Our Publications

All Publications 

(undergraduate authors in italics)

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2023

Hellmich, U.A. (2023) Dynamic ion channel defies dogma.
Nature, doi: d41586-023-02486-9

  •  invited News and Views Article for paper by the Scheuring lab on the first pentameric TRP channel structure 
  • Read their paper here: Lansky et al (2023) A pentameric TRPV3 channel with a dilated pore. Nature, https://doi.org/10.1038/s41586-023-06470-1 


Li, K.K., Cho, Y.I., Tran, M.A., Wiedemann, C., Koweek, R.S., Khánh Hoàng, N., Hamrick, G.S., Bowen, M.A., Koknona, B., Beld, J., Hellmich*, U.A., Charkoudian*, L. (2023) Strategic engineering unlocks in vitro type II polyketide biosynthesis. (*co-corresponding authors)
preprint available @ BioRxiv, doi: 10.1101/2023.08.02.551649v1 


Wiedemann, C., Whittaker, J.J., Pérez Carrillo, V.H., Goretzki, B., Dajka, M., Tebbe, F., Harder, J.-M., T., Krajczy, P., Joseph, B., Hausch, F., Guskov, A., Hellmich, U.A. (2023) Legionella pneumophila macrophage infectivity potentiator protein appendage domains modulate protein dynamics and inhibitor binding.
Int. J. Biol. Macromol., accepted


Deutscher, R., Karagöz, S., Purder, P., Kolos, J., Meyners, C., Sugiarto, W., Krajczy, P., Tebbe, F., Geiger, T., Ünal. C., Hellmich, U.A., Steinert, M., Hausch, F. (2023) [4.3.1] Bicyclic FKBP ligands inhibit Legionella pneumophila infection by LpMip-dependent and LpMip independent mechanisms.
ChemBioChem, accepted, doi: 10.1002/cbic.202300442 


Goretzki, B., Wiedemann, C., McCray, B.A., Schäfer, S.L., Jansen, J., Tebbe, F., Mitrovic, S.A., Nöth, J.,  Claveras Cabezudo, A., Donohue, J., Jeffries, J.M., Steinchen, W., Stengel, F., Sumner, C.J., Hummer, G., Hellmich, U.A. (2023) Crosstalk between regulatory elements in the disordered TRPV4 N-terminus modulates lipid-dependent channel activity.
Nature Commun. 14: 4165, doi: 10.1038/s41467-023-39808-4


Maus, H., Hammerschmidt, S.J., Hinze, G., Barthels, F., Pérez Carrillo, V.H., Hellmich, U.A., Basché, T., Schirmeister, T. (2023) The effects of allosteric and competitive inhibitors on ZIKV protease conformational dynamics explored through smFRET, nanoDSF, DSF, and 19F-NMR.
Eur. J. Med. Chem., 258: 115573, doi: 10.1016/j.ejmech.2023.115573

Stallforth*, P., Mittag, M., Brakhage, A.A., Hertweck, C., Hellmich*, U.A. (2023) Functional Modulation of Chemical Mediators in Microbial Communities. (*corresponding authors) 

Trends Biochem. Sci., 48(1): 71-81 doi: 10.1016/j.tibs.2022.07.006 


2022

Zhang, L., Simonsen, C., Zimova, L., Wang, K., Moparthi, L., Gaudet, R., Ekoff, M., Nilsson, G., Hellmich, U.A., Vlachova, V., Gourdon, P.E., Zygmunt, P.M. (2022) Cannabinoid non-cannabidiol site modulation of TRPV2 structure and function.
Nature Commun. 13: 7483, doi:s41467-022-35163-y

El Hamdaoui, Y., Zheng, F., Ye L., Fritz, N., Tran, M.A., Schwickert, K., Schirmeister, T., Braeuning, A., Lichtenstein, D., Hellmich. U.A., Weikert, D., Heinrich, M., Treccani, G., Schäfer, M.K.E., Nowak, G., Nürnberg, B., Alzheimer, C., Müller, C.P., Friedland, K. (2022) Analysis of hyperforin (St John’s wort) action at TRPC6 channels in mood disorders leads to new anti-depressants.
Molecular Psychiatry, 27: 5070–5085, doi: 10.1038/s41380-022-01804-3.


Wiedemann, C., Goretzki, B., Merz, Z.N., Tebbe, F., Schmitt, P., Hellmich, U.A. (2022) Extent of intrinsic disorder and NMR chemical shift assignments of the distal N-termini from human TRPV1, TRPV2 and TRPV3 ion channels.

