Статті в журналах з теми "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.
Повний текст джерелаWatkins, 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.
Повний текст джерелаNadig, 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.
Повний текст джерелаZuckermann, 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.
Повний текст джерелаAsano, 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.
Повний текст джерелаEhrat, 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.
Повний текст джерелаEhrat, 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.
Повний текст джерелаHamachi, 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.
Повний текст джерелаNishimura, 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.
Повний текст джерелаScolaro, 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.
Повний текст джерелаHaris, Parvez I., David C. Lee, and Dennis Chapman. "A Fourier transform infrared investigation of the structural differences between ribonuclease A and ribonuclease S." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 874, no. 3 (December 1986): 255–65. http://dx.doi.org/10.1016/0167-4838(86)90024-5.
Повний текст джерелаTakeda, Naohiro, Minoru Kato, and Yoshihiro Taniguchi. "Pressure-induced secondary structure changes of ribonuclease A and ribonuclease S studied by FTIR spectroscopy." Biospectroscopy 1, no. 3 (1995): 207–16. http://dx.doi.org/10.1002/bspy.350010305.
Повний текст джерелаPal-Bhowmick, Ipsita, Ramendra Pati Pandey, Gotam K. Jarori, Santosh Kar, and Dinkar Sahal. "Structural and functional studies on Ribonuclease S, retro S and retro-inverso S peptides." Biochemical and Biophysical Research Communications 364, no. 3 (December 2007): 608–13. http://dx.doi.org/10.1016/j.bbrc.2007.10.056.
Повний текст джерелаMcElligott, M. A., P. Miao, and J. F. Dice. "Lysosomal degradation of ribonuclease A and ribonuclease S-protein microinjected into the cytosol of human fibroblasts." Journal of Biological Chemistry 260, no. 22 (October 1985): 11986–93. http://dx.doi.org/10.1016/s0021-9258(17)38974-3.
Повний текст джерелаTravis Gallagher, D., Carrie Stover, David Charlton, Leonard Arnowitz, and David R. Black. "X-ray topography of microgravity-grown ribonuclease S crystals." Journal of Crystal Growth 255, no. 3-4 (August 2003): 403–13. http://dx.doi.org/10.1016/s0022-0248(03)01309-5.
Повний текст джерелаCatanzano, Francesca, Concetta Giancola, Giuseppe Graziano, and Guido Barone. "Temperature-Induced Denaturation of Ribonuclease S: A Thermodynamic Study†." Biochemistry 35, no. 41 (January 1996): 13378–85. http://dx.doi.org/10.1021/bi960855h.
Повний текст джерелаKim, Jin-Soo, and Ronald T. Raines. "Ribonuclease S-peptide as a carrier in fusion proteins." Protein Science 2, no. 3 (December 31, 2008): 348–56. http://dx.doi.org/10.1002/pro.5560020307.
Повний текст джерелаPulido, Daniel, Jorge Pedro López-Alonso, Vicente Marchán, Carlos González, Anna Grandas, and Douglas V. Laurents. "Preparation of Ribonuclease S Domain-Swapped Dimers Conjugated with DNA and PNA: Modulating the Activity of Ribonucleases." Bioconjugate Chemistry 19, no. 1 (January 2008): 263–70. http://dx.doi.org/10.1021/bc700374q.
Повний текст джерелаKim, Eunice E., Raghavan Varadarajan, Harold W. Wyckoff, and Frederic M. Richards. "Refinement of the crystal structure of ribonuclease S. Comparison with and between the various ribonuclease A structures." Biochemistry 31, no. 49 (December 15, 1992): 12304–14. http://dx.doi.org/10.1021/bi00164a004.
Повний текст джерелаStelea, Simona D., and Timothy A. Keiderling. "Pretransitional Structural Changes in the Thermal Denaturation of Ribonuclease S and S Protein." Biophysical Journal 83, no. 4 (October 2002): 2259–69. http://dx.doi.org/10.1016/s0006-3495(02)73986-6.
Повний текст джерелаHegedüs, Attila, Zoltán Szabó, József Nyéki, Júlia Halász, and Andrzej Pedryc. "Molecular Analysis of S-haplotypes in Peach, a Self-compatible Prunus Species." Journal of the American Society for Horticultural Science 131, no. 6 (November 2006): 738–43. http://dx.doi.org/10.21273/jashs.131.6.738.
Повний текст джерелаWeizhong, Ke, and Wu Jianzhong. "Influence of the Nitrobenzene Extraction Technique on the Protein Molecule Conformation." Applied Spectroscopy 48, no. 2 (February 1994): 209–13. http://dx.doi.org/10.1366/0003702944028506.
Повний текст джерелаVetter, W. M., D. T. Gallagher, and M. Dudley. "Synchrotron white-beam X-ray topography of ribonuclease S crystals." Acta Crystallographica Section D Biological Crystallography 58, no. 4 (March 22, 2002): 579–84. http://dx.doi.org/10.1107/s090744490200121x.
