Lori Frappier focuses on Molecular biology, Cell biology, Replication protein A, DNA replication and Binding domain. Her study in Molecular biology is interdisciplinary in nature, drawing from both Mutation, Virus, Origin of replication and Epstein–Barr virus nuclear antigen 1. Her work carried out in the field of Virus brings together such families of science as Plasma protein binding and Antigen.
Her research integrates issues of Plasmid, IL-2 receptor, CD40, Immunology and DNA-binding domain in her study of Cell biology. Lori Frappier has included themes like HMG-box, Protein subunit, Origin recognition complex and DNA in her Replication protein A study. Her Binding domain study integrates concerns from other disciplines, such as Protein domain and Single-stranded binding protein.
Her main research concerns Molecular biology, Cell biology, DNA replication, Epstein–Barr virus and Virology. Her studies deal with areas such as Plasmid, Origin of replication, Replication protein A, Mitosis and Nuclear protein as well as Molecular biology. Her Cell biology research is multidisciplinary, incorporating perspectives in Gene expression, MCM complex, Chromatin, Cell cycle and Transcription.
Her DNA replication study combines topics from a wide range of disciplines, such as HMG-box and DNA-binding protein. Her Epstein–Barr virus research is multidisciplinary, incorporating perspectives in Gene silencing, Lytic cycle, DNA damage and Cancer research. Her Origin recognition complex research focuses on SeqA protein domain and how it relates to DNA-binding domain and Ter protein.
Lori Frappier focuses on Cell biology, Epstein–Barr virus, Lytic cycle, Virology and Molecular biology. Her Cell biology research includes elements of Gene expression, DNA damage, Viral replication, Ubiquitin ligase and Viral protein. Epstein–Barr virus is a subfield of Virus that she studies.
Her Lytic cycle study combines topics in areas such as Cell cycle, Cell Cycle Protein, DNA and F-box protein. Lori Frappier performs multidisciplinary study on Molecular biology and GTPase-activating protein in her works. Her work in Histone addresses subjects such as Chromatin, which are connected to disciplines such as DNA replication.
Lori Frappier spends much of her time researching Epstein–Barr virus, Lytic cycle, Molecular biology, Genome and Regulation of gene expression. Virus and Virology are inextricably linked to her Epstein–Barr virus research. The Virus study combines topics in areas such as RNA, APOBEC, Somatic hypermutation and DNA.
Her research integrates issues of Cell cycle, Cell Cycle Protein and Cell biology in her study of Lytic cycle. Borrowing concepts from GTPase-activating protein, Lori Frappier weaves in ideas under Molecular biology. Her work deals with themes such as Virus latency, Cancer research, microRNA, Messenger RNA and Gene silencing, which intersect with Regulation of gene expression.
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Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA
Alexey Bochkarev;Richard A. Pfuetzner;Aled M. Edwards;Lori Frappier.
Structure of the p53 binding domain of HAUSP/USP7 bound to Epstein-Barr nuclear antigen 1 implications for EBV-mediated immortalization.
Vivian Saridakis;Yi Sheng;Feroz Sarkari;Melissa N. Holowaty.
Molecular Cell (2005)
Human CD8+ T cell responses to EBV EBNA1: HLA class I presentation of the (Gly-Ala)-containing protein requires exogenous processing.
Neil Blake;Steven Lee;Irina Redchenko;Wendy Thomas.
Structural Basis for the Recognition of DNA Repair Proteins UNG2, XPA, and RAD52 by Replication Factor RPA
Georges Mer;Alexey Bochkarev;Alexey Bochkarev;Rajesh Gupta;Elena Bochkareva.
Molecular recognition of p53 and MDM2 by USP7/HAUSP
Yi Sheng;Vivian Saridakis;Feroz Sarkari;Shili Duan.
Nature Structural & Molecular Biology (2006)
Protein profiling with Epstein-Barr nuclear antigen-1 reveals an interaction with the herpesvirus-associated ubiquitin-specific protease HAUSP/USP7.
Melissa N. Holowaty;Mahel Zeghouf;Hong Wu;Judy Tellam.
Journal of Biological Chemistry (2003)
Crystal Structure of the DNA-Binding Domain of the Epstein–Barr Virus Origin-Binding Protein, EBNA1, Bound to DNA
Alexey Bochkarev;Jean A Barwell;Richard A Pfuetzner;Elena Bochkareva.
The crystal structure of the complex of replication protein A subunits RPA32 and RPA14 reveals a mechanism for single‐stranded DNA binding
Alexey Bochkarev;Alexey Bochkarev;Elena Bochkareva;Elena Bochkareva;Lori Frappier;Aled M. Edwards;Aled M. Edwards.
The EMBO Journal (1999)
EBP2, a Human Protein That Interacts with Sequences of the Epstein-Barr Virus Nuclear Antigen 1 Important for Plasmid Maintenance
Kathy Shire;Derek F. J. Ceccarelli;Tina M. Avolio-Hunter;Lori Frappier.
Journal of Virology (1999)
Crystal structure of the DNA-binding domain of the Epstein-Barr virus origin-binding protein EBNA1
Alexey Bochkarev;Jean A. Barwell;Richard A. Pfuetzner;William Furey.
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