Affiliation: Frankfurt am Main
- Intracellular localization of the 90 kDA heat shock protein (HSP90alpha) determined by expression of a EGFP-HSP90alpha-fusion protein in unstressed and heat stressed 3T3 cellsThomas Langer
Institut für Biochemie und Biophysikalische Chemie der Johann Wolfgang Goethe Universität Frankfurt am Main, Marie Curie Str 9, 60439 Frankfurt am Main, Germany
Cell Biol Int 27:47-52. 2003..As the most remarkable finding under these conditions, an association of EGFP-Hsp90alpha with the nuclear membrane became visible...
- Folding and activity of cAMP-dependent protein kinase mutantsThomas Langer
Johann Wolfgang Goethe University Frankfurt, Institute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance, Marie Curie Strasse 11, D 60439 Frankfurt am Main, Germany
FEBS Lett 579:4049-54. 2005..These proteins can be expressed in high yields but have reduced activity compared to the wild-type. Proper folding of all proteins was analyzed by 2D 1H, 15N-TROSY NMR experiments...
- NMR backbone assignment of a protein kinase catalytic domain by a combination of several approaches: application to the catalytic subunit of cAMP-dependent protein kinaseThomas Langer
Johann Wolfgang Goethe Universitat Frankfurt, Institute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance, Marie Curie Strasse 11, 60439 Frankfurt am Main, Germany
Chembiochem 5:1508-16. 2004..Furthermore, structural conformational changes were observed by comparison of backbone amide shifts obtained by 2D (1)H,(15)N TROSY of an inactive Thr197Ala mutant with the wild-type enzyme...
- NMR characterization of kinase p38 dynamics in free and ligand-bound formsMartin Vogtherr
Johann Wolfgang Goethe-University Frankfurt, Institute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance, Germany
Angew Chem Int Ed Engl 45:993-7. 2006
- How much NMR data is required to determine a protein-ligand complex structure?Ulrich Schieborr
Institute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance, Johann Wolfgang Goethe Universitat Frankfurt, Marie Curie Strasse 11, 60439 Frankfurt am Main, Germany
Chembiochem 6:1891-8. 2005....
- The human Cdc37.Hsp90 complex studied by heteronuclear NMR spectroscopySridhar Sreeramulu
Institute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance, Johann Wolfgang Goethe University, Max von Laue Strasse 7, Frankfurt am Main D 60438, Germany
J Biol Chem 284:3885-96. 2009..NMR and mutagenesis experiments reveal Leu-205 in Cdc37 as a key residue enabling complex formation. These findings can be very useful in the development of small molecule inhibitors against cancer...
- A novel function for the 90 kDa heat-shock protein (Hsp90): facilitating nuclear export of 60 S ribosomal subunitsHarald Schlatter
, , Marie Curie-Str. 9, 60439 Frankfurt am Main, Germany
Biochem J 362:675-84. 2002..These findings suggest that Hsp90 facilitates the nuclear export of 60 S ribosomal subunits, probably by chaperoning protein interactions during the export process...
- 1H, 13C and 15N backbone resonance assignment of the integrin alpha2 I-domainBettina Elshorst
Johann Wolfgang Goethe-University Frankfurt, Institute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance, Marie-Curie-Strasse 11, D-60439 Frankfurt am Main, Germany
J Biomol NMR 27:191-2. 2003
- Backbone NMR assignment of the C-terminal haemopexin-like domain (HPLD) of human matrix metalloproteinase MMP-13Doris M Jacobs
J Biomol NMR 32:337. 2005
- 1H, 13C and 15N backbone resonance assignment of the peptidyl-prolyl cis-trans isomerase Pin1Doris M Jacobs
J Biomol NMR 23:163-4. 2002
- NMR analysis of a Tau phosphorylation patternIsabelle Landrieu
CNRS UMR 8525, Institut Pasteur de Lille, 59019 Lille Cedex, France
J Am Chem Soc 128:3575-83. 2006..We finally demonstrate that the NMR approach can equally be used to evaluate potential kinase inhibitors in a straightforward manner...
- Variable and tissue-specific subunit composition of mitochondrial m-AAA protease complexes linked to hereditary spastic paraplegiaMirko Koppen
Institut fur Genetik, Universitat zu Koln, Zulpicher Strasse, 0674 Köln, Germany
Mol Cell Biol 27:758-67. 2007..We therefore propose that the formation of m-AAA proteases with altered substrate specificities leads to axonal degeneration in HSP...
- NMR backbone assignment of the N-terminal domain of human HSP90Doris M Jacobs
, , , Max-von-Laue-Str. 7, Building N160, Room 314, D-60439, Frankfurt am Main, Germany
J Biomol NMR 36:52. 2006
- m-AAA protease-driven membrane dislocation allows intramembrane cleavage by rhomboid in mitochondriaTakashi Tatsuta
Institute for Genetics and Center for Molecular Medicine CMMC, University of Cologne, Cologne, Germany
EMBO J 26:325-35. 2007..These findings reveal for the first time a non-proteolytic function of the m-AAA protease during mitochondrial biogenesis and rationalise the requirement of a preceding step for intramembrane cleavage by rhomboid...
