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Genetic analysis reveals a role for the C terminus of the Saccharomyces cerevisiae GTPase Snu114 during spliceosome activation
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scholarly article
1 reference
stated in
PubMed
PubMed ID
15911574
retrieved
1 December 2016
title
Genetic analysis reveals a role for the C terminus of the Saccharomyces cerevisiae GTPase Snu114 during spliceosome activation
(English)
1 reference
stated in
PubMed
PubMed ID
15911574
retrieved
1 December 2016
main subject
Saccharomyces cerevisiae
0 references
spliceosome
0 references
U5 snRNP GTPase SNU114 YKL173W
1 reference
stated in
GOA release 2020-03-11
author name string
Tamara J Brenner
series ordinal
1
0 references
Christine Guthrie
series ordinal
2
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language of work or name
English
0 references
publication date
July 2005
0 references
published in
Genetics
1 reference
stated in
PubMed
PubMed ID
15911574
retrieved
1 December 2016
volume
170
0 references
page(s)
1063-80
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issue
3
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cites work
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A conserved Lsm-interaction motif in Prp24 required for efficient U4/U6 di-snRNP formation
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MPN+, a putative catalytic motif found in a subset of MPN domain proteins from eukaryotes and prokaryotes, is critical for Rpn11 function
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A novel genetic screen for snRNP assembly factors in yeast identifies a conserved protein, Sad1p, also required for pre-mRNA splicing
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The human U5-220kD protein (hPrp8) forms a stable RNA-free complex with several U5-specific proteins, including an RNA unwindase, a homologue of ribosomal elongation factor EF-2, and a novel WD-40 protein
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PRP16, a DEAH-box RNA helicase, is recruited to the spliceosome primarily via its nonconserved N-terminal domain
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The human U5-200kD DEXH-box protein unwinds U4/U6 RNA duplices in vitro
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Snt309p, a component of the Prp19p-associated complex that interacts with Prp19p and associates with the spliceosome simultaneously with or immediately after dissociation of U4 in the same manner as Prp19p
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An evolutionarily conserved U5 snRNP-specific protein is a GTP-binding factor closely related to the ribosomal translocase EF-2.
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Cross-intron bridging interactions in the yeast commitment complex are conserved in mammals
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Spliceosome activation by PRP2 ATPase prior to the first transesterification reaction of pre-mRNA splicing
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Transcriptional pulse-chase analysis reveals a role for a novel snRNP-associated protein in the manufacture of spliceosomal snRNPs
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Yeast precursor mRNA processing protein PRP19 associates with the spliceosome concomitant with or just after dissociation of U4 small nuclear RNA.
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The crystal structure of elongation factor G complexed with GDP, at 2.7 A resolution
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A cold-sensitive mRNA splicing mutant is a member of the RNA helicase gene family
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PRP16 is an RNA-dependent ATPase that interacts transiently with the spliceosome
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Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome
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7 April 2017
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Allosteric cascade of spliceosome activation
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7 April 2017
G protein mechanisms: insights from structural analysis
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Distinct domains of splicing factor Prp8 mediate different aspects of spliceosome activation
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Deletion of MUD2, the yeast homolog of U2AF65, can bypass the requirement for sub2, an essential spliceosomal ATPase
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RNA helicase dynamics in pre-mRNA splicing
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The question remains: is the spliceosome a ribozyme?
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Suppressors of a cold-sensitive mutation in yeast U4 RNA define five domains in the splicing factor Prp8 that influence spliceosome activation
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The first ATPase domain of the yeast 246-kDa protein is required for in vivo unwinding of the U4/U6 duplex
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29 September 2017
Prp43: An RNA helicase-like factor involved in spliceosome disassembly
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29 September 2017
Mutagenesis of the yeast gene PRP8 reveals domains governing the specificity and fidelity of 3' splice site selection
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29 September 2017
The ribosomal translocase homologue Snu114p is involved in unwinding U4/U6 RNA during activation of the spliceosome
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Functional contacts with a range of splicing proteins suggest a central role for Brr2p in the dynamic control of the order of events in spliceosomes of Saccharomyces cerevisiae
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2 June 2018
Large-scale movement of elongation factor G and extensive conformational change of the ribosome during translocation
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An RNA switch at the 5' splice site requires ATP and the DEAD box protein Prp28p
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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1451163
retrieved
2 June 2018
Roles of PRP8 protein in the assembly of splicing complexes
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1451163
retrieved
2 June 2018
Mutagenesis Suggests Several Roles of Snu114p in Pre-mRNA Splicing
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1451163
retrieved
27 November 2018
Small nuclear ribonucleoprotein remodeling during catalytic activation of the spliceosome.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1451163
retrieved
27 November 2018
GTPase activation of elongation factors Tu and G on the ribosome
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1451163
retrieved
27 November 2018
Structure-based sequence alignment of elongation factors Tu and G with related GTPases involved in translation.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1451163
retrieved
27 November 2018
A mechanism to enhance mRNA splicing fidelity: the RNA-dependent ATPase Prp16 governs usage of a discard pathway for aberrant lariat intermediates
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1451163
retrieved
27 November 2018
A ribosomal protein module in EF-G and DNA gyrase.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1451163
retrieved
27 November 2018
A novel role for a U5 snRNP protein in 3' splice site selection.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1451163
retrieved
27 November 2018
Domain IV of elongation factor G from Thermus thermophilus is strictly required for translocation
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/15911574
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Protein-RNA interactions in the U5 snRNP of Saccharomyces cerevisiae
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/15911574
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Splicing factor Prp8 governs U4/U6 RNA unwinding during activation of the spliceosome
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/15911574
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Role of Domains 4 and 5 in Elongation Factor G Functions on the Ribosome
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/15911574
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Specific alterations of U1-C protein or U1 small nuclear RNA can eliminate the requirement of Prp28p, an essential DEAD box splicing factor
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/15911574
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Primer extension analysis of RNA
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/15911574
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Four yeast spliceosomal proteins (PRP5, PRP9, PRP11, and PRP21) interact to promote U2 snRNP binding to pre-mRNA
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/15911574
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1534/GENETICS.105.042044
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2173032
Fatcat ID
release_us5u5gopgzer3mt4t6gi4o4sde
1 reference
stated in
Fatcat
reference URL
https://api.fatcat.wiki/v0/release/us5u5gopgzer3mt4t6gi4o4sde
retrieved
24 November 2022
based on heuristic
mapped directly with Wikidata item
OpenCitations bibliographic resource ID
2173032
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2173032
PMCID
1451163
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2173032
PubMed ID
15911574
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2173032
ResearchGate publication ID
7829288
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