Biomol. NMR Assign., 16: 289–296, doi: 10.1007/s12104-022-10093-4


Goretzki, B., Tebbe, F., Mitrovic, S.-A., Hellmich, U.A. (2022) Backbone NMR assignments of the extensive human and chicken TRPV4 N-terminal intrinsically disordered regions as important players in ion channel regulation.

Biomol. NMR Assign., 16: 205–212, doi: 10.1007/s12104-022-10080-9


Bothe, S., Hänzelmann, P., Boehler, S., Kehrein, J., Zehe., M., Wiedemann, C., Hellmich, U.A., Brenk, R., Schindelin, H., Sotriffer, C. (2022) Fragment screening using biolayer interferometry reveals ligands targeting the SHP-motif binding site of the AAA+ ATPase p97. 

Commun. Chem. 5,  169, doi:  10.1038/s42004-022-00782-5 


Previti, S., Ettari, R., Di Chio, C., Ravichandran, R., Bogacz, M., Hellmich, U.A., Schirmeister, T., Cosconati, S., Zappalà. M. (2022) Development of Reduced Peptide Bond Pseudopeptide Michael Acceptors for the Treatment of Human African Trypanosomiasis.

Molecules. 27(12):3765. doi: 10.3390/molecules27123765


Jung, S., Fuchs, N., Grathwohl, C., Hellmich, U.A., Wagner, A., Diehl, E., Willmes, T., Sotriffer, C., Schirmeister, T. (2022) New peptidomimetic rhodesain inhibitors with improved selectivity towards human cathepsins.

Eur. J. Med. Chem., 238: 114460, doi: 10.1016/j.ejmech.2022.114460 


Di Chio, C., Previti, S., Amendola, G., Ravichandran, R., Wagner, A., Cosconati, S., Hellmich, U.A., Schirmeister, T., Zappalà, M., Ettari, R. (2022) Development of novel dipeptide nitriles as inhibitors of rhodesain of Trypanosoma brucei rhodesiense.
Eur. J. Med. Chem.,  236: 114328, doi: 10.1016/j.ejmech.2022.114328 


Aisenberg, W.H., McCray, B.A., Sullivan, J.M., Diehl, E., Devine, L.R., Bagnell, A.M., Alevy, J., Carr, P., Goretzki, B., Cole, R.N., Hellmich, U.A., Sumner, C. (2022) Multi-ubiquitination of TRPV4 reduces channel activity independent of surface localization.

J. Biol. Chem., 298(4): 101826  doi: 10.1016/j.jbc.2022.101826

Bando, Y., Hou, Y., Seyfarth, L., Probst, J., Götze, S., Bogacz, M., Hellmich, U.A., Stallforth, P., Mittag, M., Arndt, H.-D. (2022) Total Synthesis and Structural Correction of the Cyclic Lipodepsipeptide Orfamide A.
Chem. Eur. J.,  28(20): e202104417, doi: 10.1002/chem.202104417


Taga, A., Peyton, M., Goretzki, B., Gallagher, T.G., Ritter, A., Harper, A., Crawford, T.O., Hellmich, U.A., Sumner, C.J., McCray, B.A. (2022) TRPV4 mutations associated with mixed neuropathy and skeletal dysplasia phenotypes result in severe gain of ion channel function.
Ann. Clin. Transl. Neurol.,  9(3): 375-391, doi:10.1002/acn3.51523


Pérez Carrillo, V.H., Rose-Sperling, D., Tran, M.A., Wiedemann, C., Hellmich, U.A. (2022) Backbone NMR assignments of the nucleotide binding domain of the Bacillus subtilis ABC multidrug transporter BmrA in the post-hydrolysis state.
Biomol. NMR Assign., 16(1):81-86, doi:10.1007/s12104-021-10063-2

Hellmich*, U.A., Delemotte, L. (2022) TRP channels: branching out into the fungal kingdom

Structure, 30(4): 2-4, doi.org/10.1016/j.str.2021.12.006  (*corr. author)

  • invited preview for paper by the Moiseenkova-Bell lab on the first fungal TRP channel structure 
  • Read their paper here: Ahmed et al (2021) Structure of the ancient TRPY1 channel from Saccharomyces cerevisiae reveals mechanisms of modulation by lipids and calcium. Structure, S0969-2126(21)00298-7. 


