| scholarly article | Q13442814 |
| P50 | author | Tamar F Barlam | Q56816274 |
| P2093 | author name string | C S Crumpacker | |
| D S Parris | |||
| S J Monahan | |||
| P2860 | cites work | Genetics of resistance to phosphonoacetic acid in strain KOS of herpes simplex virus type 1 | Q37506935 |
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| Mutations in the C terminus of herpes simplex virus type 1 DNA polymerase can affect binding and stimulation by its accessory protein UL42 without affecting basal polymerase activity. | Q40043667 | ||
| Functional analysis of the herpes simplex virus UL42 protein. | Q40044170 | ||
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| DNA-binding protein associated with herpes simplex virus DNA polymerase | Q40134865 | ||
| Physical mapping of paar mutations of herpes simplex virus type 1 and type 2 by intertypic marker rescue | Q40254451 | ||
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| Polymerization activity of an alpha-like DNA polymerase requires a conserved 3'-5' exonuclease active site | Q40640573 | ||
| Interactions between Herpes Simplex Virus DNA-binding Proteins | Q41529862 | ||
| A novel functional domain of an alpha-like DNA polymerase. The binding site on the herpes simplex virus polymerase for the viral UL42 protein | Q42083798 | ||
| Formation of DNA replication structures in herpes virus-infected cells requires a viral DNA binding protein | Q44786271 | ||
| The intranuclear location of a herpes simplex virus DNA-binding protein is determined by the status of viral DNA replication | Q45796861 | ||
| Interaction between the DNA polymerase and single-stranded DNA-binding protein (infected cell protein 8) of herpes simplex virus 1. | Q45835100 | ||
| Mapping of epitopes on the 65k DNA-binding protein of herpes simplex virus type 1. | Q45847077 | ||
| The herpes simplex virus 1 origin binding protein: a DNA helicase | Q45855769 | ||
| Functional interaction between the herpes simplex-1 DNA polymerase and UL42 protein. | Q45999696 | ||
| Herpes simplex-1 DNA polymerase. Identification of an intrinsic 5'----3' exonuclease with ribonuclease H activity | Q46344823 | ||
| Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins | Q27860987 | ||
| Empirical Predictions of Protein Conformation | Q28300310 | ||
| Transcription factors: structural families and principles of DNA recognition | Q29615317 | ||
| Herpes simplex virus DNA replication: the UL9 gene encodes an origin-binding protein | Q33634580 | ||
| Herpes simplex virus 1 helicase-primase: a complex of three herpes-encoded gene products | Q33846286 | ||
| Molecular genetics of herpes simplex virus. VII. Characterization of a temperature-sensitive mutant produced by in vitro mutagenesis and defective in DNA synthesis and accumulation of gamma polypeptides | Q35235288 | ||
| Prokaryotic DNA replication | Q35671078 | ||
| Enzymatic activities of overexpressed herpes simplex virus DNA polymerase purified from recombinant baculovirus-infected insect cells | Q35832194 | ||
| Inhibition of herpes simplex virus type 1 DNA polymerase activity by peptides from the UL42 accessory protein is largely nonspecific | Q36639336 | ||
| The UL5 gene of herpes simplex virus type 1: isolation of a lacZ insertion mutant and association of the UL5 gene product with other members of the helicase-primase complex | Q36656286 | ||
| The six conserved helicase motifs of the UL5 gene product, a component of the herpes simplex virus type 1 helicase-primase, are essential for its function | Q36656301 | ||
| Isolation of a herpes simplex virus type 1 mutant deleted for the essential UL42 gene and characterization of its null phenotype | Q36679955 | ||
| Correct intranuclear localization of herpes simplex virus DNA polymerase requires the viral ICP8 DNA-binding protein | Q36681369 | ||
| Purification and characterization of UL9, the herpes simplex virus type 1 origin-binding protein | Q36698650 | ||
| The UL8 subunit of the herpes simplex virus helicase-primase complex is required for efficient primer utilization | Q36700459 | ||
| Kinetics of expression of the gene encoding the 65-kilodalton DNA-binding protein of herpes simplex virus type 1. | Q36780061 | ||
