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Peter Schreier

Researcher at Bayer

Publications -  81
Citations -  2779

Peter Schreier is an academic researcher from Bayer. The author has contributed to research in topics: Gene & Nucleic acid. The author has an hindex of 19, co-authored 81 publications receiving 2656 citations. Previous affiliations of Peter Schreier include Max Planck Society & University of Mainz.

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Journal ArticleDOI

Insights from the genome of the biotrophic fungal plant pathogen Ustilago maydis

Jörg Kämper, +80 more
- 02 Nov 2006 - 
TL;DR: The discovery of the secreted protein gene clusters and the functional demonstration of their decisive role in the infection process illuminate previously unknown mechanisms of pathogenicity operating in biotrophic fungi.
Patent

Chimaeric gene coding for a transit peptide and a heterologous polypeptide

TL;DR: In this paper, the chimaeric DNA sequence is used as a vector for transforming a plant cell so that a chimaeric precursor of the heterologous protein or polypeptide is produced in the cytoplasm of the cell and the chamaeric precursor then transports the heterology in vivo into a chloroplast of a cell.
Patent

Stilbene synthase gene

TL;DR: A stilbene synthase gene unit which comprises approximately 6,700 base pairs and exhibits 3 EcoRI, 3 HindIII and 1 PstI cleavage sites, and which can be obtained by partial cleavage of the plasmid PGS 828.1 using EcoRI and HindIII, or from PLASMID 828,1 using SstI and PvuII as discussed by the authors.
Journal ArticleDOI

An ozone-responsive region of the grapevine resveratrol synthase promoter differs from the basal pathogen-responsive sequence.

TL;DR: Analysis of an ozone inducible STS transcript and its corresponding promoter (Vst1), combined with the β-glucuronidase (GUS) reporter gene, showed that the Vst1 promoter was induced in palisade and spongy parenchyma cells and to a lesser extent in epidermal cells.
Journal ArticleDOI

Identification and characterization of secreted and pathogenesis-related proteins in Ustilago maydis

TL;DR: The isolation of secreted proteins using a signal sequence trap approach with bioinformatic analyses and the subsequent characterization of knock-out mutants indicates that Hum3 and Rsp1 are pathogenicity proteins that share an essential function in early stages of the infection.