Clamp loader structure predicts the architecture of DNA polymerase III holoenzyme and RFC
- 1 November 2001
- journal article
- review article
- Published by Elsevier in Current Biology
- Vol. 11 (22) , R935-R946
- https://doi.org/10.1016/s0960-9822(01)00559-0
Abstract
No abstract availableKeywords
This publication has 64 references indexed in Scilit:
- Mechanism of β Clamp Opening by the δ Subunit ofEscherichia coli DNA Polymerase III HoloenzymeJournal of Biological Chemistry, 2001
- ATP-dependent structural change of the eukaryotic clamp-loader protein, replication factor CProceedings of the National Academy of Sciences, 2000
- The δ Subunit of DNA Polymerase III Holoenzyme Serves as a Sliding Clamp Unloader in Escherichia coliJournal of Biological Chemistry, 2000
- Mechanisms of DNA replicationCurrent Opinion in Chemical Biology, 2000
- A Unique Organization of the Protein Subunits of the DNA Polymerase Clamp Loader in the Archaeon Methanobacterium thermoautotrophicum ΔHPublished by Elsevier ,2000
- Crystal structure of the DNA polymerase processivity factor of T4 bacteriophage 1 1Edited by I. A. WilsonJournal of Molecular Biology, 2000
- Replication Factor C Interacts with the C-terminal Side of Proliferating Cell Nuclear AntigenPublished by Elsevier ,1997
- Structure of the C-Terminal Region of p21WAF1/CIP1 Complexed with Human PCNACell, 1996
- Clamp loading, unloading and intrinsic stability of the PCNA, β and gp45 sliding clamps of human, E. coli and T4 replicasesGenes to Cells, 1996
- Mechanism of elongation of primed DNA by DNA polymerase delta, proliferating cell nuclear antigen, and activator 1.Proceedings of the National Academy of Sciences, 1990