-
3
-
-
0028874533
-
Freeze-trapping of reaction intermediates
-
3. Moffat K, Henderson R: Freeze-trapping of reaction intermediates. Curr Opin Struct Biol 1995, 5:656-663.
-
(1995)
Curr Opin Struct Biol
, vol.5
, pp. 656-663
-
-
Moffat, K.1
Henderson, R.2
-
4
-
-
0003448574
-
-
Catalytic RNA. Berlin: Springer-Verlag
-
4. Eckstein F, Lilley DMJ (Eds): Nucleic Acids and Molecular Biology, vol 10 Catalytic RNA. Berlin: Springer-Verlag; 1997. A complete and up-to-date text on the various types of catalytic RNAs, with chapters written by many of those most active in the field.
-
(1997)
Nucleic Acids and Molecular Biology
, vol.10
-
-
Eckstein, F.1
Lilley, D.M.J.2
-
5
-
-
0028063567
-
Three-dimensional structure of a hammerhead ribozyme
-
5. Pley HW, Flaherty KM, McKay DB: Three-dimensional structure of a hammerhead ribozyme. Nature 1994, 372:68-74.
-
(1994)
Nature
, vol.372
, pp. 68-74
-
-
Pley, H.W.1
Flaherty, K.M.2
McKay, D.B.3
-
6
-
-
0029073091
-
The crystal-structure of an all-RNA hammerhead ribozyme - A proposed mechanism for RNA catalytic cleavage
-
6. Scott WG, Finch JT, Klug A: The crystal-structure of an all-RNA hammerhead ribozyme - a proposed mechanism for RNA catalytic cleavage. Cell 1995, 81:991-1002.
-
(1995)
Cell
, vol.81
, pp. 991-1002
-
-
Scott, W.G.1
Finch, J.T.2
Klug, A.3
-
7
-
-
0030476765
-
Capturing the structure of a catalytic RNA intermediate: The hammerhead ribozyme
-
7. Scott WG, Murray JB, Arnold JRP, Stoddard BL, Klug A: Capturing the structure of a catalytic RNA intermediate: the hammerhead ribozyme. Science 1996, 274:2065-2069.
-
(1996)
Science
, vol.274
, pp. 2065-2069
-
-
Scott, W.G.1
Murray, J.B.2
Arnold, J.R.P.3
Stoddard, B.L.4
Klug, A.5
-
8
-
-
0029820625
-
Crystal structure of a group-I ribozyme domain - Principles of RNA packing
-
8. Cate JH, Gooding AR, Podell E, Zhou KH, Golden BL, Kundrot CE, Cech TR, Doudna JA: Crystal structure of a group-I ribozyme domain - principles of RNA packing. Science 1996, 273:1678-1685.
-
(1996)
Science
, vol.273
, pp. 1678-1685
-
-
Cate, J.H.1
Gooding, A.R.2
Podell, E.3
Zhou, K.H.4
Golden, B.L.5
Kundrot, C.E.6
Cech, T.R.7
Doudna, J.A.8
-
9
-
-
0032500731
-
A preorganized active site in the crystal structure of the Tetrahymena ribozyme
-
9. Golden BL, Gooding AR, Podell ER, Cech TR: A preorganized active site in the crystal structure of the Tetrahymena ribozyme. Science 1998, 282:259-264. The 5 Å resolution map of the ribozyme reveals the backbone fold of the catalytic core of the group I intron, which appears to be consistent with many of the detailed features presented in the models of the group I intron core that were deduced by Michel and Westhof [46]. The ribozyme core resembles that of many protein enzymes in that it is compact and globular.
-
(1998)
Science
, vol.282
, pp. 259-264
-
-
Golden, B.L.1
Gooding, A.R.2
Podell, E.R.3
Cech, T.R.4
-
10
-
-
0032497521
-
Crystal structure of a hepatitis delta virus ribozyme
-
10. Ferré-D'Amaré AR, Zhou K, Doudna JA: Crystal structure of a hepatitis delta virus ribozyme. Nature 1998, 395:567-574. This structure of the cleaved form of the HDV ribozyme is intriguing from several standpoints. It is the first high resolution structure of a very compact and organized RNA catalytic site and consists of a nested, double pseudoknot structure. Crystals were obtained by grafting a U1A protein-binding site onto a nonessential stem-loop of the ribozyme, in complex with the U1A RNA-binding protein. Although it appears to be unique among small ribozymes in its requirement for a divalent metal ion, none have so far been located in the active site.
