A catalytically active group II intron domain 5 can function in the U12-dependent spliceosome (Q34131822)

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Language	Label	Description	Also known as
English	A catalytically active group II intron domain 5 can function in the U12-dependent spliceosome	scientific article

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

A catalytically active group II intron domain 5 can function in the U12-dependent spliceosome (English)

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

0 references

Girish C. Shukla

object named as

Girish C Shukla

1

0 references

Richard A Padgett

object named as

Richard A Padgett

2

0 references

publication date

1 May 2002

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

9

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Europe PubMed Central

PubMed publication ID

31 July 2017

5

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

1145-1150

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Europe PubMed Central

PubMed publication ID

31 July 2017

Catalytic role of 2'-hydroxyl groups within a group II intron active site

1 reference

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Multiple processing-defective mutations in a mammalian histone pre-mRNA are suppressed by compensatory changes in U7 RNA both in vivo and in vitro

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A tertiary interaction that links active-site domains to the 5' splice site of a group II intron

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The generality of self-splicing RNA: relationship to nuclear mRNA splicing

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Frequent use of the same tertiary motif by self-folding RNAs

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Tight binding of the 5' exon to domain I of a group II self-splicing intron requires completion of the intron active site

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A group II self-splicing intron from the brown alga Pylaiella littoralis is active at unusually low magnesium concentrations and forms populations of molecules with a uniform conformation

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Differential chemical probing of a group II self-splicing intron identifies bases involved in tertiary interactions and supports an alternative secondary structure model of domain V

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Metal ion coordination by the AGC triad in domain 5 contributes to group II intron catalysis

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Trans-activation of group II intron splicing by nuclear U5 snRNA.

1 reference

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Base pairing with U6atac snRNA is required for 5' splice site activation of U12-dependent introns in vivo

1 reference

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Group II intron domain 5 facilitates a trans-splicing reaction

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Ribozyme catalysis from the major groove of group II intron domain 5.

1 reference

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Comparative and functional anatomy of group II catalytic introns—a review

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Evidence for two active sites in the spliceosome provided by stereochemistry of pre-mRNA splicing

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The stereochemical course of group II intron self-splicing.

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Recognition of the TACTAAC box during mRNA splicing in yeast involves base pairing to the U2-like snRNA.

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A self-splicing RNA excises an intron lariat

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Catalytically critical nucleotide in domain 5 of a group II intron

1 reference

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Self-splicing of group II introns in vitro: mapping of the branch point and mutational inhibition of lariat formation

1 reference

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On the origin of RNA splicing and introns

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"Five easy pieces"

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Conservation of functional features of U6atac and U12 snRNAs between vertebrates and higher plants

1 reference

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The intramolecular stem-loop structure of U6 snRNA can functionally replace the U6atac snRNA stem-loop

1 reference

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Metal ion binding sites in a group II intron core

1 reference

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Metal ion catalysis during group II intron self-splicing: parallels with the spliceosome

1 reference

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Highly diverged U4 and U6 small nuclear RNAs required for splicing rare AT-AC introns

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A novel spliceosome containing U11, U12, and U5 snRNPs excises a minor class (AT-AC) intron in vitro

1 reference

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mRNA splicing and autocatalytic introns: distant cousins or the products of chemical determinism?

1 reference

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Metal-ion coordination by U6 small nuclear RNA contributes to catalysis in the spliceosome.

1 reference

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7 January 2021

based on heuristic

inferred from DOI database lookup

Identifiers

10.1016/S1097-2765(02)00505-1

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

31 July 2017

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