| Freitag A, Khilji SK, Nedielkov R, M Kumar S, Krummhaar M, Arndt J, Moreira GMSG, Lühle J, Goerdeler F, Kamphues C, Mroginski MA, Roth C, Seeberger PH, Möller HM and Moscovitz O (2026), "Integrative Approach to Develop and Characterize Antibodies against the Cancer-Associated Antigen Sialyl Lewis A (CA 19-9)", JACS Au., April, 2026. American Chemical Society (ACS). |
BibTeX:
@article{Freitag2026,
author = {Freitag, Anika and Khilji, Sana K. and Nedielkov, Ruslan and M Kumar, Shalini and Krummhaar, Michael and Arndt, Janine and Moreira, Gustavo M. S. G. and Lühle, Jost and Goerdeler, Felix and Kamphues, Carsten and Mroginski, Maria A. and Roth, Christian and Seeberger, Peter H. and Möller, Heiko M. and Moscovitz, Oren},
title = {Integrative Approach to Develop and Characterize Antibodies against the Cancer-Associated Antigen Sialyl Lewis A (CA 19-9)},
journal = {JACS Au},
publisher = {American Chemical Society (ACS)},
year = {2026},
doi = {10.1021/jacsau.5c01596}
}
|
| Freitag A, Khilji SK, Nedielkov R, Kumar SM, Krummhaar M, Arndt J, Garcia Moreira GMS, Luhle J, Goerdeler F, Kamphues C, Mroginski MA, Roth C, Seeberger PH, Moller HM and Moscovitz O (2025), "An Integrative Approach to Develop and Characterise Antibodies Against the Cancer Associated Antigen Sialyl Lewis A (CA 19-9)", bioRxiv., June, 2025. |
BibTeX:
@article{Freitag2025,
author = {Freitag, Anika and Khilji, Sana Khan and Nedielkov, Ruslan and Kumar, Shalini Murali and Krummhaar, Michael and Arndt, Janine and Garcia Moreira, Gustavo Marçal Schmidt and Luhle, Jost and Goerdeler, Felix and Kamphues, Carsten and Mroginski, Maria Andrea and Roth, Christian and Seeberger, Peter H. and Moller, Heiko M. and Moscovitz, Oren},
title = {An Integrative Approach to Develop and Characterise Antibodies Against the Cancer Associated Antigen Sialyl Lewis A (CA 19-9)},
journal = {bioRxiv},
year = {2025},
doi = {10.1101/2025.06.15.659274}
}
|
| Perevedentseva Y, Waurick L, Marlina D, Techert G, Müllers Y, Lederer F, Möller H, Kumke M, Glebe U and Drobot B (2025), "An integrative approach towards bio-inspired sequestration of rare earth elements", ChemRxiv., December, 2025. |
BibTeX:
@article{Perevedentseva2025,
author = {Perevedentseva, Yulia and Waurick, Lukas and Marlina, Dini and Techert, Gerda and Müllers, Yannic and Lederer, Franziska and Möller, Heiko and Kumke, Michael and Glebe, Ulrich and Drobot, Björn},
title = {An integrative approach towards bio-inspired sequestration of rare earth elements},
journal = {ChemRxiv},
year = {2025},
doi = {10.26434/chemrxiv-2025-lrfbx}
}
|
| Richtsmeier P, Nedielkov R, Haring M, Yücel O, Elsner L, Lülf RH, Wöhlbrand L, Rabus R, Moeller H, Philipp B and Mueller FM (2025), "7β-Hydroxysteroid dehydratase Hsh3 eliminates the 7-hydroxy group of the bile salt ursodeoxycholate during degradation by Sphingobium sp. strain Chol11 and other Sphingomonadaceae", Applied and Environmental Microbiology., June, 2025. Vol. 91(6) American Society for Microbiology. |
BibTeX:
@article{Richtsmeier2025,
author = {Richtsmeier, Phil and Nedielkov, Ruslan and Haring, Malte and Yücel, Onur and Elsner, Lea and Lülf, Rebekka Herdis and Wöhlbrand, Lars and Rabus, Ralf and Moeller, Heiko and Philipp, Bodo and Mueller, Franziska Maria},
editor = {Nikel, Pablo Ivan},
title = {7β-Hydroxysteroid dehydratase Hsh3 eliminates the 7-hydroxy group of the bile salt ursodeoxycholate during degradation by Sphingobium sp. strain Chol11 and other Sphingomonadaceae},
journal = {Applied and Environmental Microbiology},
publisher = {American Society for Microbiology},
year = {2025},
volume = {91},
number = {6},
doi = {10.1128/aem.00185-25}
}
|
| Steinbrecher R, Lehmann F, Nedielkov R, Klamroth T, Möller H, Taubert A, Hinderberger D, Müller-Buschbaum P, Papadakis CM and Laschewsky A (2025), "Toward Fully Photoresponsive Amphiphilic Polymers via Azopyrazole-Functionalized Polyacrylamides", Macromolecules., October, 2025. Vol. 58(20), pp. 11088-11098. American Chemical Society (ACS). |
BibTeX:
@article{Steinbrecher2025,
author = {Steinbrecher, René and Lehmann, Florian and Nedielkov, Ruslan and Klamroth, Tillmann and Möller, Heiko and Taubert, Andreas and Hinderberger, Dariush and Müller-Buschbaum, Peter and Papadakis, Christine M. and Laschewsky, André},
title = {Toward Fully Photoresponsive Amphiphilic Polymers via Azopyrazole-Functionalized Polyacrylamides},
journal = {Macromolecules},
publisher = {American Chemical Society (ACS)},
year = {2025},
volume = {58},
number = {20},
pages = {11088--11098},
doi = {10.1021/acs.macromol.5c01176}
}
|
| Baade T, Michaelis M, Prestel A, Paone C, Klishin N, Herbinger M, Scheinost L, Nedielkov R, Hauck CR and Möller HM (2024), "A flexible loop in the paxillin LIM3 domain mediates its direct binding to integrin β subunits", PLOS Biology., September, 2024. Vol. 22(9), pp. e3002757. Public Library of Science (PLoS). |
BibTeX:
@article{Baade2024,
author = {Baade, Timo and Michaelis, Marcus and Prestel, Andreas and Paone, Christoph and Klishin, Nikolai and Herbinger, Marleen and Scheinost, Laura and Nedielkov, Ruslan and Hauck, Christof R. and Möller, Heiko M.},
editor = {Parent, Carole A.},
title = {A flexible loop in the paxillin LIM3 domain mediates its direct binding to integrin β subunits},
journal = {PLOS Biology},
publisher = {Public Library of Science (PLoS)},
year = {2024},
volume = {22},
number = {9},
pages = {e3002757},
doi = {10.1371/journal.pbio.3002757}
}
|
| Martin J, Michaelis M, Petrović S, Lehnen A, Müllers Y, Wendler P, Möller HM, Hartlieb M and Glebe U (2024), "Application of Sortase‐Mediated Ligation for the Synthesis of Block Copolymers and Protein‐Polymer Conjugates", Macromolecular Bioscience., October, 2024. Vol. 25(1) Wiley. |
BibTeX:
@article{Martin2024,
author = {Martin, Johannes and Michaelis, Marcus and Petrović, Saša and Lehnen, Anne‐Catherine and Müllers, Yannic and Wendler, Petra and Möller, Heiko M. and Hartlieb, Matthias and Glebe, Ulrich},
title = {Application of Sortase‐Mediated Ligation for the Synthesis of Block Copolymers and Protein‐Polymer Conjugates},
journal = {Macromolecular Bioscience},
publisher = {Wiley},
year = {2024},
volume = {25},
number = {1},
doi = {10.1002/mabi.202400316}
}
|
| Piemontese E, Herfort A, Perevedentseva Y, Möller HM and Seitz O (2024), "Multiphosphorylation-Dependent Recognition of Anti-pS2 Antibodies against RNA Polymerase II C-Terminal Domain Revealed by Chemical Synthesis", Journal of the American Chemical Society., April, 2024. Vol. 146(17), pp. 12074-12086. American Chemical Society (ACS). |
BibTeX:
@article{Piemontese2024,
author = {Piemontese, Emanuele and Herfort, Alina and Perevedentseva, Yulia and Möller, Heiko M. and Seitz, Oliver},
title = {Multiphosphorylation-Dependent Recognition of Anti-pS2 Antibodies against RNA Polymerase II C-Terminal Domain Revealed by Chemical Synthesis},
journal = {Journal of the American Chemical Society},
publisher = {American Chemical Society (ACS)},
year = {2024},
volume = {146},
number = {17},
pages = {12074--12086},
doi = {10.1021/jacs.4c01902}
}
|
| Baade T, Michaelis M, Prestel A, Paone C, Klishin N, Scheinost L, Nedielkov R, Hauck CR and Möller HM (2023), "A flexible loop in the paxillin LIM3 domain mediates direct binding to integrin β3", jan, 2023. Cold Spring Harbor Laboratory. |
BibTeX:
@article{Baade2023,
author = {Timo Baade and Marcus Michaelis and Andreas Prestel and Christoph Paone and Nikolai Klishin and Laura Scheinost and Ruslan Nedielkov and Christof R. Hauck and Heiko M. Möller},
title = {A flexible loop in the paxillin LIM3 domain mediates direct binding to integrin β3},
publisher = {Cold Spring Harbor Laboratory},
year = {2023},
doi = {10.1101/2023.01.26.525744}
}
|
| Goerdeler F, Reuber EE, Lühle J, Leichnitz S, Freitag A, Nedielkov R, Groza R, Ewers H, Möller HM, Seeberger PH and Moscovitz O (2023), "Thiol-Mediated Uptake of a Cysteine-Containing Nanobody for Anticancer Drug Delivery", ACS Central Science., may, 2023. American Chemical Society (ACS). |
BibTeX:
@article{Goerdeler2023,