-
(1998)
Nature
, vol.395
, pp. 567-574
-
-
Ferré-D'Amaré, A.R.1
Zhou, K.2
Doudna, J.A.3
-
11
-
-
0030747007
-
Unusual dynamics and pK(a) shift at the active site of a lead-dependent ribozyme
-
11. Legault P, Pardi A: Unusual dynamics and pK(a) shift at the active site of a lead-dependent ribozyme. J Am Chem Soc 1997, 119:6621-6628. The leadzyme NMR-derived RNA structure and its effect upon biochemical function is emerging. The leadzyme is an in vitro selected ribozyme that catalyzes a two-step reaction, the first of which is similar to that of the hammerhead, hairpin, VS and hepatitis delta virus ribozymes.
-
(1997)
J Am Chem Soc
, vol.119
, pp. 6621-6628
-
-
Legault, P.1
Pardi, A.2
-
12
-
-
0031252479
-
Structure of a conserved RNA component of the peptidyl transferase center
-
12. Puglisi EV, Green R, Noller HF, Puglisi JD: Structure of a conserved RNA component of the peptidyl transferase center. Nat Struct Biol 1997, 4:775-778. The structure determination of a conserved hairpin loop involved in peptidyl-tRNA recognition by 23S RNA reveals that the loop is closed by a novel G·C base pair and presents guanine residues for tRNA recognition.
-
(1997)
Nat Struct Biol
, vol.4
, pp. 775-778
-
-
Puglisi, E.V.1
Green, R.2
Noller, H.F.3
Puglisi, J.D.4
-
13
-
-
0032489357
-
The structural basis of hammerhead ribozyme self-cleavage
-
13. Murray JB, Terwep DP, Maloney L, Karpeisky A, Usman N, Beigelman L, Scott WG: The structural basis of hammerhead ribozyme self-cleavage. Cell 1998, 92:665-673. The authors report the structure of a conformational change at the cleavage site of the hammerhead ribozyme that appears to be sufficient for the future formation of a transition state that is compatible with an in-line attack mechanism.
-
(1998)
Cell
, vol.92
, pp. 665-673
-
-
Murray, J.B.1
Terwep, D.P.2
Maloney, L.3
Karpeisky, A.4
Usman, N.5
Beigelman, L.6
Scott, W.G.7
-
14
-
-
0030832614
-
Group II intron endonucleases use both RNA and protein subunits for recognition of specific sequences in double-stranded DNA
-
14. Guo HT, Zimmerly S, Perlman PS, Lambowitz AM: Group II intron endonucleases use both RNA and protein subunits for recognition of specific sequences in double-stranded DNA. EMBO J 1997, 16:6835-6848. The authors describe this unique protein-RNA complex, in which the protein subunit recognizes and nicks one strand of double-stranded DNA and the catalytic RNA subunit recognizes and nicks the other. These reactions are critical to the 'homing' replicative behavior observed with many group II introns.
-
(1997)
EMBO J
, vol.16
, pp. 6835-6848
-
-
Guo, H.T.1
Zimmerly, S.2
Perlman, P.S.3
Lambowitz, A.M.4
-
15
-
-
0029410699
-
Group-II intron ribozymes that cleave DNA and RNA linkages with similar efficiency, and lack contacts with substrate 2′-hydroxyl groups
-
15. Griffin EA, Qin ZF, Michels WJ, Pyle AM: Group-II intron ribozymes that cleave DNA and RNA linkages with similar efficiency, and lack contacts with substrate 2′-hydroxyl groups. Chem Biol 1995, 2:761-770.
-
(1995)
Chem Biol
, vol.2
, pp. 761-770
-
-
Griffin, E.A.1
Qin, Z.F.2
Michels, W.J.3
Pyle, A.M.4
-
16
-
-
0032502997
-
Ribosome-catalyzed peptide-bond formation with an A-site substrate covalently linked to 23S ribosomal RNA
-
16. Green R, Switzer C, Noller HF: Ribosome-catalyzed peptide-bond formation with an A-site substrate covalently linked to 23S ribosomal RNA. Science 1998, 280:286-289. A covalently linked substrate reacts with a peptidyl-tRNA analog, forming a peptide bond in a peptidyl transferase-catalyzed reaction. This result places a conserved loop of 23S rRNA at the peptidyl transferase A-site and suggests that peptide bond formation can occur uncoupled from movement of the A-site tRNA, which the peptidyl-tRNA helps to create.
