ライフサイエンスコーパス: RNase T1

1 ied ONs from native total tRNA digested with RNase T1.

2 rimental D49A and D49H mutant stabilities of RNase T1.

3 and treated them with single-strand specific RNase T1.

4 shift perturbations are observed compared to RNase T1.

5 l amide bonds in peptides and in the protein RNase T1.

6 as not susceptible to cleavage by RNase A or RNase T1.

7 f dequenching were observed with RNase A and RNase T1.

8 ickel reagent rather than in the presence of RNase T1.

9 isooctane is used to solubilize the protein RNase T1.

10 spectroscopy and enzymatic footprinting with RNase T1.

11 higher sequence coverage was achieved by the RNase T1 (71%), which is the same as the off-line mode.

12 Under these experimental conditions, the RNase T1, A and U2 signature digestion products that pot

13 achieved using unique fragments generated by RNase T1, A, and U2 parallel digestions.

14 onunique digestion products generated by the RNase T1 and A, respectively.

15 ro synthesized transcripts are digested with RNase T1 and hybridized to two DNA oligonucleotides.

16 al changes in variant tRNA susceptibility to RNase T1 and RNase A did not coincide with processing di

17 embers of the microbial ribonuclease family, RNase T1 and RNase Ba (barnase), and with a member of th

18 s measured as a function of pH for wild-type RNase T1 and the D76N mutant and showed that the pH depe

19 RNA structure probing by RNase T1 and the RT pause profile during synthesis indic

20 cates little difference between fully folded RNase T1 and the variants in terms of its lifetime, acce

21 Hydrogen-exchange rates were measured for RNase T1 and three variants with Ala --> Gly substitutio

22 Studies involving a series of nuclease (RNase T1) and protease (trypsin) digestions along with r

23 asparagine at position 39 in RNase Sa, 44 in RNase T1, and 58 in RNase Ba (barnase).

24 stive surface mutagenesis of the cold shock, RNase T1, and CheY proteins.

25 on with exonuclease III, lambda exonuclease, RNAse T1, and treatment with KMnO(4).

26 X-ray crystal structures of the variant and RNase T1 are nearly superimposable.

27 Ala --> Gly mutations in the helix of RNase T1 at both helical positions alter the native-stat

28 butes more than half of the net stability of RNase T1 at pH 7.

29 Data on the quenching of fluorescence of RNase T1 by DNP-poly(A) indicate the existence of more t

30 tified which are protected from digestion by RNase T1 by extracts enriched for the 81-, 47-, and 38-k

31 age, in comparison with the benchmark enzyme RNase T1, by producing a larger population of uniquely m

32 RNase T1, colicin E5, and mazF were applied in parallel

33 rnal positions (m/z 207 --> 164), and in the RNase T1-derived product Psi pGp (m/z 668 --> 207) arisi

34 imethylcytidine, is detected in 25 pmol of a RNase T1 digest and localized to the fragment 1402-CCCGp

35 We apply ON-MS to determine the ONs from an RNase T1 digest of in vitro transcribed tRNA, which are

36 Using pre- and post-RNase T1-digested substrate RNAs, it was determined that

37 When using RNase T1 digestion alone, a maximal sequence coverage of

38 e mapping methods, which utilize in-solution RNase T1 digestion followed by LC-MS/MS analysis, face c

39 Simulating the RNase T1 digestion of test analytes spanning up to 1869

40 h (FT)-based strategy to achieve the limited RNase T1 digestion of therapeutic mRNAs, leading to impr

41 Here, MALDI analysis of RNase T1 digestion products before and after modificatio

42 Nondenaturing PAGE and RNase T1 digestion showed that base pairs form less homo

43 ofiles and sequence coverages obtained after RNase T1 digestion were discussed.

44 o 14 nt to be expected instead from putative RNase T1 digestion.

45 med by several methods including analysis of RNase T1 digests and nearest-neighbor analysis.

46 A) tail was first cleaved from mRNA with the RNase T1 enzyme.

47 ficant increase in the extent of cleavage by RNase T1 following the conserved G26 (the 3' nucleotide

48 r masses of all oligonucleotides produced by RNase T1 hydrolysis with a mean error of 0.1 Da.

49 Partial RNase digestions using RNase T1 immobilized on magnetic particles were performe

50 One RNA sample is digested with RNase T1 in 18O-labeled ("heavy") water with the 18O bei

51 A second RNA sample is digested with RNase T1 in normal ("light") water.

52 cipitation (DRIP) are RNase H1 sensitive and RNase T1 insensitive.

53 chain carboxyl of Asp 76 in ribonuclease T1 (RNase T1) is buried, charged, non-ion-paired, and forms

54 en implicated in decelerating the folding of RNase T1; it is this tertiary restraint which appears to

55 nked MTF was hydrolyzed with nuclease P1 and RNase T1, leaving behind an oxidized fragment of [32P]AM

56 RNase T1 mapping and oligodeoxynucleotide competition st

57 RNase T1 mapping demonstrates binding of proteins to a 2

58 RNase T1 mapping revealed that the RNA sequences interac

59 nked products by native and denaturing PAGE, RNase T1 mapping, Pb(II) cleavage, UV cross-linking and

60 of full or partial rRNA sequences, including RNase T1 oligonucleotide catalogs reported in earlier li

61 In contrast, Trp59 in RNase T1, on which Y55W is based, has a 10-fold greater

62 Using gel mobility shift RNase T1 protection assays and secondary structure model

63 e prepared from these two tumors and used in RNase T1 protection assays that employed [32P]human GLUT

64 mutant and wild-type UV melting profiles and RNase T1 protection gel shifts further indicate that the

65 panied by an extended region of RNase V1 and RNase T1 protection in the telomerase RNA subunit that i

66 sed site 21 as seen by other methods for the RNase T1 protein and peptide helix, while it is destabil

67 These RNase T1 quantitative signature digestion products were

68 print experiments, using mammalian cells and RNase T1, revealed the binding of iron-responsive elemen

69 erent nucleotide-bound states of the enzyme, RNase T1, RNase T2, kethoxal and DMS footprinting of Dbp

70 probing of the monomeric RNA structure using RNAse T1, RNAse V1, RNAse U2, lead acetate, and dimethyl

71 Kinetic measurements with RNase B and RNase T1 showed DNP-poly(A) to be a reversible competiti

72 , and the linearity and sequence identify of RNase T1 signature digestion products were experimentall

73 bilizes structure in the denatured states of RNase T1 that is not present in D76N, D76S, and D76A.

74 0.66 microM for RNase B and 0.48 microM for RNase T1; the corresponding binding capacities were foun

75 dimethyl sulfate and minimal reactivity with RNase T1, this residue was the major target of both meta

76 Refolding of denatured RNase T1 to its native conformation also was catalyzed b

77 ing was, however, significantly sensitive to RNase T1, which specifically degrades RNA.