2021

Jung, S., Fuchs, N., Johé, P., Wagner, A., Diehl, E., Yuliani, T., Zimmer, C., Barthels, F., Klein, P., Opatz, T., Tenzer, S., Distler, U., Räder, H.-J., Weil, T., Kersten, C., Hellmich, U.A., Klein, J., Schirmeister, T. (2021) Fluorovinylsulfones and -sulfonates as potent covalent reversible inhibitors of the trypanosomal cysteine protease rhodesain: SAR, inhibition mechanism, metabolism and in vivo studies.
J. Med. Chem., 64(16):12322-12358, doi: 10.1021/acs.jmedchem.1c01002


Götz, C., Hinze, G., Gellert, A., Maus, H., von Hammerstein, F., Hammerschmidt, S., Lauth, L.M., Hellmich, U.A., Schirmeister, T., Basché, T. (2021) Conformational Dynamics of the Dengue Virus Protease revealed by Fluorescence Correlation and Single-Molecule FRET studies.
J. Phys. Chem. B,  125(25): 6837–6846, doi: 10.1021/acs.jpcb.1c01797


Johé, P., Jaenicke, E., Neuweiler, H., Schirmeister, T., Kersten, C., Hellmich, U.A (2021) Structure, interdomain dynamics and pH-dependent autoactivation of pro-rhodesain, the main lysosomal cysteine protease from African trypanosomes.

J. Biol. Chem., 296:100565, doi: 10.1016/j.jbc.2021.100565 


Goretzki, B., Guhl, C., Tebbe, F., Harder, J.-M., Hellmich, U.A. (2021) Unstructural Biology of TRP Ion Channels: The Role of Intrinsically Disordered Regions in Channel Function and Regulation.
J. Mol. Biol., 166931, doi:10.1016/j.jmb.2021.166931

Johé, P., Jung, S., Endres, E., Kersten, C., Zimmer, C., Ye, W., Sönnichsen, C., Hellmich, U.A., Sotriffer, C., Schirmeister, T., Neuweiler, H. (2021) Warhead reactivity limits the speed of inhibition of the cysteine protease rhodesain.
ACS Chem. Biol., 16(4):661–670, doi: 10.1021/acschembio.0c00911

McCray, B.A., Diehl, E., Sullivan, J.M., Aisenberg, W.H., Zaccor, N.W., Lau, A.R., Rich, D., Goretzki, B., Hellmich, U.A., Lloyd, T.E., Sumner, C.J. (2021) Neuropathy-causing TRPV4 mutations disrupt TRPV4-RhoA interactions and impair neurite extension.
Nature Commun., 12:1444,  doi: 10.1038/s41467-021-21699-y

Hamdoun*, A., Hellmich*, U.A., Kuchler*, K., Szakacs*, G. (2021) The Incredible Diversity of Structures and Functions of ABC Transporters.
FEBS Lett.,  595(6):671-674. doi: 10.1002/1873-3468.14061 (invited editorial) (*corresponding authors)

Zengerling, L., Kemper. B., Hellmich, U.A., Besenius, P. (2021) Synthesis and Structural Stability of α-Helical Au(I)-Metallopeptides. 

Synlett, 32:344-349, doi: 10.1055/a-1290-8412

2020

Wesenberg, L., Diehl, E., Zähringer, T.B., Dörr, C., Schollmeyer, D., Shimizu, A., Yoshida, J., Hellmich, U.A., Waldvogel, S.R. (2020) Metal-free Twofold Electrochemical C-H Amination of Activated Arenes: Application to Medicinally Relevant Precursor Syntheses.
Chem. Eur. J., 26(72):17574-17580. doi: 10.1002/chem.202003852

Jungglas, B., Orru, R., Axt, A., Siebenaller, C., Steinchen, W., Heidrich, J., Hellmich, U.A., Hellmann, N., Wolf, E., Weber, S.L., Schneider, D. (2020) IM30 IDPs form a membrane protective carpet upon super-complex disassembly.
Commun. Biol., 3(1):595. doi: 10.1038/s42003-020-01314-4


Ford*, R. C., Hellmich*, U. A. (2020) What monomeric nucleotide binding domains can teach us about dimeric ABC proteins. 