author = {Felix Goerdeler and Emelie E. Reuber and Jost Lühle and Sabrina Leichnitz and Anika Freitag and Ruslan Nedielkov and Raluca Groza and Helge Ewers and Heiko M. Möller and Peter H. Seeberger and Oren Moscovitz},
title = {Thiol-Mediated Uptake of a Cysteine-Containing Nanobody for Anticancer Drug Delivery},
journal = {ACS Central Science},
publisher = {American Chemical Society (ACS)},
year = {2023},
doi = {10.1021/acscentsci.3c00177}
}
|
| Oloya B, Namukobe J, Heydenreich M, Ssengooba W, Martin J, Möller HM, Schmidt B and Byamukama R (2023), "Two new compounds and the anti-mycobacterial activity of the constituents from Zanthoxylum leprieurii root bark", Phytochemistry Letters., apr, 2023. Vol. 54, pp. 107-113. Elsevier BV. |
BibTeX:
@article{Oloya2023,
author = {Benson Oloya and Jane Namukobe and Matthias Heydenreich and Willy Ssengooba and Johannes Martin and Heiko Michael Möller and Bernd Schmidt and Robert Byamukama},
title = {Two new compounds and the anti-mycobacterial activity of the constituents from Zanthoxylum leprieurii root bark},
journal = {Phytochemistry Letters},
publisher = {Elsevier BV},
year = {2023},
volume = {54},
pages = {107--113},
doi = {10.1016/j.phytol.2023.02.002}
}
|
| Madani A, Anghileri L, Heydenreich M, Moller HM and Pieber* B (2022), "Benzylic Fluorination Induced by a Charge-Transfer Complex with a Solvent-Dependent Selectivity Switch", Org Lett. Vol. 24(29), pp. 5376-5380. |
| Abstract: We present a divergent strategy for the fluorination of phenylacetic acid derivatives that is induced by a charge-transfer complex between Selectfluor and 4-(dimethylamino)pyridine. A comprehensive investigation of the conditions revealed a critical role of the solvent on the reaction outcome. In the presence of water, decarboxylative fluorination through a single-electron oxidation is dominant. Non-aqueous conditions result in the clean formation of alpha-fluoro-alpha-arylcarboxylic acids. |
BibTeX:
@article{Madani2022,
author = {Madani, A. and Anghileri, L. and Heydenreich, M. and Moller, H. M. and Pieber*, B.},
title = {Benzylic Fluorination Induced by a Charge-Transfer Complex with a Solvent-Dependent Selectivity Switch},
journal = {Org Lett},
year = {2022},
volume = {24},
number = {29},
pages = {5376--5380},
doi = {10.1021/acs.orglett.2c02050}
}
|
| Feller FM, Eilebrecht S, Nedielkov R, Yucel O, Alvincz J, Salinas G, Ludwig KC, Möller H and Philipp* B (2021), "Investigations on the Degradation of the Bile Salt Cholate via the 9,10-Seco-Pathway Reveals the Formation of a Novel Recalcitrant Steroid Compound by a Side Reaction in Sphingobium sp. Strain Chol11", Microorganisms. Vol. 9(10) |
| Abstract: Bile salts such as cholate are steroid compounds from the digestive tracts of vertebrates, which enter the environment upon excretion, e.g., in manure. Environmental bacteria degrade bile salts aerobically via two pathway variants involving intermediates with Delta(1,4)- or Delta(4,6)-3-keto-structures of the steroid skeleton. Recent studies indicated that degradation of bile salts via Delta(4,6)-3-keto intermediates in Sphingobium sp. strain Chol11 proceeds via 9,10-seco cleavage of the steroid skeleton. For further elucidation, the presumptive product of this cleavage, 3,12beta-dihydroxy-9,10-seco-androsta-1,3,5(10),6-tetraene-9,17-dione (DHSATD), was provided to strain Chol11 in a co-culture approach with Pseudomonas stutzeri Chol1 and as purified substrate. Strain Chol11 converted DHSATD to the so far unknown compound 4-methyl-3-deoxy-1,9,12-trihydroxyestra-1,3,5(10)7-tetraene-6,17-dione (MDTETD), presumably in a side reaction involving an unusual ring closure. MDTETD was neither degraded by strains Chol1 and Chol11 nor in enrichment cultures. Functional transcriptome profiling of zebrafish embryos after exposure to MDTETD identified a significant overrepresentation of genes linked to hormone responses. In both pathway variants, steroid degradation intermediates transiently accumulate in supernatants of laboratory cultures. Soil slurry experiments indicated that bacteria using both pathway variants were active and also released their respective intermediates into the environment. This instance could enable the formation of recalcitrant steroid metabolites by interspecies cross-feeding in agricultural soils. |
BibTeX:
@article{Feller2021,
author = {Feller, F. M. and Eilebrecht, S. and Nedielkov, R. and Yucel, O. and Alvincz, J. and Salinas, G. and Ludwig, K. C. and Möller, H. and Philipp*, B.},
title = {Investigations on the Degradation of the Bile Salt Cholate via the 9,10-Seco-Pathway Reveals the Formation of a Novel Recalcitrant Steroid Compound by a Side Reaction in Sphingobium sp. Strain Chol11},
journal = {Microorganisms},
year = {2021},
volume = {9},
number = {10},
doi = {10.3390/microorganisms9102146}
}
|
| Samaha D, Hamdo HH, Cong X, Schumacher F, Banhart S, Aglar Ö, Möller HM, Heuer D, Kleuser B, Saied EM and Arenz C (2020), "Liposomal FRET Assay Identifies Potent Drug-Like Inhibitors of the Ceramide Transport Protein (CERT)", Chemistry – A European Journal., nov, 2020. Vol. 26(70), pp. 16616-16621. Wiley. |
| Abstract: Ceramide transfer protein (CERT) mediates non- the past from cell lysates or with purified enzymes, at the ex-
vesicular transfer of ceramide from endoplasmic reticulum pense of topological information. While topological consider- to Golgi apparatus and thus catalyzes the rate-limiting ations may be simple for pathways converting soluble sub- step of sphingomyelin biosynthesis. Usually, CERT ligands strates, they are crucial and complex for lipid substrates. By are evaluated in tedious binding assays or non-homoge- definition, lipids are not water-soluble and transitions between nous transfer assays using radiolabeled ceramides. Herein, different membranes require either complex vesicular transport a facile and sensitive assay for CERT, based on Fçrster res- mechanisms or specific transport proteins.[1] Like many other onance energy transfer (FRET), is presented. To this end, biosynthetic pathways, the biosynthesis of sphingolipids ex- we mixed donor and acceptor vesicles, each containing a tends throughout the membranes of different organelles, different fluorescent ceramide species. By CERT-mediated which makes specific transport processes essential compo- transfer of fluorescent ceramide, a FRET system was estab- nents of the individual pathway.[2] A growing body of evidence lished, which allows readout in 96-well plate format, de- suggests that such transport processes are the rate-limiting spite the high hydrophobicity of the components. Screen- steps of the whole sphingolipid biosynthetic pathway and ing of a 2 000 compound library resulted in two new sphingolipid transport proteins are now considered as pharma- potent CERT inhibitors. One is approved for use in cological target molecules.[3] |
BibTeX:
@article{Samaha2020,
author = {Doaa Samaha and Housam H. Hamdo and Xiaojing Cong and Fabian Schumacher and Sebastian Banhart and Öznur Aglar and Heiko M. Möller and Dagmar Heuer and Burkhard Kleuser and Essa M. Saied and Christoph Arenz},
title = {Liposomal FRET Assay Identifies Potent Drug-Like Inhibitors of the Ceramide Transport Protein (CERT)},
journal = {Chemistry – A European Journal},
publisher = {Wiley},
year = {2020},
volume = {26},
number = {70},
pages = {16616--16621},
doi = {10.1002/chem.202003283}
}
|
| Buyinza D, Yang LJ, Derese S, Ndakala A, Coghi P, Heydenreich M, Wong* VKW, Möller HM and Yenesew* A (2019), "Cytotoxicity of isoflavones from Millettia dura", Natural Product Research. , pp. 1-4. |
BibTeX:
@article{Buyinza2019,
author = {Buyinza, Daniel and Yang, Li Jun and Derese, Solomon and Ndakala, Albert and Coghi, Paolo and Heydenreich, Matthias and Wong*, Vincent Kam Wai and Möller, Heiko M. and Yenesew*, Abiy},
title = {Cytotoxicity of isoflavones from Millettia dura},
journal = {Natural Product Research},
year = {2019},
pages = {1--4},
doi = {10.1080/14786419.2019.1660335}
}
|
