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Raspudin Saleem-Batcha

Researcher at University of Freiburg

Publications -  18
Citations -  545

Raspudin Saleem-Batcha is an academic researcher from University of Freiburg. The author has contributed to research in topics: Effector & Immune receptor. The author has an hindex of 8, co-authored 15 publications receiving 436 citations. Previous affiliations of Raspudin Saleem-Batcha include University of Lübeck & Indian Institute of Science.

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Fungal effector Ecp6 outcompetes host immune receptor for chitin binding through intrachain LysM dimerization

TL;DR: Structural analysis of the LysM effector Ecp6 of the fungal tomato pathogen Cladosporium fulvum reveals a novel mechanism for chitin binding, mediated by intrachain LysM dimerization, leading to a chitIn-binding groove that is deeply buried in the effector protein.
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Molecular dissection of the mycobacterial stringent response protein Rel

TL;DR: Rel protein from Mycobacterium smegmatis, which is highly homologous to M. tuberculosis Rel, is functional even in the absence of ribosome and uncharged tRNA, and the unique cysteine, of six present in Rel, required for tRNA‐mediated synthesis of ppGpp is identified.
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ppGpp analogues inhibit synthetase activity of Rel proteins from Gram-negative and Gram-positive bacteria.

TL;DR: A prominent feature of the stringent response is the accumulation of two unusual phosphorylated derivatives of GTP and GDP within a few seconds after the onset of amino-acid starvation, which appears to be a very attractive approach for the development of novel antibacterial agents.
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Aminoperoxide adducts expand the catalytic repertoire of flavin monooxygenases.

TL;DR: It is demonstrated that overlooked flavin-N5-oxygen adducts are more widespread and may facilitate versatile chemistry, thus upending the notion that flavin monooxygenases exclusively function as nature’s equivalents to organic peroxides in synthetic chemistry.
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Enzymatic control of dioxygen binding and functionalization of the flavin cofactor.

TL;DR: This study unambiguously demonstrates how enzymes may control the O 2 functionalization of an organic cofactor as prerequisite for oxidative catalysis and provides crucial knowledge for future rational design of O 2 -reactive enzymes.