FEBS Lett., 594(23):3857–3875. doi: 10.1002/1873-3468.13921 (*corresponding authors)

Maiorana, S., Ettari, R., Previti, S., Amendola, G., Wagner, A., Cosconati, S., Hellmich, U.A., Schirmeister, T., Zappalà, M. (2020) Peptidyl vinyl ketone irreversible inhibitors of rhodesain: modifications of the P2 fragment.
ChemMedChem, 15(16):1552-1561. doi: 10.1002/cmdc.202000360


Dietschreit, J.C.B., Wagner, A., Le, T.A., Klein, P., Schindelin, H., Opatz, T., Engels, B., Hellmich*, U.A., Ochsenfeld*, C. (2020) Predicting 19F NMR Chemical Shifts: A Combined Computational and Experimental Study of a Trypanosomal Oxidoreductase-Inhibitor Complex.
Angew. Chem. Int. Ed. Engl., 59(31):12669-12673 doi: 10.1002/anie.202000539 (*corresponding authors)

Klein, P., Barthels, F., Johé, P., Wagner, A., Tenzer, S., Distler, U., Le, T.A., Schmid, P., Engel, V., Engels, B., Hellmich, U.A., Opatz, T., Schirmeister, T.  (2020) Naphthoquinones as inhibitors of cysteine proteases.
Molecules, 25(9):2064. doi: 10.3390/molecules25092064

Klein, P., Johé, P., Wagner, A., Jung, S., Kühlborn, J., Tenzer, S., Distler, U., Waigel, W., Engels, B., Hellmich, U.A., Opatz, T., Schirmeister, T. (2020) New Cysteine Protease Inhibitors: Electrophilic (Het)arenes and unexpected Prodrug Identification.
Molecules, 25(6):1451. doi: 10.3390/molecules25061451

Goretzki, B., Heiby, J., Hacker, C. Neuweiler, H., Hellmich, U.A. (2020) NMR assignments of a dynamically perturbed and dimerization inhibited N-terminal domain variant of a spider silk protein from E. australis.
Biomol NMR Assign. 14:67–71. doi: 10.1007/s12104-019-09922-w.

Steiert, E., Ewald, J., Wagner, A., Hellmich, U.A., Frey, H., Wich, P.R. (2020) pH-Responsive Protein Nanoparticles via Conjugation of Degradable PEG to the Surface of Cytochrome c.
Polymer Chem. 11:551-559. doi: 10.1039/C9PY01162E

FEBS Letters Special Edition "Diversity of Structure and Function of ABC Transporters", Guest Editors: Amro Hamdoun, Ute A. Hellmich, Karl Kuchler, Gergely Szakacs

2019

Millies, B., von Hammerstein, F., Gellert, A., Hammerschmidt, S., Barthels, F., Göppel, U., Immerheiser, M., Elgner, F., Jung, N., Basic, M., Kersten, C., Kiefer, W., Bodem, J., Hildt, E., Windbergs, M., Hellmich*, U.A., Schirmeister*, T. (2019) Proline-based allosteric inhibitors of Zika and Dengue virus NS2B/NS3 proteases.
J. Med. Chem. 62(24):11359-11382. doi: 10.1021/acs.jmedchem.9b01697 (*corresponding authors)

Ettari, R., Previti, S., Maiorana, S., Amendola, G., Wagner, A., Cosconati, S., Schirmeister, T., Hellmich, U.A., Zappalà, M. (2019) Optimization strategy of novel peptide-based Michael acceptors for the treatment of Human African Trypanosomiasis.
J. Med. Chem. 62(23):10617-10629. doi: 10.1021/acs.jmedchem.9b00908

Heiby*, J., Goretzki*, B., Johnson, C., Hellmich#, U.A., Neuweiler#, H. (2019) Methionine in a protein hydrophobic core drives tight interactions required for assembly of spider silk.
Nature Commun. 10(1):4378.  doi: 10.1038/s41467-019-12365-5. (*shared first authors, #corresponding authors)


von Hammerstein*, F., Lauth*, L. M., Hammerschmidt, S., Wagner, A., Schirmeister, T., Hellmich, U.A. (2019) Cis autocatalytic cleavage of glycine‐linked Zika virus NS2B‐NS3 protease constructs.
FEBS Lett. 593(16):2204-2213. doi: 10.1002/1873-3468.13507. (*shared first authors)


Viet*, K.K., Wagner*, A., Schwickert*, K., Hellwig, N., Brennich, M., Bader, N., Schirmeister, T., Morgner, N., Schindelin, H., Hellmich, U.A. (2019) Structure of the human TRPML2 ion channel extracytosolic/lumenal domain.
Structure, 27(8):1246-1257. doi: 10.1016/j.str.2019.04.016. (*shared first authors) 


Rose-Sperling, D., Tran, M. A., Lauth, L.M., Goretzki, B., Hellmich, U.A. (2019) 19F NMR as a versatile tool to study membrane protein structure and dynamics.
Biol. Chem., 400(10):1277-1288. doi: 10.1515/hsz-2018-0473

