Π€Π°ΠΊΡΠΎΡΡ, ΠΎΠΏΡΠ΅Π΄Π΅Π»ΡΡΡΠΈΠ΅ ΡΠΈΠ±ΠΎΠ½ΡΠΊΠ»Π΅Π°Π·Π½ΡΡ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΡ ΠΌΠΈΠΌΠ΅ΡΠΈΠΊΠΎΠ² ΡΠΈΠ±ΠΎΠ½ΡΠΊΠ»Π΅Π°Π·: ΡΡΡΡΠΊΡΡΡΠ° Ρ ΠΈΠΌΠΈΡΠ΅ΡΠΊΠΈΡ ΡΠΈΠ±ΠΎΠ½ΡΠΊΠ»Π΅Π°Π·, ΠΏΠΎΡΠ»Π΅Π΄ΠΎΠ²Π°ΡΠ΅Π»ΡΠ½ΠΎΡΡΡ ΠΈ ΠΏΡΠΎΡΡΡΠ°Π½ΡΡΠ²Π΅Π½Π½Π°Ρ ΠΎΡΠ³Π°Π½ΠΈΠ·Π°ΡΠΈΡ Π ΠΠ
ΠΠ°Π²Π½ΠΎ ΠΈΠ·Π²Π΅ΡΡΠ½ΠΎ, ΡΡΠΎ ΡΠΎΡΡΠΎΠ΄ΠΈΡΡΠΈΡΠ½ΡΠ΅ ΡΠ²ΡΠ·ΠΈ, Π½Π°Ρ ΠΎΠ΄ΡΡΠΈΠ΅ΡΡ ΠΌΠ΅ΠΆΠ΄Ρ ΡΠΈΡΠΈΠ΄ΠΈΠ½ΠΎΠΌ ΠΈ Π°Π΄Π΅Π½ΠΈΠ½ΠΎΠΌ ΠΈ ΠΌΠ΅ΠΆΠ΄Ρ ΡΡΠΈΠ΄ΠΈΠ½ΠΎΠΌ ΠΈ Π°Π΄Π΅Π½ΠΈΠ½ΠΎΠΌ (Π‘ΡΠ, 11ΡΠ) Π½Π°ΠΈΠ±ΠΎΠ»Π΅Π΅ Π»Π΅Π³ΠΊΠΎ ΠΏΠΎΠ΄Π²Π΅ΡΠ³Π°ΡΡΡΡ ΡΠ°ΡΡΠ΅ΠΏΠ»Π΅Π½ΠΈΡ ΠΊΠ°ΠΊ ΡΠΏΠΎΠ½ΡΠ°Π½Π½ΠΎΠΌΡ, ΡΠ°ΠΊ ΠΈ ΠΏΠΎΠ΄ Π΄Π΅ΠΉΡΡΠ²ΠΈΠ΅ΠΌ ΡΠΈΠ±ΠΎΠ½ΡΠΊΠ»Π΅Π°Π·, Π² ΡΠΎ Π²ΡΠ΅ΠΌΡ ΠΊΠ°ΠΊ ΠΎΡΡΠ°Π»ΡΠ½ΡΠ΅ ΡΠΎΡΡΠΎΠ΄ΠΈΡΡΠΈΡΠ½ΡΠ΅ ΡΠ²ΡΠ·ΠΈ Π ΠΠ ΠΏΡΠΎΡΠ²Π»ΡΡΡ ΡΠ°Π·Π½ΠΎΠΎΠ±ΡΠ°Π·Π½ΡΡ ΡΡΠ²ΡΡΠ²ΠΈΡΠ΅Π»ΡΠ½ΠΎΡΡΡ ΠΊ ΡΠ°ΡΡΠ΅ΠΏΠ»Π΅Π½ΠΈΡ. ΠΡΡΠ»Π΅Π΄ΠΎΠ²Π°Π½ΠΈΡ ΡΡΠ²ΡΡΠ²ΠΈΡΠ΅Π»ΡΠ½ΠΎΡΡΠΈ ΡΠ°Π·Π»ΠΈΡΠ½ΡΡ ΡΠΎΡΡΠΎΠ΄ΠΈΡΡΠΈΡΠ½ΡΡ ΡΠ²ΡΠ·Π΅ΠΉ ΠΊ ΡΠ°ΡΡΠ΅ΠΏΠ»Π΅Π½ΠΈΡ Π²Π΅Π»ΠΈΡΡ… Π§ΠΈΡΠ°ΡΡ Π΅ΡΡ >
Π‘ΠΏΠΈΡΠΎΠΊ Π»ΠΈΡΠ΅ΡΠ°ΡΡΡΡ
- Min D., Xue S., Li H., Yang W. 'In-line attack' conformational effect plays a modest role in an enzyme-catalyzed RNA cleavage: a free energy simulation study// Nucleic Acids Res. 2007. V. 35. P. 4001−4006.
- Gu J., Wang J., Leszczynski J. Molecular basis of the recognition process: hydrogen-bonding patterns in the guanine primary recognition site of ribonuclease T1// J. Phys. Chem. B. 2006. V. 110. P. 13 590−13 596.
- Mignon P., Steyaert J., Loris R., Geerlings P., Loverix S. A nucleophile activation dyad in ribonucleases. A combined X-ray crystallographic/ab initio quantum chemical study// J. Biol. Chem. 2002. V. 277. P. 36 770−36 774.
- Klahn M., Rosta E., Warshel A. On the mechanism of hydrolysis of phosphate monoesters dianions in solutions and proteins//J. Am. Chem. Soc. 2006. V. 128. P. 15 310−15 323.
- Oivanen M., Kuusela S" Lonnberg H. Kinetics and Mechanisms for the Cleavage and Isomerization of the Phosphodiester Bonds of RNA by Bronsted Acids and Bases// Chem Rev.1998. V. 98. P. 961−990.
- Glennon T.M., Warshel A. Energetics of the catalytic reaction of ribonuclease A: A computational study of alternative mechanisms.// J. Am. Chem. Soc. 1998. V. 120. P. 1 023 410 247.
- Trawick B.N., Daniher A.T., Bashkin J.K. Inorganic Mimics of Ribonucleases and Ribozymes: From Random Cleavage to Sequence-Specific Chemistry to Catalytic Antisense Drugs// Chem. Rev. 1998. V. 98. P. 939−960.
- Ciesiolka J., Michalowski D., Wrzesinski J., Krajewski J., Krzyzosiak W.J. Patterns of cleavages induced by lead ions in defined RNA secondary structure motifs// J. Mol. Biol. 1998. V. 275. P. 211−220.
- Morrow J.R. Artificial ribonucleases//Adv. Inorg. Biochem. 1994. V. 9. P. 41−74.
- Shinozuka K., Nakashima Y., Shimizu K., Sawai H. Synthesis and characterization of polyamine-based biomimetic catalysts as artificial ribonuclease// Nucleosides Nucleotides Nucleic Acids. 2001. V. 20. P. 117−130.
- Bashkin J.K., Frolova E.I., Sampath U.S. Sequence-specific cleavage of HIV mRNA by a ribozyme mimic.// J. Am. Chem. Soc. 1994. V. 116. P. 5981−5982.
- Yoshinan K., Komiyama M. Facile cleavage of RNAs by oligoamines. Correlation between amine structure and catalytic activity// Nucleic Acids Symp. Ser. 1991. P. 23−24.
- Bibillo A., Ziomek K., Figlerowicz M., Kierzek R. Nonenzymatic hydrolysis of oligoribonucleotides. V. The elements affecting the process of self-hydrolysis// Acta Biochim. Pol.1999. V. 46. P. 145−153.
- Kierzek R. Hydrolysis of oligoribonucleotides: influence of sequence and length// Nucleic Acids Res. 1992. V. 20. P. 5073−5077.
- Mironova N.L., Pyshnyi D.V., Shtadler D.V., Fedorova A.A., Vlassov V.V., Zenkova M.A. RNase T1 mimicking artificial ribonuclease// Nucleic Acids Res. 2007. V. 35. P. 2356−2367.