| Localization of the herpes simplex virus type 1 65-kilodalton DNA-binding protein and DNA polymerase in the presence and absence of viral DNA synthesis | Q36795670 | ||
| The herpes simplex virus type 1 UL42 gene product: a subunit of DNA polymerase that functions to increase processivity | Q36796087 | ||
| Isolation and characterization of herpes simplex virus mutants containing engineered mutations at the DNA polymerase locus | Q36805852 | ||
| Translational regulation of herpes simplex virus DNA polymerase | Q36805877 | ||
| Identification of herpes simplex virus type 1 genes required for origin-dependent DNA synthesis | Q36826810 | ||
| The essential 65-kilodalton DNA-binding protein of herpes simplex virus stimulates the virus-encoded DNA polymerase | Q36831999 | ||
| Expression of herpes simplex virus type 1 DNA polymerase gene by in vitro translation and effects of gene deletions on activity | Q36872321 | ||
| Expression of herpes simplex virus type 1 DNA polymerase in Saccharomyces cerevisiae and detection of virus-specific enzyme activity in cell-free lysates | Q36873422 | ||
| A temperature-sensitive mutation in a herpes simplex virus type 1 gene required for viral DNA synthesis maps to coordinates 0.609 through 0.614 in UL | Q36875479 | ||
| Identification of the gene encoding the 65-kilodalton DNA-binding protein of herpes simplex virus type 1. | Q36875880 | ||
| Purification of the herpes simplex virus type 1 65-kilodalton DNA-binding protein: properties of the protein and evidence of its association with the virus-encoded DNA polymerase. | Q36878929 | ||
| The 65,000-Mr DNA-binding and virion trans-inducing proteins of herpes simplex virus type 1. | Q36915866 | ||
| Genetic analysis of temperature-sensitive mutants which define the gene for the major herpes simplex virus type 1 DNA-binding protein | Q36929419 | ||
| Association of DNA helicase and primase activities with a subassembly of the herpes simplex virus 1 helicase-primase composed of the UL5 and UL52 gene products | Q37395148 | ||
| A DNA binding protein specific for an origin of replication of herpes simplex virus type 1. | Q37396712 | ||
| P433 | issue | 10 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | Herpes simplex virus type 1 | Q655331 |
| P304 | page(s) | 5922-5931 | |
| P577 | publication date | 1993-10-01 | |
| P1433 | published in | Journal of Virology | Q1251128 |
| P1476 | title | Two regions of the herpes simplex virus type 1 UL42 protein are required for its functional interaction with the viral DNA polymerase | |
| P478 | volume | 67 |
| Q36435827 | A novel processive mechanism for DNA synthesis revealed by structure, modeling and mutagenesis of the accessory subunit of human mitochondrial DNA polymerase |
| Q35834562 | Bipartite DNA-binding region of the Epstein-Barr virus BMRF1 product essential for DNA polymerase accessory function |
| Q39597623 | Characterization of human herpesvirus 8 ORF59 protein (PF-8) and mapping of the processivity and viral DNA polymerase-interacting domains |
| Q35838622 | Cloning, sequencing, and functional characterization of the two subunits of the pseudorabies virus DNA polymerase holoenzyme: evidence for specificity of interaction |
| Q34348919 | Evidence against a simple tethering model for enhancement of herpes simplex virus DNA polymerase processivity by accessory protein UL42. |
| Q35856977 | Functional order of assembly of herpes simplex virus DNA replication proteins into prereplicative site structures. |
| Q36624461 | Interaction of herpes simplex virus type 1 DNA polymerase and the UL42 accessory protein with a model primer template |
| Q35850793 | Mutations that specifically impair the DNA binding activity of the herpes simplex virus protein UL42 |
| Q33964152 | Processing of lagging-strand intermediates in vitro by herpes simplex virus type 1 DNA polymerase |
| Q34621250 | Specific inhibition of herpes simplex virus DNA polymerase by helical peptides corresponding to the subunit interface |
| Q36423471 | The accessory subunit of mtDNA polymerase shares structural homology with aminoacyl-tRNA synthetases: implications for a dual role as a primer recognition factor and processivity clamp |
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