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RNA unwinding by the Trf4/Air2/Mtr4 polyadenylation (TRAMP) complex
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scholarly article
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stated in
PubMed
PubMed ID
22532666
retrieved
1 December 2016
title
RNA unwinding by the Trf4/Air2/Mtr4 polyadenylation (TRAMP) complex
(English)
1 reference
stated in
PubMed
PubMed ID
22532666
retrieved
1 December 2016
main subject
TRAMP complex RNA-binding subunit YDL175C
1 reference
stated in
GOA release 2020-03-11
Non-canonical poly(A) polymerase PAP2 YOL115W
1 reference
stated in
GOA release 2020-03-11
author
Eckhard Jankowsky
series ordinal
4
0 references
Huijue Jia
object named as
Huijue Jia
series ordinal
1
0 references
author name string
Xuying Wang
series ordinal
2
0 references
James T Anderson
series ordinal
3
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language of work or name
English
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publication date
8 May 2012
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published in
Proceedings of the National Academy of Sciences of the United States of America
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stated in
PubMed
PubMed ID
22532666
retrieved
1 December 2016
volume
109
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issue
19
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page(s)
7292-7
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describes a project that uses
ImageQuant
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stated in
Europe PubMed Central
retrieved
11 June 2022
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/PMC3358879/fullTextXML
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inferred from PubMed Central ID database lookup
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Structural analysis reveals the characteristic features of Mtr4, a DExH helicase involved in nuclear RNA processing and surveillance
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TRAMP complex enhances RNA degradation by the nuclear exosome component Rrp6
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Characterization of the essential activities of Saccharomyces cerevisiae Mtr4p, a 3'->5' helicase partner of the nuclear exosome
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Degradation of hypomodified tRNA(iMet) in vivo involves RNA-dependent ATPase activity of the DExH helicase Mtr4p
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Structural basis for DNA duplex separation by a superfamily-2 helicase
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ATP- and ADP-dependent modulation of RNA unwinding and strand annealing activities by the DEAD-box protein DED1.
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Cryptic pol II transcripts are degraded by a nuclear quality control pathway involving a new poly(A) polymerase
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From unwinding to clamping - the DEAD box RNA helicase family
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DEAD-box proteins unwind duplexes by local strand separation
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Studies on three E. coli DEAD-box helicases point to an unwinding mechanism different from that of model DNA helicases
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Common design principles in the spliceosomal RNA helicase Brr2 and in the Hel308 DNA helicase.
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The DEAD-box protein Ded1 unwinds RNA duplexes by a mode distinct from translocating helicases
1 reference
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Crossref
reference URL
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retrieved
21 January 2018
The DExH protein NPH-II is a processive and directional motor for unwinding RNA
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1073%2FPNAS.1201085109
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21 January 2018
Biochemical and kinetic characterization of the RNA helicase activity of eukaryotic initiation factor 4A
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/22532666
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Nuclear RNA surveillance: no sign of substrates tailing off
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/22532666
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1073/PNAS.1201085109
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ADS bibcode
2012PNAS..109.7292J
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PMCID
3358879
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PubMed ID
22532666
1 reference
stated in
PubMed
PubMed ID
22532666
retrieved
1 December 2016
ResearchGate publication ID
224836302
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