Повний текст джерелаJames, D. Andrew, Darcy C. Burns, and G. Andrew Woolley. "Kinetic characterization of ribonuclease S mutants containing photoisomerizable phenylazophenylalanine residues." Protein Engineering, Design and Selection 14, no. 12 (December 2001): 983–91. http://dx.doi.org/10.1093/protein/14.12.983.
Повний текст джерелаLiu, David, John Karanicolas, Catherine Yu, Zhihua Zhang, and G. Andrew Woolley. "Site-specific incorporation of photoisomerizable azobenzene groups into ribonuclease S." Bioorganic & Medicinal Chemistry Letters 7, no. 20 (October 1997): 2677–80. http://dx.doi.org/10.1016/s0960-894x(97)10044-0.
Повний текст джерелаFafarman, Aaron T., and Steven G. Boxer. "Nitrile Bonds as Infrared Probes of Electrostatics in Ribonuclease S." Journal of Physical Chemistry B 114, no. 42 (October 28, 2010): 13536–44. http://dx.doi.org/10.1021/jp106406p.
Повний текст джерелаGenz, Maika, Valentin Köhler, Michel Krauss, David Singer, Ralf Hoffmann, Thomas R. Ward, and Norbert Sträter. "An Artificial Imine Reductase based on the Ribonuclease S Scaffold." ChemCatChem 6, no. 3 (February 3, 2014): 736–40. http://dx.doi.org/10.1002/cctc.201300995.
Повний текст джерелаRatnaparkhi, Girish S., and R. Varadarajan. "X-ray crystallographic studies of the denaturation of ribonuclease S." Proteins: Structure, Function, and Genetics 36, no. 3 (August 15, 1999): 282–94. http://dx.doi.org/10.1002/(sici)1097-0134(19990815)36:3<282::aid-prot3>3.0.co;2-f.
Повний текст джерелаNelson, Jeffrey W., та Neville R. Kallenbach. "Stabilization of the ribonuclease S-peptide α-helix by trifluoroethanol". Proteins: Structure, Function, and Genetics 1, № 3 (березень 1986): 211–17. http://dx.doi.org/10.1002/prot.340010303.
Повний текст джерелаSchleker, Wolfgang, and Jörg Fleischhauer. "Zum Circulardichroismus von Disulfidbrücken in Proteinen. Teil 2. Vergleichende CNDO/S- und INDO/S-CI-Rechnungen." Zeitschrift für Naturforschung A 42, no. 4 (April 1, 1987): 361–66. http://dx.doi.org/10.1515/zna-1987-0404.
Повний текст джерелаMarchiori, Fernando, Gianfranco Borin, and Luis Moroder. "STUDIES ON RIBONUCLEASE S: THE ROLE OF LYSINE-7 FOR ACTIVATION OF S-PROTEIN*." International Journal of Peptide and Protein Research 6, no. 6 (January 12, 2009): 419–34. http://dx.doi.org/10.1111/j.1399-3011.1974.tb02403.x.
Повний текст джерелаHegedűs, Attila, Júlia Halász, Zoltán Szabó, József Nyéki, and Andrzej Pedryc. "How does the S-locus determining self-incompatibility in stone fruits work in self-compatible peach?" Acta Agraria Debreceniensis, no. 17 (September 14, 2005): 93–100. http://dx.doi.org/10.34101/actaagrar/17/3277.
Повний текст джерелаJankovic, Dragana, Svenja Steinfelder, John F. Andersen, and Alan Sher. "Helminth secretory product Ribonuclease T2 is a Th2-inducing agent (43.8)." Journal of Immunology 178, no. 1_Supplement (April 1, 2007): S37. http://dx.doi.org/10.4049/jimmunol.178.supp.43.8.
Повний текст джерелаGilmanshin, Rudolf, Jeroen Van Beek, and Robert Callender. "Study of the Ribonuclease S-Peptide/S-Protein Complex by Means of Raman Difference Spectroscopy." Journal of Physical Chemistry 100, no. 41 (January 1996): 16754–60. http://dx.doi.org/10.1021/jp9611941.
Повний текст джерелаLoo, Rachel R. Ogorzalek, David R. Goodlett, Richard D. Smith, and Joseph A. Loo. "Observation of a noncovalent ribonuclease S-protein/S-peptide complex by electrospray ionization mass spectrometry." Journal of the American Chemical Society 115, no. 10 (May 1993): 4391–92. http://dx.doi.org/10.1021/ja00063a079.
Повний текст джерелаCORIGLIANO-MURPHY, M. ANGELA, XUN LIANG, CYRIL PONNAMPERUMA, DANIELE DALZOPPO, ANGELO FONTANA, TATSUHIKO KANMERA, and IRWIN M. CHAIKEN. "Synthesis and properties of an all-D model ribonuclease S-peptide." International Journal of Peptide and Protein Research 25, no. 3 (January 12, 2009): 225–31. http://dx.doi.org/10.1111/j.1399-3011.1985.tb02168.x.