| Toulouse C, Schmucker S, Metesch K, Pfannstiel J, Michel B, Starke I, Möller HM, Stefanski V and Steuber J (2019), "Mechanism and impact of catecholamine conversion by Vibrio cholerae", Biochimica et Biophysica Acta (BBA) - Bioenergetics., jun, 2019. Vol. 1860(6), pp. 478-487. Elsevier BV. |
| Abstract: Bacterial pathogens are influenced by signaling molecules including the catecholamines adrenaline and noradrenaline which are host-derived hormones and neurotransmitters. Adrenaline and noradrenaline modulate growth, motility and virulence of bacteria. We show that adrenaline is converted by the pathogen Vibrio cholerae to adrenochrome in the course of respiration, and demonstrate that superoxide produced by the respiratory, Na + − translocating NADH:quinone oxidoreductase (NQR) acts as electron acceptor in the oxidative conversion of adrenaline to adrenochrome. Adrenochrome stimulates growth of V. cholerae, and triggers specific responses in V. cholerae and in immune cells. We performed a quantitative proteome analysis of V. cholerae grown in minimal medium with glucose as carbon source without catecholamines, or with adrenaline, noradrenaline or adrenochrome. Significant regulation of proteins participating in iron transport and iron homeostasis, in energy metabolism, and in signaling was observed upon exposure to adrenaline, noradrenaline or adrenochrome. On the host side, adrenochrome inhibited lipopolysaccharide-triggered formation of TNF-α by THP-1 monocytes, though to a lesser extent than adrenaline. It is proposed that adrenochrome produced from adrenaline by respiring V. cholerae functions as effector molecule in pathogen-host interaction. |
BibTeX:
@article{Toulouse2019,
author = {Charlotte Toulouse and Sonja Schmucker and Kristina Metesch and Jens Pfannstiel and Bernd Michel and Ines Starke and Heiko M. Möller and Volker Stefanski and Julia Steuber},
title = {Mechanism and impact of catecholamine conversion by Vibrio cholerae},
journal = {Biochimica et Biophysica Acta (BBA) - Bioenergetics},
publisher = {Elsevier BV},
year = {2019},
volume = {1860},
number = {6},
pages = {478--487},
doi = {10.1016/j.bbabio.2019.04.003}
}
|
| Abbas IM, Vranic M, Hoffmann H, El-Khatib AH, Montes-Bayón M, Möller* HM and Weller* MG (2018), "Investigations of the Copper Peptide Hepcidin-25 by LC-MS/MS and NMR", International Journal of Molecular Sciences. Vol. 19(8), pp. 2271. |
BibTeX:
@article{Abbas2018,
author = {Abbas, Ioana M. and Vranic, Marija and Hoffmann, Holger and El-Khatib, Ahmed H. and Montes-Bayón, María and Möller*, Heiko M. and Weller*, Michael G.},
title = {Investigations of the Copper Peptide Hepcidin-25 by LC-MS/MS and NMR},
journal = {International Journal of Molecular Sciences},
year = {2018},
volume = {19},
number = {8},
pages = {2271},
doi = {10.3390/ijms19082271}
}
|
| Starke I, Koch A, Kammer S, Holdt H-J and Möller HM (2018), "Electrospray mass spectrometry and molecular modeling study of formation and stability of silver complexes with diazaperylene and bisisoquinoline", Journal of Mass Spectrometry., mar, 2018. Vol. 53(5), pp. 408-418. Wiley. |
| Abstract: The complex formation of the following diazaperylene ligands (L) 1,12-diazaperylene 1, 1,1′bisisoquinoline 2, 2,11-disubstituted 1,12-diazaperylenes (alkyl = methyl, ethyl, isopropyl, 3, 5, 7), 3,3′-disubstituted 1,1′-bisisoquinoline (alkyl = methyl, ethyl, isopropyl, 4, 6, 8 and with R = phenyl, 11 and with pyridine 12), and the 5,8-dimethoxy-substituted diazaperylene 9, 6,6′dimethoxy-substituted bisisoquinoline 10 with AgBF4 was investigated. Collision-induced dissociation measurements were used to evaluate the relative stabilities of the ligands themselves and for the [1:1] + complexes as well as for the homoleptic and heteroleptic silver [1:2] + complexes in the gas phase. This method is very useful in rapid screening of the stabilities of new complexes in the gas phase. The influence of the spatial arrangement of the ligands and the type of substituents employed for the complexation were examined. The effect of the preorganization of the diazaperylene on the threshold activation voltages and thus of the relative binding energies of the different complexes are discussed. Density functional theory calculations were used to calculate the optimized structures of the silver complexes and compared with the stabilities of the complexes in the gas phase for the first time. |
BibTeX:
@article{Starke2018,
author = {Ines Starke and Andreas Koch and Stefan Kammer and Hans-Jürgen Holdt and Heiko Michael Möller},
title = {Electrospray mass spectrometry and molecular modeling study of formation and stability of silver complexes with diazaperylene and bisisoquinoline},
journal = {Journal of Mass Spectrometry},
publisher = {Wiley},
year = {2018},
volume = {53},
number = {5},
pages = {408--418},
doi = {10.1002/jms.4071}
}
|
| Hildebrand V, Heydenreich M, Laschewsky* A, Möller HM, Müller-Buschbaum P, Papadakis CM, Schanzenbach D and Wischerhoff E (2017), "``Schizophrenic'' self-assembly of dual thermoresponsive block copolymers bearing a zwitterionic and a non-ionic hydrophilic block", Polymer. Vol. 122, pp. 347-357. |
BibTeX:
@article{Hildebrand2017,
author = {Hildebrand, Viet and Heydenreich, Matthias and Laschewsky*, André and Möller, Heiko M. and Müller-Buschbaum, Peter and Papadakis, Christine M. and Schanzenbach, Dirk and Wischerhoff, Erik},
title = {``Schizophrenic'' self-assembly of dual thermoresponsive block copolymers bearing a zwitterionic and a non-ionic hydrophilic block},
journal = {Polymer},
year = {2017},
volume = {122},
pages = {347--357},
doi = {10.1016/j.polymer.2017.06.063}
}
|
| Holert J, Yücel O, Jagman N, Prestel A, Möller HM and Philipp* B (2016), "Identification of bypass reactions leading to the formation of one central steroid degradation intermediate in metabolism of different bile salts in Pseudomonas sp. strain Chol1", Environ Microbiol. Vol. 18(10), pp. 3373-3389. |
BibTeX:
@article{Holert2016,
author = {Holert, J. and Yücel, O. and Jagman, N. and Prestel, A. and Möller, H. M. and Philipp*, B.},
title = {Identification of bypass reactions leading to the formation of one central steroid degradation intermediate in metabolism of different bile salts in Pseudomonas sp. strain Chol1},
journal = {Environ Microbiol},
year = {2016},
volume = {18},
number = {10},
pages = {3373--3389},
doi = {10.1111/1462-2920.13192}
}
|
| Maier SK, Poluektov G, Jester* S-S, Möller* HM and Höger* S (2016), "Fast Oxidative Cyclooligomerization towards Low- and High-Symmetry Thiophene Macrocycles", Chem Eur J. Vol. 22(4), pp. 1379-1384. |
BibTeX:
@article{Maier2016,
author = {Maier, S. K. and Poluektov, G. and Jester*, S.-S. and Möller*, H. M. and Höger*, S.},
title = {Fast Oxidative Cyclooligomerization towards Low- and High-Symmetry Thiophene Macrocycles},
journal = {Chem Eur J},
year = {2016},
volume = {22},
number = {4},
pages = {1379--1384},
doi = {10.1002/chem.201503211}
}
|
| Pavashe P, Elamparuthi E, Hettrich C, Möller HM and Linker* T (2016), "Correction to textquotedblSynthesis of 2-Thiocarbohydrates and Their Binding to Concanavalin Atextquotedbl", J Org Chem. |
BibTeX:
@article{Pavashe2016,
author = {Pavashe, P. and Elamparuthi, E. and Hettrich, C. and Möller, H. M. and Linker*, T.},
title = {Correction to textquotedblSynthesis of 2-Thiocarbohydrates and Their Binding to Concanavalin Atextquotedbl},
journal = {J Org Chem},
year = {2016},
doi = {10.1021/acs.joc.6b02308}
}
|
| Pavashe P, Elamparuthi E, Hettrich C, Möller HM and Linker* T (2016), "Synthesis of 2-Thiocarbohydrates and Their Binding to Concanavalin A", J Org Chem. Vol. 81(18), pp. 8595-8603. |
| Abstract: A convenient and general synthesis of 2-thiocarbohydrates via cerium ammonium nitrate oxidation of the thiocyanate ion is described. Radical addition to glycals proceeds with excellent regio- and good stereoselectivities in only one step, deprotection affords water-soluble 2-thio saccharides. Binding studies to Con A have been performed by isothermal titration calorimetry (ITC) and saturation transfer difference (STD) NMR spectroscopy. The 2-thiomannose derivative binds even stronger to Con A than the natural substrate, offering opportunities for new lectin or enzyme inhibitors. |
