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Publications

Rampelt H, van der Laan M (2017) The yin and yang of mitochondrial architecture – interplay of MICOS and F1Fo-ATP synthase in cristae formation. Microb. Cell 4: 236-239.

Ellenrieder L, Rampelt H, Becker T (2017) Connection of protein transport and organelle contact sites in mitochondria. J. Mol. Biol. 429: 2148-2160.

Hessenberger M, Zerbes RM, Rampelt H, Kunz S, Xavier AH, Purfürst B, Lilie H, Pfanner N, van der Laan M, Daumke O (2017) Regulated membrane remodeling by Mic60 controls formation of mitochondrial crista junctions. Nat. Commun. 8: 15258.

Rampelt H, Bohnert M, Zerbes RM, Horvath SE, Warscheid B, Pfanner N, van der Laan M (2017) Mic10, a core subunit of the mitochondrial contact site and cristae organizing system, interacts with the dimeric F1Fo-ATP synthase. J. Mol. Biol. 429: 1162-1170.

Rampelt H, Zerbes RM, van der Laan M, Pfanner N (2017) Role of the mitochondrial contact site and cristae organizing system in membrane architecture and dynamics. Biochim. Biophys. Acta 1864: 737-746.

Rampelt H, Pfanner N (2016) Coordination of two genomes by mitochondrial translational plasticity. Cell 167: 308-310.

Bohnert M, Zerbes RM, Davies KM, Mühleip AW, Rampelt H, Horvath SE, Boenke T, Kram A, Perschil I, Veenhuis M, Kühlbrandt W, van der Klei IJ, Pfanner N, van der Laan M (2015) Central role of Mic10 in the mitochondrial contact site and cristae organizing system. Cell Metab. 21: 745-755.

Rampelt H, van der Laan M (2015) Metabolic remodeling: a pyruvate transport affair. EMBO J. 34: 835-837.

Horvath SE, Rampelt H, Oeljeklaus S, Warscheid B, van der Laan M, Pfanner N (2015) Role of membrane contact sites in protein import into mitochondria. Protein Sci. 24: 277-297.

Mehnert CS, Rampelt H, Gebert M, Oeljeklaus S, Schrempp SG, Kochbeck L, Guiard B, Warscheid B, van der Laan M (2014) The mitochondrial ADP/ATP carrier associates with the inner membrane presequence translocase in a stoichiometric manner. J. Biol. Chem. 289: 27352-27362.

Rampelt H, Kirstein-Miles J, Nillegoda NB, Chi K, Scholz SR, Morimoto RI, Bukau B (2012) Metazoan Hsp70 machines use Hsp110 to power protein disaggregation.

EMBO J. 31: 4221-4235.

Rampelt H, Mayer MP, Bukau B (2011) Nucleotide Exchange Factors for Hsp70 Chaperones. Methods Mol. Biol. 787: 83-91.

Andréasson C, Rampelt H, Fiaux J, Druffel-Augustin S, Bukau B (2010) The endoplasmic reticulum Grp170 acts as a nucleotide exchange factor of Hsp70 via a mechanism similar to that of the cytosolic Hsp110. J. Biol. Chem. 285: 12445-12453.

Andréasson C, Fiaux J, Rampelt H, Druffel-Augustin S, Bukau B (2008) Insights into the structural dynamics of the Hsp110-Hsp70 interaction reveal the mechanism for nucleotide exchange activity. Proc. Natl. Acad. Sci. U S A 105: 16519-16524.

Andréasson C, Fiaux J, Rampelt H, Mayer MP, Bukau B (2008) Hsp110 is a Nucleotide-activated Exchange Factor for Hsp70. J. Biol. Chem. 283: 8877-8884.

Sadlish H, Rampelt H, Shorter J, Wegrzyn RD, Andréasson C, Lindquist S, Bukau B (2008) Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities. PLoS ONE 3: e1763 (2008). doi:10.1371/journal.pone.0001763.

Kwon C, Neu C, Pajonk S, Yun HS, Lipka U, Humphry M, Bau S, Straus M, Kwaaitaal M, Rampelt H, El Kasmi F, Jürgens G, Parker J, Panstruga R, Lipka V, Schulze-Lefert P (2008) Co-option of a default secretory pathway for plant immune responses. Nature 451: 835-840.