-
(1998)
Science
, vol.280
, pp. 286-289
-
-
Green, R.1
Switzer, C.2
Noller, H.F.3
-
17
-
-
0032584644
-
Reconstitution of peptide bond formation with Escherichia coli 23S ribosomal RNA domain
-
17. Nitta I, Kamada Y, Noda H, Ueda T, Watanabe K: Reconstitution of peptide bond formation with Escherichia coli 23S ribosomal RNA domain. Science 1998, 281:666-669. Proof that the 23S RNA subunit of the ribosome is an autonomous catalyst of the peptide bond-formation reaction has proven to be extremely elusive. By combining various domains of 23S RNA in vitro, the authors report an approximately fourfold increase in the rate of peptide bond formation when the domain that is known to be required for catalysis is present. Further conformation that the 23S RNA is in fact a true ribozyme awaits positive identification of the reaction product as a peptide adduct.
-
(1998)
Science
, vol.281
, pp. 666-669
-
-
Nitta, I.1
Kamada, Y.2
Noda, H.3
Ueda, T.4
Watanabe, K.5
-
18
-
-
0000917638
-
In vitro selections of catalytic polynucleotides
-
18. Breaker RR: In vitro selections of catalytic polynucleotides. Chem Rev 1997, 97:371-390.
-
(1997)
Chem Rev
, vol.97
, pp. 371-390
-
-
Breaker, R.R.1
-
19
-
-
0032542574
-
Structural and kinetic characterization of an acyl transferase ribozyme
-
19. Suga H, Lohse PA, Szostak JW: Structural and kinetic characterization of an acyl transferase ribozyme. J Am Chem Soc 1998, 120:1151-1156. In this paper, a previously reported ribozyme that is capable of acyl transfer reactions is characterized both structurally and kinetically.
-
(1998)
J Am Chem Soc
, vol.120
, pp. 1151-1156
-
-
Suga, H.1
Lohse, P.A.2
Szostak, J.W.3
-
20
-
-
0030688863
-
Peptide bond formation by in vitro selected ribozymes
-
20. Zhang BL, Cech TR: Peptide bond formation by in vitro selected ribozymes. Nature 1997, 390:96-100. A ribozyme that is analogous to that developed by Szostak and co-workers [19•] and can carry out peptide bond formation is described in detail. This result further strengthens the argument that, in principle, RNA can have peptidyl transferase activity.
-
(1997)
Nature
, vol.390
, pp. 96-100
-
-
Zhang, B.L.1
Cech, T.R.2
-
21
-
-
0031882441
-
A novel ribozyme with ester transferase activity
-
21. Jenne A, Famulok M: A novel ribozyme with ester transferase activity. Chem Biol 1998, 5:23-34. A description of another in vitro selected ribozyme that constitutes further expansion of the catalytic repertoire of RNA.
-
(1998)
Chem Biol
, vol.5
, pp. 23-34
-
-
Jenne, A.1
Famulok, M.2
-
22
-
-
0031194873
-
A unique mechanism for RNA catalysis: The role of metal cofactors in hairpin ribozyme cleavage
-
22. Hampel A, Cowan JA: A unique mechanism for RNA catalysis: the role of metal cofactors in hairpin ribozyme cleavage. Chem Biol 1997, 4:513-517. This first report that the hairpin ribozyme does not require divalent metal ions shattered the belief that all ribozymes are metalloenzymes. Hampel also originally characterized the hairpin ribozyme.
-
(1997)
Chem Biol
, vol.4
, pp. 513-517
-
-
Hampel, A.1
Cowan, J.A.2
-
23
-
-
0031215134
-
An unusual pH-independent and metal-ion-independent mechanism for hairpin ribozyme catalysis
-
23. Nesbitt S, Hegg LA, Fedor MJ: An unusual pH-independent and metal-ion-independent mechanism for hairpin ribozyme catalysis. Chem Biol 1997, 4:619-630. A careful, independent documentation of the divalent metal ion independence of the chemical step of hairpin ribozyme catalytic cleavage confirms the original observation [22•].
