The solution structure of the Zalpha domain of the human RNA editing enzyme ADAR1 reveals a prepositioned binding surface for Z-DNA (Q24654539)

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1 November 2019

title

The solution structure of the Zalpha domain of the human RNA editing enzyme ADAR1 reveals a prepositioned binding surface for Z-DNA (English)

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1 November 2019

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1

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1 November 2019

K Lowenhaupt

5

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1 November 2019

Hartmut Oschkinat

8

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1 November 2019

author name string

C J Turner

2

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1 November 2019

R Kühne

3

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1 November 2019

P Schmieder

4

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1 November 2019

A Herbert

6

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1 November 2019

A Rich

7

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1 November 2019

language of work or name

English

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publication date

1 October 1999

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Proceedings of the National Academy of Sciences of the United States of America

1 November 2019

published in

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1 November 2019

volume

96

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1 November 2019

issue

22

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1 November 2019

page(s)

12465-12470

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Structural basis of DNA recognition by the heterodimeric cell cycle transcription factor E2F-DP

1 November 2019

cites work

1 reference

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The Zalpha domain from human ADAR1 binds to the Z-DNA conformer of many different sequences

7 April 2017

1 reference

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A Z-DNA binding domain present in the human editing enzyme, double-stranded RNA adenosine deaminase

7 April 2017

1 reference

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Crystal structure of the Zalpha domain of the human editing enzyme ADAR1 bound to left-handed Z-DNA

7 April 2017

1 reference

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Structure of the metal-ion-activated diphtheria toxin repressor/tox operator complex

7 April 2017

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Structure of the even-skipped homeodomain complexed to AT-rich DNA: new perspectives on homeodomain specificity

7 April 2017

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Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5

7 April 2017

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Mapping the protein universe

7 April 2017

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NMRPipe: a multidimensional spectral processing system based on UNIX pipes

7 April 2017

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Regulation of serotonin-2C receptor G-protein coupling by RNA editing

7 April 2017

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RNA editing in brain controls a determinant of ion flow in glutamate-gated channels

7 April 2017

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Crystal structure of a CAP-DNA complex: the DNA is bent by 90 degrees

7 April 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=22950

Structure-function analysis of the Z-DNA-binding domain Zalpha of dsRNA adenosine deaminase type I reveals similarity to the (alpha + beta) family of helix-turn-helix proteins

7 April 2017

1 reference

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Spectroscopic characterization of a DNA-binding domain, Z alpha, from the editing enzyme, dsRNA adenosine deaminase: evidence for left-handed Z-DNA in the Z alpha-DNA complex

28 September 2017

1 reference

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Recommendations for the presentation of NMR structures of proteins and nucleic acids

28 September 2017

1 reference

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Hydration and DNA recognition by homeodomains

28 September 2017

1 reference

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The biology of left-handed Z-DNA.

28 September 2017

1 reference

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Differential DNA-binding specificity of the engrailed homeodomain: the role of residue 50.

28 September 2017

1 reference

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Preferential selection of adenosines for modification by double-stranded RNA adenosine deaminase.

28 September 2017

1 reference

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Sampling and efficiency of metric matrix distance geometry: a novel partial metrization algorithm.

28 September 2017

1 reference

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PROCHECK: a program to check the stereochemical quality of protein structures

30 May 2018

1 reference

Crossref

https://api.crossref.org/works/10.1073%2FPNAS.96.22.12465

A 6 bp Z-DNA hairpin binds two Zα domains from the human RNA editing enzyme ADAR1

21 January 2018

1 reference

Crossref

https://api.crossref.org/works/10.1073%2FPNAS.96.22.12465

Chemical shift as a probe of molecular interfaces: NMR studies of DNA binding by the three amino-terminal zinc finger domains from transcription factor IIIA

21 January 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/10535945

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1073/PNAS.96.22.12465

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1 November 2019

0 references

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1 November 2019

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