H
Heidi Scholze
Researcher at Martin Luther University of Halle-Wittenberg
Publications - 7
Citations - 3331
Heidi Scholze is an academic researcher from Martin Luther University of Halle-Wittenberg. The author has contributed to research in topics: TAL effector & Base pair. The author has an hindex of 6, co-authored 7 publications receiving 3059 citations.
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Journal ArticleDOI
Breaking the Code of DNA Binding Specificity of TAL-Type III Effectors
Jens Boch,Heidi Scholze,Sebastian Schornack,Angelika Landgraf,Simone Hahn,Sabine Kay,Thomas Lahaye,Anja Nickstadt,Ulla Bonas +8 more
TL;DR: The functionality of a distinct type of DNA binding domain is described and allows the design ofDNA binding domains for biotechnology.
Journal ArticleDOI
Transcriptional activators of human genes with programmable DNA-specificity.
TL;DR: Synthetic TAL proteins with designed repeat compositions were created using a novel modular cloning strategy termed “Golden TAL Technology” and activated targeted expression of exogenous as well as endogenous genes.
Journal ArticleDOI
TAL Effectors Are Remote Controls for Gene Activation
Heidi Scholze,Jens Boch +1 more
TL;DR: How TAL specificity is encoded, first structural data and first data on site-specific TAL nucleases are summarized are summarized.
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Recognition of AvrBs3-Like Proteins Is Mediated by Specific Binding to Promoters of Matching Pepper Bs3 Alleles
Patrick Römer,Tina Strauss,Simone Hahn,Heidi Scholze,Robert Morbitzer,Jan Grau,Ulla Bonas,Thomas Lahaye +7 more
TL;DR: It is demonstrated that the UPAAvrBs3 box retains its functionality at different positions within the pepper Bs3 promoter and confers AvrBs3 inducibility in a novel promoter context, suggesting that selective promoter binding of AvRBs3-like proteins is the basis for promoter activation specificity.
Journal ArticleDOI
TAL effector-DNA specificity.
Heidi Scholze,Jens Boch +1 more
TL;DR: The predicted DNA specificities of TAL effectors were predicted and artificial TAL proteins with novel DNA recognition specificities were generated, enabling design of proteins with potentially any given DNA recognition specificity enabling many uses for biotechnology.