F
Fred W. Perrino
Researcher at Wake Forest University
Publications - 77
Citations - 4895
Fred W. Perrino is an academic researcher from Wake Forest University. The author has contributed to research in topics: DNA polymerase & Exonuclease. The author has an hindex of 33, co-authored 72 publications receiving 4385 citations. Previous affiliations of Fred W. Perrino include University of Maryland, Baltimore County & Research Triangle Park.
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Mutations in the gene encoding the 3'-5' DNA exonuclease TREX1 are associated with systemic lupus erythematosus.
Min Ae Lee-Kirsch,Maolian Gong,Dipanjan Chowdhury,Lydia Senenko,Kerstin Engel,Young-Ae Lee,Young-Ae Lee,Udesh de Silva,Suzanna L. Bailey,Torsten Witte,Timothy J. Vyse,Juha Kere,Christiane Pfeiffer,Scott Harvey,Andrew Wong,Sari Koskenmies,Oliver Hummel,Klaus Rohde,Reinhold E. Schmidt,Anna F. Dominiczak,M. Gahr,Thomas Hollis,Fred W. Perrino,Judy Lieberman,Norbert Hubner +24 more
TL;DR: This work reports monoallelic frameshift or missense mutations and one 3′ UTR variant of TREX1 present in 9/417 individuals with systemic lupus erythematosus but absent in 1,712 controls, and demonstrates that two mutant TREx1 alleles alter subcellular targeting.
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Heterozygous Mutations in TREX1 Cause Familial Chilblain Lupus and Dominant Aicardi-Goutières Syndrome
Gillian I. Rice,William G. Newman,John Dean,Teresa Patrick,Rekha Parmar,Kim Flintoff,Peter Robins,Scott Harvey,Thomas Hollis,Ann O'Hara,Ariane L. Herrick,Andrew Bowden,Fred W. Perrino,Tomas Lindahl,Deborah E. Barnes,Yanick J. Crow,Yanick J. Crow +16 more
TL;DR: A de novo heterozygous mutation, affecting a critical catalytic residue in TREX1, that results in typical Aicardi-Goutieres syndrome is described.
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Aicardi-Goutières Syndrome Gene and HIV-1 Restriction Factor SAMHD1 Is a dGTP-regulated Deoxynucleotide Triphosphohydrolase
TL;DR: The physiological function of the SAMHD1 protein was determined, the gene was cloned, recombinant protein was produced, and the catalytic activity of the purified enzyme was identified, and it was shown that SAM HD1 contains a dGTP-regulated deoxynucleotide triphosphohydrolase.
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The exonuclease TREX1 is in the SET complex and acts in concert with NM23-H1 to degrade DNA during granzyme A-mediated cell death.
Dipanjan Chowdhury,Paul J. Beresford,Pengcheng Zhu,Dong Zhang,Jung-Suk Sung,Bruce Demple,Fred W. Perrino,Judy Lieberman +7 more
TL;DR: This work has found the 3'-to-5' exonuclease TREX1, but not its close homolog TREX2, in the SET complex, which resides in an endoplasmic reticulum-associated complex that translocates to the nucleus in response to superoxide generation by granzyme A.
Journal ArticleDOI
Identification and Expression of the TREX1 and TREX2 cDNA Sequences Encoding Mammalian 3′→5′ Exonucleases
Dan J. Mazur,Fred W. Perrino +1 more
TL;DR: Identification of the TREX1 and TREX2 cDNA sequences provides the genetic tools to investigate the physiological roles of these exonucleases in mammalian DNA replication, repair, and recombination pathways.