BibTeX:
@article{Pavashe2016a,
author = {Pavashe, P. and Elamparuthi, E. and Hettrich, C. and Möller, H. M. and Linker*, T.},
title = {Synthesis of 2-Thiocarbohydrates and Their Binding to Concanavalin A},
journal = {J Org Chem},
year = {2016},
volume = {81},
number = {18},
pages = {8595--8603},
doi = {10.1021/acs.joc.6b00987}
}
|
| Prestel A and Möller* HM (2016), "Spatio-temporal control of cellular uptake achieved by photoswitchable cell-penetrating peptides", Chem Commun. Vol. 52, pp. 701-704. |
BibTeX:
@article{Prestel2016,
author = {Prestel, A. and Möller*, H. M.},
title = {Spatio-temporal control of cellular uptake achieved by photoswitchable cell-penetrating peptides},
journal = {Chem Commun},
year = {2016},
volume = {52},
pages = {701--704},
doi = {10.1039/C5CC06848G}
}
|
| Trautwein M, Fredriksson K, Möller HM and Exner* TE (2016), "Automated assignment of NMR chemical shifts based on a known structure and 4D spectra", J Biomol NMR. Vol. 65(3-4), pp. 217-236. |
| Abstract: Apart from their central role during 3D structure determination of proteins the backbone chemical shift assignment is the basis for a number of applications, like chemical shift perturbation mapping and studies on the dynamics of proteins. This assignment is not a trivial task even if a 3D protein structure is known and needs almost as much effort as the assignment for structure prediction if performed manually. We present here a new algorithm based solely on 4D [(1)H,(15)N]-HSQC-NOESY-[(1)H,(15)N]-HSQC spectra which is able to assign a large percentage of chemical shifts (73-82 %) unambiguously, demonstrated with proteins up to a size of 250 residues. For the remaining residues, a small number of possible assignments is filtered out. This is done by comparing distances in the 3D structure to restraints obtained from the peak volumes in the 4D spectrum. Using dead-end elimination, assignments are removed in which at least one of the restraints is violated. Including additional information from chemical shift predictions, a complete unambiguous assignment was obtained for Ubiquitin and 95 % of the residues were correctly assigned in the 251 residue-long N-terminal domain of enzyme I. The program including source code is available at https://github.com/thomasexner/4Dassign . |
BibTeX:
@article{Trautwein2016,
author = {Trautwein, M. and Fredriksson, K. and Möller, H. M. and Exner*, T. E.},
title = {Automated assignment of NMR chemical shifts based on a known structure and 4D spectra},
journal = {J Biomol NMR},
year = {2016},
volume = {65},
number = {3-4},
pages = {217--236},
doi = {10.1007/s10858-016-0050-0}
}
|
| Vorburger T, Nedielkov R, Brosig A, Bok E, Schunke E, Steffen W, Mayer S, Götz F, Möller* HM and Steuber* J (2016), "Role of the Na+-translocating NADH: Quinone oxidoreductase in voltage generation and Na+ extrusion in Vibrio cholerae", Biochim Biophys Acta - Bioenergetics. Vol. 1857(4), pp. 473-482. |
BibTeX:
@article{Vorburger2016,
author = {Vorburger, T. and Nedielkov, R. and Brosig, A. and Bok, E. and Schunke, E. and Steffen, W. and Mayer, S. and Götz, F. and Möller*, H. M. and Steuber*, J.},
title = {Role of the Na+-translocating NADH: Quinone oxidoreductase in voltage generation and Na+ extrusion in Vibrio cholerae},
journal = {Biochim Biophys Acta - Bioenergetics},
year = {2016},
volume = {1857},
number = {4},
pages = {473--482},
doi = {10.1016/j.bbabio.2015.12.010}
}
|
| Kastl J, Braun J, Prestel A, Möller HM, Huhn T and Mayer* TU (2015), "Mad2 Inhibitor-1 (M2I-1): A Small Molecule Protein--Protein Interaction Inhibitor Targeting the Mitotic Spindle Assembly Checkpoint", ACS Chem Biol. Vol. 10(7), pp. 1661-1666. |
BibTeX:
@article{Kastl2015,
author = {Kastl, J. and Braun, J. and Prestel, A. and Möller, H. M. and Huhn, T. and Mayer*, T. U.},
title = {Mad2 Inhibitor-1 (M2I-1): A Small Molecule Protein--Protein Interaction Inhibitor Targeting the Mitotic Spindle Assembly Checkpoint},
journal = {ACS Chem Biol},
year = {2015},
volume = {10},
number = {7},
pages = {1661--1666},
doi = {10.1021/acschembio.5b00121.}
}
|
| Schildknecht* S, Pape R, Meiser J, Karreman C, Strittmatter T, Odermatt M, Cirri E, Friemel A, Ringwald M, Pasquarelli N, Ferger B, Brunner T, Marx A, Möller HM, Hiller K and Leist M (2015), "Preferential Extracellular Generation of the Active Parkinsonian Toxin MPP+ by Transporter-Independent Export of the Intermediate MPDP+", Antiox Redox Signal. Vol. 23(13), pp. 1001-1016. |
BibTeX:
@article{Schildknecht*2015,
author = {Schildknecht*, S. and Pape, R. and Meiser, J. and Karreman, C. and Strittmatter, T. and Odermatt, M. and Cirri, E. and Friemel, A. and Ringwald, M. and Pasquarelli, N. and Ferger, B. and Brunner, T. and Marx, A. and Möller, H. M. and Hiller, K. and Leist, M.},
title = {Preferential Extracellular Generation of the Active Parkinsonian Toxin MPP+ by Transporter-Independent Export of the Intermediate MPDP+},
journal = {Antiox Redox Signal},
year = {2015},
volume = {23},
number = {13},
pages = {1001--1016},
doi = {10.1089/ars.2015.6297}
}
|
| Sommer R, Hauck D, Varrot A, Wagner S, Audfray A, Prestel A, Möller HM, Imberty A and Titz* A (2015), "Cinnamide Derivatives of d-Mannose as Inhibitors of the Bacterial Virulence Factor LecB from Pseudomonas aeruginosa", ChemistryOpen. Vol. 4(6), pp. 756-767. |
BibTeX:
@article{Sommer2015,
author = {Sommer, R. and Hauck, D. and Varrot, A. and Wagner, S. and Audfray, A. and Prestel, A. and Möller, H. M. and Imberty, A. and Titz*, A.},
title = {Cinnamide Derivatives of d-Mannose as Inhibitors of the Bacterial Virulence Factor LecB from Pseudomonas aeruginosa},
journal = {ChemistryOpen},
year = {2015},
volume = {4},
number = {6},
pages = {756--767},
doi = {10.1002/open.201500162}
}
|
| Holert J, Yücel O, Suvekbala V, Kulić Ž, Möller HM and Philipp* B (2014), "Evidence of distinct pathways for bacterial degradation of the steroid compound cholate suggests the potential for metabolic interactions by interspecies cross-feeding", Environ Microbiol. Vol. 16, pp. 1424-1440. |
BibTeX:
@article{Holert2014,
author = {Holert, J. and Yücel, O. and Suvekbala, V. and Kulić, Ž. and Möller, H. M. and Philipp*, B.},
title = {Evidence of distinct pathways for bacterial degradation of the steroid compound cholate suggests the potential for metabolic interactions by interspecies cross-feeding},
journal = {Environ Microbiol},
year = {2014},
volume = {16},
pages = {1424--1440},
doi = {10.1111/1462-2920.12407.}
}
|
| Victora A, Möller HM and Exner* TE (2014), "Accurate ab initio prediction of NMR chemical shifts of nucleic acids and nucleic acids/protein complexes.", Nucl Acids Res. Vol. 42(22), pp. e173. |
BibTeX:
@article{Victora2014,
author = {Victora, A. and Möller, H. M. and Exner*, T. E.},
title = {Accurate ab initio prediction of NMR chemical shifts of nucleic acids and nucleic acids/protein complexes.},
journal = {Nucl Acids Res},
year = {2014},
volume = {42},
number = {22},
pages = {e173},
doi = {10.1093/nar/gku1006}
}
|
| Vohl G, Nedielkov R, Claussen B, Casutt MS, Vorburger T, Diederichs K, Möller HM, Steuber J and Fritz* G (2014), "Crystallization and preliminary analysis of the NqrA and NqrC subunits of the Na+-translocating NADH:ubiquinone oxidoreductase from Vibrio cholerae", Acta Crystallogr F Struct Biol Commun. Vol. 70, pp. 987-992. |
BibTeX:
@article{Vohl2014,
author = {Vohl, G. and Nedielkov, R. and Claussen, B. and Casutt, M. S. and Vorburger, T. and Diederichs, K. and Möller, H. M. and Steuber, J. and Fritz*, G.},
title = {Crystallization and preliminary analysis of the NqrA and NqrC subunits of the Na+-translocating NADH:ubiquinone oxidoreductase from Vibrio cholerae},
journal = {Acta Crystallogr F Struct Biol Commun},
year = {2014},
volume = {70},
pages = {987--992},
doi = {10.1107/S2053230X14009881}
}
|