- Podyminogin M.A., Vlassov V.V., Giege R. Synthetic RNA-cleaving molecules mimicking ribonuclease A active center. Design and cleavage of tRNA transcripts// Nucleic Acids Res. 1993. V. 21. P. 5950−5956.
- Zenkova M., Beloglazova N., Sil’nikov V., Vlassov V., Giege R. RNA cleavage by 1,4-diazabicyclo2.2.2.octane-imidazole conjugates// Meth. Enzymol. 2001. V. 341. P. 468−490.
- Tung C.H., Wei Z, Leibowitz M.J., Stein S. Design of peptide-acridine mimics of ribonuclease activity// Proc. Natl. Acad Sci. USA. 1992. V. 89. P. 7114−7118.
- Kierzek R. Nonenzymatic hydrolysis of oligoribonucleotides// Nucleic Acids Res. 1992. V. 20. P. 5079−5084.
- Koroleva L.S., Serpokrylova I.Y., Vlassov V.V., Silnikov V.N. Design and synthesis of metalfree artificial ribonucleases// Protein Pept. Lett. 2007. V. 14. P. 151−163.
- ΠΠ»Π°ΡΠΎΠ² Π.Π., Π‘ΠΈΠ»ΡΠ½ΠΈΠΊΠΎΠ² Π. Π., ΠΠ΅Π½ΠΊΠΎΠ²Π° Π. Π. Π₯ΠΈΠΌΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΡΠΈΠ±ΠΎΠ½ΡΠΊΠ»Π΅Π°Π·Ρ// ΠΠΎΠ»Π΅ΠΊΡΠ»ΡΡ. Π±ΠΈΠΎΠ»ΠΎΠ³ΠΈΡ. 1998. Π’. 32. Π‘. 62−70.
- HanerR., Hall J. The sequence-specific cleavage of RNA by artificial chemical ribonucleases// Antisense Nucleic Acid Drug Dev. 1997. V. 7. P. 423−430.
- Niittymaki Π’., Lonnberg H. Artificial ribonucleases// Org. Biomol. Chem. 2006. V. 4. P. 15−25.
- Ushijima K., Gouzu H., Hosono K, Shirakawa M., Kagosima K, Takai K., Takaku H. Site-specific cleavage of tRNA by imidazole and/or primary amine groups bound at the 5'-end of oligodeoxyribonucleotides// Biochim Biophys Acta. 1998. V. 1379. P. 217−223.
- Π‘ΠΈΠ»ΡΠ½ΠΈΠΊΠΎΠ² B.H., ΠΡΠΊΡΡΠ½ΡΡΠΊ Π. Π., Π¨ΠΈΡΠΊΠΈΠ½ Π. Π., ΠΠΈΠΆΠ΅ Π ., ΠΠ»Π°ΡΠΎΠ² Π. Π. ΠΠΌΠΈΠ΄Π°Π·ΠΎΠ»ΡΠΎΠ΄Π΅ΡΠΆΠ°ΡΠΈΠ΅ ΠΏΡΠΎΠΈΠ·Π²ΠΎΠ΄Π½ΡΠ΅, ΠΌΠΎΠ΄Π΅Π»ΠΈΡΡΡΡΠΈΠ΅ Π°ΠΊΡΠΈΠ²Π½ΡΠΉ ΡΠ΅Π½ΡΡ Π ΠΠΠ°Π·Ρ Π. Π‘ΠΈΠ½ΡΠ΅Π· ΠΈ Π ΠΠ-ΡΠ°ΡΡΠ΅ΠΏΠ»ΡΡΡΠ°Ρ Π°ΠΊΡΠΈΠ²Π½ΠΎΡΡΡ.//ΠΠΎΠΊΠ». ΠΠΊΠ°Π΄. ΠΠ°ΡΠΊ. 1999. Π’. 364. Π‘. 690−694.
- Kuznetsova I.L., Zenkova Π.Π., Gross H.J., Vlassov V.V. Enhanced RNA cleavage within bulge-loops by an artificial ribonuclease// Nucleic Acids Res. 2005. V. 33. P. 1201−1212.
- Bibillo A., Figlerowicz M., Ziomek K., Kierzek R. The nonenzymatic hydrolysis of oligoribonucleotides. VII. Structural elements affecting hydrolysis// Nucleosides Nucleotides Nucleic Acids. 2000. V. 19. P. 977−994.
- Zagorowska I., Kuusela S., Lonnberg H. Metal ion-dependent hydrolysis of RNA phosphodiester bonds within hairpin loops. A comparative kinetic study on chimeric ribo/2-O-methylribo oligonucleotides// Nucleic Acids Res. 1998. V. 26. P. 3392−3396.
- Kaukinen U., Lonnberg H., Perakyla M. Stabilisation of the transition state of phosphodiester bond cleavage within linear single-stranded oligoribonucleotides// Org. Biomol. Chem. 2004. V. 2. P. 66−73.
- Kaukinen U., Lyytikainen S., Mikkola S" Lonnberg H. The reactivity of phosphodiester bonds within linear single-stranded oligoribonucleotides is strongly dependent on the base sequence// Nucleic Acids Res. 2002. V. 30. P. 468−474.
- Soukup G.A., Breaker R.R. Relationship between intemucleotide linkage geometry and the stability of RNA// RNA. 1999. V. 5. P. 1308−1325.
- Hosaka H., Sakabe I., Sakamoto K, Yokoyama S., Takaku H. Sequence-specific cleavage of oligoribonucleotide capable of forming a stem and loop structure// J. Biol. Chem. 1994. V. 269. P. 20 090−20 094.
- Raines R.T. Ribonuclease All Chem. Rev. 1998. V. 98. P. 1045−1066.
- Oh B.K., Frank D.N., Pace N.R. Participation of the Π'-Π‘Π‘Π of tRNA in the binding of catalytic Mg2+ ions by ribonuclease P// Biochemistry. 1998. V. 37. P. 7277−7283.
- ΠΠ°ΡΡΠΎΠ»ΠΎΠΌΠ΅Π΅Π² Π‘.Π., ΠΡΡΠ΅Π²ΠΈΡ Π. Π. ΠΠΈΠΎΠΊΠΈΠ½Π΅ΡΠΈΠΊΠ°. Π.: Π€Π°ΠΈΡ-ΠΡΠ΅ΡΡ, 1998, 715
- Barnard Π.Π. Biological function of pancreatic ribonuclease// Nature. 1969. V. 221. P. 340−344.
- Smith B.D., Raines R.T. Genetic selection for critical residues in ribonucleases// J Moi Biol. 2006. V. 362. P. 459−478.
- Rutkoski T.J., Kurten E.L., Mitchell J.C., Raines R.T. Disruption of shape-complementarity markers to create cytotoxic variants of ribonuclease A// J. Mol. Biol. 2005. V. 354. P. 41−54.
- Beintema J.J., Schuller C., Irie M., Carsana A. Molecular evolution of the ribonuclease superfamily// Prog. Biophys. Mol. Biol. 1988. V. 51. P. 165−192.
- Kartha G., Bello J., HarkerD. Tertiary structure of ribonuclease// Nature. 1967. V. 213. P. 862 865.
- Rico M., Bruix M., Santoro J., Gonzalez C., Neira J.L., Nieto J.L., Herranz J. Sequential 1H-NMR assignment and solution structure of bovine pancreatic ribonuclease All Eur. J. Biochem. 1989. V. 183. P. 623−638.
- Robertson A.D., Purisima E.O., Eastman M.A., Scheraga H.A. Proton NMR assignments and regular backbone structure of bovine pancreatic ribonuclease A in aqueous solution// Biochemistry. 1989. V. 28. P. 5930−5938.
- Udgaonkar J.B., Baldwin R.L. NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A// Nature. 1988. V. 335. P. 694−699.
- Richardson J.S. The anatomy and taxonomy of protein structure//Adv. Protein Chem. 1981. V. 34. P. 167−339.
