Structural biology of replication initiation factor Mcm10.

No abstract is available for this paper.

• Publication year

  2012

• Venue

  Sub-cellular biochemistry

• Publication date

  Unknown publication date

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1007/978-94-007-4572-8_11PMID 22918587PMCID PMC5023279
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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• Uncoupling of sister replisomes during eukaryotic DNA replication.

  2010cited by this paper
• Solution NMR Structure of the C-terminal DNA Binding Domain of Mcm10 Reveals a Conserved MCM Motif*

  2010cited by this paper
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  2010cited by this paper
• Activation of the MCM2-7 helicase by association with Cdc45 and GINS proteins.

  2010cited by this paper
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  2010influential reference
• Mcm10 Mediates the Interaction Between DNA Replication and Silencing Machineries

  2009cited by this paper
• Alternative Mechanisms for Coordinating Polymerase α and MCM Helicase

  2009influential reference
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  2009influential reference
• A key role for Ctf4 in coupling the MCM2‐7 helicase to DNA polymerase α within the eukaryotic replisome

  2009cited by this paper
• MCM10 mediates RECQ4 association with MCM2‐7 helicase complex during DNA replication

  2009influential reference
• Novel DNA Binding Properties of the Mcm10 Protein from Saccharomyces cerevisiae*

  2009influential reference
• Concerted loading of Mcm2-7 double hexamers around DNA during DNA replication origin licensing.

  2009influential reference
• Physical Interactions between Mcm10, DNA, and DNA Polymerase α*

  2009cited by this paper
• Domain Architecture and Biochemical Characterization of Vertebrate Mcm10*

  2008cited by this paper
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  2008cited by this paper
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  2008cited by this paper
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  2007influential reference
• Hexameric ring structure of human MCM10 DNA replication factor

  2007influential reference
• Human Mcm10 regulates the catalytic subunit of DNA polymerase-alpha and prevents DNA damage during replication.

  2007cited by this paper
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  2007cited by this paper
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  2007cited by this paper
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  2006influential reference
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  2006cited by this paper
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  2006influential reference
• A Conserved Hsp10-like Domain in Mcm10 Is Required to Stabilize the Catalytic Subunit of DNA Polymerase-α in Budding Yeast*

  2006influential reference
• Fission Yeast Mcm10p Contains Primase Activity*

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• Double Hexamer Disruption and Biochemical Activities of Methanobacterium thermoautotrophicum MCM*

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  2005influential reference
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  2004influential reference
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  2004cited by this paper
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  2004influential reference
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  2003influential reference
• The structure and function of MCM from archaeal M. Thermoautotrophicum

  2003influential reference
• Hexameric ring structure of the full‐length archaeal MCM protein complex

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  2003influential reference
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  2002influential reference
• DNA replication in eukaryotic cells.

  2002influential reference
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  2002influential reference
• Structure of the RPA trimerization core and its role in the multistep DNA‐binding mechanism of RPA

  2002cited by this paper
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  2001influential reference
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  2001cited by this paper
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  2000influential reference
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  2000influential reference
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  2000influential reference
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  2000influential reference
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