ライフサイエンスコーパス: ribonuclease H

1 ribonucleic acid (RNA) backbone catalyzed by ribonuclease H.

2 , plastocyanin, staphylococcal nuclease, and ribonuclease H.

3 ne the folding landscape of Escherichia coli ribonuclease H, a protein well characterized by hydrogen

4 Although ribonuclease H activity has long been implicated as a mo

5 ted DNA polymerase activities coupled with a ribonuclease H activity to synthesize a double-stranded

6 DNA 3'-end-directed and RNA 5'-end-directed ribonuclease H activity.

7 to study the stabilities of Escherichia coli ribonuclease H and its variants, both in purified form a

8 cleavage of the RBG mRNA in the presence of ribonuclease H and ODNs of varying association kinetics

9 election by reverse transcriptase-associated ribonuclease H and subsequent removal from nascent (+)-D

10 members of the 5'-3' exonuclease family: T4 ribonuclease H and the N-terminal domain of Thermus aqua

11 ation data collected on the proteins E. coli ribonuclease H and the trimeric E. coli membrane associa

12 nto 4 domains (terminal protein, spacer, rt, ribonuclease H) and each of these can be numbered separa

13 RNA/DNA hybrid could aid in positioning the ribonuclease H catalytic center at the PPT/U3 junction a

14 oligonucleotides and deoxyribonuclease I and ribonuclease H cleavages.

15 all reduction in activity of T. thermophilus ribonuclease H compared to its mesophilic E. coli homolo

16 o F61Y included 3'-PPT insertions suggesting ribonuclease H defect.

17 folding, dimerization and subunit-selective ribonuclease H domain (RH) proteolysis.

18 lambda-Cro repressor, interleukin 8, and the ribonuclease H domain of HIV-1 reverse transcriptase.

19 Mutations within a cryptic ribonuclease H domain within Argonaute2, as identified b

20 wn how often mutations in the connection and ribonuclease H domains of reverse transcriptase (RT) eme

21 lds, such as Rossmann fold, ferredoxin fold, ribonuclease H fold, and TIM beta/alpha-barrel.

22 TEFM contains two HhH motifs and a Ribonuclease H fold, similar to the nuclear transcriptio

23 ino acid change can convert Escherichia coli ribonuclease H from a three-state folder that populates

24 y essential aspartate to Mg(2+) or Ca(2+) in ribonuclease H from two organisms were computed using um

25 Ribonucleases H from organisms that grow at different te

26 Ribonucleases H from the thermophilic bacterium Thermus

27 because it is specifically recognized by the ribonuclease H function of HIV reverse transcriptase.

28 Ribonucleases H have mostly been implicated in eliminati

29 Our findings demonstrate a role for ribonuclease H in human neurological disease and suggest

30 Mutation analyses and analogies to ribonuclease H indicate that insertion of this glutamate

31 ich act upon DNA.RNA hybrid substrates (e.g. ribonuclease H) is impacted when the hybrids contain pho

32 the native cofactor in many enzymes such as ribonuclease H, its competitor Ca(2+) may also bind to t

33 Ribonuclease H-like (RNHL) superfamily, also called the

34 motif for heterochromatic silencing and for ribonuclease H-like cleavage (slicing) of target message

35 ant, form stable ON/RNA duplexes and support ribonuclease H mediated heteroduplex cleavage, all with

36 ence of the free energy of unfolding for two ribonucleases H, one from the mesophile Escherichia coli

37 ificantly larger than derived previously for ribonuclease H or recently, using "meta-analysis" for ub

38 Since the ribonuclease H (RH) domain contains an occult cleavage s

39 rse transcriptase (RT) contains a C-terminal ribonuclease H (RH) domain on its p66 subunit that can b

40 ed to allow interaction with residues in the ribonuclease H (RNase H) active site and thumb subdomain

41 e nucleic acid duplex in the vicinity of the ribonuclease H (RNase H) active site.

42 structural elements, the DNA polymerase and ribonuclease H (RNase H) activities of enzymes bearing a

43 (BBNH) inhibits both the DNA polymerase and ribonuclease H (RNase H) activities of the human immunod

44 everse transcriptase (RT) DNA polymerase and ribonuclease H (RNase H) activities reside in spatially

45 tase (RT) coordinates DNA polymerization and ribonuclease H (RNase H) activities using two discrete a

46 he site of T --> F substitution and enhanced ribonuclease H (RNase H) activity approximately 12-13 bp

47 suitable for screening compounds against the ribonuclease H (RNase H) activity of HIV-1 reverse trans

48 of mesoxalic acid, was found to inhibit the ribonuclease H (RNase H) activity of HIV-1 RT under stra

49 7447, was proposed to allosterically inhibit ribonuclease H (RNase H) activity of human immunodeficie

