Journal articles: '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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Shugar, David. "Dynamics of proteins and nucleic acids." FEBS Letters 253, no. 1-2 (August 14, 1989): 289. http://dx.doi.org/10.1016/0014-5793(89)80979-2.

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Smith, BB. "Dynamics of Proteins and Nucleic Acids." Biochemical Education 17, no. 4 (October 1989): 220. http://dx.doi.org/10.1016/0307-4412(89)90164-7.

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Kerkut, G. A. "Dynamics of proteins and nucleic acids." Comparative Biochemistry and Physiology Part A: Physiology 92, no. 1 (January 1989): 152. http://dx.doi.org/10.1016/0300-9629(89)90770-6.

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Bailey, C. "Dynamics of proteins and nucleic acids." FEBS Letters 230, no. 1-2 (March 28, 1988): 215. http://dx.doi.org/10.1016/0014-5793(88)80677-x.

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Buckle, M. "Dynamics of proteins and nucleic acids." Biochimie 70, no. 1 (January 1988): 131. http://dx.doi.org/10.1016/0300-9084(88)90167-8.

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Fritzsche, H. "Dynamics of Proteins and Nucleic Acids." Bioelectrochemistry and Bioenergetics 19, no. 3 (September 1988): 595–96. http://dx.doi.org/10.1016/0302-4598(88)80049-7.

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Rice, David. "Crystallization of nucleic acids and proteins." Trends in Biochemical Sciences 17, no. 9 (September 1992): 364. http://dx.doi.org/10.1016/0968-0004(92)90316-2.

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W.S.B. "NMR of proteins and nucleic acids." Journal of Magnetic Resonance (1969) 79, no. 3 (October 1988): 586. http://dx.doi.org/10.1016/0022-2364(88)90098-4.

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Lesk, V. I., and A. M. Lesk. "Schematic diagrams of nucleic acids and protein–nucleic acid complexes." Journal of Applied Crystallography 22, no. 6 (December 1, 1989): 569–71. http://dx.doi.org/10.1107/s0021889889008265.

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Simplified representations of components of nucleic acids have been designed and implemented as programs integrated with other software that draws schematic diagrams of proteins. Examples illustrating the structures of oligonucleotides, tRNA and a protein–nucleic acid complex indicate the utility of these representations for making intelligible illustrations of complex structures containing nucleic acids.

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Mashaghi, Alireza, Roeland J. van Wijk, and Sander J. Tans. "Circuit Topology of Proteins and Nucleic Acids." Structure 22, no. 9 (September 2014): 1227–37. http://dx.doi.org/10.1016/j.str.2014.06.015.

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Alongi, Jenny, Fabio Cuttica, Alessandro Di Blasio, Federico Carosio, and Giulio Malucelli. "Intumescent features of nucleic acids and proteins." Thermochimica Acta 591 (September 2014): 31–39. http://dx.doi.org/10.1016/j.tca.2014.06.020.

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Harborne, Jeffrey B. "Proteins and nucleic acids in plant systematics." Phytochemistry 24, no. 1 (January 1985): 209. http://dx.doi.org/10.1016/s0031-9422(00)80849-3.

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Karger, B. L., Y. H. Chu, and F. Foret. "Capillary Electrophoresis of Proteins and Nucleic Acids." Annual Review of Biophysics and Biomolecular Structure 24, no. 1 (June 1995): 579–610. http://dx.doi.org/10.1146/annurev.bb.24.060195.003051.

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IKEHARA, M. "ChemInform Abstract: From Nucleic Acids to Proteins." ChemInform 22, no. 35 (August 22, 2010): no. http://dx.doi.org/10.1002/chin.199135322.

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Leavy, Olive. "HMGB proteins: universal sensors for nucleic acids." Nature Reviews Immunology 9, no. 12 (December 2009): 819. http://dx.doi.org/10.1038/nri2676.

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van Gunsteren, W. F. "Molecular dynamics of proteins and nucleic acids." Fresenius' Zeitschrift für analytische Chemie 327, no. 1 (January 1987): 69–70. http://dx.doi.org/10.1007/bf00474578.

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von Hippel, Peter H. "Close encounters of nucleic acids and proteins." Cell 42, no. 2 (September 1985): 407–8. http://dx.doi.org/10.1016/0092-8674(85)90095-9.

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Paleček, Emil, Martin Bartošík, Veronika Ostatná, and Mojmír Trefulka. "Electrocatalysis in proteins, nucleic acids and carbohydrates." Chemical Record 12, no. 1 (January 30, 2012): 27–45. http://dx.doi.org/10.1002/tcr.201100029.

