Our publications

Low, HH., Gubellini, F., Rivera-Calzada, A., Braun, N., Connery, S., Dujeancourt, A., Lu, F., Redzej, A., Fronzes, R., Orlova, EV., Waksman, G. (2014). Structure of a type IV secretion system. Nature 508(7497):550-3.

Peschek, J., Braun, N., Rohrberg, J., Back, KC., Kriehuber, T., Kastenmüller, A., Weinkauf, S., Buchner, J., (2013).Regulated structural transitions unleash the chaperone activity of B-crystallin. PNAS 110(40):E3780-9.

Bepperling, A., Alte, F., Kriehuber, T., Braun, N., Weinkauf, S., Groll, M., Haslbeck, M., Buchner, J. (2012). Alternative bacterial two-component small heat shock protein systems. PNAS 109(50):20407-12.

Gebendorfer, KM., Drazic, A., Le, Y., Gundlach, J., Bepperling, A., Kastenmüller, A., Ganzinger, KA., Braun, N., Franzmann, TM., Winter, J. (2012). Identification of a Hypochlorite-Specific Transcription Factor from Escherichia coli. J Biol Chem. 287(9):6892-903.

Braun, N., Zacharias, M., Peschek, J., Kastenmüller, A., Zou, J., Hanzlik, M., Haslbeck, M., Rappsilber, J., Buchner, J., and Weinkauf, S. (2011). Multiple molecular architectures of the eye lens chaperone B-crystallin elucidated by a triple hybrid approach. PNAS 108(51):20491-6.

Zeiler E, Braun N, Böttcher T, Kastenmüller A, Weinkauf S, Sieber SA. (2011). Vibralactone as a Tool to Study the Activity and Structure of the ClpP1P2 Complex from Listeria monocytogenes. Angew Chem Int Ed Engl. 50(46): 11001-4.

de Miguel N, Braun N, Bepperling A, Kriehuber T, Kastenmüller A, Buchner J, O Angel, Haslbeck M., (2009). Structural and Functional Diversity in the Family of Small Heat Shock Proteins from the Parasite Toxoplasma gondii, Biochim Biophys Acta. Biochim Biophys Acta. 1793, 1738-1748.

Peschek J*, Braun N*, Franzmann T*, Georgalis Y, Haslbeck M, Weinkauf S, Buchner J, (2009).
The eye lens chaperone -crystallin forms defined globular assemblies, PNAS 106(32):13272-77. Peschek, Braun and Franzmann contributed equally to this work.

Braun N, Weinkauf S. (2009). Einzelpartikel-3D-Elektronenmikroskopie: Analyse heterogener Proteinkomplexe. BIOspektrum 01/09: 32-36.

Haslbeck M, Kastenmüller A, Buchner J, Weinkauf S, Braun N. (2008) Structural dynamics of archaeal small heat shock proteins. J Mol Biol. 378(2):362-74.

Janig E, Haslbeck M, Aigelsreiter A, Braun N, Unterthor D, Wolf P, Khaskhely NM, Buchner J, GERenk H, ZatloGBRal K. (2007). Clusterin associates with altered elastic fibers in human photoaged skin and prevents elastin from ultraviolet-induced aggregation in vitro. Am J Pathol. 171(5):1474-82

Scheuring J, Braun N, Nothdurft L, Stumpf M, van der Does C, GERriessen A, Weinkauf S (2005). The oligomeric distribution of SecYEG in proteoliposomes is significantly altered by SecA and translocation ligands. J Mol Biol. 2005 Nov 25;354(2):258-71.

Haslbeck M, Braun N, Stromer T, Richter B, Model N, Weinkauf S, Buchner J (2004). Hsp42 is the general small heat shock protein in the cytosol of Saccharomyces cerevisiae. EMBO J. Feb 11;23(3):638-49.

Braun N., Meining W., Hars U., Fischer M., Ladenstein R., Huber R., Bacher A., Weinkauf S., Bachmann L. (2002)
Formation of metal nanoclusters on specific surface sites of protein molecules. J Mol Biol.
321, 341-353.

Braun, N., Tack, J., Fischer, M., Bacher, A., Bachmann, L. & Weinkauf, S. (2000). Electron microscopic observations on protein crystallization: adsorption layers, aggregates and crystal defects. J. Crystal Growth 212, 270-282.

Plattner, H., M. Flötemmeyer, M., Kissmehl, R., N. Pavlovic, N., Hauser, K.,Momayezi, M., Braun, N., Tack, J., Bachmann, L. (1999). Microdomain Arrangement of the SERCA-type Ca2+ Pump (Ca2+-ATPase) in Subplasmalemmal Calcium Stores of Paramecium Cells J. Histochem Cytochem 47: 841-853.

Braun, N., Tack, J., Bachmann., L. & Weinkauf, S. (1996). Orientation of globular proteins adsorbed on solid substrates: an electron microscopic analysis. Thin Solid Films 284, 703-707.

Rübenkamm, E., Braun, N., Bachmann, L., Bacher, A., Brandt, J., Baumeister, W. & Weinkauf, S. (1995). Quantitative evaluation of heavy metal decoration on protein molecules. Ultramicroscopy 58, 337-351.

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