• A Wolf, C Schneider, TY Kim, K Kirchberg, P Volz, U Alexiev.
          A simulation-guided fluorescence correlation spectroscopy tool to investigate to protonation dynamics of cytrochrome c oxidase. Phys. Chem. Chem. Phys. 2016. doi: 10.1039/c5cp07925j.Epub2016Apr22

        • RH Müller, U Alexiev, P Sinambela, CM Keck.
          Nanostructured Lipid Carriers (NLC): The Second Generation of Solid Lipid Nanoparticles. In: Percutaneous Penetration Enhancer Chemical Methods in Penetration Enhancement: Nanocarriers, Eds. Nina Dragicevic, Howard I. Maibach (Springer). 2016

        • A Boreham, J Pikkemaat, P Volz, R Brodwolf, C Kuehne, K Licha, R Haag, J Dernedde, U Alexiev.
          Detecting and Quantifiying Biomolecular Interactions of a Dendritic Polyglycerol Sulfate Nanoparticle Using Fluorescence Lifetime Measurements. Molecules. 2016. doi:10.3390/molecules21010022


        • C Richter, C Schneider, MT Quick, P Volz, R Mahrwald, J Hughes, B Dick, U Alexiev, NP Ernsting.
          Dual-fluorescence pH probe for bio-labelling. Phys. Chem. Chem. Phys. 2015. doi: 10.1039/c5cp05454k

        • M Witting, A Boreham, R Brodwolf, K Vavrova, U Alexiev, W Friess, S. Hedtrich.
          Interactions of Hyaluronic Acid with the Skin and Implications for the Dermal Delivery of Biomacromolecules. Molecular Pharmaceutics. 2015. doi: 10.1021/mp500676e

        • P Volz, A Boreham, A. Wolf, TY Kim, J Balke, J Frombach, S Hadam, Z Afraz, F Rancan, U Flume-Peytavi, A Vogt, U Alexiev.
          Application of Single Molecule Fluorescence Microscopy to Characterize the Penetration of a Large Amphiphilic Molecule in the Stratum Conerum of Human Skin. International Journal of Molecular Sciences. 2015. doi:10.3390/ijms16046960

        • A Ostrowski, D Nordmeyer, A Boreham, C Holzhausen, L Mundhenk, C Graf, MC Meinke, A Vogt, S Hadam, J Lademann, E Rühl, U Alexiev, AD Gruber.
          Overview on the Localization of Nanoparticles in Tissue and Cellular Context by Different Imaging Techniques. Beilstein Journal of Nanotechnology. 2015. doi:10.3762/bjnano.6.25

        • YJ Zhu, CS Choe, S Ahlberg, MC Meinke, U Alexiev, J Lademann, ME Darvin.
          Penetration of silver nanoparticles into porcine skin ex vivo using fluorescence lifetime imaging microscopy, Raman microscopy and surface enhanced Raman scattering microscopy. J. Biomed. Opt. 2015. doi:10.1117/1.JBO.20.5.051006

        • J Lademann, F Knorr, H Richter, S Jung, MC Meinke, E Rühl, U Alexiev, M Calderon, A Patzelt.
          Hair follicles as a target structure for nanoparticles. Journal of Innovative Optical Health Sciences. 2015. doi: 10/1142/S1793545815300049


          • A Boreham, R Brodwolf, M Pfaff, T-Y Kim, T Schlieter, L Mundhenk, AD Gruber, D Gröger, K Licha, R Haag, and U Alexiev. Temperature and environment dependent dynamic properties of a dendritic polyglycerol sulfate. Polym. Adv. Technol. 2014. doi: 10.1002/pat.3355

          • U Alexiev, DL Farrens.
            Fluorescence spectroscopy of rhodopsins: Insights and approaches. Biochim Biophys Acta. 2014 May. 1837(5), SI: 694-709.

          • A Ostrowski, D Nordmeyer, A Boreham, R Brodwolf, L Mundhenk, JW Fluhr, J Lademann, C Graf, E Rühl, U Alexiev, AD Gruber. Skin barrier disruptions in tape stripped and allergic dermatitis models have no effect on dermal penetration and systemic distribution of AHAPS-functionalized silica nanoparticles. Nanomedicine. 2014 Apr 22. pii: S1549-9634(14)00187-7. doi: 10.1016/j.nano.2014.04.004.

          • N Alnasif, C Zoschke, E Fleige, R Brodwolf, A Boreham, E Rühl, KM Eckl, HF Merk, HC Hennies, U Alexiev, R Haag, S Küchler, M Schäfer-Korting. Penetration of normal, damaged and diseased skin - An in vitro study on dendritic core-multishell nanotransporters. J Control Release. 2014 Jul 10;185:45-50. doi: 10.1016/j.jconrel.2014.04.006. Epub 2014 Apr 13.

