Published in J Biol Chem on April 12, 2016
Functions and regulation of the Brr2 RNA helicase during splicing. Cell Cycle (2016) 0.75
The spliceosome: design principles of a dynamic RNP machine. Cell (2009) 12.82
Spliceosome structure and function. Cold Spring Harb Perspect Biol (2011) 4.01
SF1 and SF2 helicases: family matters. Curr Opin Struct Biol (2010) 3.79
RNA unwinding in U4/U6 snRNPs requires ATP hydrolysis and the DEIH-box splicing factor Brr2. Curr Biol (1998) 3.17
Prp8 protein: at the heart of the spliceosome. RNA (2005) 2.89
Structural basis for DNA duplex separation by a superfamily-2 helicase. Nat Struct Mol Biol (2007) 2.77
A role for ubiquitin in the spliceosome assembly pathway. Nat Struct Mol Biol (2008) 2.12
The EF-G-like GTPase Snu114p regulates spliceosome dynamics mediated by Brr2p, a DExD/H box ATPase. Mol Cell (2006) 2.09
Autosomal-dominant retinitis pigmentosa caused by a mutation in SNRNP200, a gene required for unwinding of U4/U6 snRNAs. Am J Hum Genet (2009) 1.73
Molecular architecture of the human U4/U6.U5 tri-snRNP. Science (2016) 1.71
Structure of a multipartite protein-protein interaction domain in splicing factor prp8 and its link to retinitis pigmentosa. Mol Cell (2007) 1.70
Structure of a yeast spliceosome at 3.6-angstrom resolution. Science (2015) 1.64
The first ATPase domain of the yeast 246-kDa protein is required for in vivo unwinding of the U4/U6 duplex. RNA (1999) 1.62
ATP-dependent unwinding of U4/U6 snRNAs by the Brr2 helicase requires the C terminus of Prp8. Nat Struct Mol Biol (2008) 1.50
Structural evidence for consecutive Hel308-like modules in the spliceosomal ATPase Brr2. Nat Struct Mol Biol (2009) 1.40
The architecture of the spliceosomal U4/U6.U5 tri-snRNP. Nature (2015) 1.24
Next generation sequencing of pooled samples reveals new SNRNP200 mutations associated with retinitis pigmentosa. Hum Mutat (2011) 1.23
A novel locus (RP33) for autosomal dominant retinitis pigmentosa mapping to chromosomal region 2cen-q12.1. Hum Genet (2006) 1.22
Structure of the DNA repair helicase hel308 reveals DNA binding and autoinhibitory domains. J Biol Chem (2007) 1.21
Inhibition of RNA helicase Brr2 by the C-terminal tail of the spliceosomal protein Prp8. Science (2013) 1.17
The Prp8 RNase H-like domain inhibits Brr2-mediated U4/U6 snRNA unwinding by blocking Brr2 loading onto the U4 snRNA. Genes Dev (2012) 1.17
Cryo-EM structure of the yeast U4/U6.U5 tri-snRNP at 3.7 Å resolution. Nature (2016) 1.17
Brr2p-mediated conformational rearrangements in the spliceosome during activation and substrate repositioning. Genes Dev (2012) 1.13
The 3.8 Å structure of the U4/U6.U5 tri-snRNP: Insights into spliceosome assembly and catalysis. Science (2016) 1.12
Structural basis for functional cooperation between tandem helicase cassettes in Brr2-mediated remodeling of the spliceosome. Proc Natl Acad Sci U S A (2012) 1.08
Mutations in ASCC3L1 on 2q11.2 are associated with autosomal dominant retinitis pigmentosa in a Chinese family. Invest Ophthalmol Vis Sci (2009) 1.03
Structural basis of Brr2-Prp8 interactions and implications for U5 snRNP biogenesis and the spliceosome active site. Structure (2013) 0.99
Ski2-like RNA helicase structures: common themes and complex assemblies. RNA Biol (2012) 0.97
Structural bioinformatics of the human spliceosomal proteome. Nucleic Acids Res (2012) 0.96
Archaeal Hel308 domain V couples DNA binding to ATP hydrolysis and positions DNA for unwinding over the helicase ratchet. J Mol Biol (2007) 0.90
Novel regulatory principles of the spliceosomal Brr2 RNA helicase and links to retinal disease in humans. RNA Biol (2014) 0.87
The large N-terminal region of the Brr2 RNA helicase guides productive spliceosome activation. Genes Dev (2015) 0.83
Brr2 plays a role in spliceosomal activation in addition to U4/U6 unwinding. Nucleic Acids Res (2015) 0.83
The Mtr4 ratchet helix and arch domain both function to promote RNA unwinding. Nucleic Acids Res (2014) 0.83
A noncanonical PWI domain in the N-terminal helicase-associated region of the spliceosomal Brr2 protein. Acta Crystallogr D Biol Crystallogr (2015) 0.81
pH-dependent conformational changes in the HCV NS3 protein modulate its ATPase and helicase activities. PLoS One (2014) 0.79