Wagner, A., Le, T.A., Brennich, M., Klein, P., Bader, N., Diehl, E., Paszek, D., Weickhmann, A.K., Dirdjaja, N., Krauth-Siegel, R.L., Engels, B., Opatz, T., Schindelin, H., Hellmich, U.A. (2019) Inhibitor-Induced Dimerization of an Essential Oxidoreductase from African Trypanosomes.
Angewandte Chemie Int. Ed. 58(11):3640-3644. doi: 10.1002/anie.201810470


Wagner, A., Le, T. A., Brennich, M., Klein, P., Bader, N., Diehl, E., Paszek, D., Weickhmann, A. K., Dirdjaja, N., Krauth-Siegel, R. L., Engels, B., Opatz, T., Schindelin, H., Hellmich, U.A. (2019) Inhibitor-induzierte Dimerisierung einer essentiellen Oxidoreduktase aus Afrikanischen Trypanosomen. doi: 10.1002/ange.201810470
Angewandte Chemie, 131(11):3679-3683


2018

Goretzki*, B., Glogowski*, N.A., Diehl, E., Duchardt-Ferner, E., Hacker, C., Gaudet, R., Hellmich, U. A. (2018) Structural basis of TRPV4 N-terminus interaction with Syndapin/PACSIN1-3 and PIP2.
Structure, 26(12):1583-1593. doi: 10.1016/j.str.2018.08.002 (*shared first authors) 


Howard*, R.J., Carnevale*, V., Delemotte*, L., Hellmich*, U. A., Rothberg*, B. (2018) Permeating disciplines: overcoming barriers between molecular simulations and classical structure-function approaches in biological ion transport.
Biochim. Biophys. Acta Biomembr. 1860(4):927-942. doi: 10.1016/j.bbamem.2017.12.013. Front Cover. (*corresponding authors)

Szöllösi, D., Rose-Sperling, D, Hellmich, U. A., Stockner, T. (2018) Comparison of mechanistic transport cycle models of ABC exporters.
Biochim. Biophys. Acta Biomembr. 1860(4):818-832. doi: 10.1016/j.bbamem.2017.10.028.

Hellmich*, U.A., McILwain*, B., Doshi*, R. (2018) Where do we go from here? Membrane protein research beyond the structure-function horizon. (invited editorial)
Biochim. Biophys. Acta Biomembr. 1860(4):801-803. doi: 10.1016/j.bbamem.2017.12.016. (*corresponding authors)

BBA Biomembranes Special Edition "Beyond the Structure-Function Horizon of Membrane Proteins", Guest Editors: Ute A. Hellmich, Rupak Doshi, Benjamin McIlwain

 

2017

Preveti, S., Ettari, R., Cosconati, S., Amendola, G., Chouchene, K., Wagner, A., Hellmich, U.A., Ulrich, K., Krauth-Siegel, R.L., Wich, P.R., Schmid, I., Schirmeister, T., Gut, J., Rosenthal, P.J., Grasso, S., Zappalà, M. (2017) Development of novel peptide-based Michael acceptors targeting rhodesain and falcipain-2 for the treatment of Neglected Tropical Diseases (NTDs).

J. Med. Chem. 60(16):6911-6923.

Wagner, A., Diehl, E., Krauth-Siegel, R.L., Hellmich, U. A. (2017) Backbone NMR assignments of tryparedoxin, the central protein in the hydroperoxide detoxification cascade of African trypanosomes, in the oxidized and reduced form.
Biomol. NMR Assign. 11(2):193-196.

Neumann, J., Rose-Sperling, D. and Hellmich, U. A. (2017) Diverse relations between lipids and ABC transporters: an overview.
Biochim. Biophys. Acta Biomembr.  1859(4):605-618.

 

2016

Latorre, A., Schirmeister, T., Kesselring, J., Jung, S., Johé, P., Hellmich, U. A., Heilos, A., Engels, B., Krauth-Siegel, R. L., Dirdjaja, N., Bou-Iserte, L., Rodríguez, S., González, F. V. (2016) Dipeptidyl Nitroalkenes as Potent Reversible Inhibitors of Cysteine Proteases Rhodesain and Cruzain.

ACS Med. Chem. Lett. 7(12):1073-1076.

