Zobrazeno 1 - 10
of 100
pro vyhledávání: '"Alan M Weiner"'
Publikováno v:
PLoS Genetics, Vol 8, Iss 9, p e1002972 (2012)
The CSB-PGBD3 fusion protein arose more than 43 million years ago when a 2.5-kb piggyBac 3 (PGBD3) transposon inserted into intron 5 of the Cockayne syndrome Group B (CSB) gene in the common ancestor of all higher primates. As a result, full-length C
Externí odkaz:
https://doaj.org/article/c945c18cde3f4cd48feae247565eb367
Publikováno v:
PLoS Genetics, Vol 4, Iss 3, p e1000031 (2008)
Cockayne syndrome (CS) is a devastating progeria most often caused by mutations in the CSB gene encoding a SWI/SNF family chromatin remodeling protein. Although all CSB mutations that cause CS are recessive, the complete absence of CSB protein does n
Externí odkaz:
https://doaj.org/article/35a6c90c3e694185b36ddc02b7bcf841
Publikováno v:
BioTechniques, Vol 23, Iss 6, Pp 1036-1038 (1997)
Externí odkaz:
https://doaj.org/article/584cae443e7b440b8e73b5cb7bc24d50
Autor:
Thomas Pavelitz, Alan M. Weiner, Kiyoji Tanaka, Lucas T. Gray, John C. Newman, Katsuyoshi Horibata, Arnold D. Bailey
Publikováno v:
DNA Repair. 11:488-501
Cockayne syndrome is a segmental progeria most often caused by mutations in the CSB gene encoding a SWI/SNF-like ATPase required for transcription-coupled DNA repair (TCR). Over 43 Mya before marmosets diverged from humans, a piggyBac3 (PGBD3) transp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f51ecd46286b18996904216b299e4f2f
https://doi.org/10.1016/j.dnarep.2012.02.004
https://doi.org/10.1016/j.dnarep.2012.02.004
Publikováno v:
Molecular and Cellular Biology. 28:3573-3588
In mammals, small multigene families generate spliceosomal U snRNAs that are nearly as abundant as rRNA. Using the tandemly repeated human U2 genes as a model, we show by footprinting with DNase I and permanganate that nearly all sequences between th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d54b99b04e1e0c3bff307a9082c845a0
https://doi.org/10.1128/mcb.00087-08
https://doi.org/10.1128/mcb.00087-08
Cockayne syndrome group B protein (CSB) plays a general role in chromatin maintenance and remodeling
Publikováno v:
Proceedings of the National Academy of Sciences. 103:9613-9618
Cockayne syndrome (CS) is an inherited neurodevelopmental disorder with progeroid features. Although the genes responsible for CS have been implicated in a variety of DNA repair- and transcription-related pathways, the nature of the molecular defect
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b164e6999d317e5f1919aab5d61e03c
https://doi.org/10.1073/pnas.0510909103
https://doi.org/10.1073/pnas.0510909103
Publikováno v:
Journal of Biological Chemistry. 281:9801-9811
The CCA-adding enzyme adds CCA to the 3′-end of tRNA one nucleotide at a time, using CTP and ATP as substrates. We found previously that tRNA does not rotate or translocate on the enzyme during the addition of C75 and A76. We therefore predicted th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::47ee65222490c9a35d7d8d8ec0a13f5a
https://doi.org/10.1074/jbc.m512603200
https://doi.org/10.1074/jbc.m512603200
Publikováno v:
Journal of Biological Chemistry. 280:9555-9566
The CCA-adding enzyme (tRNA nucleotidyltransferase) builds and repairs the 3′ end of tRNA. A single active site adds both CTP and ATP, but the enzyme has no nucleic acid template, and tRNA does not translocate or rotate during C75 and A76 addition.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f1c77327bd817f84d268f82bec98f698
https://doi.org/10.1074/jbc.m412594200
https://doi.org/10.1074/jbc.m412594200
Publikováno v:
Molecular Cell. 12(5):1165-1172
CCA-adding enzymes catalyze the addition of CCA onto the 3' terminus of immature tRNAs without using a nucleic acid template and have been divided into two classes based on their amino acid sequences. We have determined the crystal structures of a cl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::72d477d64c4f522620f916ffa65848b1
Publikováno v:
RNA. 9:970-981
We explored the specificity and nature of the nucleotide-binding pocket of the CCA-adding enzyme (tRNA nucleotidyltransferase) by using CTP and ATP analogs as substrates for a panel of class I and class II enzymes. Overall, class I and class II enzym
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::99d0958f76291b7824a24f86dbf5615b
https://doi.org/10.1261/rna.2110903
https://doi.org/10.1261/rna.2110903