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Hollis, Thomas

One or more keywords matched the following items that are connected to Hollis, Thomas

Item Type	Name
Academic Article	The human TREX2 3' -> 5'-exonuclease structure suggests a mechanism for efficient nonprocessive DNA catalysis.
Academic Article	A mutation in TREX1 that impairs susceptibility to granzyme A-mediated cell death underlies familial chilblain lupus.
Academic Article	Mutations in the gene encoding the 3'-5' DNA exonuclease TREX1 are associated with systemic lupus erythematosus.
Academic Article	The TREX1 exonuclease R114H mutation in Aicardi-Goutières syndrome and lupus reveals dimeric structure requirements for DNA degradation activity.
Academic Article	Sequence variants in the 3'-->5' deoxyribonuclease TREX2: identification in a genetic screen and effects on catalysis by the recombinant proteins.
Academic Article	The crystal structure of TREX1 explains the 3' nucleotide specificity and reveals a polyproline II helix for protein partnering.
Academic Article	Heterozygous mutations in TREX1 cause familial chilblain lupus and dominant Aicardi-Goutieres syndrome.
Academic Article	Cooperative DNA binding and communication across the dimer interface in the TREX2 3' --> 5'-exonuclease.
Academic Article	The TREX1 double-stranded DNA degradation activity is defective in dominant mutations associated with autoimmune disease.
Academic Article	DNA binding induces active site conformational change in the human TREX2 3'-exonuclease.
Academic Article	Dominant mutation of the TREX1 exonuclease gene in lupus and Aicardi-Goutieres syndrome.
Academic Article	Defects in DNA degradation revealed in crystal structures of TREX1 exonuclease mutations linked to autoimmune disease.
Concept	Phosphoproteins
Academic Article	The TREX1 C-terminal region controls cellular localization through ubiquitination.
Academic Article	The Arg-62 residues of the TREX1 exonuclease act across the dimer interface contributing to catalysis in the opposing protomers.
Academic Article	Exonuclease TREX1 degrades double-stranded DNA to prevent spontaneous lupus-like inflammatory disease.

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Phosphoproteins