-
(1997)
Chem Biol
, vol.4
, pp. 619-630
-
-
Nesbitt, S.1
Hegg, L.A.2
Fedor, M.J.3
-
24
-
-
0030967825
-
Metal ions play a passive role in the hairpin ribozyme catalysed reaction
-
24. Young KJ, Gill F, Grasby JA: Metal ions play a passive role in the hairpin ribozyme catalysed reaction. Nucleic Acids Res 1997, 25:3760-3766. Further confirmation of the hairpin ribozyme result described in [22•,23•].
-
(1997)
Nucleic Acids Res
, vol.25
, pp. 3760-3766
-
-
Young, K.J.1
Gill, F.2
Grasby, J.A.3
-
25
-
-
0032192761
-
The hammerhead, hairpin and VS ribozymes are catalytically proficient in monovalent cations alone
-
25. Murray JB, Seyhan AA, Walter NG, Burke JM, Scott WG: The hammerhead, hairpin and VS ribozymes are catalytically proficient in monovalent cations alone. Chem Biol 1998, 5:587-595. The authors demonstrate unambiguously that metal ions are not required for ribozyme catalysis in at least three of the seven naturally occurring ribozymes. The fundamental requirement is simply one of a relatively dense positive charge. Whether this charge is required for catalysis per se or simply for RNA folding remains to be determined.
-
(1998)
Chem Biol
, vol.5
, pp. 587-595
-
-
Murray, J.B.1
Seyhan, A.A.2
Walter, N.G.3
Burke, J.M.4
Scott, W.G.5
-
26
-
-
0032472205
-
Inhibition of the hammerhead ribozyme cleavage reaction by site-specific binding of Tb(III)
-
26. Feig AL, Scott WG, Uhlenbeck OC: Inhibition of the hammerhead ribozyme cleavage reaction by site-specific binding of Tb(III). Science 1998, 279:81-84. Tb(III) is shown to inhibit the hammerhead ribozyme by competing with a single Mg(II) ion. These experiments were designed in order to correlate Tb(III) binding to the hammerhead ribozyme in solution, as observed with sensitized luminescence spectroscopy, with binding sites observed in the crystal when Tb(III) is soaked in. The correlations are not completely unambiguous.
-
(1998)
Science
, vol.279
, pp. 81-84
-
-
Feig, A.L.1
Scott, W.G.2
Uhlenbeck, O.C.3
-
27
-
-
0029949701
-
Structure and function of the hammerhead ribozyme: An unfinished story
-
27. McKay DB: Structure and function of the hammerhead ribozyme: an unfinished story. RNA 1996, 2:395-403.
-
(1996)
RNA
, vol.2
, pp. 395-403
-
-
McKay, D.B.1
-
28
-
-
0031860104
-
Crystallographic structures of the hammerhead ribozyme: Relationship to ribozyme folding and catalysis
-
28. Wedekind JE, McKay DB: Crystallographic structures of the hammerhead ribozyme: relationship to ribozyme folding and catalysis. Annu Rev Biophys Biomol Struct 1998, 27:475-502. A comprehensive and up-to-date review of the hammerhead ribozyme structure and its biochemical properties.
-
(1998)
Annu Rev Biophys Biomol Struct
, vol.27
, pp. 475-502
-
-
Wedekind, J.E.1
McKay, D.B.2
-
29
-
-
0029951474
-
Ribozymes: Structure and mechanism in RNA catalysis
-
29. Scott WG, Klug A: Ribozymes: structure and mechanism in RNA catalysis. Trends Biochem Sci 1996, 246:220-224.
-
(1996)
Trends Biochem Sci
, vol.246
, pp. 220-224
-
-
Scott, W.G.1
Klug, A.2
-
30
-
-
0030761058
-
RNA structure comes of age
-
30. Uhlenbeck OC, Pardi A, Feigon J: RNA structure comes of age. Cell 1997, 90:833-840. A useful meeting summary of the 1997 Santa Cruz RNA Structure symposium.
-
(1997)
Cell
, vol.90
, pp. 833-840
-
-
Uhlenbeck, O.C.1
Pardi, A.2
Feigon, J.3
-
31
-
-
0030876444
-
Involvement of a specific metal ion in the transition of the hammerhead ribozyme to its catalytic conformation
-
2+, to ensure folding of the RNA. The assertion made in this paper that the hammerhead ribozyme mechanism is slowed significantly by crystal packing is not correct.