| Dračínský* M, Möller HM and Exner* TE (2013), "Conformational Sampling by Ab Initio Molecular Dynamics Simulations Improves NMR Chemical Shift Predictions", J Chem Theory Comput. Vol. 9, pp. 3806-3815. |
BibTeX:
@article{Dracinsky*2013,
author = {Dračínský*, M. and Möller, H. M. and Exner*, T. E.},
title = {Conformational Sampling by Ab Initio Molecular Dynamics Simulations Improves NMR Chemical Shift Predictions},
journal = {J Chem Theory Comput},
year = {2013},
volume = {9},
pages = {3806--3815},
doi = {10.1021/ct400282h}
}
|
| Frank A, Berkefeld A, Drexler M, Möller HM and Exner* TE (2013), "Small Changes - Huge Influences: NMR Chemical Shifts of Ni(II) Complexes with Polar Substrates", Int J Quantum Chem. Vol. 113(13), pp. 1787-1793. |
BibTeX:
@article{Frank2013,
author = {Frank, A. and Berkefeld, A. and Drexler, M. and Möller, H. M. and Exner*, T. E.},
title = {Small Changes - Huge Influences: NMR Chemical Shifts of Ni(II) Complexes with Polar Substrates},
journal = {Int J Quantum Chem},
year = {2013},
volume = {113},
number = {13},
pages = {1787--1793},
doi = {10.1002/qua.24401}
}
|
| Hauck D, Joachim I, Frommeyer B, Varrot A, Philipp B, Möller HM, Imberty A, Exner TE and Titz* A (2013), "Discovery of two classes of potent glycomimetic inhibitors of Pseudomonas aeruginosa LecB with distinct binding modes", ACS Chem Biol. Vol. 8, pp. 1775-1784. |
BibTeX:
@article{Hauck2013,
author = {Hauck, D. and Joachim, I. and Frommeyer, B. and Varrot, A. and Philipp, B. and Möller, H. M. and Imberty, A. and Exner, T. E. and Titz*, A.},
title = {Discovery of two classes of potent glycomimetic inhibitors of Pseudomonas aeruginosa LecB with distinct binding modes},
journal = {ACS Chem Biol},
year = {2013},
volume = {8},
pages = {1775--1784},
doi = {10.1021/cb400371r}
}
|
| Kulić Ž, Fritz G and Möller* HM (2013), "1H, 13C, and 15N resonance assignment of the second Immunoglobulin domain of the protein neurolin from Goldfish", J Biomol NMR Assignments. Vol. 7(1), pp. 65-67. |
BibTeX:
@article{Kulic2013,
author = {Kulić, Ž. and Fritz, G. and Möller*, H. M.},
title = {1H, 13C, and 15N resonance assignment of the second Immunoglobulin domain of the protein neurolin from Goldfish},
journal = {J Biomol NMR Assignments},
year = {2013},
volume = {7},
number = {1},
pages = {65--67},
doi = {10.1007/s12104-012-9379-9}
}
|
| Lavrynenko O, Nedielkov R, Möller HM and Shevchenko A (2013), "Girard Derivatization for LC-MS/MS Profiling of Endogenous Ecdysteroids in Drosophila", J Lipid Res. Vol. 54(8), pp. 2265-2272. |
BibTeX:
@article{Lavrynenko2013,
author = {Lavrynenko, O. and Nedielkov, R. and Möller, H. M. and Shevchenko, A.},
title = {Girard Derivatization for LC-MS/MS Profiling of Endogenous Ecdysteroids in Drosophila},
journal = {J Lipid Res},
year = {2013},
volume = {54},
number = {8},
pages = {2265--2272},
doi = {10.1194/jlr.D035949}
}
|
| Nedielkov R, Steffen W, Steuber* J and Möller* HM (2013), "NMR reveals double occupancy of quinone-type ligands in the catalytic quinone binding site of the Na+-translocating NADH:quinone oxidoreductase from Vibrio cholerae", J Biol Chem. Vol. 288, pp. 30597-30606.
[BibTeX] |
BibTeX:
@article{Nedielkov2013,
author = {Nedielkov, R. and Steffen, W. and Steuber*, J. and Möller*, H. M.},
title = {NMR reveals double occupancy of quinone-type ligands in the catalytic quinone binding site of the Na+-translocating NADH:quinone oxidoreductase from Vibrio cholerae},
journal = {J Biol Chem},
year = {2013},
volume = {288},
pages = {30597--30606}
}
|
| Soshnikov IE, Semikolenova NV, Zakharov VA, Möller HM, Ölscher F, Osichow A, Göttker-Schnetmann I, Mecking* S, Talsi EP and Bryliakov* KP (2013), "Formation and Evolution of Chain-Propagating Species Upon Ethylene Polymerization with Neutral Salicylaldiminato Nickel(II) Catalysts", Chem Eur J. Vol. 19, pp. 11409-11417. |
BibTeX:
@article{Soshnikov2013,
author = {Soshnikov, I. E. and Semikolenova, N. V. and Zakharov, V. A. and Möller, H. M. and Ölscher, F. and Osichow, A. and Göttker-Schnetmann, I. and Mecking*, S. and Talsi, E. P. and Bryliakov*, K. P.},
title = {Formation and Evolution of Chain-Propagating Species Upon Ethylene Polymerization with Neutral Salicylaldiminato Nickel(II) Catalysts},
journal = {Chem Eur J},
year = {2013},
volume = {19},
pages = {11409--11417},
doi = {10.1002/chem.201301037}
}
|
| Beckmann HSG, Möller HM and Wittmann* V (2012), "High-affinity multivalent wheat germ agglutinin ligands by one-pot click reaction", Beilstein J Org Chem. Vol. 8, pp. 819-826. |
BibTeX:
@article{Beckmann2012,
author = {Beckmann, H. S. G. and Möller, H. M. and Wittmann*, V.},
title = {High-affinity multivalent wheat germ agglutinin ligands by one-pot click reaction},
journal = {Beilstein J Org Chem},
year = {2012},
volume = {8},
pages = {819--826},
doi = {10.3762/bjoc.8.91}
}
|
| Dempwolff F, Möller HM and Graumann* PL (2012), "Synthetic motility and cell shape defects for deletions of flotillin/reggie paralogs in Bacillus subtilis and interplay with NfeD proteins", J Bacteriol. Vol. 194, pp. 4652-4661. |
| Abstract: Flotillin/reggie proteins are membrane proteins present in all kinds of cells and belong to the family of proteins carrying the SPFH domain. In addition to this domain of unknown function, flotillin proteins are characterized by the flotillin domain that is rich in heptad repeats. Bacterial flotillin orthologs have recently been shown to be part of lipid rafts, like their eukaryotic counterparts, and to be involved in signalling events. Double deletions of floT and the gene encoding for the second flotillin-like protein in Bacillus subtilis, floA, show strong synthetic defects in cell morphology, motility and transformation efficiency. By TIRF microscopy we show that both proteins localize in characteristic focal structures within the cell membrane, which move in a highly dynamic and random manner, but localize independently of each other. Thus, flotillin paralogs act spatially in a distinct manner. Flotillin domains in both FloA and FloT are essential for focal assemblies, and for the proper function of flotillins. Both flotillin genes are situated next to genes encoding for NfeD proteins. NfeD2 affects the localization of FloT, and vice versa, but not of FloA, and colocalizes with FloT, showing a close interaction between flotillins and NfeDs in bacteria. FloA does not show a spatial connection with the upstream-encoded NfeD1b. Our work establishes that bacterial flotillin-like proteins play overlapping functions in a multitude of membrane-associated processes, and that flotillin domain-mediated interactions and NfeD proteins play important roles in setting up the flotillin raft-like structures in vivo. |
BibTeX:
@article{Dempwolff2012,
author = {Dempwolff, F. and Möller, H. M. and Graumann*, P. L.},
title = {Synthetic motility and cell shape defects for deletions of flotillin/reggie paralogs in Bacillus subtilis and interplay with NfeD proteins},
journal = {J Bacteriol},
year = {2012},
volume = {194},
pages = {4652--4661}
}
|
| Exner* TE, Frank A, Onila I and Möller* HM (2012), "Toward the Quantum Chemical Calculation of NMR Chemical Shifts of Proteins 3: Conformational Sampling and Explicit Solvents Model", J Chem Theory Comput. Vol. 8(11), pp. 4818-4827. |
BibTeX:
@article{Exner*2012,
author = {Exner*, T. E. and Frank, A. and Onila, I. and Möller*, H. M.},
title = {Toward the Quantum Chemical Calculation of NMR Chemical Shifts of Proteins 3: Conformational Sampling and Explicit Solvents Model},
journal = {J Chem Theory Comput},
year = {2012},
volume = {8},
number = {11},
pages = {4818--4827},
doi = {10.1021/ct300701m}
}
|
| Frank A, Möller HM and Exner* TE (2012), "Towards the Quantum Chemical Calculation of NMR Chemical Shifts of Proteins 2: Level of Theory, Basis Set, and Solvents Model Dependence", J Chem Theory Comput. Vol. 8, pp. 1480-1492. |
BibTeX:
@article{Frank2012,
author = {Frank, A. and Möller, H. M. and Exner*, T. E.},
title = {Towards the Quantum Chemical Calculation of NMR Chemical Shifts of Proteins 2: Level of Theory, Basis Set, and Solvents Model Dependence},