- Klink T.A., Woycechowsky K.J., Taylor K.M., Raines R.T. Contribution of disulfide bonds to the conformational stability and catalytic activity of ribonuclease A// Eur. J. Biochem. 2000. V. 267. P. 566−572.
- McPherson A., Brayer G., Morrison R. Structure of the crystalline complex between ribonuclease A and D (pA)4// Biophys. J. 1986. V. 49. P. 209−219.
- McPherson A., Brayer G., Cascio D., Williams R. The mechanism of binding of a polynucleotide chain to pancreatic ribonuclease// Science. 1986. V. 232. P. 765−768.
- Birdsall D.L., McPherson A. Crystal structure disposition of thymidylic acid tetramer in complex with ribonuclease All J. Biol. Chem. 1992. V. 267. P. 22 230−22 236.
- Fontecilla-Camps J.C., de Llorens R., le Du M.H., Cuchillo C.M. Crystal structure of ribonuclease A. d (ApTpApApG) complex. Direct evidence for extended substrate recognition// J. Biol. Chem. 1994. V. 269. P. 21 526−21 531.
- Zegers I., Maes D., Dao-Thi M.H., Poortmans F., Palmer R., Wyns L. The structures of RNase A complexed with Π'-Π‘ΠΠ and d (CpA): active site conformation and conserved water molecules//-Protein Sci. 1994. V. 3. P. 2322−2339.
- AguilarC.F., Thomas P.J., Mills A., Moss D.S., Palmer R.A. Newly observed binding mode in pancreatic ribonuclease//J. Mol. Biol. 1992. V. 224. P. 265−267.
- Nogues M.V., Vilanova M., Cuchillo C.M. Bovine pancreatic ribonuclease A as a model of an enzyme with multiple substrate binding sites// Biochim. Biophys. Acta. 1995. V. 1253. P. 16−24.
- Pares X., Nogues M.V., de Llorens R., Cuchillo C.M. Structure and function of ribonuclease A binding subsites// Essays Biochem. 1991. V. 26. P. 89−103.
- Mousaoui M., Cuchillo C.M., Nogues M.V. A phosphate-binding subsite in bovine pancreatic ribonuclease A can be converted into a very efficient catalytic site.// Protein Science. 2006. P. 99 109.
- Barnard E.A. Ribonucleases//Annu. Rev. Biochem. 1969. V. 38. P. 677−732.
- Hemes D.G., Mathias A.P., Rabin B.R. The active site and mechanism of action of bovine pancreatic ribonuclease. 3. The pH-dependence of the kinetic parameters for the hydrolysis of cytidine 2', 3-phosphate// Biochem. J. 1962. V. 85. P. 127−134.
- Thompson J.E., Venegas F.D., Raines R.T. Energetics of catalysis by ribonucleases: fate of the 2', 3-cyclic phosphodiester intermediate// Biochemistry. 1994. V. 33. P. 7408−7414.
- Trautwein K., Holliger P., Stackhouse J., Benner S. A Site-directed mutagenesis of bovine pancreatic ribonuclease: lysine-41 and aspartate-121// FEBS Lett. 1991. V. 281. P. 275−277.
- Roberts G.C., Dennis E.A., Meadows D.H., Cohen J.S., Jardetzky O. The mechanism of action of ribonuclease// Proc. Natl. Acad. Sci. USA. 1969. V. 62. P. 1151−1158.
- Gerlt J.A., Gassman P.G. Understanding the rates of certain enzyme-catalyzed reactions: proton abstraction from carbon acids, acyl-transfer reactions, and displacement reactions of phosphodiesters//Biochemistry. 1993. V. 32. P. 11 943−11 952.
- Quirk D.J., Raines R. T His. Asp catalytic dyad of ribonuclease A: histidine pKa values in the wild-type, D121N, and D121A enzymes// Biophys. J. 1999. V. 76. P. 1571−1579.
- Schultz L.W., Quirk D.J., Raines R. T His.Asp catalytic dyad of ribonuclease A: structure and function of the wild-type, D121N, and D121A enzymes// Biochemistry. 1998. V. 37. P. 8886−8898.
- Veenstra T.D., Lee L. NMR study of the positions of His-12 and His-119 in the ribonuclease A-uridine vanadate complex// Biophys. J. 1994. V. 67. P. 331−335.
- Lin M.C., Gutte B., Caldi D.G., Moore S., Merrifield R.B. Reactivation of des (119−124) ribonuclease A by mixture with synthetic COOH-terminal peptides- the role of phenylalanine-120// J. Biol. Chem. 1972. V. 247. P. 4768−4774.
- Lin M.C., Gutte B., Moore S., Merrifield R.B. Regeneration of activity by mixture of ribonuclease enzymically degraded from the COOH terminus and a synthetic COOH-terminal tetradecapeptide// J. Biol. Chem. 1970. V. 245. P. 5169−5170.
- Quirk D.J., Park C., Thompson J.E., Raines R.T. His. Asp catalytic dyad of ribonuclease A: conformational stability of the wild-type, D121N, D121A, and H119A enzymes// Biochemistry. 1998. V. 37. P. 17 958−17 964.
- Watt E.D., Shimada H., Kovrigin E.L., Loria J.P. The mechanism of rate-limiting motions in enzyme function// Proc. Natl. Acad. Sci. USA. 2007. V. 104. P. 11 981−11 986.
- Toiron C., Gonzalez C., Bruix M., Rico M. Three-dimensional structure of the complexes of ribonuclease A with 2', 5-CpA and 3', 5'-d (CpA) in aqueous solution, as obtained by NMR and restrained molecular dynamics// Protein Sci. 1996. V. 5. P. 1633−1647.
- Borkakoti N. The active site of ribonuclease A from the crystallographic studies of ribonuclease-A-inhibitor complexes//Eur. J. Biochem. 1983. V. 132. P. 89−94.
- Wlodawer A., Miller M., Sjolin L. Active site of RNase: neutron diffraction study of a complex with uridine vanadate, a transition-state analog// Proc. Natl. Acad. Sci. USA. 1983. V. 80. P. 36 283 631.
- Burbaum J. J., Raines R.T., Albery W.J., Knowles J.R. Evolutionary optimization of the catalytic effectiveness of an enzyme// Biochemistry. 1989. V. 28. P. 9293−9305.
- Albery W.J., Knowles J.R. Evolution of enzyme function and the development of catalytic efficiency// Biochemistry. 1976. V. 15. P. 5631−5640.
- FindlayD., Hemes D.G., Mathias A.P., Rabin B.R., Ross C.A. The active site and mechanism of action of bovine pancreatic ribonuclease// Nature. 1961. V. 190. P. 781−784.
- Usher D.A., Erenrich E.S., Eckstein F. Geometry of the first step in the action of ribonuclease-A (in-line geometry-uridine2', 3,-cyclic thiophosphate- 31 P NMR)// Proc. Natl. Acad. Sci. USA. 1972. V. 69. P. 115−118.
- Usher D.A., Richardson D.I., Jr., Eckstein F. Absolute stereochemistry of the second step of ribonuclease action// Nature. 1970. V. 228. P. 663−665.
- Ladner J.E., Wladkowski B.D., Svensson L.A., Sjolin L, Gilliland G. L X-ray structure of a ribonuclease A-uridine vanadate complex at 1.3 A resolution// Acta. Crystallogr. D. Biol. Crystallogr. 1997. V. 53. P. 290−301.
- Warshel A., Sharma P.K., Kato M., Xiang Y., Liu H., Olsson M.H. Electrostatic basis for enzyme catalysis// Chem. Rev. 2006. V. 106. P. 3210−3235.
- Ui N. Isoelectric points and conformation of proteins. I. Effect of urea on the behavior of some proteins in isoelectric focusing// Biochim. Biophys. Acta. 1971. V. 229. P. 567−581.
- Felsenfeld G., Sandeen G., Vonhippel P.H. The Destabilizing Effect Of Ribonuclease On The Helical Dna Structure// Proc. Natl. Acad. Sci. USA. 1963. V. 50. P. 644−651.
