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Items: 17


Proteome Profiling of the Rhodobacter capsulatus Molybdenum Response Reveals a Role of IscN in Nitrogen Fixation by Fe-Nitrogenase.

Hoffmann MC, Wagner E, Langklotz S, Pfänder Y, Hött S, Bandow JE, Masepohl B.

J Bacteriol. 2015 Dec 7;198(4):633-43. doi: 10.1128/JB.00750-15.


Activation of RidA chaperone function by N-chlorination.

Müller A, Langklotz S, Lupilova N, Kuhlmann K, Bandow JE, Leichert LI.

Nat Commun. 2014 Dec 17;5:5804. doi: 10.1038/ncomms6804.


Chromophore composition of the phycobiliprotein Cr-PC577 from the cryptophyte Hemiselmis pacifica.

Overkamp KE, Langklotz S, Aras M, Helling S, Marcus K, Bandow JE, Hoef-Emden K, Frankenberg-Dinkel N.

Photosynth Res. 2014 Dec;122(3):293-304. doi: 10.1007/s11120-014-0029-1. Epub 2014 Aug 19.


Short antibacterial peptides with significantly reduced hemolytic activity can be identified by a systematic L-to-D exchange scan of their amino acid residues.

Albada HB, Prochnow P, Bobersky S, Langklotz S, Bandow JE, Metzler-Nolte N.

ACS Comb Sci. 2013 Nov 11;15(11):585-92. doi: 10.1021/co400072q. Epub 2013 Oct 30.


Differential control of Salmonella heat shock operons by structured mRNAs.

Cimdins A, Roßmanith J, Langklotz S, Bandow JE, Narberhaus F.

Mol Microbiol. 2013 Aug;89(4):715-31. doi: 10.1111/mmi.12308. Epub 2013 Jul 11.


Analysis of the mechanism of action of potent antibacterial hetero-tri-organometallic compounds: a structurally new class of antibiotics.

Wenzel M, Patra M, Senges CH, Ott I, Stepanek JJ, Pinto A, Prochnow P, Vuong C, Langklotz S, Metzler-Nolte N, Bandow JE.

ACS Chem Biol. 2013 Jul 19;8(7):1442-50. doi: 10.1021/cb4000844. Epub 2013 Apr 26.


FtsH-mediated coordination of lipopolysaccharide biosynthesis in Escherichia coli correlates with the growth rate and the alarmone (p)ppGpp.

Schäkermann M, Langklotz S, Narberhaus F.

J Bacteriol. 2013 May;195(9):1912-9. doi: 10.1128/JB.02134-12. Epub 2013 Feb 15.


Tuning the activity of a short arg-trp antimicrobial Peptide by lipidation of a C- or N-terminal lysine side-chain.

Albada HB, Prochnow P, Bobersky S, Langklotz S, Schriek P, Bandow JE, Metzler-Nolte N.

ACS Med Chem Lett. 2012 Sep 4;3(12):980-4. doi: 10.1021/ml300148v. eCollection 2012 Dec 13.


Silyl-based alkyne-modifying linker for the preparation of C-terminal acetylene-derivatized protected peptides.

Strack M, Langklotz S, Bandow JE, Metzler-Nolte N, Albada HB.

J Org Chem. 2012 Nov 16;77(22):9954-8. doi: 10.1021/jo302305d. Epub 2012 Nov 8.


A trapping approach reveals novel substrates and physiological functions of the essential protease FtsH in Escherichia coli.

Westphal K, Langklotz S, Thomanek N, Narberhaus F.

J Biol Chem. 2012 Dec 14;287(51):42962-71. doi: 10.1074/jbc.M112.388470. Epub 2012 Oct 22.


Structure and function of the bacterial AAA protease FtsH.

Langklotz S, Baumann U, Narberhaus F.

Biochim Biophys Acta. 2012 Jan;1823(1):40-8. doi: 10.1016/j.bbamcr.2011.08.015. Epub 2011 Sep 8. Review.


The Escherichia coli replication inhibitor CspD is subject to growth-regulated degradation by the Lon protease.

Langklotz S, Narberhaus F.

Mol Microbiol. 2011 Jun;80(5):1313-25. doi: 10.1111/j.1365-2958.2011.07646.x. Epub 2011 Apr 6.


Control of lipopolysaccharide biosynthesis by FtsH-mediated proteolysis of LpxC is conserved in enterobacteria but not in all gram-negative bacteria.

Langklotz S, Schäkermann M, Narberhaus F.

J Bacteriol. 2011 Mar;193(5):1090-7. doi: 10.1128/JB.01043-10. Epub 2010 Dec 30.


Degradation of cytoplasmic substrates by FtsH, a membrane-anchored protease with many talents.

Narberhaus F, Obrist M, Führer F, Langklotz S.

Res Microbiol. 2009 Nov;160(9):652-9. doi: 10.1016/j.resmic.2009.08.011. Epub 2009 Sep 8. Review.


Region C of the Escherichia coli heat shock sigma factor RpoH (sigma 32) contains a turnover element for proteolysis by the FtsH protease.

Obrist M, Langklotz S, Milek S, Führer F, Narberhaus F.

FEMS Microbiol Lett. 2009 Jan;290(2):199-208. doi: 10.1111/j.1574-6968.2008.01423.x. Epub 2008 Nov 13.


Sequence and length recognition of the C-terminal turnover element of LpxC, a soluble substrate of the membrane-bound FtsH protease.

Führer F, Müller A, Baumann H, Langklotz S, Kutscher B, Narberhaus F.

J Mol Biol. 2007 Sep 14;372(2):485-96. Epub 2007 Jul 3.


The C-terminal end of LpxC is required for degradation by the FtsH protease.

Führer F, Langklotz S, Narberhaus F.

Mol Microbiol. 2006 Feb;59(3):1025-36.

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