The use of native T7 DNA polymerase for site-directed mutagenesis
about
Processing sites in the human immunodeficiency virus type 1 (HIV-1) Gag-Pro-Pol precursor are cleaved by the viral protease at different rates.Replacement of the P1 amino acid of human immunodeficiency virus type 1 Gag processing sites can inhibit or enhance the rate of cleavage by the viral proteaseBiological properties of single chemical-DNA adducts: a twenty year perspectiveProbing the CD lumenal loop region of the D2 protein of photosystem II in Synechocystis sp. strain PCC 6803 by combinatorial mutagenesis.Mammalian assay for site-specific DNA damage processing using the human H-ras proto-oncogene.Repair of heteroduplex DNA molecules with multibase loops in Escherichia coli.Use of the rep technique for allele replacement to construct mutants with deletions of the pstSCAB-phoU operon: evidence of a new role for the PhoU protein in the phosphate regulon.Membrane topography of ColE1 gene products: the hydrophobic anchor of the colicin E1 channel is a helical hairpin.Characterization of promoter elements required for cell-specific expression of the neurotensin/neuromedin N gene in a human endocrine cell line.Segments of the POU domain influence one another's DNA-binding specificityRepair of DNA heteroduplexes containing small heterologous sequences in Escherichia coliOligonucleotide-directed site-specific integration of high complexity libraries into ssDNA templatesLow-fidelity DNA synthesis by the L979F mutator derivative of Saccharomyces cerevisiae DNA polymerase zeta.Construction of a circular single-stranded DNA template containing a defined lesionThe vinyl chloride DNA derivative N2,3-ethenoguanine produces G----A transitions in Escherichia coli.Diverse effects of mutation on the activity of the Escherichia coli export chaperone SecB.The dimer interfaces of protease and extra-protease domains influence the activation of protease and the specificity of GagPol cleavage.Rapid site-directed mutagenesis by a method that selects for full length mutated DNA.The p2 domain of human immunodeficiency virus type 1 Gag regulates sequential proteolytic processing and is required to produce fully infectious virions.Initial cleavage of the human immunodeficiency virus type 1 GagPol precursor by its activated protease occurs by an intramolecular mechanism.Ordered processing of the human immunodeficiency virus type 1 GagPol precursor is influenced by the context of the embedded viral proteaseStructural and functional characterization of Streptomyces plicatus beta-N-acetylhexosaminidase by comparative molecular modeling and site-directed mutagenesis.
P2860
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P2860
The use of native T7 DNA polymerase for site-directed mutagenesis
description
1989 nî lūn-bûn
@nan
1989 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
name
The use of native T7 DNA polymerase for site-directed mutagenesis
@ast
The use of native T7 DNA polymerase for site-directed mutagenesis
@en
The use of native T7 DNA polymerase for site-directed mutagenesis
@nl
type
label
The use of native T7 DNA polymerase for site-directed mutagenesis
@ast
The use of native T7 DNA polymerase for site-directed mutagenesis
@en
The use of native T7 DNA polymerase for site-directed mutagenesis
@nl
prefLabel
The use of native T7 DNA polymerase for site-directed mutagenesis
@ast
The use of native T7 DNA polymerase for site-directed mutagenesis
@en
The use of native T7 DNA polymerase for site-directed mutagenesis
@nl
P356
P1476
The use of native T7 DNA polymerase for site-directed mutagenesis
@en
P2093
P2860
P356
10.1093/NAR/17.13.5408
P407
P577
1989-07-11T00:00:00Z