- Jensen D.E., von Hippel P.H. DNA «melting» proteins. I. Effects of bovine pancreatic ribonuclease binding on the conformation and stability of DNA// J. Biol. Chem. 1976. V. 251. P. 7198−7214.
- Record M.T., Jr., Woodbury C.P., Lohman T.M. Na+ effects on transition of DNA and polynucleotides of variable linear charge density// Biopolymers. 1976. V. 15. P. 893−915.
- FisherB.M., Grilley J.E., Raines R.T. A new remote subsite in ribonuclease A// J. Biol. Chem. 1998. V. 273. P. 34 134−34 138.
- Irie M., Watanabe H., Ohgi K., Tobe M., Matsumura G., Arata Y., Hirose T., Inayama S. Some evidence suggesting the existence of P2 and B3 sites in the active site of bovine pancreatic ribonuclease A// J. Biochem (Tokyo). 1984. V. 95. P. 751−759.
- Sawada F., Irie M. Interaction of uridine-2'(3'), 5'-diphosphate withibonuclease A and carboxymethylribonuclease A//J. Biochem (Tokyo). 1969. V. 66. P. 415−418.
- Richardson R.M., Pares X., Llorens R., Nogues M.V., Cuchillo C.M. Nucleotide binding and affinity labelling support the existence of the phosphate-binding subsite p2 in bovine pancreatic ribonuclease A// Biochim. Biophys. Acta. 1988. V. 953. P. 70−78.
- Pares X., Llorens R" Arus C., Cuchillo C.M. The reaction of bovine pancreatic ribonuclease A with 6-chloropurineriboside 5'-monophosphate. Evidence on the existence of a phosphate-binding sub-site// Eur. J. Biochem. 1980. V. 105. P. 571−579.
- Cuchillo C.M., Moussaoui M" Barman T., Travers F., Nogues M.V. The exo- or endonucleolytic preference of bovine pancreatic ribonuclease A depends on its subsites structure and on the substrate size// Protein Sci. 2002. V. 11. P. 117−128.
- Beintema J. J., Campagne R.N. Molecular evolution of rodent insulins// Mol. Biol. Evol. 1987. V. 4. P. 10−18.
- Wlodawer A., Svensson L.A., Sjolin L., Gilliland G.L. Structure of phosphate-free ribonuclease A refined at 1.26 A// Biochemistry. 1988. V. 27. P. 2705−2717.
- Fisher B.M., Ha J.H., Raines R.T. Coulombic forces in protein-RNA interactions: binding and cleavage by ribonuclease A and variants at Lys7, Arg10, and Lys66// Biochemistry. 1998. V. 37. P. 12 121−12 132.
- Beintema J.J. Presence of a basic amino acid residue at either position 66 or 122 is a condition for enzymic activity in the ribonuclease superfamily// FEBS Lett. 1989. V. 254. P. 1−4.
- Anderson C.F., Record M.T., Jr. Salt-nucleic acid interactions// Annu Rev Phys Chem. 1995. V. 46. P. 657−700.
- Park C., Raines R.T. Catalysis by ribonuclease A is limited by the rate of substrate association// Biochemistry. 2003. V. 42. P. 3509−3518.
- Haffner P.H., Wang J.H. Chemical kinetic and proton magnetic resonance studies of 5'-adenosine monophosphate binding to ribonuclease A// Biochemistry. 1973. V. 12. P. 1608−1617.
- Beintema J.J. Structure, properties and molecular evolution of pancreatic-type ribonucleases.// Life Chem.Rep. 1987. V. 4. P. 333−389.
- Bruenger A., Brooks, C. & Karplus, M. Active site dynamics of ribonuclease.// Proc. Natl Acad. Sci. USA. 1985. V. 82. P. 8458−8462.
- Sorrentino S., Libonati M. Human pancreatic-type and nonpancreatic-type ribonucleases: a direct side-by-side comparison of their catalytic properties//Arch. Biochem. Biophys. 1994. V. 312. P. 340−348.
- Tarragona-Fiol A., Eggelte H.J., Harbron S., Sanchez E., Taylorson C.J., Ward J.M., Rabin B.R. Identification by site-directed mutagenesis of amino acids in the B2 subsite of bovine pancreatic ribonuclease A// Protein Eng. 1993. V. 6. P. 901−906.
- Witzel H., Barnard E.A. Mechanism and binding sites in the ribonuclease reaction. II. Kinetic studies on the first step of the reaction// Biochem Biophys Res Commun. 1962. V. 7. P. 295−299.
- Gilliland GL D.J., Pechik I, Svensson LA & Sjolin L. The active site of bovine pancreatic ribonuclease: an example of solvent modulated specificity.// Protein Pept. Lett. 1994. V. 1. P. 6065.
- Wodak S.Y. The structure of cytidilyl (2', 5')adenosine when bound to pancreatic ribonuclease S// J. Mol. Bio! 1977. V. 116. P. 855−875.
- Leonidas D.D., Shapiro R., Irons L.I., Russo N., Acharya K.R. Crystal structures of ribonuclease A complexes with 5'-diphosphoadenosine 3'-phosphate and 5'-diphosphoadenosine 2'-phosphate at 1.7 A resolution// Biochemistry. 1997. V. 36. P. 5578−5588.
- Jardine A.M., Leonidas D.D., Jenkins J.L., Park C., Raines R.T., Acharya K.R., Shapiro R. Cleavage of 3', 5'-pyrophosphate-linked dinucleotides by ribonuclease A and angiogenin// Biochemistry. 2001. V. 40. P. 10 262−10 272.
- Hatzopoulos G.N., Leonidas D.D., Kardakaris R" Kobe J., Oikonomakos N.G. The binding of IMP to ribonuclease A// FEBS J. 2005. V. 272. P. 3988−4001.
- Seshadri K, Rao V.S., Vishveshwara S. Interaction of substrate uridyl 3', 5'-adenosine with ribonuclease A: a molecular dynamics study// Biophys. J. 1995. V. 69. P. 2185−2194.
- Irie M., Mikami F., Monma K., Ohgi K., Watanabe H., Yamaguchi R., Nagase H. Kinetic studies on the cleavage of oligouridylic acids and poly U by bovine pancreatic ribonuclease A/I J. Biochem (Tokyo). 1984. V. 96. P. 89−96.
- Boque L., Gracia Coll M., Vilanova M., Cuchillo C.M., Fita I. Structure of ribonuclease A derivative II at 2.1-A resolution// J. Biol. Chem. 1994. V. 269. P. 19 707−19 712.
- Strydom D.J., FettJ.W., Lobb R.R., Alderman E.M., Bethune J.L., Riordan J.F., Vallee B.L. Amino acid sequence of human tumor derived angiogenin// Biochemistry. 1985. V. 24. P. 54 865 494.
- Kurachi K., Davie E.W., Strydom D.J., Riordan J.F., Vallee B.L. Sequence of the cDNA and gene for angiogenin, a human angiogenesis factor// Biochemistry. 1985. V. 24. P. 5494−5499.
- Mosimann S.C., Ardelt W., James M.N. Refined 1.7 A X-ray crystallographic structure of P-30 protein, an amphibian ribonuclease with anti-tumor activity// J. Mol. Biol. 1994. V. 236. P. 11 411 153.
- Ardelt W., Mikulski S.M., Shogen K. Amino acid sequence of an anti-tumor protein from Rana pipiens oocytes and early embryos. Homology to pancreatic ribonucleases// J. Biol. Chem. 1991. V. 266. P. 245−251.
- Liao Y.D. A pyrimidine-guanine sequence-specific ribonuclease from Rana catesbeiana (bullfrog) oocytes// Nucleic Acids Res. 1992. V. 20. P. 1371−1377.
- Titani K" Takio K., Kuwada M" Nitta K" Sakakibara F., Kawauchi H., Takayanagi G., Hakomori S. Amino acid sequence of sialic acid binding lectin from frog (Rana catesbeiana) eggs// Biochemistry. 1987. V. 26. P. 2189−2194.
