A domain of the Klenow fragment of Escherichia coli DNA polymerase I has polymerase but no exonuclease activity.
about
Structural basis for the 3'-5' exonuclease activity of Escherichia coli DNA polymerase I: a two metal ion mechanismFrameshift errors initiated by nucleotide misincorporation.Cocrystal structure of an editing complex of Klenow fragment with DNAT5 DNA polymerase: structural--functional relationships to other DNA polymerases.Dissection of functional domains of adenovirus DNA polymerase by linker-insertion mutagenesis.The thermodynamics of template-directed DNA synthesis: base insertion and extension enthalpies.Re-engineering the polymerase domain of Klenow fragment and evaluation of overproduction and purification strategiesThe 3'-5' exonuclease of DNA polymerase I of Escherichia coli: contribution of each amino acid at the active site to the reaction.Conformational changes induced in herpes simplex virus DNA polymerase upon DNA binding.Streptococcus pneumoniae DNA polymerase I lacks 3'-to-5' exonuclease activity: localization of the 5'-to-3' exonucleolytic domain.Genetic characterization of the vaccinia virus DNA polymerase: cytosine arabinoside resistance requires a variable lesion conferring phosphonoacetate resistance in conjunction with an invariant mutation localized to the 3'-5' exonuclease domain.Structure-function studies of the herpes simplex virus type 1 DNA polymerase.Site-specific mutagenesis of a highly conserved region of the herpes simplex virus type 1 DNA polymerase gene.Synthetic lethality with the dut defect in Escherichia coli reveals layers of DNA damage of increasing complexity due to uracil incorporation.Structural aspects of protein-DNA recognition.Continuous microspectrophotometric measurement of DNA polymerase activity: application to the Klenow fragment of Escherichia coli DNA polymerase I and human immunodeficiency virus type 1 reverse transcriptase.Structural studies of protein-nucleic acid interaction: the sources of sequence-specific binding.Deoxynucleoside triphosphate and pyrophosphate binding sites in the catalytically competent ternary complex for the polymerase reaction catalyzed by DNA polymerase I (Klenow fragment).Subgenes expressing single lipoyl domains of the pyruvate dehydrogenase complex of Escherichia coli.Replisome Dynamics during Chromosome Duplication.Polymerization activity of an alpha-like DNA polymerase requires a conserved 3'-5' exonuclease active site.Multi-stage proofreading in DNA replication.Herpes simplex virus type 1 DNA polymerase. Mutational analysis of the 3'-5'-exonuclease domain.Automated structural comparisons clarify the phylogeny of the right-hand-shaped polymerases.Structural and functional organization of the DNA polymerase of bacteriophage T7.
P2860
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P2860
A domain of the Klenow fragment of Escherichia coli DNA polymerase I has polymerase but no exonuclease activity.
description
1986 nî lūn-bûn
@nan
1986年の論文
@ja
1986年論文
@yue
1986年論文
@zh-hant
1986年論文
@zh-hk
1986年論文
@zh-mo
1986年論文
@zh-tw
1986年论文
@wuu
1986年论文
@zh
1986年论文
@zh-cn
name
A domain of the Klenow fragmen ...... e but no exonuclease activity.
@en
type
label
A domain of the Klenow fragmen ...... e but no exonuclease activity.
@en
prefLabel
A domain of the Klenow fragmen ...... e but no exonuclease activity.
@en
P2093
P356
P1433
P1476
A domain of the Klenow fragmen ...... se but no exonuclease activity
@en
P2093
P356
10.1002/PROT.340010111
P407
P577
1986-09-01T00:00:00Z