          • A Boreham, M Pfaff, E Fleige, R Haag, U Alexiev., Nanodynamics of dendritic core-multishell nanocarriers. Langmuir. 2014 Feb 18;30(6):1686-95. doi: 10.1021/la4043155. Epub 2014 Feb 5.


          • C Hoppmann, U Alexiev, E Irran, K Rück-Braun.
            Synthesis and fluorescence of xanthone amino acids, Tetrahedron Letters, 2013 Aug 21, 54, 34, 4585-4587.

          • K Kirchberg, H Michel, U Alexiev. 
            Exploring the entrance of proton pathways in cytochrome c oxidase from Paracoccus denitrificans: surface charge, buffer capacity and redox-dependent polarity changes at the internal surface. Biochim Biophys Acta. 2013 Mar;1827(3):276-84

          • U Alexiev.
            Dynamics of Helix 8 in GPCR Function. Encyclopedia of Biophysics , 978-3-642-16711-9, 2013, pp 549-552

          • CM Keck, A Boreham, T Schlieter, D Peters, RH Müller, U Alexiev.
            Nanostructures and drug distribution within Nanostructured Lipid Carriers (NLC), In: “Proceedings of the 40th Annual Meeting of the Controlled Release Society (CRS)” ID 100536 (2013).



          • B. Repen, E. Schneider, and U. Alexiev.
            Optimization of a malachite green assay for detection of ATP hydrolysis by solubilized membrane proteins. Anal. Biochemistry, 2012, 2012 Jul 15;426(2):103-5.


          • K. Kirchberg, H. Michel, and U. Alexiev.
            Net Proton Uptake Is Preceded by Multiple Proton Transfer Steps upon Electron Injection into Cytochrome c Oxidase. J. Biol. Chem., 2012, 287, 8187-93.


          • T.-Y. Kim , T. Schlieter , S. Haase, and U. Alexiev.
            Activation and molecular recognition of the GPCR rhodopsin - Insights from time-resolved fluorescence depolarisation and single molecule experiments. Eur J Cell Biol., 2012, 91, 300-310.



          • A. Boreham, T.-Y. Kim, V. Spahn, C. Stein, L. Mundhenk, A. D. Gruber, R. Haag, P. Welker, K. Licha, and U. Alexiev.
            Exploiting fluorescence lifetime plasticity in FLIM: Target molecule localisation in cells and tissues.  ACS Med. Chem. Lett., 2011, 2 (10), 724–728.


          • K. Kirchberg, T.-Y. Kim, M. Möller, D. Skegro, G. Dasara Raju, J. Granzin, G. Büldt, R. Schlesinger, and U. Alexiev.
            Conformational dynamics of helix-8 in the GPCR rhodopsin controls arrestin activation in the desensitization process. PNAS, 2011, 108 (46), 18690-18695.



          • A. Dutta, K. C. Tirupula, U. Alexiev, and J. Klein-Seetharaman.
            Characterization of membrane protein non-native states. 1. Extent of unfolding and aggregation of rhodopsin in the presence of chemical denaturants. Biochemistry, 2010, 49, 6317-6328.

          • A. Dutta, T.-Y. Kim, M. Moeller, J. Wu, U. Alexiev, and J. Klein-Seetharaman.
            Characterization of membrane protein non-native states. 2. The SDS-unfolded states of rhodopsin. Biochemistry, 2010, 49, 6329-6340.

          • K. Kirchberg, T.-Y. Kim, S. Haase, and U. Alexiev.
            Functional interaction structures of the photochromic retinal protein rhodopsin. Photochem. Photobiol. Sci., 2010, 9, 226-33.



          • T.-Y. Kim, H. Uji-i, M. Moeller, B. Muls, J. Hofkens, and U. Alexiev.
            Monitoring the interaction of a single G-protein key binding site with rhodopsin disk membranes upon light-activation. Biochemistry, 2009, 48(18), 3801-3.

          • T.-Y. Kim, M. Moeller, K. Winkler, K. Kirchberg, and U. Alexiev.
            Dissection of environmental changes at the cytoplasmic surface of light-activated bacteriorhodopsin and visual rhodopsin: sequence of spectrally silent steps. Photochemistry and Photobiology, 2009, 85, 570–577.

          • M. Moeller and U. Alexiev.
            Surface Charge Changes upon Formation of the Signaling State in Visual Rhodopsin. Photochemistry and Photobiology, 2009, 85, 501–508.