- Lou Y.C., Huang Y.C., Pan Y.R., Chen C., Liao Y.D. Roles of N-terminal pyroglutamate in maintaining structural integrity and pKa values of catalytic histidine residues in bullfrog ribonuclease 3// J. Mol. Biol. 2006. V. 355. P. 409−421.
- Leland P.A., Raines R.T. Cancer chemotherapy-ribonucleases to the rescue// Chem. Biol. 2001. V. 8. P. 405−413.
- Arnold U., Schulenburg C., Schmidt D., Ulbrich-Hofmann R. Contribution of structural peculiarities of onconase to its high stability and folding kinetics// Biochemistry. 2006. V. 45. P. 3580−3587.
- Acharya K.R., Shapiro R., Allen S.C., Riordan J.F., Vallee B.L. Crystal structure of human angiogenin reveals the structural basis for its functional divergence from ribonuclease// Proc. Natl. Acad. Sci. USA. 1994. V. 91. P. 2915−2919.
- Nogues M.V., Moussaoui M" Boix ?., Vilanova M., Ribo M., Cuchillo C.M. The contribution of noncatalytic phosphate-binding subsites to the mechanism of bovine pancreatic ribonuclease A// Cell Mol. Life Sci. 1998. V. 54. P. 766−774.
- Liao Y.D., Huang H.C., Leu Y J., Wei C.W., Tang P.C., Wang S.C. Purification and cloning of cytotoxic ribonucleases from Rana catesbeiana (bullfrog)// Nucleic Acids Res. 2000. V. 28. P. 4097−4104.
- Russo N., Acharya K.R., Vallee B.L., Shapiro R. A combined kinetic and modeling study of the catalytic center subsites of human angiogeninII Proc. Natl. Acad. Sci. USA. 1996. V. 93. P. 804−808.
- Hartley R.W. Homology between prokaryotic and eukaryotic ribonucleases// J. Mol. Evol. 1980. V. 15. P. 355−358.
- Sato K., Egami F. The specificity of T1 ribonuclease.// C R Seances Soc. Biol. Fil. 1957. V. 151. P. 1792−1796.
- Heinemann U., Saenger W. Specific protein-nucleic acid recognition in ribonuclease T1−2'-guanylic acid complex: an X-ray study// Nature. 1982. V. 299. P. 27−31.
- Osterman H.L., Walz F.G., Jr. Subsites and catalytic mechanism of ribonuclease T1: kinetic studies using GpA, GpC, GpG, and GpU as substrates// Biochemistry. 1978. V. 17. P. 4124−4130.
- Irie M. A kinetic study on ribonuclease T1 using dinucleoside phosphates as substrates// J. Biochem (Tokyo). 1968. V. 63. P. 649−653.
- Kanaya S., Uchida T. Purification of ribonuclease T1 by affinity chromatography// J. Biochem (Tokyo). 1981. V. 89. P. 591−597.
- Jo ChitesterB., Walz F.G., Jr. Kinetic studies of guanine recognition and a phosphate group subsite on ribonuclease T1 using substitution mutants at GIu46 and Lys41// Arch. Biochem. Biophys. 2002. V. 406. P. 73−77.
- Walz F.G., Jr. Upstream subsite interactions for oligonucleotide binding with ribonuclease T1// Biochim. Biophys. Acta. 1997. V. 1350. P. 183−188.
- Egami F., Oshima T., Uchida T. Specific interaction of base-specific nucleases with nucleosides and nucleotides// Mol. Biol. Biochem. Biophys. 1980. V. 32. P. 250−277.
- Backmann J., Doray C.C., Grunert H.P., Landt O., Hahn U. Extended kinetic analysis of ribonuclease T1 variants leads to an improved scheme for the reaction mechanism// Biochem. Biophys. Res. Commun. 1994. V. 199. P. 213−219.
- Heinemann U., Saenger W. Crystallographic study of mechanism of ribonuclease T1-catalysed specific RNA hydrolysis// J. Biomol. Struct. Dyn. 1983. V. 1. P. 523−538.
- De Vos S" Doumen J., Langhorst U., Steyaert J. Dissecting histidine interactions of ribonuclease T1 with asparagine and glutamine replacements: analysis of double mutant cycles at one position// J. Mol. Biol. 1998. V. 275. P. 651−661.
- Steyaert J., Hallenga K., Wyns L., Stanssens P. Histidine-40 of ribonuclease T1 acts as base catalyst when the true catalytic base, glutamic acid-58, is replaced by alanine// Biochemistry. 1990. V. 29. P. 9064−9072.
- Loverix S., Winqvist A., Stromberg R., Steyaert J. Mechanism of RNase T1: concerted triester-like phosphoryl transfer via a catalytic three-centered hydrogen bond// Chem. Biol. 2000. V. 7. P. 651−658.
- Sugio S., Amisaki T., Ohishi H., Tomita K. Refined X-ray structure of the low pH form of ribonuclease T1−2'-guanylic acid complex at 1.9 A resolution// J. Biochem (Tokyo). 1988. V. 103. P. 354−366.
- Ami R., Heinemann U., Tokuoka R., Saenger W. Three-dimensional structure of the ribonuclease T1 2-GMP complex at 1.9-A resolution// J. Biol. Chem. 1988. V. 263. P. 1 535 815 368.
- Inagaki F., Shimada I., Miyazawa T. Binding modes of inhibitors to ribonuclease T1 as studied by nuclear magnetic resonance// Biochemistry. 1985. V. 24. P. 1013−1020.
- Takahashi K. The structure and function of ribonuclease T1. IX. Photooxidation of ribonuclease T1 in the presence of rose bengal// J. Biochem (Tokyo). 1970. V. 67. P. 833−839.
- Walz F.G., Jr. Spectrophotometry titration of a single carboxyl group at the active site of ribonuclease T1// Biochemistry. 1977. V. 16. P. 4568−4571.
- Koepke J., Maslowska M., Heinemann U., Saenger W. Three-dimensional structure of ribonuclease T1 complexed with guanylyl-2', 5'-guanosine at 1.8 A resolution// J. Mol. Biol. 1989. V. 206. P. 475−488.
- Sugio S., Oka K, Ohishi H., Tomita K, Saenger W. Three-dimensional structure of the ribonuclease T1 X 3-guanylic acid complex at 2.6 A resolution// FEBS Lett. 1985. V. 183. P. 115 118.
- Kostrewa D., Choe H.W., Heinemann U., Saenger W. Crystal structure of guanosine-free ribonuclease T1, complexed with vanadate (V), suggests conformational change upon substrate binding// Biochemistry. 1989. V. 28. P. 7592−7600.
- Zegers I., Verheist P., Choe H.W., Steyaert J., Heinemann U., Saenger W., Wyns L. Role of histidine-40 in ribonuclease T1 catalysis: three-dimensionalstructures of the partially active His40Lys mutant// Biochemistry. 1992. V. 31. P. 11 317−11 325.
- Koellner G., Choe H.W., Heinemann U., Grunert H.P., Zouni A., Hahn U., Saenger W. His92Ala mutation in ribonuclease T1 induces segmental flexibility. An X-ray study// J. Mol. Biol. 1992. V. 224. P. 701−713.
- Koellner G., Grunert H.P., Landt O., Saenger W. Crystal structure of the Tyr45Trp mutant of ribonuclease T1 in a complex with 2-adenylic acid//Eur. J. Biochem. 1991. V. 201. P. 199−202.
- Martinez-Oyanedel J., Choe H.W., Heinemann U., Saenger W. Ribonuclease T1 with free recognition and catalytic site: crystal structure analysis at 1.5 A resolution// J. Mol. Biol. 1991. V. 222. P. 335−352.
- Malin R" Zieienkiewicz P., Saenger W. Structurally conserved water molecules in ribonuclease T1// J. Biol. Chem. 1991. V. 266. P. 4848−4852.
- Steyaert J., Haikal A.F., Wyns L., Stanssens P. Subsite interactions of ribonuclease T1: Asn36 and Asn98 accelerate GpN transesterification through interactions with the leaving nucleoside N// Biochemistry. 1991. V. 30. P. 8666−8670.