50 e) as potent and selective inhibitors of the ribonuclease H (RNase H) activity of human immunodeficie

51 RNA degradation via the ribonuclease H (RNase H) activity of human immunodeficie

52 account the possible effects of NNRTI on the ribonuclease H (RNase H) activity of RT, despite recent

53 se (IN) and reverse transcriptase-associated ribonuclease H (RNase H) are both selective targets for

54 li maltose binding protein (MBP) and E. coli ribonuclease H (RNase H) as our model proteins, we monit

55 Ribonuclease H (RNase H) belongs to the nucleotidyl-tran

56 Ribonuclease H (RNase H) belongs to the nucleotidyl-tran

57 and approximately 4-9 bp downstream from the ribonuclease H (RNase H) catalytic center.

58 The PPT is resistant to ribonuclease H (RNase H) cleavage and is used as a prime

59 Ribonuclease H (RNase H) cleavages and nucleocapsid prot

60 zing RTs prevents polymerization-independent ribonuclease H (RNase H) cleavages of the donor template

61 DNTP) occupies the interface between the p66 ribonuclease H (RNase H) domain and p51 thumb of human i

62 (AZT) selected for the Q509L mutation in the ribonuclease H (RNase H) domain of HIV-1 reverse transcr

63 s in the connection subdomain and C-terminal ribonuclease H (RNase H) domain of human immunodeficienc

64 he highly conserved Asp549 of the retroviral ribonuclease H (RNase H) domain were evaluated in the he

65 inant p66 polypeptides containing a modified ribonuclease H (RNase H) domain were purified and evalua

66 associated with both the DNA polymerase and ribonuclease H (RNase H) domains.

67 The ribonuclease H (RNase H) family of enzymes selectively d

68 ng trajectories of ancestral proteins of the ribonuclease H (RNase H) family using ancestral sequence

69 idated reverse transcriptase (RT) associated ribonuclease H (RNase H) for human immunodeficiency viru

70 The well-characterized protein ribonuclease H (RNase H) from Escherichia coli populates

71 at a site at which the reverse transcriptase ribonuclease H (RNase H) has created a nick or short gap

72 s duplex include the thumb subdomain and the ribonuclease H (RNase H) primer grip, the latter compris

73 (HIV) reverse transcriptase (RT) associated ribonuclease H (RNase H) remains an unvalidated antivira

74 (HIV) reverse transcriptase (RT)-associated ribonuclease H (RNase H) remains the only virally encode

75 Reverse transcriptase (RT) associated ribonuclease H (RNase H) remains the only virally encode

76 Ribonuclease H (RNase H) selectively degrades the RNA st

77 The kinetics of the ribonuclease H (RNase H) surface hydrolysis of RNA-DNA h

78 -H(epsilon) bond vectors of Escherichia coli ribonuclease H (RNase H) were determined by NMR spin rel

79 ric oligodeoxynucleotide (ODN) libraries and ribonuclease H (RNase H) were used to identify regions o

80 structure of a hybrid duplex in complex with ribonuclease H (RNase H), suggested that this flexibilit

81 associated DNA polymerase, and RT-associated ribonuclease H (RNase H).

82 NA microarrays with either ribonuclease S or ribonuclease H (RNase H).

83 INSTIs) that also displayed activity against ribonuclease H (RNase H).

84 Ribonucleases H (RNases H) are endonucleases which cleav

85 Ribonucleases H (RNases H) comprise a family of metal-de

86 Previous studies of bacterial ribonucleases H (RNases H) from the thermophile Thermus

87 Although ribonucleases H (RNases H) have long been implicated in

88 mains and the acquisition of an Archaea-like ribonuclease H (RNH) domain.

89 The reverse transcriptase-associated ribonuclease H (RT/RNase H) domains from the gypsy group

90 Loss-of-function mutations in ribonuclease H, senataxin, and topoisomerase I that reso

91 ed by five alpha-helices that belongs to the ribonuclease H superfamily.

92 synthesis causes an increase in the ratio of ribonuclease H to polymerase activity thereby promoting

93 t constitutively express an Escherichia coli ribonuclease H transgene show a marked reduction in RNA/

94 These RNA.DNA hybrids are eliminated by ribonuclease H treatment.

95 the folding process of Thermus thermophilus ribonuclease H using circular dichroism, fluorescence, a

96 The kinetic folding of ribonuclease H was studied by hydrogen exchange (HX) pul

97 ing intermediate of the Thermus thermophilus ribonuclease H, which forms before the rate-limiting tra

98 s of 6 randomly chosen internal positions in ribonuclease H with Lys and Glu suggest that the ability

99 n (named for the protein piwi) is similar to ribonuclease H, with a conserved active site aspartate-a