The Crystal Structure of an Unusual Processivity Factor, Herpes Simplex Virus UL42, Bound to the C Terminus of Its Cognate Polymerase

This publication has 62 references indexed in Scilit:

• Secondary Structure and Structure-Activity Relationships of Peptides Corresponding to the Subunit Interface of Herpes Simplex Virus DNA Polymerase
  Journal of Biological Chemistry, 2000
• The Accessory Subunit of Xenopus laevis Mitochondrial DNA Polymerase γ Increases Processivity of the Catalytic Subunit of Human DNA Polymerase γ and Is Related to Class II Aminoacyl-tRNA Synthetases
  Molecular and Cellular Biology, 1999
• Conserved domains in DNA repair proteins and evolution of repair systems
  Nucleic Acids Research, 1999
• Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
  Acta Crystallographica Section D-Biological Crystallography, 1998
• Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
  Nucleic Acids Research, 1997
• [27] Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
  Published by Elsevier ,1997
• Methods used in the structure determination of bovine mitochondrial F1 ATPase
  Acta Crystallographica Section D-Biological Crystallography, 1996
• Specific inhibition of herpes simplex virus DNA polymerase by helical peptides corresponding to the subunit interface.
  Proceedings of the National Academy of Sciences, 1995
• The CCP4 suite: programs for protein crystallography
  Acta Crystallographica Section D-Biological Crystallography, 1994
• Herpes simplex-1 DNA polymerase
  Journal of Biological Chemistry, 1989