- Steyaert J., Wyns L., Stanssens P. Subsite interactions of ribonuclease T1: viscosity effects indicate that the rate-limiting step of GpN transesterification depends on the nature of N// Biochemistry. 1991. V. 30. P. 8661−8665.
- Zegers I., Loris R., Dehoiiander G., Fattah Haikal A., Poortmans F., Steyaert J., Wyns L. Hydrolysis of a slow cyclic thiophosphate substrate of RNase T1 analyzed by time-resolved crystallography// Nat. Struct. Biol. 1998. V. 5. P. 280−283.
- Thompson J.E.R., R.T. Value of general acid-base catalysis to ribonuclease A.// J. Am. Chem. Soc. 1994. V. 116. P. 5467−5468.
- Herschlag D. Ribonuclease revisited: catalysis via the classical general acid-base mechanism or a triester-like mechanism?// J. Am. Chem. Soc. 1994. V. 116. P. 11 631−11 635.
- Breslow R., Chapman W.H., Jr. On the mechanism of action of ribonuclease A: relevance of enzymatic studies with a p-nitrophenylphosphate ester and a thiophosphate ester// Proc. Natl. Acad. Sci. USA. 1996. V. 93. P. 10 018−10 021.
- Wladkowski B.D., Krauss, M. & Stevens, W.J. Transphosphorylation catalyzed by ribonuclease A: computational study using ab initio effective fragment potentials.// J. Am. Chem. Soc. 1995. V. 117. P. 10 537−10 545.
- Eckstein F., Schulz H.H., Ruterjans H., Haar W., Maurer W. Stereochemistry of the transesterification step of ribonuclease T 1// Biochemistry. 1972. V. 11. P. 3507−3512.
- Pletinckx J., Steyaert J., Zegers I., Choe H.W., Heinemann U., Wyns L. Crystallographic study of Glu58Ala RNase T1 x 2'-guanosine monophosphate at 1.9-A resolution// Biochemistry. 1994. V. 33. P. 1654−1662.
- Ding J., Koellner G., Grunert H.P., Saenger W. Crystal structure of ribonuclease T1 complexed with adenosine 2'-monophosphate at 1.8-A resolution// J. Biol. Chem. 1991. V. 266. P. 15 128−15 134.
- Czaja R., Struhalla M" Hoschler K., Saenger W., Strater N. Hahn U. RNase T1 variant RV cleaves single-stranded RNA after purines due to specific recognition by the Asn46 side chain amide// Biochemistry. 2004. V. 43. P. 2854−2862.
- Campbell M.K., Ts’o P.O. Binding of purine nucleoside monophosphates by ribonuclease T-1. A model system for protein nucleic acid interaction// Biochim. Biophys. Acta. 1971. V. 232. P. 427−435.
- Hirono S., Kollman P.A. Calculation of the relative binding free energy of 2'GMP and 2AMP to ribonuclease T1 using molecular dynamics/free energy perturbation approaches// J. Mol. Biol. 1990. V. 212. P. 197−209.
- Lovehx S., Doumen J., Steyaert J. Additivity of protein-guanine interactions in ribonuclease T1// J. Biol. Chem. 1997. V. 272. P. 9635−9639.
- Granzin J., Puras-Lutzke R., Landt O., Grunert H.P., Heinemann U., Saenger W., Hahn U. RNase T1 mutant Glu46Gln binds the inhibitors 2'GMP and 2AMP at the 3' subsite// J. Mol. Biol. 1992. V. 225. P. 533−542.
- Steyaert J., Opsomer C" Wyns L, Stanssens P. Quantitative analysis of the contribution of Glu46 and Asn98 to the guanosine specificity of ribonuclease T1// Biochemistry. 1991. V. 30. P. 494−499.
- Hirono S., Kollman P.A. Relative binding free energy calculations of inhibitors to two mutants (Glu46—Ala/Gin) of ribonuclease T1 using molecular dynamics/free energy perturbation approaches// Protein Eng. 1991. V. 4. P. 233−243.
- Hubner Π., Haensler M., Hahn U. Modification of ribonuclease T1 specificity by random mutagenesis of the substrate binding segment// Biochemistry. 1999. V. 38. P. 1371−1376.
- Hoschler K., Hoier H., Hubner Π., Saenger W" Orth P., Hahn U. Structural analysis of an RNase T1 variant with an altered guanine binding segment// J. Mol. Biol. 1999. V. 294. P. 12 311 238.
- Czaja R., Perbandt M., Betzel C" Hahn U. Purine activity of RNase T1RV is further improved by substitution of Trp59 by tyrosine// Biochem. Biophys. Res. Commun. 2005. V. 336. P. 882−889.
- Walz F.G., Jr., Osterman H.L., Libertin C. Base-group specificity at the primary recognition site of ribonuclease T for minimal RNA substrates//Arch. Biochem. Biophys. 1979. V. 195. P. 95 102.
- Yoshida H. The ribonuclease T1 family// Methods Enzymol. 2001. V. 341. P. 28−41.
- Noguchi S., Satow Y., Uchida Π’., Sasaki C" Matsuzaki T. Crystal structure of Ustilago sphaerogena ribonuclease U2 at 1.8 A resolution// Biochemistry. 1995. V. 34. P. 15 583−15 591.
- Breslow R., Xu R. Recognition and catalysis in nucleic acid chemistry.// Proc. Natl. Acad. Sci. 1986. V. 90. P. 1201−1207.
- Fouace S., Gaudin C., Picard S., Corvaisier S., Renault J., Carboni Π., Felden B. Polyamine derivatives as selective RNaseA mimics// Nucleic Acids Res. 2004. V. 32. P. 151−157.
- Bibillo A., Figlerowicz M., Kierzek R. The non-enzymatic hydrolysis of oligoribonucleotides VI. The role of biogenic polyamines// Nucleic Acids Res. 1999. V. 27. P. 3931−3937.
- Vlassov V.V., ZuberG., Felden Π., BehrJ.P., Giege R. Cleavage of tRNA with imidazole and spermine imidazole constructs: a new approach for probing RNA structure// Nucleic Acids Res. 1995. V. 23. P. 3161−3167.
- ΠΠ΅Π½Π³Π΅Ρ Π. ΠΡΠΈΠ½ΡΠΈΠΏΡ ΡΡΡΡΠΊΡΡΡΠ½ΠΎΠΉ ΠΎΡΠ³Π°Π½ΠΈΠ·Π°ΡΠΈΠΈ Π½ΡΠΊΠ»Π΅ΠΈΠ½ΠΎΠ²ΡΡ ΠΊΠΈΡΠ»ΠΎΡ. Π.: ΠΠΈΡ, 1987, Ρ. 584.
- Walt F., Lima V., Crooke S.T. Highly efficient endonucleolytic cleavage of RNA by a Cys2His2 zinc-finger peptide.// Proc. Natl. Acad. Sei. 1999. V. 96. P. 10 010−10 015.
- Mironova N.L., Pyshnyi D.V., Ivanova E.M., Zenkova M.A., Gross H.J., Vlassov V.V. Covalently attached oligodeoxyribonucleotides induce RNase activity of a short peptide and modulate its base specificity// Nucleic Acids Res. 2004. V. 32. P. 1928−1936.
- Michaelis Π, Kaiesse M. Selective cleavage of unpaired uridines with a tyrosine-cyclen conjugate// Chembiochem. 2001. V. 2. P. 79−83.