          • D. Narzi, K. Winkler, J. Saidowsky, R. Misselwitz, A. Ziegler, R.A. Böckmann, and U. Alexiev
            Molecular determinants of MHC class I complex stability: Shaping antigenic features through long-range electrostatic interactions.
            J. Biol. Chem. 2008, 283, 23093-23103.



          • K. Winkler, A. Winter, C. Rückert, B. Uchanska-Ziegler, and U. Alexiev.
            Natural MHC Class I Polymorphism Controls the Pathway of Peptide Dissociation from HLA-B27 complexes.
            Biophys. J., 2007, 93(8),  2743-55.

          • K. Winkler, J. Saidowsky, A. Ziegler, and U. Alexiev.
            Molecular determinants of MHC class I stability.
            In:International Proceedings of the 13th International Congress of Immunology (Kalil, J. et al eds.), Medimont Bologna (2007) ISBN 978-88-7587-379-0

          • T.-Y. Kim, K. Winkler, and U. Alexiev.
            Picosecond Multi-dimensional Fluorescence Spectroscopy: A tool to measure real-time protein dynamics during function.
            Photochemistry and Photobiology 83, 378-384 (2007)

          • N. Lehmann, U. Alexiev, and K. Fahmy.
            Linkage Between the Intramembrane H-bond Network Around Aspartic Acid83 and the Cytosolic Environment of Helix 8 in Photoactivated Rhodopsin.
            J. Mol. Biol. 366, 1129-1141 (2007)



          • B. Uchanska-Ziegler, U. Alexiev, R. Hillig, M. Hülsmeyer, T. Pöhlmann, W. Saenger, A. Volz, and A. Ziegler.
            X-ray crystallography and dynamic studies of HLA-B*2705 and B*2709 molecules complexed with the same peptide.
            In: Immunobiology of the Human MHC: Proceedings of the 13th International Histocompatibility Workshop and Conference (Hansen, J.A., ed.), IHWG Press, Seattle (2006) ISBN:0-945278-03-9


          • G. Schröder, U. Alexiev, and H. Grubmüller.
            Simulation of fluorescence anisotropy experiments: Probing protein dynamics.
            Biophys. J. 89(6), 3757-70 (2005)

          • A. Selle, C. Kappelt, M. A. Bader, G. Marowsky, K. Winkler, U. and Alexiev.
            Picosecond pulse induced two-photon fluorescence enhancement in biological material applying grating waveguide structures.
            Optics Lett. 30, 1683-1685 (2005)

          • V. Jaakola, M. Rehn, M. Möller, U. Alexiev, A. Goldman, and G. J. Turner.
            G-protein-coupled receptor domain over-expression in Halobacterium salinarium: Long-range allosteric interactions from the intracellular to the extracellular side in heptahelical membrane proteins.
            Proteins 60, 412-23 (2005)

          • M. Hülsmeyer, K. Welfle, T. Pöhlmann, R. Misselwitz, U. Alexiev, H. Welfle, W. Saenger, B. Uchanska- Ziegler, and A. Ziegler.
            Thermodynamic and structural equivalence of two HLA-B27 subtypes complexed with a Self-peptide.
            J. Mol. Biol. 346, 1367-1379 (2005)



          • T. Pöhlmann, R. A. Böckmann, H. Grubmüller, B. Uchanska-Ziegler, A. Ziegler, and U. Alexiev.
            Differential peptide dynamics is linked to MHC polymorphism.
            J. Biol. Chem. 279, 28197-28201 (2004)



          • U. Alexiev, I. Rimke, and T. Pöhlmann.
            Elucidation of the nature of the conformational changes of the EF-interhelical loop in  bacteriorhodopsin and of the helix VIII on the cytoplasmic surface of rhodopsin: A time-resolved fluorescence depolarization study.
            J. Mol. Biol. 328, 705-719 (2003)

          • B. Uchanska-Ziegler, U. Alexiev, R. Hillig, M. Hülsmeyer, T. Pöhlmann, W. Saenger, A. Volz, and A. Ziegler (2003).
            In HLA 2002. The immunobiology of the human MHC. Eds. Dupont B, Hansen J. IHWG Press, Seattle



          • T. Mielke, U. Alexiev, M. Gläsel, H. Otto, and M. P. Heyn.
            Light-induced changes in the structure and accessibility of the cytoplasmic loops of rhodopsin in the activated MII-state.
            Biochemistry 41, 7875-84 (2002)

          • R. A. Krebs, U. Alexiev, R. Parthasarathy, A.-M. DeVita, and  M. S. Braiman.
            Detection of light-activated H+-release and M-intermediate formation from purified proteorhodopsin.
            BMC Physiology 2 (2002)