Повний текст джерелаTanaka, T., and Y. Kikuchi. "Mutational analysis on the S-domain of bacterial ribonuclease P ribozyme." Nucleic Acids Symposium Series 51, no. 1 (November 1, 2007): 371–72. http://dx.doi.org/10.1093/nass/nrm186.
Повний текст джерелаSmith, George P., David A. Schultz, and John E. Ladbury. "A ribonuclease S-peptide antagonist discovered with a bacteriophage display library." Gene 128, no. 1 (June 1993): 37–42. http://dx.doi.org/10.1016/0378-1119(93)90150-2.
Повний текст джерелаRatnaparkhi, Girish S., and Raghavan Varadarajan. "Osmolytes Stabilize Ribonuclease S by Stabilizing Its Fragments S Protein and S Peptide to Compact Folding-competent States." Journal of Biological Chemistry 276, no. 31 (May 23, 2001): 28789–98. http://dx.doi.org/10.1074/jbc.m101906200.
Повний текст джерелаRatnaparkhi, Girish S., Satish Kumar Awasthi, P. Rani, P. Balaram та R. Varadarajan. "Structural and thermodynamic consequences of introducing α-aminoisobutyric acid in the S peptide of ribonuclease S". Protein Engineering, Design and Selection 13, № 10 (жовтень 2000): 697–702. http://dx.doi.org/10.1093/protein/13.10.697.
Повний текст джерелаPechik, I. V., and G. L. Gilliland. "Crystallization and refined structure of ribonuclease S complexed with a substrate analog." Acta Crystallographica Section A Foundations of Crystallography 52, a1 (August 8, 1996): C165. http://dx.doi.org/10.1107/s0108767396092665.
Повний текст джерелаChun, P. W. "A Thermodynamic Molecular Switch in Biological Systems: Ribonuclease S' Fragment Complementation Reactions." Biochemical Society Transactions 28, no. 5 (October 1, 2000): A410. http://dx.doi.org/10.1042/bst028a410b.
Повний текст джерелаVaradarajan, Raghavan, Patrick R. Connelly, Julian M. Sturtevant, and Frederic M. Richards. "Heat capacity changes for protein-peptide interactions in the ribonuclease S system." Biochemistry 31, no. 5 (February 11, 1992): 1421–26. http://dx.doi.org/10.1021/bi00120a019.
Повний текст джерелаChun, Paul W. "A Thermodynamic Molecular Switch in Biological Systems: Ribonuclease S′ Fragment Complementation Reactions." Biophysical Journal 78, no. 1 (January 2000): 416–29. http://dx.doi.org/10.1016/s0006-3495(00)76604-5.
Повний текст джерелаKresge, Nicole, Robert D. Simoni, and Robert L. Hill. "Structure-Function Relationships in Ribonuclease S: the Work of Frederic M. Richards." Journal of Biological Chemistry 284, no. 39 (September 2009): e14-e15. http://dx.doi.org/10.1016/s0021-9258(20)38533-1.
Повний текст джерелаBacker, Marina V., Timur I. Gaynutdinov, Renee Aloise, Kristen Przekop, and Joseph M. Backer. "Engineering S-protein fragments of bovine ribonuclease A for targeted drug delivery." Protein Expression and Purification 26, no. 3 (December 2002): 455–61. http://dx.doi.org/10.1016/s1046-5928(02)00546-6.
Повний текст джерелаMcclure, BA, V. Haring, PR Ebert, MA Anderson, A. Bacic, and AE Clarke. "Molecular Genetics and Biology of Self-Incompatibility in Nicotiana alata, an Ornamental Tobacco." Functional Plant Biology 17, no. 3 (1990): 345. http://dx.doi.org/10.1071/pp9900345.
Повний текст джерелаAbruscato, Vincenzo, Graziella Ranghino, and Anna Maria Villa. "Conformational Behaviour of an Analogue of the S-Peptide: A Molecular Dynamics Study." Protein & Peptide Letters 3, no. 4 (August 1996): 275–82. http://dx.doi.org/10.2174/092986650304220615162309.
Повний текст джерелаHa, Lisha, Jennifer Colquhoun, Nicholas Noinaj, Chittaranjan Das, Paul M. Dunman, and Daniel P. Flaherty. "Crystal structure of the ribonuclease-P-protein subunit from Staphylococcus aureus." Acta Crystallographica Section F Structural Biology Communications 74, no. 10 (September 19, 2018): 632–37. http://dx.doi.org/10.1107/s2053230x18011512.
Повний текст джерелаChun, Paul W. "Planck−Benzinger Thermal Work Function: Thermodynamic Approach to Site-Specific S-Protein and S-Peptides Interactions in the Ribonuclease S‘ System." Journal of Physical Chemistry B 101, no. 39 (September 1997): 7835–43. http://dx.doi.org/10.1021/jp9703364.
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