- Substrate recognition by AAA+ ATPases: distinct substrate binding modes in ATP-dependent protease Yme1 of the mitochondrial intermembrane spaceMartin Graef
Institut fur Genetik, Universitat zu Koln, Zulpicher Strasse 47, 50674 Koln, Germany
Mol Cell Biol 27:2476-85. 2007..Our findings therefore reveal the existence of alternative substrate recognition pathways within AAA proteases and shed new light on molecular mechanisms ensuring the specificity of proteolysis by energy-dependent proteases...
- Regulation of mitochondrial fusion by the F-box protein Mdm30 involves proteasome-independent turnover of Fzo1Mafalda Escobar-Henriques
Institute of Genetics and Center for Molecular Medicine, University of Cologne, D 50923 Cologne, Germany
J Cell Biol 173:645-50. 2006....
- Translating m-AAA protease function in mitochondria to hereditary spastic paraplegiaElena I Rugarli
Istituto Nazionale Neurologico C. Besta, Division of Biochemistry and Genetics, 20126 Milan, Italy
Trends Mol Med 12:262-9. 2006..Here, we will discuss implications of the dual role of the m-AAA protease in protein activation and degradation for mitochondrial dysfunction and axonal degeneration...
- OPA1 processing reconstituted in yeast depends on the subunit composition of the m-AAA protease in mitochondriaStéphane Duvezin-Caubet
Institute for Physiological Chemistry, Ludwig Maximilians University, 81377 Munich, Germany
Mol Biol Cell 18:3582-90. 2007....
- Nonredundant roles of mitochondria-associated F-box proteins Mfb1 and Mdm30 in maintenance of mitochondrial morphology in yeastMark Dürr
Institut fur Zellbiologie, Universitat Bayreuth, 95440 Bayreuth, Germany
Mol Biol Cell 17:3745-55. 2006..We propose that mitochondria-associated F-box proteins Mfb1 and Mdm30 are key components of a complex machinery that regulates mitochondrial dynamics throughout yeast's entire life cycle...
- Substrate specific consequences of central pore mutations in the i-AAA protease Yme1 on substrate engagementMartin Graef
Institute for Genetics and Center for Molecular Medicine, CMMC, University of Cologne, Cologne, Germany
J Struct Biol 156:101-8. 2006..Our findings therefore suggest an essential function of the central pore loop for the ATP-dependent translocation of membrane proteins into a proteolytic cavity formed by AAA proteases...
- Using wavelet de-noised spectra in NMR screeningNikola Trbovic
Center for Biomolecular Magnetic Resonance (BMRZ, Institute of Biophysical Chemistry, J.W. Goethe University, Marie-Curie-Str. 9, 60439 Frankfurt, Germany
J Magn Reson 173:280-7. 2005..The combination of wavelet de-noising and PCA is most efficient when PCA is applied to wavelet coefficients. This new algorithm yields good clustering and can be applied to series of one- or two-dimensional spectra...
- Reversible assembly of the ATP-binding cassette transporter Mdl1 with the F1F0-ATP synthase in mitochondriaDominik Galluhn
, , , Germany
J Biol Chem 279:38338-45. 2004..These results are consistent with an activation of Mdl1 upon dissociation from the ATP synthase and suggest a link of peptide export from mitochondria to the activity of the F(1)F(0)-ATP synthase and the cellular energy metabolism...
- Membrane protein turnover by the m-AAA protease in mitochondria depends on the transmembrane domains of its subunitsDaniel Korbel
Institut fur Genetik, Universitat zu Koln, Zulpicher Strasse 47, 50674 Koln, Germany
EMBO Rep 5:698-703. 2004..We therefore propose that transmembrane segments of m-AAA protease subunits have a direct role in the dislocation of membrane-embedded substrates...
- NMR backbone assignment of the mitogen-activated protein (MAP) kinase p38Martin Vogtherr
J Biomol NMR 32:175. 2005
- 1H, 13C and 15N backbone resonance assignment of the Hsp90 binding domain of human Cdc37Sridhar Sreeramulu
J Biomol NMR 32:262. 2005
- Discovery of Mycobacterium tuberculosis protein tyrosine phosphatase A (MptpA) inhibitors based on natural products and a fragment-based approachMichael Manger
, Abteilung Chemische Biologie, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany
Chembiochem 6:1749-53. 2005
- Backbone NMR assignment of the human E2 ubiquitin conjugating enzyme UbcH5alpha (F72K,F82S) double mutantKrishna Saxena
J Biomol NMR 32:338. 2005
- Backbone NMR assignment of the low-molecular-weight protein tyrosine phosphatase (MPtpA) from Mycobacterium tuberculosisKrishna Saxena
J Biomol NMR 33:136. 2005
- Formation of membrane-bound ring complexes by prohibitins in mitochondriaTakashi Tatsuta
Institut für Genetik and Zentrum für Molekulare Medizin, Universitat zu Koln, 50674 Koln, Germany
Mol Biol Cell 16:248-59. 2005..Implications of these findings for proposed cellular activities of prohibitins are discussed...