journal = {J Chem Theory Comput},
year = {2012},
volume = {8},
pages = {1480--1492},
doi = {10.1021/ct200913r}
}
|
| Holert J, Kulić Ž, Yücel O, Suvekbala V, Suter MJ-F, Möller* HM and Philipp* B (2012), "Degradation of the acyl side chain of the steroid compound cholate in Pseudomonas sp. strain Chol1 proceeds via an aldehyde intermediate", J Bacteriol. Vol. 195(3), pp. 585-595. |
BibTeX:
@article{Holert2012,
author = {Holert, J. and Kulić, Ž. and Yücel, O. and Suvekbala, V. and Suter, M. J.-F. and Möller*, H. M. and Philipp*, B.},
title = {Degradation of the acyl side chain of the steroid compound cholate in Pseudomonas sp. strain Chol1 proceeds via an aldehyde intermediate},
journal = {J Bacteriol},
year = {2012},
volume = {195},
number = {3},
pages = {585--595},
doi = {10.1128/JB.01961-12}
}
|
| Holzberger B, Pszolla MG, Marx A and Möller* HM (2012), "KlenTaq DNA polymerase adopts unique recognition states when encountering matched, mismatched, and abasic template sites - An NMR study", ChemBioChem. Vol. 13, pp. 635-639. |
BibTeX:
@article{Holzberger2012,
author = {Holzberger, B. and Pszolla, M. G. and Marx, A. and Möller*, H. M.},
title = {KlenTaq DNA polymerase adopts unique recognition states when encountering matched, mismatched, and abasic template sites - An NMR study},
journal = {ChemBioChem},
year = {2012},
volume = {13},
pages = {635--639},
doi = {10.1002/cbic.201100802}
}
|
| Möller* HM, Baier MC, Mecking S, Talsi EP and Bryliakov* KP (2012), "The Origin of Living Polymerization with an o-Fluorinated Catalyst: NMR-Spectroscopic Characterization of Chain-Propagating Species", Chem Eur J. Vol. 18(3), pp. 848-856. |
BibTeX:
@article{Moeller*2012,
author = {Möller*, H. M. and Baier, M. C. and Mecking, S. and Talsi, E. P. and Bryliakov*, K. P.},
title = {The Origin of Living Polymerization with an o-Fluorinated Catalyst: NMR-Spectroscopic Characterization of Chain-Propagating Species},
journal = {Chem Eur J},
year = {2012},
volume = {18},
number = {3},
pages = {848--856},
doi = {10.1002/chem.201102408}
}
|
| Rösle P, Dürr CJ, Möller* HM, Cavallo L, Caporaso* L and Mecking* S (2012), "Mechanistic Features of Isomerizing Alkoxycarbonylation of Methyl Oleate", J Am Chem Soc. Vol. 134(42), pp. 17696-17703. |
BibTeX:
@article{Roesle2012,
author = {Rösle, P. and Dürr, C. J. and Möller*, H. M. and Cavallo, L. and Caporaso*, L. and Mecking*, S.},
title = {Mechanistic Features of Isomerizing Alkoxycarbonylation of Methyl Oleate},
journal = {J Am Chem Soc},
year = {2012},
volume = {134},
number = {42},
pages = {17696--17703},
doi = {10.1021/ja307411p}
}
|
| Rünzi T, Tritschler U, Rösle P, Göttker-Schnetmann I, Möller HM, Caporaso* L, Poater A, Cavallo L and Mecking* S (2012), "Activation and Deactivation of Neutral Palladium(II) Phosphinesulfonato Polymerization Catalysts", Organometallics. Vol. 31(23), pp. 8388-8406. |
BibTeX:
@article{Ruenzi2012,
author = {Rünzi, T. and Tritschler, U. and Rösle, P. and Göttker-Schnetmann, I. and Möller, H. M. and Caporaso*, L. and Poater, A. and Cavallo, L. and Mecking*, S.},
title = {Activation and Deactivation of Neutral Palladium(II) Phosphinesulfonato Polymerization Catalysts},
journal = {Organometallics},
year = {2012},
volume = {31},
number = {23},
pages = {8388--8406},
doi = {10.1021/om300969d}
}
|
| Birkenmaier A, Möller HM and Philipp* B (2011), "Identification of a thiolase gene essential for b-oxidation of the acyl side chain of the steroid compound cholate in Pseudomonas sp. strain Chol1", FEMS Microbiol Lett. Vol. 318(2), pp. 123-130. |
BibTeX:
@article{Birkenmaier2011,
author = {Birkenmaier, A. and Möller, H. M. and Philipp*, B.},
title = {Identification of a thiolase gene essential for b-oxidation of the acyl side chain of the steroid compound cholate in Pseudomonas sp. strain Chol1},
journal = {FEMS Microbiol Lett},
year = {2011},
volume = {318},
number = {2},
pages = {123--130},
doi = {10.1111/j.1574-6968.2011.02250.x}
}
|
| Casutt MS, Nedielkov R, Wendelspiess S, Vossler S, Gerken U, Murai M, Miyoshi H, Möller* HM and Steuber* J (2011), "Localization of ubiquinone-8 in the Na+-pumping NADH:quinone oxidoreductase from Vibrio cholerae", J Biol Chem. Vol. 286(46), pp. 40075-40082.
[BibTeX] |
BibTeX:
@article{Casutt2011,
author = {Casutt, M. S. and Nedielkov, R. and Wendelspiess, S. and Vossler, S. and Gerken, U. and Murai, M. and Miyoshi, H. and Möller*, H. M. and Steuber*, J.},
title = {Localization of ubiquinone-8 in the Na+-pumping NADH:quinone oxidoreductase from Vibrio cholerae},
journal = {J Biol Chem},
year = {2011},
volume = {286},
number = {46},
pages = {40075--40082}
}
|
| Frank A, Onila I, Möller HM and Exner* TE (2011), "Towards the Quantum Chemical Calculation of NMR Chemical Shifts of Proteins", Proteins. Vol. 79(7), pp. 2189-2202. |
BibTeX:
@article{Frank2011,
author = {Frank, A. and Onila, I. and Möller, H. M. and Exner*, T. E.},
title = {Towards the Quantum Chemical Calculation of NMR Chemical Shifts of Proteins},
journal = {Proteins},
year = {2011},
volume = {79},
number = {7},
pages = {2189--2202},
doi = {10.1002/prot.23041}
}
|
| Lukzen N and Möller* HM (2011), "Theoretical description of protein NMR saturation transfer to a bioactive ligand", Appl Magn Reson. Vol. 41, pp. 325-336. |
BibTeX:
@article{Lukzen2011,
author = {Lukzen, N. and Möller*, H. M.},
title = {Theoretical description of protein NMR saturation transfer to a bioactive ligand},
journal = {Appl Magn Reson},
year = {2011},
volume = {41},
pages = {325--336},
doi = {10.1007/s00723-011-0268-7}
}
|
| Orbán E, Gábor Mezö G, Schlage P, Csík G, Kulić Ž, Ansorge P, Fellinger E, Möller HM and Manea* M (2011), "In vitro degradation and antitumor activity of oxime bond-linked daunorubicin-GnRH-III bioconjugates and DNA-binding properties of daunorubicin-amino acid metabolites", Amino Acids. Vol. 41(2), pp. 469-483. |
BibTeX:
@article{Orban2011,
author = {Orbán, E. and Gábor Mezö, G. and Schlage, P. and Csík, G. and Kulić, Ž. and Ansorge, P. and Fellinger, E. and Möller, H. M. and Manea*, M.},
title = {In vitro degradation and antitumor activity of oxime bond-linked daunorubicin-GnRH-III bioconjugates and DNA-binding properties of daunorubicin-amino acid metabolites},
journal = {Amino Acids},
year = {2011},
volume = {41},
number = {2},
pages = {469--483},
doi = {10.1007/s00726-010-0766-1}
}
|
| Bryliakov* KP, Talsi EP, Möller HM, Baier M and Mecking* S (2010), "Noncovalent Interactions in o-Fluorinated Post-titanocene Living Ethylene Polymerization Catalyst", Organometallics. Vol. 29(20), pp. 4428-4430. |
BibTeX:
@article{Bryliakov*2010,
author = {Bryliakov*, K. P. and Talsi, E. P. and Möller, H. M. and Baier, M. and Mecking*, S.},
title = {Noncovalent Interactions in o-Fluorinated Post-titanocene Living Ethylene Polymerization Catalyst},
journal = {Organometallics},
year = {2010},
volume = {29},
number = {20},
pages = {4428--4430},
doi = {10.1021/om100729y}
}
|
| Fischer GM, Jüngst C, Isomaki-Krondahl M, Gauss D, Möller HM, Daltrozzo E and Zumbusch* A (2010), "Asymmetric PPCys: Strongly fluorescing NIR labels", Chem Commun (Camb). Vol. 46, pp. 5289-5291. |
| Abstract: By a stepwise synthesis strategy biofunctionalized Pyrrolopyrrole Cyanines (PPCy) with an asymmetric substitution pattern were obtained. These exhibit extremely strong and narrowband NIR absorption and fluorescence. Internalization of a peptide bound PPCy is demonstrated using live cell microscopy. |
BibTeX:
@article{Fischer2010,
author = {Fischer, G. M. and Jüngst, C. and Isomaki-Krondahl, M. and Gauss, D. and Möller, H. M. and Daltrozzo, E. and Zumbusch*, A.},
title = {Asymmetric PPCys: Strongly fluorescing NIR labels},
journal = {Chem Commun (Camb)},
year = {2010},
volume = {46},
pages = {5289--5291},
doi = {10.1039/c0cc00359j}
}
|
| Hinderhofer M, Boos W and Möller* HM (2010), "The Escherichia coli Transcription Factor Mlc Covers a Face of the Phosphotransferase System EIIBGlc that Overlaps the EIIAGlc Binding Site", Recommended for resubmission to FEBS J. after major revisions..
