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Department of Biochemistry

Calendar of Events

Publications of the Dutzler Group (in alphabetical order)

Lam, AKM. & Dutzler, R. Mechanism of pore opening in the calcium-activated chloride channel TMEM16A. Nat Commun 12, 786 (2021). PMID: 33542228.

Lam, AKM., Rheinberger, J., Paulino, C. & Dutzler, R. Gating the pore of the calcium-activated chloride channel TMEM16A. Nat Commun 12, 785 (2021). PMID: 33542223.

Drożdżyk, K., Sawicka, M., Bahamonde-Santos, MI., Jonas, Z., Deneka, D., Albrecht, C. & Dutzler, R. Cryo-EM structures and functional properties of CALHM channels of the human placenta. Elife 9, (2020). PMID: 32374262.

Quesada, R. & Dutzler, R. Alternative chloride transport pathways as pharmacological targets for the treatment of cystic fibrosis. J. Cyst. Fibros. 19 Suppl 1, S37-S41 (2020). PMID: 31662238.

Alvadia, C., Lim, NK., Clerico Mosina, V., Oostergetel, GT., Dutzler, R. & Paulino, C. Cryo-EM structures and functional characterization of the murine lipid scramblase TMEM16F. Elife 8, (2019). PMID: 30785399.

Kalienkova, V., Clerico Mosina, V., Bryner, L., Oostergetel, GT., Dutzler, R. & Paulino, C. Stepwise activation mechanism of the scramblase nhTMEM16 revealed by cryo-EM. Elife 8, (2019). PMID: 30785398.

Manatschal, C., Pujol-Giménez, J., Poirier, M., Reymond, JL., Hediger, MA. & Dutzler, R. Mechanistic basis of the inhibition of SLC11/NRAMP-mediated metal ion transport by bis-isothiourea substituted compounds. Elife 8, (2019). PMID: 31804182.

Walter, JD., Sawicka, M. & Dutzler, R. Cryo-EM structures and functional characterization of murine Slc26a9 reveal mechanism of uncoupled chloride transport. Elife 8, (2019). PMID: 31339488.

Deneka, D., Sawicka, M., Lam, AKM., Paulino, C. & Dutzer, R. Structure of a volume-regulated anion channel of the LRRC8 family. Nature 558, 254-259 (2018).  PMID: 29769723.

Lam, AKM. & Dutzler, R. Calcium-dependent electrostatic control of anion access to the pore of the calcium-activated cloride channel TMEM16A. Elife 7 pii: e39122 (2018). PMID: 30311910.

Ehrnstorfer IA, Manatschal C, Arnold FM, Laederach J, Dutzler R. Structural and mechanistic basic of proton-coupled metal ion transport in the SLC11/NRAMP family. Nat Commun. 8:140343 (2017). PMID: 28059071.

Paulino, C., Kalienkova, V., Lam, AKM., Neldner, Y. & Dutzler, R. Activation mechanism of the calcium-activated chloride channel TMEM16A revealed by cryo-EM. Nature 552, 421-425 (2017). PMID: 29236691.

Paulino C, Neldner Y, Lam AK, Kalienkova V, Brunner JD, Schenck S &  Dutzler R. Structural basis for anion conduction in the calcium-activated chloride channel TMEM16A. Elife. May 31;6. pii: e26232 (2017). PMID: 28561733.

Schenck, S., Kunz, L., Sahlender, D., Pardon, E., Geertsma, ER., Savtchouk, I., Suzuki, T., Neldner, Y., Štefanić, S., Steyaert, J., Volterra, A. & Dutzler, R. Generation and Characterization of Anti-VGLUT Nanobodies Acting as Inhibitors of Transport. Biochemistry 56, 3962-3971 (2017). PMID: 28731329.

Bertozzi, C., Zimmermann, I., Engeler, S., Hilf, RJ. & Dutzler, R. Signal Transduction at the Domain Interface of Prokaryotic Pentameric Ligand-Gated Ion Channels. PLoS Biol. 14, e1002393 (2016). PMID: 26943937

Brunner, JD., Schenck, S. & Dutzler, R. Structural basis for phospholipid scrambling in the TMEM16 family. Curr. Opin. Struct. Biol. 39, 61-70 (2016). PMID: 27295354.

Lim, NK., Lam, AK. & Dutzler, R. Independent activation of ion conduction pores in the double-barreled calcium-activated chloride channel TMEM16A. J. Gen. Physiol. 148, 375-392 (2016). PMID: 27799318.

Geertsma, ER., Chang, YN., Shaik, FR., Neldner, Y., Pardon, E., Steyaert, J. & Dutzler, R. Structure of a prokaryotic fumarate transporter reveals the architecture of the SLC26 family.  Nat. Struct. Mol. Biol. 22, 803-8 (2015). PMID: 26367249.

Brunner, JD., Lim, NK., Schenck, S., Duerst, A. & Dutzler, R. X-ray structure of a calcium-activated TMEM16 lipid scramblase. Nature 516, 207-12 (2014). PMID: 25383531.

Ehrnstorfer, IA., Geertsma, ER., Pardon, E., Steyaert, J. & Dutzler, R. Crystal structure of a SLC11 (NRAMP) transporter reveals the basis for transition-metal ion transport. Nat. Struct. Mol. Biol. 21, 990-6 (2014). PMID: 25326704.