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van Gijlswijk, Rob PM, Eduard G. Talman, Inge Peekel, Judith Bloem, Marcel A. van Velzen, Rob J. Heetebrij, and Hans J. Tanke. "Use of Horseradish Peroxidase- and Fluorescein-modified Cisplatin Derivatives for Simultaneous Labeling of Nucleic Acids and Proteins." Clinical Chemistry 48, no. 8 (August 1, 2002): 1352–59. http://dx.doi.org/10.1093/clinchem/48.8.1352.

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Abstract Background: Microarray platforms will change immunochemical and nucleic acid-based analysis of cell homogenates and body fluids compared with classic analyses. Microarrays use labeled target and immobilized probes, rather than fixed targets and labeled probes. We describe a method for simultaneous labeling of nucleic acids and proteins. Methods: Horseradish peroxidase- and fluorescein-modified cisplatin derivatives were used for labeling of nucleic acids and proteins. These reagents, called the Universal Linkage System (ULS), bind to sulfur- and nitrogen-donor ligands present in amino acids and nucleotides. For automated screening of proteins and nucleic acids on microarrays, it is advantageous to label these biomolecules without pre- or postpurification procedures. The labeling of antibodies and nucleic acids in whole serum was therefore pursued. Results: Immunoglobulins in nonpurified serum were labeled efficiently enough to be used for immunochemistry. To investigate whether protein-adapted labeling allowed nucleic acid labeling as well, 1 μg of plasmid DNA was added to 1 μL of serum. DNA and serum proteins were simultaneously labeled, and this labeled DNA could be used as a probe for direct fluorescence in situ hybridization. Conclusion: ULS provides a direct labeling tool for the (simultaneous) modification of proteins and nucleic acids even in unpurified samples.

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Roller, R. J., A. L. McCormick, and B. Roizman. "Cellular proteins specifically bind single- and double-stranded DNA and RNA from the initiation site of a transcript that crosses the origin of DNA replication of herpes simplex virus 1." Proceedings of the National Academy of Sciences 86, no. 17 (September 1989): 6518–22. http://dx.doi.org/10.1073/pnas.86.17.6518.

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The small-component origins of herpes simplex virus 1 DNA synthesis are transcribed late in infection by an RNA with heterogeneous initiation sites approximately 290-360 base pairs from the origins. We report that cellular proteins react with a labeled RNA probe representing the 5' terminus of a subset of this RNA but not with the complementary strand of this RNA. The proteins form two complexes. Complex 2 was formed by all nuclear extracts tested, whereas complex 1 was invariably formed by proteins present only in nuclear extracts of mock-infected cells. Complex 1 protects a contiguous stretch of 40 nucleotides of the labeled RNA probe from nuclease degradation. Formation of complex 1 was competitively inhibited in a sequence-specific fashion by single-stranded RNA and DNA and by double-stranded RNA and DNA. The protein(s) forming complex 1 is, thus, quite distinct from known nucleic acid-binding proteins in that they recognize a specific nucleotide sequence, irrespective of the nature (single- and double-stranded RNA and DNA) of the nucleic acid. We conclude the following: (i) the proteins forming complex 1 and 2 are probably different, (ii) complex 1 is neither required throughout infection for viral replication nor able to hinder viral replication in cells in culture, and (iii) cells susceptible to infection encode one or more proteins that recognize specific sequences in single-stranded nucleic acids; either these proteins impart a compatible conformation on single-stranded nucleic acids with the conformation of the same strand in the double-stranded nucleic acid, or these proteins confer a specific, distinct conformation to both single-stranded and double-stranded nucleic acids.

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Kang, Hong Soon, Ju Youn Beak, Yong-Sik Kim, Robert M. Petrovich, Jennifer B. Collins, Sherry F. Grissom, and Anton M. Jetten. "NABP1, a novel RORγ-regulated gene encoding a single-stranded nucleic-acid-binding protein." Biochemical Journal 397, no. 1 (June 14, 2006): 89–99. http://dx.doi.org/10.1042/bj20051781.