- ΠΠ΅Π½ΠΊΠΎΠ²Π° Π.Π., Π§ΡΠΌΠ°ΠΊΠΎΠ²Π° Π. Π., ΠΠ»Π°ΡΠΎΠ² A.B., ΠΠΎΠΌΠ°ΡΠΎΠ²Π° Π. Π., ΠΠ΅Π½ΡΡΠΌΠΈΠ½ΠΎΠ²Π° Π. Π., ΠΠ»Π°ΡΠΎΠ² Π. Π., Π‘ΠΈΠ»ΡΠ½ΠΈΠΊΠΎΠ² Π. Π. Π‘ΠΈΠ½ΡΠ΅ΡΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΠΊΠΎΠ½ΡΡΡΡΠΊΡΠΈΠΈ, ΡΡΠ½ΠΊΡΠΈΠΎΠ½Π°Π»ΡΠ½ΠΎ ΠΈΠΌΠΈΡΠΈΡΡΡΡΠΈΠ΅ ΡΠΈΠ±ΠΎΠ½ΡΠΊΠ»Π΅Π°Π·Ρ Π.// ΠΠΎΠ». ΠΠΈΠΎΠ»ΠΎΠ³ΠΈΡ. 2000. Π’. 34. Π‘. 456−460.
- ΠΠΎΠ½Π΅Π²Π΅Ρ Π.Π., ΠΠ΅Π½ΠΊΠΎΠ²Π° M.A., Π‘ΠΈΠ»ΡΠ½ΠΈΠΊΠΎΠ² B.H., ΠΠ»Π°ΡΠΎΠ² B.B. Π‘ΠΈΠ½ΡΠ΅ΡΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΠΌΠΎΠ»Π΅ΠΊΡΠ»Ρ, ΠΊΠ°ΡΠ°Π»ΠΈΠ·ΠΈΡΡΡΡΠΈΠ΅ Π³ΠΈΠ΄ΡΠΎΠ»ΠΈΠ· Π ΠΠ// ΠΠΎΠΊΠ». Π ΠΠ. 1998. Π’. 360. Π‘. 554−558.
- Burakova Π.Π., Kovalev N.A., Kuznetsova IL., Zenkova M.A., Vlasov V.V., Sil’nikov V.N. Polycationic catalysts for phosphodiester bond cleavage on the basis of 1,4-diazabicyclo[2.2.2.octane]// Bioorg. Khim. 2007. V. 33. P. 563−570.
- Kovalev N., Burakova E" Silnikov V., Zenkova M., Vlassov V. Artificial ribonucleases: from combinatorial libraries to efficient catalysts of RNA cleavage// Bioorg. Chem. 2006. V. 34. P. 274 286.
- Kovalev N.A., Medvedeva D.A., Zenkova M.A., Vlassov V.V. Cleavage of RNA by an amphiphilic compound lacking traditional catalytic groups// Bioorg. Chem. 2008. V. 36. P. 33−45.
- Emilsson G.M., Nakamura S., Roth A., Breaker R.R. Ribozyme speed limits// Rna. 2003. V. 9. P. 907−918.
- ΠΠ΅Π»ΠΎΠ³Π»Π°Π·ΠΎΠ²Π° Π.Π., Π’Π°ΠΌΠΊΠΎΠ²ΠΈΡ H.B., ΠΠΈΠΊΠΈΡΠΈΠ½ Π. Π., ΠΡΠ·Π½Π΅ΡΠΎΠ²Π° Π. Π., ΠΠ΅Π½ΠΊΠΎΠ²Π° Π. Π., ΠΠ»Π°ΡΠΎΠ² Π. Π. ΠΡΠΊΡΡΡΡΠ²Π΅Π½Π½ΡΠ΅ ΡΠΈΠ±ΠΎΠ½ΡΠΊΠ»Π΅Π°Π·Ρ Π½ΠΎΠ²ΡΠΉ ΠΊΠ»Π°ΡΡ Π΄Π»Ρ Π±ΠΈΠΎΠ»ΠΎΠ³ΠΈΠΈ ΠΈ ΠΌΠ΅Π΄ΠΈΡΠΈΠ½Ρ.// ΠΠ΅ΡΡΠ½ΠΈΠΊ ΠΠΠΠΈΠ‘. 2006. Π’. 10. Π‘. 382 — 395.
- Dock-Bregeon A.C., Moras D. Conformational changes and dynamics of tRNAs: evidence from hydrolysis patterns// Cold Spring Harb Symp Quant Biol. 1987. V. 52. P. 113−121.
- Milligan J.F., Uhlenbeck O.C. Synthesis of small RNAs using T7 RNA polymerase// Methods Enzymol. 1989. V. 180. P. 51−62.
- England Π’.Π., Bruce A.G., Uhlenbeck O.C. Specific labeling of 3' termini of RNA with T4 RNA ligase// Methods Enzymol. 1980. V. 65. P. 65−74.
- Silberklang M., Prochiantz A., Haenni A.L., Rajbhandary U.L. Studies on the sequence of the Π'-terminal region of turnip-yellow-mosaic-virus RNA// Eur. J. Biochem. 1977. V. 72. P. 465−478.
- Donis-Keller H., Maxam A.M., Gilbert W. Mapping adenines, guanines, and pyrimidines in RNA// Nucleic Acids Res. 1977. V. 4. P. 2527−2538.
- ΠΠ»Π°ΡΠΎΠ² A.B., ΠΠ»Π°ΡΠΎΠ² Π. Π., ΠΡΠ΅ΠΆΠ΅ Π . ΠΠ°ΡΠ°Π»ΠΈΠ·ΠΈΡΡΠ΅ΠΌΡΠΉ ΠΈΠΌΠΈΠ΄Π°Π·ΠΎΠ»ΠΎΠΌ Π³ΠΈΠ΄ΡΠΎΠ»ΠΈΠ· Π ΠΠ ΠΊΠ°ΠΊ ΡΠ΅Π°ΠΊΡΠΈΡ Π΄Π»Ρ ΠΈΡΡΠ»Π΅Π΄ΠΎΠ²Π°Π½ΠΈΡ Π²ΡΠΎΡΠΈΡΠ½ΠΎΠΉ ΡΡΡΡΠΊΡΡΡΡ Π ΠΠ ΠΈ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠΎΠ² Π ΠΠ Ρ ΠΎΠ»ΠΈΠ³ΠΎΠ½ΡΠΊΠ»Π΅ΠΎΡΠΈΠ΄Π°ΠΌΠΈ//ΠΠΎΠΊΠ». ΠΠΊΠ°Π΄. ΠΠ°ΡΠΊ. 1996. Π’. 349. Π‘. 411−413.
- Ehresmann Π‘., Baudin F., Mougel Π., Romby P., Ebel J.P., Ehresmann B. Probing the structure of RNAs in solution// Nucleic Acids Res. 1987. V. 15. P. 9109−9128.
- Giege R., Felden Π., Zenkova M.A., Sil’nikov V.N., Vlassov V.V. Cleavage of RNA with synthetic ribonuclease mimics// Meth. Enzymol. 2000. V. 318. P. 147−165.
- Endo M., Hirata K., Inokawa Π’., Matsumura K., Komiyama M" lhara Π’., Sueda S., Takagi M. Site-specific hydrolysis of yeast tRNAPhe by anthraquinone-glycine and anthraquinone-iminodiacetate conjugates// Nucleic Acids Symp. Ser. 1995. P. 109−110.
- Zhong M., Kallenbach N.R. Mapping tRNA and 5S RNA tertiary structures by charge dependent Fe (ll)-catalyzed cleavage// J. Biomol. Struct. Dyn. 1994. V. 11. P. 901−911.
- Komiyama M., Inokawa T. Selective hydrolysis of tRNA by ethylenediamine bound to a DNA oligomer//J. Biochem (Tokyo). 1994. V. 116. P. 719−720.
- Komiyama M" Inokawa Π’., Shiiba Π’., Takeda N., Yoshinari K, Yashiro M. Molecular design of artificial hydrolytic nucleases and ribonucleases// Nucleic Acids Symp. Ser. 1993. P. 197−198.
- Guan L.L., Totsuka R" Kuwahara J., Otsuka M., Sugiura Y. Cleavage of yeast tRNA (phe) with Ni (lll) and Co (lll) complexes of bleomycin// Biochem. Biophys. Res. Commun. 1993. V. 191. P. 1338−1346.
- Huttenhofer A., Hudson S., Noller H.F., Mascharak P.K. Cleavage of tRNA by Fe (ll)-bleomycin// J. Biol. Chem. 1992. V. 267. P. 24 471−24 475.