-
(1997)
J Biol Chem
, vol.272
, pp. 26822-26826
-
-
Peracchi, A.1
Beigelman, L.2
Scott, E.C.3
Uhlenbeck, O.C.4
Herschlag, D.5
-
32
-
-
0030929889
-
Magnesium ion core at the heart of a ribozyme domain
-
32. Cate JH, Hanna RL, Doudna JA: Magnesium ion core at the heart of a ribozyme domain. Nat Struct Biol 1997, 4:553-558. Continued studies on the autonomously folding P456 domain of the group I intron reveal important details as to how metal ions bind to and stabilize the group I intron.
-
(1997)
Nat Struct Biol
, vol.4
, pp. 553-558
-
-
Cate, J.H.1
Hanna, R.L.2
Doudna, J.A.3
-
33
-
-
0031213875
-
Crystals by design: A strategy for crystallization of a ribozyme derived from the Tetrahymena group I intron
-
33. Golden BL, Podell ER, Gooding AR, Cech TR: Crystals by design: a strategy for crystallization of a ribozyme derived from the Tetrahymena group I intron. J Mol Biol 1997, 270:711-723. Tremendous effort has gone into intelligently designing and producing crystals of the group I intron catalytic core that diffract to moderate resolution. This paper represents a tour de force of molecular biology coordinated with macromolecular crystallization that will make solving the structure of this important catalytic RNA possible.
-
(1997)
J Mol Biol
, vol.270
, pp. 711-723
-
-
Golden, B.L.1
Podell, E.R.2
Gooding, A.R.3
Cech, T.R.4
-
34
-
-
0017420380
-
Reactivity and cryoenzymology of enzymes in the crystalline state
-
34. Makinen MW, Fink AL: Reactivity and cryoenzymology of enzymes in the crystalline state. Annu Rev Biophys Bioeng 1977, 6:301-343.
-
(1977)
Annu Rev Biophys Bioeng
, vol.6
, pp. 301-343
-
-
Makinen, M.W.1
Fink, A.L.2
-
35
-
-
0029645585
-
Direct measurement of reactivity in the protein crystal by steady-state kinetic studies
-
35. Stoddard BL, Farber GK: Direct measurement of reactivity in the protein crystal by steady-state kinetic studies. Structure 1995, 3:991-996.
-
(1995)
Structure
, vol.3
, pp. 991-996
-
-
Stoddard, B.L.1
Farber, G.K.2
-
36
-
-
0029024462
-
Mutagenesis and laue structures of enzyme intermediates: Isocitrate dehydrogenase
-
36. Bolduc JM, Dyer DH, Scott WG, Singer P, Sweet RM, Koshland DE Jr, Stoddard BL: Mutagenesis and Laue structures of enzyme intermediates: isocitrate dehydrogenase. Science 1995, 268:1312-1317.
-
(1995)
Science
, vol.268
, pp. 1312-1317
-
-
Bolduc, J.M.1
Dyer, D.H.2
Scott, W.G.3
Singer, P.4
Sweet, R.M.5
Koshland D.E., Jr.6
Stoddard, B.L.7
-
37
-
-
0030968710
-
Mechanistic aspects of enzymatic catalysis: Lessons from comparison of RNA and protein enzymes
-
37. Narlikar GJ, Herschlag D: Mechanistic aspects of enzymatic catalysis: lessons from comparison of RNA and protein enzymes. Annu Rev Biochem 1997, 66:19-59. A thorough review of the similarities and differences between protein and RNA catalysis. The analysis presented is essentially an application of Jencks' work.
-
(1997)
Annu Rev Biochem
, vol.66
, pp. 19-59
-
-
Narlikar, G.J.1
Herschlag, D.2
-
38
-
-
0001417431
-
The hammerhead ribozyme
-
Edited by Eckstein F, Lilley DMJ. Berlin: Springer-Verlag
-
38. Thomson JB, Tuschl T, Eckstein F: The hammerhead ribozyme. In Nucleic Acids and Molecular Biology, vol 10. Edited by Eckstein F, Lilley DMJ. Berlin: Springer-Verlag; 1997:173-196. Another useful and very detailed summary of hammerhead ribozyme structural and biochemical studies.