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RORγ2 (retinoid-related orphan receptor γ2) plays a critical role in the regulation of thymopoiesis. Microarray analysis was performed in order to uncover differences in gene expression between thymocytes of wild-type and RORγ−/− mice. This analysis identified a novel gene encoding a 22 kDa protein, referred to as NABP1 (nucleic-acid-binding protein 1). This subsequently led to the identification of an additional protein, closely related to NABP1, designated NABP2. Both proteins contain an OB (oligonucleotide/oligosaccharide binding) motif at their N-terminus. This motif is highly conserved between the two proteins. NABP1 is highly expressed in the thymus of wild-type mice and is greatly suppressed in RORγ−/− mice. During thymopoiesis, NABP1 mRNA expression is restricted to CD4+CD8+ thymocytes, an expression pattern similar to that observed for RORγ2. These observations appear to suggest that NABP1 expression is regulated either directly or indirectly by RORγ2. Confocal microscopic analysis showed that the NABP1 protein localizes to the nucleus. Analysis of nuclear proteins by size-exclusion chromatography indicated that NABP1 is part of a high molecular-mass protein complex. Since the OB-fold is frequently involved in the recognition of nucleic acids, the interaction of NABP1 with various nucleic acids was examined. Our results demonstrate that NABP1 binds single-stranded nucleic acids, but not double-stranded DNA, suggesting that it functions as a single-stranded nucleic acid binding protein.

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Williams, LR. "Staining nucleic acids and proteins in electrophoresis gels." Biotechnic and Histochemistry 76, no. 3 (May 1, 2001): 127–32. http://dx.doi.org/10.1080/714028140.

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Meisenheimer, Kristen M., and Tad H. Koch. "Photocross-Linking of Nucleic Acids to Associated Proteins." Critical Reviews in Biochemistry and Molecular Biology 32, no. 2 (January 1997): 101–40. http://dx.doi.org/10.3109/10409239709108550.

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Maekawa, Koji. "Informational symmetry breaking between proteins and nucleic acids." Biosystems 51, no. 1 (July 1999): 21–29. http://dx.doi.org/10.1016/s0303-2647(99)00008-8.

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Ghoshroy, Soumitra, Robert Lartey, Jinsong Sheng, and Vitaly Citovsky. "TRANSPORT OF PROTEINS AND NUCLEIC ACIDS THROUGH PLASMODESMATA." Annual Review of Plant Physiology and Plant Molecular Biology 48, no. 1 (June 1997): 27–50. http://dx.doi.org/10.1146/annurev.arplant.48.1.27.

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Williams, LR. "Staining nucleic acids and proteins in electrophoresis gels." Biotechnic & Histochemistry 76, no. 3 (January 2001): 127–32. http://dx.doi.org/10.1080/bih.76.3.127.132.

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Kubasek, William L., Joel W. Hockensmith, William Vorachek, Dennis Spann, Kirsten T. Munck, Elizabeth Evertsz, and Peter H. Von Hippel. "UV laser crosslinking of proteins with nucleic acids." Berichte der Bunsengesellschaft für physikalische Chemie 93, no. 3 (March 1989): 406–10. http://dx.doi.org/10.1002/bbpc.19890930337.

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Bhat, Vinayak, Richard Cogdell, Carlos E. Crespo-Hernández, Ankona Datta, Arijit De, Stefan Haacke, John Helliwell, et al. "Photocrosslinking between nucleic acids and proteins: general discussion." Faraday Discussions 207 (2018): 283–306. http://dx.doi.org/10.1039/c8fd90005a.

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LEVY, R. M. "Biomolecular Processes: Dynamics of Proteins and Nucleic Acids." Science 241, no. 4862 (July 8, 1988): 234–35. http://dx.doi.org/10.1126/science.241.4862.234.

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Hayes, J. D., and P. K. Stockman. "Electrophoresis of proteins and nucleic acids: I--Theory." BMJ 299, no. 6703 (September 30, 1989): 843–46. http://dx.doi.org/10.1136/bmj.299.6703.843.

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Verechshagina, N. A., Yu M. Konstantinov, P. A. Kamenski, and I. O. Mazunin. "Import of Proteins and Nucleic Acids into Mitochondria." Biochemistry (Moscow) 83, no. 6 (June 2018): 643–61. http://dx.doi.org/10.1134/s0006297918060032.

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Neidle, Stephen. "Antisense Nucleic Acids and Proteins: Fundamentals and Applications." International Journal of Biological Macromolecules 16, no. 2 (April 1994): 110. http://dx.doi.org/10.1016/0141-8130(94)90025-6.

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Berendsen, Herman J. C. "Molecular dynamics studies of proteins and nucleic acids." Current Opinion in Structural Biology 1, no. 2 (April 1991): 191–95. http://dx.doi.org/10.1016/0959-440x(91)90060-7.

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Fox, Ronald F. "Structure and motion: Membranes, nucleic acids and proteins." Trends in Biochemical Sciences 11, no. 3 (March 1986): 119. http://dx.doi.org/10.1016/0968-0004(86)90048-4.

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Wills, Peter R. "Spontaneous Mutual Ordering of Nucleic Acids and Proteins." Origins of Life and Evolution of Biospheres 44, no. 4 (December 2014): 293–98. http://dx.doi.org/10.1007/s11084-014-9396-z.