[BibTeX] |
BibTeX:
@article{Hinderhofer2010,
author = {Hinderhofer, M. and Boos, W. and Möller*, H. M.},
title = {The Escherichia coli Transcription Factor Mlc Covers a Face of the Phosphotransferase System EIIBGlc that Overlaps the EIIAGlc Binding Site},
journal = {Recommended for resubmission to FEBS J. after major revisions.},
year = {2010}
}
|
| Holzberger B, Rubini M, Möller HM and Marx* A (2010), "A Highly Active DNA Polymerase with a Fluorous Core", Angew Chem Int Ed Engl. Vol. 49(7), pp. 1324-1327. |
BibTeX:
@article{Holzberger2010,
author = {Holzberger, B. and Rubini, M. and Möller, H. M. and Marx*, A.},
title = {A Highly Active DNA Polymerase with a Fluorous Core},
journal = {Angew Chem Int Ed Engl},
year = {2010},
volume = {49},
number = {7},
pages = {1324--1327},
doi = {10.1002/anie.200905978}
}
|
| Korb O, Möller HM and Exner* TE (2010), "NMR-guided Molecular Docking of a Protein-Peptide Complex Based on Ant Colony Optimization", ChemMedChem. Vol. 5(7), pp. 1001-1006. |
BibTeX:
@article{Korb2010,
author = {Korb, O. and Möller, H. M. and Exner*, T. E.},
title = {NMR-guided Molecular Docking of a Protein-Peptide Complex Based on Ant Colony Optimization},
journal = {ChemMedChem},
year = {2010},
volume = {5},
number = {7},
pages = {1001--1006},
doi = {10.1002/cmdc.201000090}
}
|
| Oberli M, Tamborrini M, Tsai Y-H, Werz DB, Horlacher T, Adibekian A, Gauss D, Möller HM, Pluschke G and Seeberger* PH (2010), "Molecular Analysis of Carbohydrate-Antibody Interactions: Case Study Using A Bacillus anthracis Tetrasaccharide", J Am Chem Soc. Vol. 132(30), pp. 10239-10241. |
BibTeX:
@article{Oberli2010,
author = {Oberli, M. and Tamborrini, M. and Tsai, Y.-H. and Werz, D. B. and Horlacher, T. and Adibekian, A. and Gauss, D. and Möller, H. M. and Pluschke, G. and Seeberger*, P. H.},
title = {Molecular Analysis of Carbohydrate-Antibody Interactions: Case Study Using A Bacillus anthracis Tetrasaccharide},
journal = {J Am Chem Soc},
year = {2010},
volume = {132},
number = {30},
pages = {10239--10241},
doi = {10.1021/ja104027w}
}
|
| Schwefel D, Maierhofer C, Beck JG, Seeberger S, Diederichs K, Möller* HM, Welte* W and Wittmann* V (2010), "Structural Basis of Multivalent Binding to Wheat Germ Agglutinin", J Am Chem Soc. Vol. 132(25), pp. 8704-8719. |
BibTeX:
@article{Schwefel2010,
author = {Schwefel, D. and Maierhofer, C. and Beck, J. G. and Seeberger, S. and Diederichs, K. and Möller*, H. M. and Welte*, W. and Wittmann*, V.},
title = {Structural Basis of Multivalent Binding to Wheat Germ Agglutinin},
journal = {J Am Chem Soc},
year = {2010},
volume = {132},
number = {25},
pages = {8704--8719},
doi = {10.1021/ja101646k}
}
|
| Berkefeld A, Drexler M, Möller HM and Mecking* S (2009), "Mechanistic Insights on the Copolymerization of Polar Vinyl Monomers with Neutral Ni(II) Catalysts", J. Am. Chem. Soc.. Vol. 131, pp. 12613-12622.
[BibTeX] |
BibTeX:
@article{Berkefeld2009,
author = {Berkefeld, A. and Drexler, M. and Möller, H. M. and Mecking*, S.},
title = {Mechanistic Insights on the Copolymerization of Polar Vinyl Monomers with Neutral Ni(II) Catalysts},
journal = {J. Am. Chem. Soc.},
year = {2009},
volume = {131},
pages = {12613--12622}
}
|
| Berkefeld A, Möller HM and Mecking* S (2009), "Unusual Reactivity of N,N,N',N'-Tetramethylethylenediamine Coordinated Neutral Ni(II) Polymerization Catalysts", Organometallics. Vol. 28, pp. 4048-4055.
[BibTeX] |
BibTeX:
@article{Berkefeld2009a,
author = {Berkefeld, A. and Möller, H. M. and Mecking*, S.},
title = {Unusual Reactivity of N,N,N',N'-Tetramethylethylenediamine Coordinated Neutral Ni(II) Polymerization Catalysts},
journal = {Organometallics},
year = {2009},
volume = {28},
pages = {4048--4055}
}
|
| Hinderhofer M, Walker CA, Friemel A, Stuermer C, Möller HM and Reuter A (2009), "Evolution of prokaryotic SPFH proteins", BMC Evolutionary Biology. Vol. 9 (equal contribution of HMM an AR)(10)
[BibTeX] |
BibTeX:
@article{Hinderhofer2009,
author = {Hinderhofer, M. and Walker, C. A. and Friemel, A. and Stuermer, C.A.O. and Möller, H. M. and Reuter, A.},
title = {Evolution of prokaryotic SPFH proteins},
journal = {BMC Evolutionary Biology},
year = {2009},
volume = {9 (equal contribution of HMM an AR)},
number = {10}
}
|
| Streckenbach F, Rangam G, Möller HM and Marx* A (2009), "Steric Constraints Dependent on Nucleobase Pair Orientation vary in different DNA Polymerase Active Sites", ChemBioChem. Vol. 10(10), pp. 1630-1632.
[BibTeX] |
BibTeX:
@article{Streckenbach2009,
author = {Streckenbach, F. and Rangam, G. and Möller, H. M. and Marx*, A.},
title = {Steric Constraints Dependent on Nucleobase Pair Orientation vary in different DNA Polymerase Active Sites},
journal = {ChemBioChem},
year = {2009},
volume = {10},
number = {10},
pages = {1630--1632}
}
|
| André A, Fontaine-Vive F, Forsyth VT, Möller HM, Fischer T, Maret G and Gisler* T (2008), "Force-induced structural transitions in cross-linked DNA Films", Eur Biophys J. Vol. 37(6), pp. 749-757.
[BibTeX] |
BibTeX:
@article{Andre2008,
author = {André, A. and Fontaine-Vive, F. and Forsyth, V. T. and Möller, H. M. and Fischer, T. and Maret, G. and Gisler*, T.},
title = {Force-induced structural transitions in cross-linked DNA Films},
journal = {Eur Biophys J},
year = {2008},
volume = {37},
number = {6},
pages = {749--757}
}
|
| Deininger S, Traub S, Aichele D, Rupp T, Baris T, Möller HM, Hartung T and von Aulock* S (2008), "Presentation of lipoteichoic acid potentiates its inflammatory activity", Immunobiology. Vol. 213(6), pp. 519-529.
