PolDIP2 interacts with human PrimPol and enhances its DNA polymerase activities
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Title
PolDIP2 interacts with human PrimPol and enhances its DNA polymerase activities
Authors
Keywords
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Journal
NUCLEIC ACIDS RESEARCH
Volume 44, Issue 7, Pages 3317-3329
Publisher
Oxford University Press (OUP)
Online
2016-03-17
DOI
10.1093/nar/gkw175
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- Primase-polymerases are a functionally diverse superfamily of replication and repair enzymes
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- Archaeal replicative primases can perform translesion DNA synthesis
- (2015) Stanislaw K. Jozwiakowski et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Molecular dissection of the domain architecture and catalytic activities of human PrimPol
- (2014) Benjamin A. Keen et al. NUCLEIC ACIDS RESEARCH
- Human PrimPol is a highly error-prone polymerase regulated by single-stranded DNA binding proteins
- (2014) Thomas A. Guilliam et al. NUCLEIC ACIDS RESEARCH
- PDIP38 is translocated to the spliceosomes/nuclear speckles in response to UV-induced DNA damage and is required for UV-induced alternative splicing of MDM2
- (2013) Agnes Wong et al. CELL CYCLE
- hPrimpol1/CCDC111 is a human DNA primase-polymerase required for the maintenance of genome integrity
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- PrimPol Bypasses UV Photoproducts during Eukaryotic Chromosomal DNA Replication
- (2013) Julie Bianchi et al. MOLECULAR CELL
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- PrimPol, an Archaic Primase/Polymerase Operating in Human Cells
- (2013) Sara García-Gómez et al. MOLECULAR CELL
- DNA polymerase -interacting protein 2 is a processivity factor for DNA polymerase during 8-oxo-7,8-dihydroguanine bypass
- (2013) G. Maga et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Y-family DNA polymerases and their role in tolerance of cellular DNA damage
- (2012) Julian E. Sale et al. NATURE REVIEWS MOLECULAR CELL BIOLOGY
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- StavroX—A Software for Analyzing Crosslinked Products in Protein Interaction Studies
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- Crosstalk between replicative and translesional DNA polymerases: PDIP38 interacts directly with Polη
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- The beginning of a beautiful friendship: Cross-linking/mass spectrometry and modelling of proteins and multi-protein complexes
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