In vitro substrate specificities of 3'-5' polymerases correlate with biological outcomes of tRNA 5'-editing reactions.

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Minimal requirements for reverse polymerization and tRNA repair by tRNAHis guanylyltransferase.

P2860

Q47680817-B52C5E7F-C1EE-4063-98FB-332B8D7FCAB6

P2860

In vitro substrate specificities of 3'-5' polymerases correlate with biological outcomes of tRNA 5'-editing reactions.

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http://www.wikidata.org/entity/Q42095505

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2015 nî lūn-bûn

@nan

2015年の論文

@ja

2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

@zh-tw

2015年论文

@wuu

2015年论文

@zh

2015年论文

@zh-cn

name

In vitro substrate specificiti ...... of tRNA 5'-editing reactions.

@en

In vitro substrate specificiti ...... of tRNA 5'-editing reactions.

@nl

type

Item

label

In vitro substrate specificiti ...... of tRNA 5'-editing reactions.

@en

In vitro substrate specificiti ...... of tRNA 5'-editing reactions.

@nl

prefLabel

In vitro substrate specificiti ...... of tRNA 5'-editing reactions.

@en

In vitro substrate specificiti ...... of tRNA 5'-editing reactions.

@nl

P1476

In vitro substrate specificiti ...... s of tRNA 5'-editing reactions

@en

P2093

Jane E Jackman

http://www.w3.org/2001/XMLSchema#string

Yicheng Long

http://www.w3.org/2001/XMLSchema#string

P2860

tRNA(His) guanylyltransferase (THG1), a unique 3'-5' nucleotidyl transferase, shares unexpected structural homology with canonical 5'-3' DNA polymerases

Predicted editing of additional transfer RNAs in Acanthamoeba castellanii mitochondria

Structural Studies of a Bacterial tRNAHIS Guanylyltransferase (Thg1)-Like Protein, with Nucleotide in the Activation and Nucleotidyl Transfer Sites

tRNAHis maturation: an essential yeast protein catalyzes addition of a guanine nucleotide to the 5' end of tRNAHis

Template-dependent 3'-5' nucleotide addition is a shared feature of tRNAHis guanylyltransferase enzymes from multiple domains of life

Depletion of Saccharomyces cerevisiae tRNA(His) guanylyltransferase Thg1p leads to uncharged tRNAHis with additional m(5)C.

3'-5' tRNAHis guanylyltransferase in bacteria.

Mitochondrial tRNA 5'-editing in Dictyostelium discoideum and Polysphondylium pallidum

Origin, evolution, and mechanism of 5' tRNA editing in chytridiomycete fungi.

Mitochondrial tRNAs in the lower fungus Spizellomyces punctatus: tRNA editing and UAG 'stop' codons recognized as leucine.

P304

2124-2130

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P31

scholarly article

P356

10.1016/J.FEBSLET.2015.06.028

http://www.w3.org/2001/XMLSchema#string

P407

English

P433

http://www.w3.org/2001/XMLSchema#string

P478

589

http://www.w3.org/2001/XMLSchema#string

P50

Yicheng Long

Jane E Jackman

P577

2015-07-02T00:00:00Z

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P5875

279754184

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P698

26143376

http://www.w3.org/2001/XMLSchema#string

P921

mitochondrial tRNA 5'-end processing

P932

4524524

http://www.w3.org/2001/XMLSchema#string

In vitro substrate specificities of 3'-5' polymerases correlate with biological outcomes of tRNA 5'-editing reactions.

about

P2860

P2860

In vitro substrate specificities of 3'-5' polymerases correlate with biological outcomes of tRNA 5'-editing reactions.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P5875

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P5875

P698

P921

P932