Garcia-Celma, J., Szydelko, A. & Dutzler, R. Functional characterization of a CIC transporter by solid-supported membrane electrophysiology. J Gen Physiol. 141, 479-491 (2013).

Zimmermann, I, Marabelli, A., Bertozzi, C., Sivilotti, LG. & Dutzler, R. Inhibition of the prokaryotic pentameric ligand-gated ion channel ELIC by divalent cations. PLOS Biol. 10, e1001429 (2012).

Geertsma, E. & Dutzler, R. A versatile and efficient high-throughput cloning tool for structural biology. Biochemistry 50, 3272-3278 (2011).

Zimmermann, I. & Dutzler, R. Ligand activation of the prokaryotic pentameric ligand-gated ion channel ELIC. PLoS Biol. 9(6): e 1001101 (2011).

Hilf, R., Bertozzi, C., Zimmermann, I., Reiter, A., Trauner, D., & Dutzler R. Structural basis of open channel block in a prokaryotic pentameric ligand-gated ion channel. Nat. Struct. Mol. Biol. 17, 1330-1336 (2010).

Hilf, R. & Dutzler, R. A prokaryotic perspective on pentameric ligand-gated ion channel structure. Curr Opin Struct Biol. 19, 418-424 (2009). 

Hilf, R. & Dutzler, R. Structure of a potentially open state of a proton-activated pentameric ligand-gated channel. Nature 457, 115-118 (2009).

Warmuth, S., Zimmermann, I. & Dutzler, R. X-ray structure of the C-terminal domain of a prokaryotic cation-chloride cotransporter. Structure 17, 538-546 (2009).

Hilf, R. & Dutzler, R. X-ray structure of a prokaryotic pentameric ligand-gated channel. Nature 452, 375-379 (2008).

Alioth, S., Meyer, S., Dutzler, R. & Pervushin, K. The cytoplasmic domain of the chloride channel ClC-0: structural and dynamic characterization of flexible regions. J. Mol. Biol. 369,1163-1169 (2007).

Dutzler R. A structural perspective on ClC channel and transporter function. FEBS Lett. 581, 2839-2844 (2007).

Markovic, S. & Dutzler, R. The Structure of the Cytoplasmic Domain of the Chloride Channel ClC-Ka Reveals a Conserved Interaction Interface. Structure 15, 715-725 (2007).

Meyer S., Savaresi S., Forster I.C. & Dutzler R. Nucleotide recognition by the cytoplasmic domain of the human chloride transporter ClC-5. Nat. Struct. Mol. Biol. 14, 60-67 (2007).

Accardi, A. Lobet, S. Williams, C. Miller, C. & Dutzler, R. Synergism between halide binding and proton transport in a CLC-type exchanger. J. Mol. Biol. 362, 691-699 (2006).

Dutzler R. The ClC family of chloride channels and transporters. Curr. Opin. Struct. Biol. 16, 439-446 (2006).

Lobet, S. & Dutzler, R. Ion-binding properties of the ClC chloride selectivity filter. EMBO J. 25, 24-33 (2006).

Meyer, S. & Dutzler, R. Crystal structure of the cytoplasmic domain of the chloride channel ClC-0. Structure 14, 299-307 (2006).

Dutzler, R. The structural basis of ClC chloride channel function. Trends Neurosci. 27, 315-20 (2004).

Dutzler, R. Structural basis for ion conduction and gating in ClC chloride channels. FEBS Lett. 564, 229-33 (2004).

Dutzler, R., Campbell, E. B. & MacKinnon, R. Gating the selectivity filter in ClC chloride channels. Science 300, 108-12 (2003).

Dutzler, R., Campbell, E. B., Cadene, M., Chait, B. T. & MacKinnon, R. X-ray structure of a ClC chloride channel at 3.0 A reveals the molecular basis of anion selectivity. Nature 415, 287-94 (2002).

Dutzler, R., Schirmer, T., Karplus, M. & Fischer, S. Translocation mechanism of long sugar chains across the maltoporin membrane channel. Structure 10, 1273-84 (2002).

Van Gelder, P., Dutzler, R., Dumas, F., Koebnik, R. & Schirmer, T. Sucrose transport through maltoporin mutants of Escherichia coli. Protein Eng. 14, 943-8 (2001).

Dutzler, R., Rummel, G., Alberti, S., Hernandez-Alles, S., Phale, P., Rosenbusch, J., Benedi, V. & Schirmer, T. Crystal structure and functional characterization of OmpK36, the osmoporin of Klebsiella pneumoniae. Structure 7, 425-34 (1999).

Ringhofer, S., Kallen, J., Dutzler, R., Billich, A., Visser, A. J., Scholz, D., Steinhauser, O., Schreiber, H., Auer, M. & Kungl, A. J. X-ray structure and conformational dynamics of the HIV-1 protease in complex with the inhibitor SDZ283-910: agreement of time-resolved spectroscopy and molecular dynamics simulations. J. Mol. Biol. 286, 1147-59 (1999).

Wang, Y. F., Dutzler, R., Rizkallah, P. J., Rosenbusch, J. P. & Schirmer, T. Channel specificity: structural basis for sugar discrimination and differential flux rates in maltoporin. J. Mol. Biol. 272, 56-63 (1997).

Dutzler, R., Wang, Y. F., Rizkallah, P., Rosenbusch, J. P. & Schirmer, T. Crystal structures of various maltooligosaccharides bound to maltoporin reveal a specific sugar translocation pathway. Structure 4, 127-34 (1996).