Structural Basis for the Bidirectional Activity of Bacillus nanoRNase NrnA.

about

The trimeric Hef-associated nuclease HAN is a 3'→5' exonuclease and is probably involved in DNA repair

P2860

Q58794843-B29E11A5-0EE4-4026-9ECF-F2F0D68984C6

P2860

Structural Basis for the Bidirectional Activity of Bacillus nanoRNase NrnA.

Item

http://www.wikidata.org/entity/Q41329737

description

2017 nî lūn-bûn

@nan

2017年の論文

@ja

2017年学术文章

@wuu

2017年学术文章

@zh-cn

2017年学术文章

@zh-hans

2017年学术文章

@zh-my

2017年学术文章

@zh-sg

2017年學術文章

@yue

2017年學術文章

@zh

2017年學術文章

@zh-hant

name

Structural Basis for the Bidirectional Activity of Bacillus nanoRNase NrnA.

@en

type

Item

label

Structural Basis for the Bidirectional Activity of Bacillus nanoRNase NrnA.

@en

prefLabel

Structural Basis for the Bidirectional Activity of Bacillus nanoRNase NrnA.

@en

P1476

Structural Basis for the Bidirectional Activity of Bacillus nanoRNase NrnA.

@en

P2093

Brad J Schmier

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

Claudiu M Nelersa

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

Exoribonuclease superfamilies: structural analysis and phylogenetic distribution

Direct detection of abortive RNA transcripts in vivo

RecJ exonuclease: substrates, products and interaction with SSB

The "open" and "closed" structures of the type-C inorganic pyrophosphatases from Bacillus subtilis and Streptococcus gordonii

The crystal structure of exonuclease RecJ bound to Mn2+ ion suggests how its characteristic motifs are involved in exonuclease activity

The C-Ala Domain Brings Together Editing and Aminoacylation Functions on One tRNA

Structure of RecJ Exonuclease Defines Its Specificity for Single-stranded DNA

Molecular basis for the recognition and cleavage of RNA by the bifunctional 5'-3' exo/endoribonuclease RNase J

Structural basis of reverse nucleotide polymerization

P2888

s41598-017-09403-x

P304

11085

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

P31

scholarly article

P356

10.1038/S41598-017-09403-X

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

P407

English

P433

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

P478

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

P50

Arun Malhotra

P577

2017-09-11T00:00:00Z

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

P698

28894100

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

P932

5593865

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

Structural Basis for the Bidirectional Activity of Bacillus nanoRNase NrnA.

about

P2860

P2860

Structural Basis for the Bidirectional Activity of Bacillus nanoRNase NrnA.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932