[BibTeX] |
BibTeX:
@article{Deininger2008,
author = {Deininger, S. and Traub, S. and Aichele, D. and Rupp, T. and Baris, T. and Möller, H. M. and Hartung, T. and von Aulock*, S.},
title = {Presentation of lipoteichoic acid potentiates its inflammatory activity},
journal = {Immunobiology},
year = {2008},
volume = {213},
number = {6},
pages = {519--529}
}
|
| Draing C, Traub S, Deininger S, Mang1 P, Möller HM, Manso M, Rossi F, Morath S, Hartung T and von Aulock* S (2008), "Polypropylene glycol is a selective binding inhibitor for LTA and other structurally related TLR2 agonists", Eur J Immunol. Vol. 38, pp. 797-808.
[BibTeX] |
BibTeX:
@article{Draing2008,
author = {Draing, C. and Traub, S. and Deininger, S. and Mang1, P. and Möller, H. M. and Manso, M. and Rossi, F. and Morath, S. and Hartung, T. and von Aulock*, S.},
title = {Polypropylene glycol is a selective binding inhibitor for LTA and other structurally related TLR2 agonists},
journal = {Eur J Immunol},
year = {2008},
volume = {38},
pages = {797--808}
}
|
| Drees C, Stürmer C, Möller* HM and Fritz* G (2008), "Expression and Purification of Neurolin Immunoglobulin domain 2 from Carrassius auratus (Goldfish) in Escherichia coli", Protein Expr. Purif.. Vol. 59, pp. 47-54.
[BibTeX] |
BibTeX:
@article{Drees2008,
author = {Drees, C. and Stürmer, C.A.O. and Möller*, H. M. and Fritz*, G.},
title = {Expression and Purification of Neurolin Immunoglobulin domain 2 from Carrassius auratus (Goldfish) in Escherichia coli},
journal = {Protein Expr. Purif.},
year = {2008},
volume = {59},
pages = {47--54}
}
|
| Walker CA, Hinderhofer M, Witte D, Boos W and Möller* HM (2008), "Solution Structure of the Soluble Domain of the NfeD Protein YuaF from Bacillus subtilis", J Biomol NMR. Vol. 42, pp. 69-76.
[BibTeX] |
BibTeX:
@article{Walker2008,
author = {Walker, C. A. and Hinderhofer, M. and Witte, D. and Boos, W. and Möller*, H. M.},
title = {Solution Structure of the Soluble Domain of the NfeD Protein YuaF from Bacillus subtilis},
journal = {J Biomol NMR},
year = {2008},
volume = {42},
pages = {69--76}
}
|
| Birkenmaier A, Holert J, Erdbrink H, Möller HM, Friemel A, Schoenenberger R, Suter MJ, Klebensberger J and Philipp* B (2007), "Biochemical and Genetic Investigation of Initial Reactions in Aerobic Degradation of the Bile Acid Cholate in Pseudomonas sp. Strain Chol1", J Bacteriol. Vol. 189(20), pp. 7165-7173. |
| Abstract: Bile acids are surface-active steroid compounds with toxic effects for bacteria. Recently, the isolation and characterization of a bacterium, Pseudomonas sp. strain Chol1, growing with bile acids as the carbon and energy source was reported. In this study, initial reactions of the aerobic degradation pathway for the bile acid cholate were investigated on the biochemical and genetic level in strain Chol1. These reactions comprised A-ring oxidation, activation with coenzyme A (CoA), and beta-oxidation of the acyl side chain with the C(19)-steroid dihydroxyandrostadienedione as the end product. A-ring oxidizing enzyme activities leading to Delta(1,4)-3-ketocholyl-CoA were detected in cell extracts and confirmed by liquid chromatography-tandem mass spectrometry (LC-MS/MS). Cholate activation with CoA was demonstrated in cell extracts and confirmed with a chemically synthesized standard by LC-MS/MS. A transposon mutant with a block in oxidation of the acyl side chain accumulated a steroid compound in culture supernatants which was identified as 7alpha,12alpha-dihydroxy-3-oxopregna-1,4-diene-20-carboxylate (DHOPDC) by nuclear magnetic resonance spectroscopy. The interrupted gene was identified as encoding a putative acyl-CoA-dehydrogenase (ACAD). DHOPDC activation with CoA in cell extracts of strain Chol1 was detected by LC-MS/MS. The growth defect of the transposon mutant could be complemented by the wild-type ACAD gene located on the plasmid pBBR1MCS-5. Based on these results, the initiating reactions of the cholate degradation pathway leading from cholate to dihydroxyandrostadienedione could be reconstructed. In addition, the first bacterial gene encoding an enzyme for a specific reaction step in side chain degradation of steroid compounds was identified, and it showed a high degree of similarity to genes in other steroid-degrading bacteria. |
BibTeX:
@article{Birkenmaier2007,
author = {Birkenmaier, A. and Holert, J. and Erdbrink, H. and Möller, H. M. and Friemel, A. and Schoenenberger, R. and Suter, M. J. and Klebensberger, J. and Philipp*, B.},
title = {Biochemical and Genetic Investigation of Initial Reactions in Aerobic Degradation of the Bile Acid Cholate in Pseudomonas sp. Strain Chol1},
journal = {J Bacteriol},
year = {2007},
volume = {189},
number = {20},
pages = {7165--7173}
}
|
| Möller HM, Martinez-Yamout MA, Dyson HJ and Wright* PE (2005), "Solution structure of the N-terminal zinc fingers of the Xenopus laevis double-stranded RNA-binding protein ZFa", J Mol Biol. Vol. 351(4), pp. 718-730. |
| Abstract: Several zinc finger proteins have been discovered recently that bind specifically to double-stranded RNA. These include the mammalian JAZ and wig proteins, and the seven-zinc finger protein ZFa from Xenopus laevis. We have determined the solution structure of a 127 residue fragment of ZFa, which consists of two zinc finger domains connected by a linker that remains unstructured in the free protein in solution. The first zinc finger consists of a three-stranded beta-sheet and three helices, while the second finger contains only a two-stranded sheet and two helices. The common structures of the core regions of the two fingers are superimposable. Each finger has a highly electropositive surface that maps to a helix-kink-helix motif. There is no evidence for interactions between the two fingers, consistent with the length (24 residues) and unstructured nature of the intervening linker. Comparison with a number of other proteins shows similarities in the topology and arrangement of secondary structure elements with canonical DNA-binding zinc fingers, with protein interaction motifs such as FOG zinc fingers, and with other DNA-binding and RNA-binding proteins that do not contain zinc. However, in none of these cases does the alignment of these structures with the ZFa zinc fingers produce a consistent picture of a plausible RNA-binding interface. We conclude that the ZFa zinc fingers represent a new motif for the binding of double-stranded RNA. |
BibTeX:
@article{Moeller2005a,
author = {Möller, H. M. and Martinez-Yamout, M. A. and Dyson, H. J. and Wright*, P. E.},
title = {Solution structure of the N-terminal zinc fingers of the Xenopus laevis double-stranded RNA-binding protein ZFa},
journal = {J Mol Biol},
year = {2005},
volume = {351},
number = {4},
pages = {718--730}
}
|
| Möller H, Serttas N, Paulsen H, Burchell JM, Taylor-Papadimitriou J and Meyer* B (2002), "NMR-based determination of the binding epitope and conformational analysis of MUC-1 glycopeptides and peptides bound to the breast cancer-selective monoclonal antibody SM3", Eur J Biochem. Vol. 269(5), pp. 1444-1455. |
| Abstract: Mucin glycoproteins on breast cancer cells carry shortened carbohydrate chains. These partially deglycosylated mucin 1 (MUC-1) structures are recognized by the monoclonal antibody SM3, which is being tested for its diagnostic utility. We used NMR spectroscopy to analyze the binding mode and the binding epitope of peptide and glycopeptide antigens to the SM3 antibody. The pentapeptide PDTRP and the glycopentapeptide PDT(O-alpha-D-GalNAc)RP are known ligands of the monoclonal antibody. The 3D structures of the ligands in the bound conformation were determined by analyzing trNOESY build-up rates. The peptide was found to adopt an extended conformation that fits into the binding pocket of the antibody. The binding epitopes of the ligands were determined by saturation transfer difference (STD) NMR spectroscopy. The peptide's epitope is predominantly located in the N-terminal PDT segment whereas the C-terminal RP segment has fewer interactions with the protein. In contrast, the glycopeptide is interacting with SM3 utilizing all its amino acids. Pro1 shows the strongest binding effect that slightly decays towards Pro5. The GalNAc residue interacts mainly via the N-acetyl residue while the other protons show less interactions similar to that of Pro5. The glycopeptide in the bound state also has an extended conformation of the peptide with the carbohydrate oriented towards the N-terminus. Docking studies showed that peptide and glycopeptide fit the binding pocket of the mAb SM3 very well. |
BibTeX:
@article{Moeller2002,
author = {Möller, H. and Serttas, N. and Paulsen, H. and Burchell, J. M. and Taylor-Papadimitriou, J. and Meyer*, B.},
title = {NMR-based determination of the binding epitope and conformational analysis of MUC-1 glycopeptides and peptides bound to the breast cancer-selective monoclonal antibody SM3},
journal = {Eur J Biochem},
year = {2002},
volume = {269},
number = {5},
pages = {1444--1455}
}
|