Schirmeister, T., Kesselring, J., Jung, S., Schneider, T., Weickert, A., Becker, J., Lee, W., Bamberger, D., Wich, P. R., Distler, U., Tenzer, S., Johé, P., Hellmich, U. A., Engels, B. (2016) Quantum chemical-based Protocol for the rational Design of covalent Inhibitors.
J. Am. Chem. Soc., 138(27):8332-5. 
 

2015

Hellmich*, U.A., Mönkemeyer, L., Velamakanni, S., van Veen, H.W., Glaubitz*, C. (2015) Effects of nucleotide binding to LmrA: A combined MAS-NMR and solution NMR study. 

Biochim. Biophys. Acta Biomembr. 1848(12):3158-65. (*corresponding authors)


Hacker, C., Christ, N. A., Duchardt-Ferner, E., Korn, S., Göbl, C., Berninger, L., Düsterhus, S., Hellmich, U. A., Madl, T., Kötter, P., Entian, K., Wöhnert, J. (2015) The solution structure of the lantibiotic immunity protein NisI and its interactions with nisin.
J. Biol. Chem.290(48):28869-86.
 

2014 and earlier

Hellmich*, U.A. and Gaudet*, R. (2014) High-resolution views of TRPV1 and their implications for the TRP channel superfamily. In Mammalian Transient Receptor Potential (TRP) cation channels, B. Nilius, and V. Flockerzi, eds. (Heidelberg, Germany: Springer DE). 
Handb. Exp. Pharmacol. 223:991-1004.  (*corresponding authors)

Hellmich*, U.A. and Gaudet*, R. (2014) Structural Biology of TRP Channels. In Mammalian Transient Receptor Potential (TRP) cation channels, B. Nilius, and V. Flockerzi, eds. (Heidelberg, Germany: Springer DE). 
Handb. Exp. Pharmacol. 223:963-90. (*corresponding authors)

Hellmich, U.A., Weis, B.L., Luitikov, A., Wurm, J.P., Christ, N.A., Hantke, K., Kötter, P., Entian, K.D., Schleiff, E. and Wöhnert, J. (2013) Essential ribosome assembly factor Fap7 regulates a hierarchy of RNA-protein interactions during small ribosomal subunit biogenesis.
Proc. Nat. Acad. Sci. USA 110(38):15253-8.

Garcia-Elias, A., Mrkonjic, S., Pardo-Pastor, C., Inada, H., Hellmich, U.A., Rubio-Moscardo, F., Plata, C., Gaudet, R., Vicente, R. and Valverde, M.A. (2013) PIP2-dependent rearrangement of TRPV4 cytosolic tails enables channel activation by physiological stimuli.
Proc. Nat. Acad. Sci. USA 110(23):9553-8.

Mörs, K., Hellmich, U.A., Basting, D., Marchand, P., Wurm, J.P., Haase, W. and Glaubitz, C. (2013) A lipid-dependent link between activity and oligomerization state of the M. tuberculosis SMR protein Tbsmr.
Biochim. Biophys. Acta Biomembr. 1828(2):561-7.

Hellmich, U.A. and Wöhnert, J. (2013) Backbone resonance assignments for a homolog of the essential ribosome biogenesis factor Fap7 from P. horikoshii in its nucleotide-free and -bound forms.
Biomol. NMR Assign. 7(2):261-5.

Christ, N.A., Bochmann, S., Gottstein, D., Duchardt-Ferner, E., Hellmich, U.A., Düsterhus, S., Kötter, P., Güntert, P., Entian, K.D. and Wöhnert, J. (2012) The first structure of a LanI protein, SpaI: The protein conferring autoimmunity against the lantibiotic subtilin in Bacillus subtilis reveals a novel fold. 
J. Biol. Chem. 287(42):35286-98.

Hellmich*, U.A., Lyubenova*, S., Kaltenborn, E., Doshi, R., van Veen, H. W., Prisner, T.F. and Glaubitz, C. (2012) Probing the ATP hydrolysis cycle of the ABC multidrug transporter LmrA by pulsed EPR Spectroscopy.
J. Am. Chem. Soc., 134(13):5857-62.(*contributed equally)

Hellmich, U.A., Duchardt-Ferner, E., Glaubitz, C. and Wöhnert, J. (2012) Backbone NMR resonance assignments of the nucleotide binding domain of the ABC multidrug transporter LmrA from Lactococcus lactis in its ADP-bound state.
Biomol. NMR Assign. 6(1):69-73.