- Isel C., Ehresmann C., Keith G., Ehresmann Π., Marquet R. Initiation of reverse transcription of HIV-1: secondary structure of the HIV-1 RNA/tRNA (3Lys) (template/primer)// J Mol Biol. 1995. V. 247. P. 236−250.
- Riepe A., Beier H., Gross H.J. Enhancement of RNA self-cleavage by micellar catalysis// FEBS Lett. 1999. V. 457. P. 193−199.
- Wang D.A., Narang A.S., Kotb M" Gaber A.O., Miller D.D., Kim S.W., Mahato R.I. Novel branched poly (ethylenimine)-cholesterol water-soluble lipopolymers for gene delivery// Biomacromolecules. 2002. V. 3. P. 1197−1207.
- Thomas M., Lu J.J., Ge Q" Zhang C" Chen J., Klibanov A.M. Full deacylation of polyethylenimine dramatically boosts its gene delivery efficiency and specificity to mouse lung// Proc. Natl. Acad. Sci. USA. 2005. V. 102. P. 5679−5684.
- Da Poian A.T., Carneiro F.A., Stauffer F. Viral membrane fusion: is glycoprotein G of rhabdoviruses a representative of a new class of viral fusion proteins?// Braz. J. Med. Biol. Res. 2005. V. 38. P. 813−823.
- Breslow R., Labelle M. Sequential general base-acid catalysis in the hydrolysis of RNA by imidazole//J. Amer. Chem. Soc. 1986. V. 108. P. 2655−2659.
- Wilson W.D., Wang Y.H., Kusuma S., Chandrasekaran S., Boykin D.W. The effect of intercalator structure on binding strength and base-pair specificity in DNA interactions// Biophys. Chem. 1986. V. 24. P. 101−109.
- ΠΠΎΡΠΎΠ½ P., ΠΠ»Π»ΠΈΠΎΡ Π., ΠΠ»Π»ΠΈΠΎΡ Π., ΠΠΆΠΎΠ½Ρ Π. Π‘ΠΏΡΠ°Π²ΠΎΡΠ½ΠΈΠΊ Π±ΠΈΠΎΡ ΠΈΠΌΠΈΠΊΠ°. ΠΠ΅Ρ. Ρ Π°Π½Π³Π». Π.: ΠΠΈΡ, 1991, 544 (R.M.C. Dawson, D.C. Elliot, W.H. Elliot, K.M. Jones. Data for boichemical research. Oxford- Oxford University Press- 1986)
- Kaukinen U" Venalainen Π’., Lonnberg H., Perakyla M. The base sequence dependent flexibility of linear single-stranded oligoribonucleotides correlates with the reactivity of the phosphodiester bond// Org. Biomol. Chem. 2003. V. 1. P. 2439−2447.
- Maglott E.J., Deo S.S., Przykorska A., Glick G.D. Conformational transitions of an unmodified tRNA: implications for RNA folding// Biochemistry. 1998. V. 37. P. 16 349−16 359.
- Petyuk V.A., Zenkova M.A., Giege R., Vlassov V. V. Hybridization of antisense oligonucleotides with the 3'part of tRNA (Phe)// FEBS Lett. 1999. V. 444. P. 217−221.
- Helm M., Brule H., Degoul F" Cepanec C" Leroux J.P., Giege R" Florentz C. The presence of modified nucleotides is required for cloverleaf folding of a human mitochondrial tRNA// Nucleic Acids Res. 1998. V. 26. P. 1636−1643.
- Serebrov V., Vasilenko K.S., Kholod N.S., Kiselev L.L. Mg2+ ions differently affect the physical properties of tRNA (Phe) and the transcript of its gene.// Mol. Biol (Mosk). 1997. V. 31. P. 894−900.
- Nagaswamy U., Gao X., Martinis S.A., Fox G.E. NMR structure of a ribosoma! RNA hairpin containing a conserved CUCAA pentaloop// Nucleic Acids Res. 2001. V. 29. P. 5129−5139.
- JuckerF.M., Pardi A. GNRA tetraloops make a U-turn// Rna. 1995. V. 1. P. 219−222.
- Freier S.M., Hill K.O., Dewey T.G., Marky L.A., BreslauerK.J., TurnerD.H. Solvent effects on the kinetics and thermodynamics of stacking in poly (cytidylic acid)// Biochemistry. 1981. V. 20. P. 1419−1426.
- Giege R" Puglisi J.D., Florentz C. tRNA structure and aminoacylation efficiency// Prog Nucleic Acid Res. Mol Biol. 1993. V. 45. P. 129−206.
- Downs W.D., Cech T.R. An ultraviolet-inducible adenosine-adenosine cross-link reflects the catalytic structure of the Tetrahymena ribozyme// Biochemistry. 1990. V. 29. P. 5605−5613.
- Branch A.D., Benenfeld B.J., Robertson H.D. Ultraviolet light-induced crosslinking reveals a unique region of local tertiary structure in potato spindle tuber viroid and HeLa 5S RNA// Proc. Natl. Acad. Sci. USA. 1985.V. 82. P. 6590−6594.
- Atmadja J., Brimacombe R., Blocker H., Frank R. Investigation of the tertiary folding of Escherichia coli 16S RNA by in situ intra-RNA cross-linking within 30S ribosomal subunits// Nucleic Acids Res. 1985. V. 13. P. 6919−6936.
- Bergstrom D.E., Leonard N.J. Photoreaction of 4-thiouracil with cytosine. Relation to photoreactions in Escherichia coli transfer ribonucleic acids// Biochemistry. 1972. V. 11. P. 1−9.
- Favre A., Yaniv M., Michelson A.M. The photochemistry of 4-thiouridine in Escherichia coli t-RNA Val1// Biochem. Biophys. Res. Commun. 1969. V. 37. P. 266−271.
- Behlen L.S., Sampson J.R., Uhlenbeck O.C. An ultraviolet light-induced crosslink in yeast tRNA (Phe)// Nucleic Acids Res. 1992. V. 20. P. 4055−4059.
- Jovine L, Djordjevic S., Rhodes D. The crystal structure of yeast phenylalanine tRNA at 2.0 A resolution: cleavage by Mg (2+) in 15-year old crystals// J. Mol. Biol. 2000. V. 301. P. 401−414.
- Norberg J., Nilsson L. Stacking Free Energy Profiles for All 16 Natural Ribodinucleoside Monophosphates in Aqueous Solution //J. Am. Chem. Soc. 1995. V. 117. P. 10 832−10 840.
- Inners L.D., Felsenfeld G. Conformation of polyribouridylic acid in solution// J. Mol. Biol. 1970. V. 50. P. 373−389.
- Cannistraro V.J., Subbarao M.N., Kennell D. Specific endonucleolytic cleavage sites for decay of Escherichia coli mRNA// J. Mol. Biol. 1986. V. 192. P. 257−274.
- Burkard M.E., Kierzek R., Turner D.H. Thermodynamics of unpaired terminal nucleotides on short RNA helixes correlates with stacking at helix termini in larger RNAs// J. Mol. Biol. 1999. V. 290. P. 967−982.
- Filimonov V.V., Privalov P.L. Thermodynamics of base interaction in (A)n and (A.U)n// J. Mol. Biol. 1978. V. 122. P. 465−470.
- Suurkuusk J., Alvarez J., Freire E., Biltonen R. Caiorimetric determination of the' heat capacity changes associated with the conformational transitions of polyriboadenylic acid and polyribouridylic acid//Biopolymers. 1977. V. 16. P. 2641−2652.
- Li Y., Breaker R.R. Kinetics of RNA Degradation by Specific Base Catalysis of Transesterification Involving the 2-Hydroxyl Group II J. Am. Chem. Soc. 1999. V. 121. P. 53 645 372.
- Ezra F.S., Lee C.H., Kondo N.S., Danyluk S.S., Sarma R.H. Conformational properties of purine-pyrimidine and pyrimidine-purine dinucleoside monophosphates// Biochemistry. 1977. V. 16. P. 1977−1987.