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

Autor: ALAN HERBERT, JENS ALFKEN, YANG-GYUN KIM, I. SAIRA MIAN, KAZUKO NISHIKURA, ALEXANDER RICH

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::2f6748fa6bd2af63866c72b4a8dd9d7f
https://doi.org/10.1142/9789813272682_0033

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Form Follows Function: The Design of Minimalistic Immunogenically Defined Gene Expression (MIDGE®) Constructs

Autor: Burghardt Wittig, Reinhold Schirmbeck, Claas Junghans, Jens Alfken, Colin A. Smith, Florian Sack, Sven Andres Koenig-Merediz, Matthias Schroff

Publikováno v: Plasmids for Therapy and Vaccination

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::644b27f2e95e32671eaa523559719499
https://doi.org/10.1002/9783527612833.ch08

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Cloning of an interferon regulatory factor 2 isoform with different regulatory ability

Autor: Sven A. Koenig Merediz, David Meraro, Manuel Schmidt, Andreas Neubauer, Georg J. Hoppe, Jens Alfken, Burghardt Wittig, Ben-Zion Levi

Interferons (IFNs) are a family of multifunctional proteins involved in immune activation, regulation of cell growth and antiviral response. They exert their functions by induction of several IFN-stimulated genes, including IFN regulatory factors (IR

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c8577a5601d19fcbf3966e15ca6c674
https://europepmc.org/articles/PMC113119/

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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

Autor: Ramasamy Manoharan, Alexander Rich, Jens Alfken, Thomas U. Schwartz, Ky Lowenhaupt, Imre Berger, and Alan Herbert, Yang-Gyun Kim, William Winston

Publikováno v: Biochemistry. 37(38)

Double-stranded RNA adenosine deaminase (ADAR1) is an ubiquitous enzyme in metazoa that edits pre-mRNA changing adenosine to inosine in regions of double-stranded RNA. Zalpha, an N-terminal domain of human ADAR1 encompassing 76 amino acid residues, s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6fd7e942349a7ba88ea2f2c3959d8750
https://pubmed.ncbi.nlm.nih.gov/9748339

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

Autor: Jens Alfken, Alexander Rich, Thomas U. Schwartz, Alan Herbert, Luda S. Shlyakhtenko, Markus Schade, Yuri L. Lyubchenko, Ky Lowenhaupt

Publikováno v: Nucleic acids research. 26(15)

Z-DNA, the left-handed conformer of DNA, is stabilized by the negative supercoiling generated during the movement of an RNA polymerase through a gene. Recently, we have shown that the editing enzyme ADAR1 (double-stranded RNA adenosine deaminase, typ

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::51a5c0ab399ece8bc2f995ef13be0b35
https://pubmed.ncbi.nlm.nih.gov/9671809

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

Autor: I. Saira Mian, Alexander Rich, Kazuko Nishikura, Yang-Gyun Kim, Alan Herbert, Jens Alfken

Editing of RNA changes the read-out of information from DNA by altering the nucleotide sequence of a transcript. One type of RNA editing found in all metazoans uses double-stranded RNA (dsRNA) as a substrate and results in the deamination of adenosin

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4648458f91cfca24c27aa826b4ef0737
https://europepmc.org/articles/PMC22942/

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