013.

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Beechem, Joseph M., Gary Geiss, Brian Filanoski, and Brian Birditt. "Abstract 4749: Simultaneous multi-omic measurement of nucleic-acids and proteins at 800-plex using single-molecule optical barcodes: Application to cancer immunotherapy." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-4749.

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Reports on the topic "Proteins. Nucleic acids"

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Whalen, Janey D. Peptide-Mediated Transduction of Proteins and Nucleic Acids to Prevent and Treat Experimental Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, April 2005. http://dx.doi.org/10.21236/ada611051.

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Richards, John H., John N. Abelson, Leroy E. Hood, Melvin I. Simon, and Judith L. Campbell. Biopolymers: Protein and Nucleic Acids. Fort Belvoir, VA: Defense Technical Information Center, September 1987. http://dx.doi.org/10.21236/ada185837.

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Silver, Pamela A. Genome-Wide Nucleic Acid/Protein Interaction in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, April 2005. http://dx.doi.org/10.21236/ada435620.

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Silver, Pamela A. Genome-Wide Nucleic Acid/Protein Interaction in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, May 2004. http://dx.doi.org/10.21236/ada426138.

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Silver, Pamela A. Genome-Wide Nucleic Acid/Protein Interactions in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, May 2003. http://dx.doi.org/10.21236/ada416691.

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Berman, Helen M., and Janet Thornton. PROTEIN NUCLEIC ACID INTERACTIONS GRANT # DE-FG02-96ER62166 FINAL REPORT. Office of Scientific and Technical Information (OSTI), February 2005. http://dx.doi.org/10.2172/836885.

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Trewhella, J., E. M. Bradbury, G. Gupta, B. Imai, R. Martinez, and C. Unkefer. Development of experimental techniques to study protein and nucleic acid structures. Office of Scientific and Technical Information (OSTI), April 1996. http://dx.doi.org/10.2172/212551.

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Pawlowski, David R. Automated Sample Preparation (ASP): Development of a Rapid Method to Sequentially Isolate Nucleic Acids and Protein from Any Sample Type by a Cartridge-Based System. Fort Belvoir, VA: Defense Technical Information Center, November 2013. http://dx.doi.org/10.21236/ada608052.

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