-
(1997)
Nucleic Acids and Molecular Biology
, vol.10
, pp. 173-196
-
-
Thomson, J.B.1
Tuschl, T.2
Eckstein, F.3
-
40
-
-
0016624901
-
Binding energy, specificity, and enzymic catalysis -the circe effect
-
40. Jencks WP: Binding energy, specificity, and enzymic catalysis -the circe effect. Adv Enzymol 1975, 43:219-410.
-
(1975)
Adv Enzymol
, vol.43
, pp. 219-410
-
-
Jencks, W.P.1
-
42
-
-
0031028479
-
A conformational change in the catalytic core of the hammerhead ribozyme upon cleavage of an RNA substrate
-
42. Simmore JP, Legault P, Hangar AB, Michiels P, Pardi A: A conformational change in the catalytic core of the hammerhead ribozyme upon cleavage of an RNA substrate. Biochemistry 1997, 36:518-525. The structure of the hammerhead ribozyme in the cleaved state reveals nuclear Overhauser enhancement contacts between U4 and U7, indicating a rearranged fold when compared to the fold observed for the uncleaved hammerhead in the crystal structures. Once cleavage lakes place, the extra degree of freedom in the backbone should, in principle, allow conformational relaxation to a state such as that observed here.
-
(1997)
Biochemistry
, vol.36
, pp. 518-525
-
-
Simmore, J.P.1
Legault, P.2
Hangar, A.B.3
Michiels, P.4
Pardi, A.5
-
43
-
-
0032514483
-
Crystal structure of the spliceosomal U2B″-U2A′ protein complex bound to a fragment of U2 small nuclear RNA
-
43. Price SR, Evans P, Nagai K: Crystal structure of the spliceosomal U2B″-U2A′ protein complex bound to a fragment of U2 small nuclear RNA. Nature 1998, 394:645-650. This paper describes the principles of spliceosome assembly in terms of RNA-protein interactions, as well as protein-protein interactions. It describes how two U2 spliceosomal proteins coordinate the recognition of an RNA stem-loop that is similar in sequence and structure to the U1A stem-loop, making detailed discrimination between similar RNAs possible.
-
(1998)
Nature
, vol.394
, pp. 645-650
-
-
Price, S.R.1
Evans, P.2
Nagai, K.3
-
44
-
-
0030990359
-
The ribosome at higher resolution - The donut takes shape
-
44. Frank J: The ribosome at higher resolution - the donut takes shape. Curr Opin Struct Biol 1997, 7:266-272. A current summary of the electron microscopy-derived ribosome structures as the push to better the 15 Å resolution limit continues. Many of the most important structural features are visible at this resolution.
-
(1997)
Curr Opin Struct Biol
, vol.7
, pp. 266-272
-
-
Frank, J.1
-
45
-
-
0004290179
-
A 9 Ångstrom resolution X-ray crystallographic map of the large ribosomal subunit
-
45. Ban N, Freeborn B, Nissen P, Penczek P, Grassucci RA, Sweet R, Frank J, Moore PB, Steitz TA: A 9 Ångstrom resolution X-ray crystallographic map of the large ribosomal subunit. Cell 1998, 93:1105-1115. Using the electron microscope-derived structure of the 50S ribosomal subunit, the authors solved the crystallographic molecular replacement problem and used the resulting low resolution phases to locate heavy-atom derivatives for subsequent multiple isomorphous replacement phasing. The resulting 9 Å electron density map was radically improved, showing density possibly corresponding to ribosomal RNA and demonstrates that a higher resolution (i.e. 3 Å) structure should be attainable using this novel approach to phasing an immense, asymmetric macromolecular complex. This paper presents a crucial methodological breakthrough that will doubtless be required for solving the various ribosome crystal structures, eventually leading to a high resolution understanding of the mechanism of peptidyl transfer.
-
(1998)
Cell
, vol.93
, pp. 1105-1115
-
-
Ban, N.1
Freeborn, B.2
Nissen, P.3
Penczek, P.4
Grassucci, R.A.5
Sweet, R.6
Frank, J.7
Moore, P.B.8
Steitz, T.A.9
-
46
-
-
0025678737
-
Modelling of the three-dimensional architecture of group 1 catalytic introns based on comparative sequence analysis
-
46. Michel F, Westhof E: Modelling of the three-dimensional architecture of group 1 catalytic introns based on comparative sequence analysis. J Mol Biol 1990, 216:585-610.
-
(1990)
J Mol Biol
, vol.216
, pp. 585-610
-
-
Michel, F.1
Westhof, E.2
|