Relevant bibliographies by topics / S-ribonuclease

Academic literature on the topic 'S-ribonuclease'

Author: Grafiati
Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "S-ribonuclease"

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Diaz-Baena, Mercedes, Elena Delgado-García, Manuel Pineda, Gregorio Galvez-Valdivieso, and Pedro Piedras. "S-Like Ribonuclease T2 Genes Are Induced during Mobilisation of Nutrients in Cotyledons from Common Bean." Agronomy 11, no. 3 (March 6, 2021): 490. http://dx.doi.org/10.3390/agronomy11030490.

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Germination and seedling development are crucial phases in a plant’s life cycle with economical and agronomical implications. The RNA quality in seeds is linked to seed viability, being an important agronomic trait since this leads to a loss in germination efficiency. In addition, RNA can be an important phosphorous reservoir in seeds, affecting the efficiency of the mobilisation of nutrients towards the seedlings. However, knowledge about the physiological function of ribonucleases during germination and seedling development is scarce. We analysed the ribonuclease activities of cotyledons during these processes and the expression of S-like ribonucleases T2. Ribonuclease activity was detected in cotyledons at 1 day after imbibition and the specific activity increased during germination and seedling development, reaching a maximal value at 10 days after imbibition. At this stage, the levels of proteins and RNA in cotyledons were very low. Using in-gel assays, three ribonucleases were detected with apparent molecular masses of 16, 17 and 19 kDa along cotyledon ontogeny. The S-like ribonucleases T2 family consists of four genes in common bean (PvRNS1 to PvRNS4). The expression of PvRNS1, PvRNS2 and PvRNS4 increased in the phase of nutrient mobilisation in cotyledons. The expression of PvRNS1 increased 1000 fold in cotyledons, from 1 to 6 days after imbibition. The suppression of the induction of ribonuclease activity and gene expression in decapitated seedlings suggests that the regulatory signal comes from the developing axes. These results clearly state that S-like ribonucleases T2 are involved in RNA turnover in cotyledons during seedling development.
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Watkins, Rex W., Ulrich Arnold, and Ronald T. Raines. "Ribonuclease S redux." Chem. Commun. 47, no. 3 (2011): 973–75. http://dx.doi.org/10.1039/c0cc03864d.

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Nadig, Gautham, Girish S. Ratnaparkhi, Raghavan Varadarajan, and Saraswathi Vishveshwara. "Dynamics of ribonuclease A and ribonuclease S: Computational and experimental studies." Protein Science 5, no. 10 (October 1996): 2104–14. http://dx.doi.org/10.1002/pro.5560051017.

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Zuckermann, Ronald N., and Peter G. Schultz. "A hybrid sequence-selective ribonuclease S." Journal of the American Chemical Society 110, no. 19 (September 1988): 6592–94. http://dx.doi.org/10.1021/ja00227a066.

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Asano, Koji, Shozo Fujita, Toshiya Senda, and Yukio Mitsui. "Crystal growth of ribonuclease S under microgravity." Journal of Crystal Growth 122, no. 1-4 (August 1992): 323–29. http://dx.doi.org/10.1016/0022-0248(92)90264-j.

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Ehrat, Markus, Douglas J. Cecchini, and Roger W. Giese. "Substrate-Leash Amplification with Ribonuclease S-Peptide and S-Protein." Clinical Chemistry 32, no. 2 (February 1, 1986): 390. http://dx.doi.org/10.1093/clinchem/32.2.390.

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Abstract p 1628, Fig. 6: Although faint, there is a band at the origin in lane g. p 1656: The accompanying figure should be substituted for the Figure 2 shown on page 1656, a figure that was to have been deleted. The figure legend is unchanged. p 1705: The second paragraph in the left column should replace the third paragraph of the Discussion. Thus the authors find it "likely...that the principal alkali-labile oxalate precursors in urine are ascorbate and some of its metabolites...." p 1927: The name of the author of a book review, Robert Rej, was omitted. p 2014: On line 7, the 95 percentile interval for plasma ammonia should be 16-53 µmol/L, as correctly stated in the Abstract. See image in the PDF file
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Ehrat, M., D. J. Cecchini, and R. W. Giese. "Substrate-leash amplification with ribonuclease S-peptide and S-protein." Clinical Chemistry 32, no. 9 (September 1, 1986): 1622–30. http://dx.doi.org/10.1093/clinchem/32.9.1622.