Ullrich*, S.J., Hellmich*, U.A., Ullrich, S. and Glaubitz, C. (2011) Interfacial enzyme kinetics of a membrane bound kinase analyzed by real-time MAS-NMR.
Nature Chem. Biol. 7(5):263-70. (*contributed equally)

Zutz, A., Hoffman, J., Hellmich, U.A., Glaubitz, C., Ludwig, B., Brutschy, B. and Tampé, R. (2011) Asymmetric ATP hydrolysis cycle of the heterodimeric multidrug ABC complex TmrAB from Thermus thermophiles.
J. Biol. Chem. 286(9):7104-15

Hellmich*, U.A. and Glaubitz, C. (2009) NMR and EPR on membrane transporters.
Biol. Chem. 390(8), 815-34. Invited Review (*corresponding author)

Pfleger, N., Wörner, A. C., Yang, J., Shastri, S., Hellmich, U.A., Aslimovska, L., Maier, M. S. M. and Glaubitz, C. (2009) Solid-state NMR and functional studies on Proteorhodopsin.
Biochim. Biophys. Acta Bioenerg. 1787(6), 697-705

Hellmich*, U.A., Pfleger*, N. and Glaubitz, C. (2009) 19F NMR on Proteorhodopsin: enhanced protocol for labeling for general application on membrane proteins.
Photochem. Photobiol. 85(2), 535-539 (*contributed equally)

Hellmich, U.A., Haase, W., Velamakanni, S., van Veen, H. W. and Glaubitz, C. (2008) Caught in the Act: ATP hydrolysis of an ABC multidrug transporter by real-time MAS NMR.
FEBS Lett. 23(23-24), 3557-3562

Siarheyeva, A., Lopez, J. J., Lehner, I., Hellmich, U.A., van Veen, H. W. and Glaubitz, C. (2007) Probing the Molecular Dynamics of the ABC Multidrug Transporter LmrA by Deuterium Solid-State Nuclear Magnetic Resonance.
Biochemistry 46(11); 3075-30839

TRP Channels

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Hellmich, U.A. (2023) Dynamic ion channel defies dogma.
Nature, doi: d41586-023-02486-9

  •  invited News and Views Article for paper by the Scheuring lab on the first pentameric TRP channel structure 
  • Read their paper here: Lansky et al (2023) A pentameric TRPV3 channel with a dilated pore. Nature, https://doi.org/10.1038/s41586-023-06470-1 


 Goretzki, B., Wiedemann, C., McCray, B.A., Schäfer, S.L., Jansen, J., Tebbe, F., Mitrovic, S.A., Nöth, J.,  Claveras Cabezudo, A., Donohue, J., Jeffries, J.M., Steinchen, W., Stengel, F., Sumner, C.J., Hummer, G., Hellmich, U.A. (2023) Crosstalk between regulatory elements in the disordered TRPV4 N-terminus modulates lipid-dependent channel activity.

Nature Commun. 14: 4165, doi: 10.1038/s41467-023-39808-4


Zhang, L., Simonsen, C., Zimova, L., Wang, K., Moparthi, L., Gaudet, R., Ekoff, M., Nilsson, G., Hellmich, U.A., Vlachova, V., Gourdon, P.E., Zygmunt, P.M. (2022) Cannabinoid non-cannabidiol site modulation of TRPV2 structure and function.
Nature Commun., 13: 7483, doi:s41467-022-35163-y

El Hamdaoui, Y., Zheng, F., Ye L., Fritz, N., Tran, M.A., Schwickert, K., Schirmeister, T., Braeuning, A., Lichtenstein, D., Hellmich. U.A., Weikert, D., Heinrich, M., Treccani, G., Schäfer, M.K.E., Nowak, G., Nürnberg, B., Alzheimer, C., Müller, C.P., Friedland, K. (2022) Analysis of hyperforin (St John’s wort) action at TRPC6 channels in mood disorders leads to new anti-depressants.
Molecular Psychiatry, 27: 5070–5085, doi: 10.1038/s41380-022-01804-3.

Wiedemann, C., Goretzki, B., Merz, Z.N., Tebbe, F., Schmitt, P., Hellmich, U.A. (2022) Extent of intrinsic disorder and NMR chemical shift assignments of the distal N-termini from human TRPV1, TRPV2 and TRPV3 ion channels.

Biomol. NMR Assign., 16: 289–296, doi: 10.1007/s12104-022-10093-4


Goretzki, B., Tebbe, F., Mitrovic, S.-A., Hellmich, U.A. (2022) Backbone NMR assignments of the extensive human and chicken TRPV4 N-terminal intrinsically disordered regions as important players in ion channel regulation.

