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1 dimethylsulphate, potassium permanganate and S1 nuclease.
2 at 37 degree C, although it is hydrolyzed by S1 nuclease.
3 digesting the resulting RNA-DNA hybrids with S1 nuclease.
4 een mapped within the OAX HindIII unit using S1 nuclease.
5 ammalian serum and to endonucleases, such as S1 nuclease.
6 if the molecules are previously treated with S1 nuclease.
16 Differences in the mRNAs were confirmed by S1 nuclease analysis of placental RNA with a cDNA probe
18 for cvaA identified by primer extension and S1 nuclease analysis, P1, lies 320 bp upstream of the tr
25 ay DNA supercoiling-dependent sensitivity to S1 nuclease and OsO4, which is consistent with a non-B-D
26 ve c-myc genes yielded different patterns of S1 nuclease and permanganate sensitivity, indicating alt
27 talurid herpesvirus 1) genome were mapped by S1 nuclease and primer extension analyses as well as by
28 mparison of the prtF and rofA transcripts by S1 nuclease and primer extension assays indicated that t
29 orter plasmids using confocal Raman spectra, S1 nuclease and restriction enzymes demonstrated that th
32 rse transcriptase polymerase chain reaction, S1 nuclease, and functional cell surface binding studies
33 in all major brain regions as determined by S1 nuclease assay and in a variety of specific neuroanat
36 l restriction fragment (TRF) length, and the S1 nuclease assay was used to determine the frequency of
38 airpin helices, is indicated by preferential S1 nuclease cleavage at the center of the oligomer(s), i
39 findings were consistent with the results of S1 nuclease cleavage observed at B-Z junctions flanking
41 22 monoclonal antibody (ZIBS assay); (ii) an S1 nuclease cleavage-primer extension assay to map B-Z j
42 t binds cruciform-specific 2D3 antibody, and S1 nuclease-cleavage and OsO4-modification assays have i
47 r nondenaturing conditions, was sensitive to S1 nuclease digestion, and hybridized to only one of two
50 rt a novel whole-genome method, S1-DRIP-seq (S1 nuclease DNA:RNA immunoprecipitation with deep sequen
51 ally amplifying conjugated polymer (CP), and S1 nuclease enzyme is capable of detecting SNPs in a sim
56 uch transcriptional control elements, the 5'-S1 nuclease-hypersensitive silencer (5'SHS; -1418 to -13
57 ich strand of a PDGF-A silencer sequence (5'-S1 nuclease-hypersensitive site (SHS)) yielded three cDN
61 ption initiation site was determined by both S1 nuclease mapping and 5' rapid amplification of cDNA e
63 site of the primary transcript was mapped by S1 nuclease mapping and the major promoter was defined b
66 ded by a TATA box in the usual position, and S1 nuclease mapping at each exon 1 revealed multiple tra
68 in these cells were analyzed by quantitative S1 nuclease mapping for nuclear accumulation, intron exc
75 transcription is feedback regulated, whereas S1 nuclease mapping suggests that emp2 mutant transcript
76 er, our data from primer extension analysis, S1 nuclease mapping, beta-galactosidase assays, and in v
79 merase chain reaction, primer extension, and S1 nuclease mapping, were located approximately 650 base
84 sive to cleavage with single-strand-specific S1 nuclease or the single-strand-selective agent potassi
86 rvation was examined by primer extension and S1 nuclease protection analyses of genes encoding enzyme
87 ATG initiation codon by primer extension and S1 nuclease protection analyses of RNA from human skin a
94 d corneal endothelial cells were analyzed by S1 nuclease protection analysis, whereas the nucleotide
98 ble during in vitro growth, as determined by S1 nuclease protection and primer extension analyses of
99 aI transcript start site, which we mapped by S1 nuclease protection and primer extension analyses.
102 stigated in M. smegmatis and M. bovis BCG by S1 nuclease protection and transcriptional fusion analys
108 By 5'-rapid amplification of cDNA ends and S1 nuclease protection assay, we determined that the tra
111 RACE (rapid amplification of cDNA ends) and S1 nuclease protection assays and was at the site of an
113 apid amplification of cDNA ends coupled with S1 nuclease protection assays demonstrate that the M3 pr
114 transcripts by primer extension and modified S1 nuclease protection assays demonstrated that transcri
122 and metabolism of btuB RNA were analyzed by S1 nuclease protection assays, and mutations that alter
123 examined by a variety of methods, including S1 nuclease protection assays, Northern blotting, Wester
124 rse transcription-PCR analyses, coupled with S1 nuclease protection assays, provided evidence that ge
133 5-HT2C-R transcript, first identified using S1 nuclease protection of total RNA isolated from the ch
134 ed both rapid amplification of cDNA ends and S1 nuclease protection protocols and examined the organi
138 tely initiated rRNA transcripts, detected by S1 nuclease protection, were paralleled by increased lev
140 ese fragments are generated from much longer S1-nuclease sensitive fragments of foreign DNA that requ
141 eric junction sequence possesses an unusual, S1 nuclease-sensitive conformation (anisomorphic DNA), w
143 he DNA was examined under native conditions, S1 nuclease-sensitive ssDNA was identified in all strain
151 rophoretic mobility shift assays (EMSAs) and S1 nuclease treatment are used to demonstrate that the R
153 mal APAF and APAD was much more sensitive to S1 nuclease treatment than similar fractions from SLE pa
154 iumhexylbromide)fluorene)-co-phenylen e] and S1 nuclease, unambiguous FRET signaling is achieved for
155 equent footprinting studies with DNase I and S1 nucleases using a supercoiled plasmid DNA containing
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