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Abstract The S-peptide and S-protein fragments of ribonuclease S (RNase S, no EC no. assigned) have been immobilized onto separate Sepharose gels via a "leash" of polycytidylic acid substrate. Each of these gels releases its RNase fragment when treated with the complementary enzyme fragment or with RNase A (EC 3.1.27.5), and the released fragments recombine to give RNase S activity. Thus this system provides substrate-leash amplification (SLA), such that more enzymatic activity is eluted from the system than is applied. For example, 100 pg of RNase applied to the S-peptide gel is amplified by 1.9 X 10(4) to the equivalent of 1.9 micrograms of activity in 20 h, when followed by combination of the released S-peptide with excess S-protein. We also tested a three-stage amplification system, with a pair of S-peptide and S-protein gels at each stage. In this system the cumulative amplification of the initial 1-ng dose of RNase A is 4.9, 52, and 25-fold after each stage, respectively. Only 2 mg of each SLA gel is used per stage in these experiments, reflecting the magnitude of their production of RNase S activity.
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Hamachi, Itaru, Yasuhiro Yamada, Ryoji Eboshi, Takashi Hiraoka, and Seiji Shinkai. "Design and semisynthesis of spermine-sensitive ribonuclease S'." Bioorganic & Medicinal Chemistry Letters 9, no. 9 (May 1999): 1215–18. http://dx.doi.org/10.1016/s0960-894x(99)00189-4.

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Nishimura, Emi, Minako Kawahara, Reina Kodaira, Marina Kume, Naoki Arai, Jun-ichi Nishikawa, and Takashi Ohyama. "S-like ribonuclease gene expression in carnivorous plants." Planta 238, no. 5 (August 20, 2013): 955–67. http://dx.doi.org/10.1007/s00425-013-1945-6.

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Scolaro, Barbara, Laura Biondi, Fernando Filira, and Raniero Rocchi. "Semisynthetic glycoproteins: preparation of glycosylated ribonuclease S′ analogues." Reactive Polymers 22, no. 3 (June 1994): 195–201. http://dx.doi.org/10.1016/0923-1137(94)90117-1.

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Dissertations / Theses on the topic "S-ribonuclease"

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Madhu, P. K. "Development Of Methodologies In NMR And Applications Of NMR To Biomolecules." Thesis, 1997. http://etd.iisc.ernet.in/handle/2005/1831.

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Book chapters on the topic "S-ribonuclease"

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Futaki, Shiroh, Michihiro Araki, Tatsuto Kiwada, Ikuhiko Nakase, and Yukio Sugiura. "A Cassette Ribonuclease: Site Selective Cleavage of RNA by a Ribonuclease S-Bearing RNA-Recognition Segment." In Peptides: The Wave of the Future, 452–53. Dordrecht: Springer Netherlands, 2001. http://dx.doi.org/10.1007/978-94-010-0464-0_209.

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Tauc, P., P. Fusi, P. Tortora, R. Lange, and J. C. Brochon. "Cold Denaturation of Proteins Under Pressure Studied by Time-Resolved Fluorescence. Application to Ribonuclease P2 from S. sofataricus." In Advances in High Pressure Bioscience and Biotechnology, 191–94. Berlin, Heidelberg: Springer Berlin Heidelberg, 1999. http://dx.doi.org/10.1007/978-3-642-60196-5_41.

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"Ribonuclease S." In Encyclopedia of Genetics, Genomics, Proteomics and Informatics, 1707. Dordrecht: Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6754-9_14652.

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Cordes, Eugene H. "Seduced by Drug Discovery." In Hallelujah Moments. Oxford University Press, 2014. http://dx.doi.org/10.1093/oso/9780199337149.003.0005.

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In autumn 1978, a gentleman scientist named Ralph Hirschmann changed my life. At the time, Ralph was a 56-year-old chemist who had just been promoted to senior vice-president for basic research in chemistry in the Merck Research Laboratories of Merck and Company, a large and—in the opinion of many—the best pharmaceutical house in the world at that time. Ralph had spent his entire professional career at Merck, starting in 1950, and he had a substantial list of scientific accomplishments to his credit. One of these stood out above all others: the laboratory synthesis of a really big molecule. The focal point of chemistry is the molecule. Linking together atoms of the elements hydrogen, oxygen, and carbon, for example, with chemical bonds (think electron glue) creates molecules. There are a lot of different molecules on planet Earth—perhaps a hundred million—some assembled by living organisms and others made in chemistry labs. Some are very small, just two or three atoms linked together. The principal components of our atmosphere—nitrogen and oxygen—are examples. Nitrogen gas consists of two nitrogen atoms (N) linked together: N2. Likewise, oxygen gas is composed of two oxygen atoms (O) linked together: O2. Water provides a slightly more complex example. Two hydrogen atoms (H) are linked to an oxygen atom, H-O-H, more commonly written as H2O. Others are really big and contain thousands of atoms. This is where Ralph comes in. The outstanding achievement for which Ralph gained fame in the arcane world of chemistry was the total laboratory synthesis of a protein—known as ribonuclease S—completed in 1969. A word of warning here: chemistry is full of long words such as ribonuclease that are difficult to spell, difficult to pronounce, and have meaning only to a chemist. There is nothing that I can do about that, so get used to it. Proteins are big molecules—thousands of atoms. The work that Ralph did was in collaboration with another chemist at Merck—Bob Denkewalter.
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Parry(xa}, Simon K., Ying-Hong Liu, Adrienne E. Clarke, and Ed Newbigin{xa). "S-RNases and Other Plant Extracellular Ribonucleases." In Ribonucleases, 191–211. Elsevier, 1997. http://dx.doi.org/10.1016/b978-012588945-2/50007-8.

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