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Baulcombe, David. "Antisense nucleic acids and proteins: Fundamentals and applications." Trends in Genetics 9, no. 3 (March 1993): 94–95. http://dx.doi.org/10.1016/0168-9525(93)90232-7.

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Sugawara-Narutaki, Ayae, and Yukiko Kamiya. "Designer Biopolymers: Self-Assembling Proteins and Nucleic Acids." International Journal of Molecular Sciences 21, no. 9 (May 6, 2020): 3276. http://dx.doi.org/10.3390/ijms21093276.

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Chhetri, Khadka Bahadur. "Biophysics : Aspects of Amino Acids Sequence in Proteins and Nucleotide Sequence in Nucleic Acids." Himalayan Physics 4 (December 23, 2013): 65–74. http://dx.doi.org/10.3126/hj.v4i0.9431.

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Protein is the polypeptide chain of amino-acid sequence. Proteins of all species, from bacteria to humans, are made up from the same set of 20 standard amino acids. In order to carry out their function they must take a particular shape which is known as fold. All the enzymes hormones and antibodies are also proteins. To treat certain toxic-microorganism or invader we need certain antigen-antibody complex in the organisms. Just as amino-acid sequence forms the proteins, the polynucleotide sequence forms the nucleic acids. The gene is a part of DNA macromolecule responsible for the synthesis of protein chains. There are 20 amino-acids responsible for the formation of protein and 4 nucleotides responsible for the formation of DNA (RNA). Therefore, we can say that protein text is written in 20-letter and the DNA (RNA) text is written in 4-letter language. The information contained in genes in DNA is transferred to mRNA during transcription.The Himalayan Physics Vol. 4, No. 4, 2013 Page: 65-74 Uploaded date: 12/23/2013

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Baziramakenga, Régis, Gilles D. Leroux, Régis R. Simard, and Paul Nadeau. "Allelopathic effects of phenolic acids on nucleic acid and protein levels in soybean seedlings." Canadian Journal of Botany 75, no. 3 (March 1, 1997): 445–50. http://dx.doi.org/10.1139/b97-047.

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Experiments were carried out, in a controlled environment during a 4-h incubation period, to examine the effects of phenolic acids on uptake by soybean (Glycine max (L.) Merr cv. Maple Bell) roots of phosphate and methionine and their incorporation into nucleic acids and proteins, respectively. Benzoic, p-hydroxy benzoic, vanillic, cinnamic, p-coumaric, and ferulic acids were used in the study. Nucleic acid and protein synthesis were assayed by the incorporation of 32P and 35S-methionine into soybean root. The uptake of 32P was reduced by benzoic, cinnamic, vanillic, and ferulic acids, while p-hydroxybenzoic and p-coumaric acids increased slightly its absorption. At 250 μM, all allelochemicals tested reduced the incorporation of 32P into DNA and RNA. Benzoic, cinnamic, ferulic, and vanillic acids reduced the uptake of 32S-methionine, whereas p-hydroxybenzoic and p-coumaric acids increased its uptake. The methionine incorporation into proteins was reduced by all phenolic acids, except for p-coumaric acid and vanillic acid at 125 μM. These results suggest that interference with nucleic acid and protein metabolism by the phenolic acids is one of the main mechanisms by which they influence plant growth. Key words: Allelochemicals, mechanism of action, phenolic acids, phosphorus, proteins, methionine, ion uptake.

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Bloomfield, Victor A., and Patricia G. Arscott. "STM of nucleic acids." Proceedings, annual meeting, Electron Microscopy Society of America 48, no. 3 (August 12, 1990): 958. http://dx.doi.org/10.1017/s0424820100162351.

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Scanning tunneling microscopy (STM) enables remarkable visualization of surface topography with a vertical resolution of 0.2 Å and horizontal resolution of 2-3 Å. The possibility of visualizing nucleic acids at this high resolution has major significance, since the binding of proteins and other aspects of gene regulation depend on structural variations at the Å level. Conventional EM has the advantage over fiber diffraction or solution techniques that local structure of individual molecules can be seen, rather than averaging over entire molecules and populations of molecules. An added advantage of STM is that contrast is achieved by detection of sample height and work function variations, rather than by chemical treatments such as shadowing or staining.We have used STM to measure the helical pitch, half-period oscillations interpreted as alternating major and minor grooves, and molecular diameters of poly(rA)-poly(rU) and DNA. Average pitches are measured by two-dimensional Fourier transforms and by topographic profile peak count vs.

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Journal articles on the topic 'Proteins. Nucleic acids'

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