F
Frank Siedler
Researcher at Max Planck Society
Publications - 42
Citations - 1964
Frank Siedler is an academic researcher from Max Planck Society. The author has contributed to research in topics: Halobacterium salinarum & Proteome. The author has an hindex of 23, co-authored 42 publications receiving 1854 citations.
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Chlamydia causes fragmentation of the Golgi compartment to ensure reproduction
Dagmar Heuer,Anette Rejman Lipinski,Nikolaus Machuy,Alexander Karlas,Andrea Wehrens,Frank Siedler,Volker Brinkmann,Thomas F. Meyer +7 more
TL;DR: This work functionally connect bacteria-induced golgin-84 cleavage, Golgi ministack formation, lipid acquisition and intracellular pathogen growth, and shows that C. trachomatis subverts the structure and function of an entire host cell organelle for its own advantage.
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The Redox Potential of Selenocystine in Unconstrained Cyclic Peptides
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Large-scale identification of N-terminal peptides in the halophilic archaea Halobacterium salinarum and Natronomonas pharaonis.
Michalis Aivaliotis,Kris Gevaert,Michaela Falb,Andreas Tebbe,Kosta Konstantinidis,Birgit Bisle,Christian Klein,L. Martens,An Staes,E. Timmerman,J. Van Damme,Frank Siedler,Friedhelm Pfeiffer,Joël Vandekerckhove,Dieter Oesterhelt +14 more
TL;DR: This work represents the first large-scale identification of N-terminal peptides from prokaryotes, of the two halophilic euryarchaeota Halobacterium salinarum and Natronomonas pharaonis, and allowed the validation/improvement of start codon assignments as automatic gene finders tend to misassign start codons for GC-rich genomes.
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Oxidative folding of cystine-rich peptides vs regioselective cysteine pairing strategies.
TL;DR: The results obtained in the oxidative folding of excised protein fragments and of relatively low mass products of posttranslational processings show that this procedure is indeed a simple way of preparing peptides with several disulfide bonds, if optimization of reaction conditions is performed in terms of redox buffer, temperature, and additives.
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The membrane proteome of Halobacterium salinarum.
Christian Klein,C. Garcı́a-Rizo,Birgit Bisle,Beatrix Scheffer,Hans Zischka,Friedhelm Pfeiffer,Frank Siedler,Dieter Oesterhelt +7 more
TL;DR: The identification of 114 integral membrane proteins from Halobacterium salinarum was achieved using liquid chromatography/tandem mass spectrometric (LC/MS/MS) techniques, representing 20% of the predicted alpha‐helical transmembrane proteins of the genome.