          • U. Alexiev, R. Mollaaghababa, H. G. Khorana, and M. P. Heyn.
            Evidence for long range allosteric interactions between the extracellular  and cytoplasmic parts of bacteriorhodopsin from the mutant R82A and its second site revertant R82A/G231C.
            J. Biol. Chem. 275, 13431-13440 (2000)

          • K. Heyne, J. Herbst, B. Dominguez  Herradon, U. Alexiev, and R. Diller.
            Reaction control in bacteriorhodopsin: Impact of Arg82 and Asp85 on the fast retinal isomerization, studied in the second site revertant Arg82Ala/Gly231Cys and various purple and blue forms of bacteriorhodopsin.
            Phys. Chem. B 104, 6053-6058 (2000)

          • M. S. Hutson, U. Alexiev , S. V. Shilov, K. J. Wise, and M. S. Braiman.
            Evidence for a perturbation of Arginine-82 in the bacteriorhodopsin photocycle from Time-­resolved Infrared spectra.
            Biochemistry 39, 13189-13200 (2000)



          • W. Behrens, U. Alexiev, R. Mollaaghababa, H. G. Khorana, and M. P. Heyn
            Structure of the interhelical loops and carboxyl terminus of bacteriorhodopsin by X-ray diffraction using site-directed heavy-atom labeling.
            Biochemistry 37, 10411-10419 (1998)

          • K. Heyne, R. Dziewior, R. Diller, and U. Alexiev.
            Single and double mutants of bacteriorhodopsin and their impact on photoisomerization.
            In Springer Series in Chemical Physics: "Ultrafast phenomena XI". Eds. T. Elsaesser, J.G. Fujimoto, D. A. Wiersma, W. Zinth, 681-683 (1998)



          • S. Moltke, U. Alexiev, and M. P. Heyn.
            Kinetics of light-induced intramolecular charge transfer and proton release in bacteriorhodopsin.
            Israel. J. Chem. 35, 235-248 (1996)



          • U. Alexiev, R. Mollaaghababa, P. Scherrer, H. G. Khorana, and M. P. Heyn.
            Rapid long ­range proton diffusion along the surface of the purple membrane and delayed proton transfer into the bulk.
            PNAS 92, 372-376 (1995)

          • U. Alexiev, P. Scherrer,  T. Marti,  H. G. Khorana, and M. P. Heyn.
            Time-resolved surface charge change on the cytoplasmic side of bacteriorhodopsin.
            FEBS Letters 373, 81-84 (1995)

          • S. Dickopf, U. Alexiev, M. P. Krebs, H. Otto, R. Mollaaghababa, H. G. Khorana, and M. P. Heyn.
            Proton transport by a bacteriorhodopsin mutant, aspartic acid-85—> asparagine, initiated in the unprotonated Schiff base state.
            PNAS 92, 11519-11523 (1995)



          • U. Alexiev, T. Marti, M. P. Heyn, H. G. Khorana, and P. Scherrer.
            Surface charge of bacteriorhodopsin detected with covalently bound pH-indicators at selected extracellular and cytoplasmic sites.
            Biochemistry 33, 298 - 306 (1994)

          • P. Scherrer, U. Alexiev, T. Marti, H. G. Khorana, and M. P. Heyn.
            Covalently bound pH­indicator dyes at selected extracellular or cytoplasmic sites in bacteriorhodopsin. I. Light­induced proton release kinetics and proton migration along the surface of bacteriorhodopsin micelles.
            Biochemistry 33, 13684-13699 (1994)

          • U. Alexiev, T. Marti, M. P. Heyn, H. G. Khorana, and  P. Scherrer.
            Covalently bound pH­indicator dyes at selected extracellular or cytoplasmic sites in bacteriorhodopsin.  II. Rotational orientation of helices D and E and kinetic correlation between M-formation and proton release in bacteriorhodopsin micelles.
            Biochemistry 33, 13693-13699 (1994)



      • P. Scherrer, U. Alexiev, M. P. Heyn, T. Marti, and H.G. Khorana.
        Proton movement and surface charge in bacteriorhodopsin detected by selectively attached pH-indicators.
        In Structures and Functions of Retinal Proteins. Ed. J.L. Rigaud. Colloque INSERM/John Libbey Eurotext Ltd. Vol. 221: 205 - 211 (1992)

      • D. A. Greenhalgh, S. Subramaniam, U. Alexiev, H. Otto, M. P. Heyn, and H. G.  Khorana.
        Effect of introducing different carboxylate-containing side chains at position 85 on chromophore formation and proton transport in bacteriorhodopsin.
        J. Biol. Chem. 267, 25734-25738 (1992)