Harder, Daniel

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2016

Harder, Daniel; Hirschi, Stephan; Ucurum Fotiadis, Zöhre; Goers, Roland; Meier, Wolfgang; Müller, Daniel J; Fotiadis, Dimitrios José (2016). Engineering a Chemical Switch into the Light-driven Proton Pump Proteorhodopsin by Cysteine Mutagenesis and Thiol Modification. Angewandte Chemie (International ed.), 55(31), pp. 8846-8849. Wiley-VCH 10.1002/anie.201601537

Hirschi, Stephan; Stauffer, Mirko; Harder, Daniel; Müller, Daniel J; Meier, Wolfgang; Fotiadis, Dimitrios José (2016). Engineering and Assembly of Protein Modules into Functional Molecular Systems. CHIMIA, 70(6), pp. 398-401. Schweizerische Chemische Gesellschaft 10.2533/chimia.2016.398

Boggavarapu, Venkata Ravi Naga Rajendr; Hirschi, Stephan; Harder, Daniel; Meury, Marcel; Ucurum Fotiadis, Zöhre; Bergeron, Marc; Fotiadis, Dimitrios José (2016). Purification of Human and Mammalian Membrane Proteins Expressed in Xenopus laevis Frog Oocytes for Structural Studies. In: Mus-Veteau, Isabelle (ed.) Heterologous Expression of Membrane Proteins. Methods and Protocols. Methods in Molecular Biology: Vol. 1432 (pp. 223-242). New York: Springer 10.1007/978-1-4939-3637-3_14

2015

Petrosyan, Rafayel; Bippes, Christian A; Walheim, Stefan; Harder, Daniel; Fotiadis, Dimitrios José; Schimmel, Thomas; Alsteens, David; Müller, Daniel J (2015). Single-molecule force spectroscopy of membrane proteins from membranes freely spanning across nanoscopic pores. Nano letters, 15(5), pp. 3624-3633. American Chemical Society 10.1021/acs.nanolett.5b01223

Boggavarapu, Venkata Ravi Naga Rajendr; Jeckelmann, Jean-Marc; Harder, Daniel; Ucurum Fotiadis, Zöhre; Fotiadis, Dimitrios José (2015). Role of electrostatic interactions for ligand recognition and specificity of peptide transporters. BMC biology, 13(58), p. 58. BioMed Central 10.1186/s12915-015-0167-8

2014

Meury, Marcel; Costa Torres, Meritxell; Harder, Daniel; Stauffer, Mirko; Jeckelmann, Jean-Marc; Brühlmann, Béla; Rosell, Albert; Ilgü, Hüseyin; Kovar, Karin; Palacín, Manuel; Fotiadis, Dimitrios José (2014). Detergent-induced stabilization and improved 3D map of the human heteromeric amino acid transporter 4F2hc-LAT2. PLoS ONE, 9(10), e109882. Public Library of Science 10.1371/journal.pone.0109882

Jeckelmann, Jean-Marc; Harder, Daniel; Ucurum Fotiadis, Zöhre; Fotiadis, Dimitrios José (2014). 2D and 3D crystallization of a bacterial homologue of human vitamin C membrane transport proteins. Journal of structural biology, 188(1), pp. 87-91. Elsevier 10.1016/j.jsb.2014.08.004

2013

Bippes, Christian A.; Ge, Lin; Meury, Marcel; Harder, Daniel; Ucurum, Zöhre; Daniel, Hannelore; Fotiadis, Dimitrios; Müller, Daniel J. (2013). Peptide transporter DtpA has two alternate conformations, one of which is promoted by inhibitor binding. Proceedings of the National Academy of Sciences of the United States of America - PNAS, 110(42), E3978-E3986. National Academy of Sciences NAS 10.1073/pnas.1312959110

Boggavarapu, Rajendra; Jeckelmann, Jean-Marc; Harder, Daniel; Schneider, Philipp; Ucurum, Zöhre; Hediger, Matthias; Fotiadis, Dimitrios (2013). Expression, purification and low-resolution structure of human vitamin C transporter SVCT1 (SLC23A1). PLoS ONE, 8(10), e76427. Public Library of Science 10.1371/journal.pone.0076427

2012

Harder, Daniel; Fotiadis, Dimitrios (2012). Measuring substrate binding and affinity of purified membrane transport proteins using the scintillation proximity assay. Nature protocols, 7(9), pp. 1569-78. London: Nature Publishing Group 10.1038/nprot.2012.090

2011

Jeckelmann, Jean-Marc; Harder, Daniel; Mari, Stefania A; Meury, Marcel; Ucurum, Zöhre; Müller, Daniel J; Erni, Bernhard; Fotiadis, Dimitrios (2011). Structure and function of the glucose PTS transporter from Escherichia coli. Journal of structural biology, 176(3), pp. 395-403. San Diego, Calif.: Elsevier 10.1016/j.jsb.2011.09.012

Meury, Marcel; Harder, Daniel; Ucurum, Zöhre; Boggavarapu, Rajendra; Jeckelmann, Jean-Marc; Fotiadis, Dimitrios (2011). Structure determination of channel and transport proteins by high-resolution microscopy techniques. Biological chemistry, 392(1-2), pp. 143-50. Berlin: De Gruyter 10.1515/BC.2011.004

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