Related references
Note: Only part of the references are listed.Opposing classes of prp8 alleles modulate the transition between the catalytic steps of pre-mRNA splicing
Li Liu et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2007)
Structure of a multipartite protein-protein interaction domain in splicing factor Prp8 and its link to Retinitis pigmentosa
Vladimir Pena et al.
MOLECULAR CELL (2007)
Crystal structure of the C-terminal domain of splicing factor Prp8 carrying retinitis pigmentosa mutants
Lingdi Zhang et al.
PROTEIN SCIENCE (2007)
Dissection of Prp8 protein defines multiple interactions with crucial RNA sequences in the catalytic core of the spliceosome
IA Turner et al.
RNA (2006)
Repositioning of the reaction intermediate within the catalytic center of the spliceosome
MM Konarska et al.
MOLECULAR CELL (2006)
Prp8 protein: At the heart of the spliceosome
RJ Grainger et al.
RNA (2005)
Crystal structure of argonaute and its implications for RISC slicer activity
JJ Song et al.
SCIENCE (2004)
Suppression of multiple substrate mutations by spliceosomal prp8 alleles suggests functional correlations with ribosomal ambiguity mutants
CC Query et al.
MOLECULAR CELL (2004)
HKL2MAP:: a graphical user interface for macromolecular phasing with SHELX programs
T Pape et al.
JOURNAL OF APPLIED CRYSTALLOGRAPHY (2004)
Insights into the decoding mechanism from recent ribosome structures
JM Ogle et al.
TRENDS IN BIOCHEMICAL SCIENCES (2003)
Distinct domains of splicing factor Prp8 mediate different aspects of spliceosome activation
AN Kuhn et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2002)
Two-metal active site binding of a Tn5 transposase synaptic complex
S Lovell et al.
NATURE STRUCTURAL BIOLOGY (2002)
Composition and functional characterization of the yeast spliceosomal Penta-snRNP
SW Stevens et al.
MOLECULAR CELL (2002)
Comparative architecture of transposase and integrase complexes
PA Rice et al.
NATURE STRUCTURAL BIOLOGY (2001)
The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
N Ban et al.
SCIENCE (2000)