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Achim Schnaufer

Researcher at University of Edinburgh

Publications -  75
Citations -  3530

Achim Schnaufer is an academic researcher from University of Edinburgh. The author has contributed to research in topics: Trypanosoma brucei & RNA editing. The author has an hindex of 29, co-authored 69 publications receiving 3145 citations. Previous affiliations of Achim Schnaufer include University of Giessen & Seattle Biomed.

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Complex management: RNA editing in trypanosomes

TL;DR: A picture of highly organized complexes is emerging that shows that the complex that catalyzes the central steps of editing is partitioned into distinct insertion and deletion editing subcomplexes.
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An RNA ligase essential for RNA editing and survival of the bloodstream form of Trypanosoma brucei.

TL;DR: Regulated repression of TbMP52 blocks editing, which shows that it is a functional component of the editing complex, indicating that editing is essential in the mammalian stage of the life cycle.
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The F1‐ATP synthase complex in bloodstream stage trypanosomes has an unusual and essential function

TL;DR: In this paper, the α subunit of the mitochondrial F1-ATP synthase complex was found to be lethal for T. brucei and T. evansi, a closely related species that lacks mitochondrial protein coding genes.
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Natural and induced dyskinetoplastic trypanosomatids: how to live without mitochondrial DNA.

TL;DR: The data available on dyskinetoplasty in trypanosomes is summarized and the roles the mitochondrion and its genome play during the life cycle of T. brucei are revisited, questioning the therapeutic value of attempts to target mitochondrial gene expression with specific drugs.
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Identification of novel components of Trypanosoma brucei editosomes.

TL;DR: Nine novel editosome proteins in Trypanosoma brucei are identified by mass spectrometric analysis of functional editosomes that were purified by serial ion exchange/gel permeation chromatography, immunoaffinity chromatography specific to the TbMP63 editosomal protein, or tandem affinity purification based on a tagged RNA editing ligase.