Biomol. NMR Assign., 16: 205–212, doi: 10.1007/s12104-022-10080-9


Aisenberg, W.H., McCray, B.A., Sullivan, J.M., Diehl, E., Devine, L.R., Bagnell, A.M., Alevy, J., Carr, P., Goretzki, B., Cole, R.N., Hellmich, U.A., Sumner, C. (2022) Multi-ubiquitination of TRPV4 reduces channel activity independent of surface localization.

J. Biol. Chem., 298(4): 101826  doi: 10.1016/j.jbc.2022.101826

Taga, A., Peyton, M., Goretzki, B., Gallagher, T.G., Ritter, A., Harper, A., Crawford, T.O., Hellmich, U.A., Sumner, C.J., McCray, B.A. (2022) TRPV4 mutations associated with mixed neuropathy and skeletal dysplasia phenotypes result in severe gain of ion channel function.
Ann. Clin. Transl. Neurol.,  9(3): 375-391, doi:10.1002/acn3.51523

Hellmich*, U.A., Delemotte, L. (2022) TRP channels: branching out into the fungal kingdom

Structure, 30(4): 2-4, doi.org/10.1016/j.str.2021.12.006  (*corr. author)

  • invited preview for paper by the Moiseenkova-Bell lab on the first fungal TRP channel structure 
  • Read their paper here: Ahmed et al (2021) Structure of the ancient TRPY1 channel from Saccharomyces cerevisiae reveals mechanisms of modulation by lipids and calcium. Structure, S0969-2126(21)00298-7. 


McCray, B.A., Diehl, E., Sullivan, J.M., Aisenberg, W.H., Zaccor, N.W., Lau, A.R., Rich, D., Goretzki, B., Hellmich, U.A., Lloyd, T.E., Sumner, C.J. (2021) Neuropathy-causing TRPV4 mutations disrupt TRPV4-RhoA interactions and impair neurite extension.
Nature Commun., 12:1444,  doi: 10.1038/s41467-021-21699-y


Goretzki, B., Guhl, C., Tebbe, F., Harder, J.-M., Hellmich, U.A. (2021) Unstructural Biology of TRP Ion Channels: The Role of Intrinsically Disordered Regions in Channel Function and Regulation.
J. Mol. Biol., 166931, doi:10.1016/j.jmb.2021.166931

Viet*, K.K., Wagner*, A., Schwickert*, K., Hellwig, N., Brennich, M., Bader, N., Schirmeister, T., Morgner, N., Schindelin, H., Hellmich, U.A. (2019) Structure of the human TRPML2 ion channel extracytosolic/lumenal domain.
Structure, 27(8):1246-1257. doi: 10.1016/j.str.2019.04.016. (*shared first authors) 


Goretzki*, B., Glogowski*, N.A., Diehl, E., Duchardt-Ferner, E., Hacker, C., Gaudet, R., Hellmich, U. A. (2018) Structural basis of TRPV4 N-terminus interaction with Syndapin/PACSIN1-3 and PIP2.
Structure, 26(12):1583-1593. doi: 10.1016/j.str.2018.08.002 (*shared first authors)

Howard*, R.J., Carnevale*, V., Delemotte*, L., Hellmich*, U. A., Rothberg*, B. (2018) Permeating disciplines: overcoming barriers between molecular simulations and classical structure-function approaches in biological ion transport.
Biochim. Biophys. Acta Biomembr. 1860(4):927-942. doi: 10.1016/j.bbamem.2017.12.013. Front Cover. (*corresponding authors)

Hellmich*, U.A. and Gaudet*, R. (2014) High-resolution views of TRPV1 and their implications for the TRP channel superfamily. In Mammalian Transient Receptor Potential (TRP) cation channels, B. Nilius, and V. Flockerzi, eds. (Heidelberg, Germany: Springer DE). 
Handb. Exp. Pharmacol. 223:991-1004.  (*corresponding authors)

Hellmich*, U.A. and Gaudet*, R. (2014) Structural Biology of TRP Channels. In Mammalian Transient Receptor Potential (TRP) cation channels, B. Nilius, and V. Flockerzi, eds. (Heidelberg, Germany: Springer DE).
Handb. Exp. Pharmacol. 223:963-90. (*corresponding authors)

Garcia-Elias, A., Mrkonjic, S., Pardo-Pastor, C., Inada, H., Hellmich, U.A., Rubio-Moscardo, F., Plata, C., Gaudet, R., Vicente, R. and Valverde, M.A. (2013) PIP2-dependent rearrangement of TRPV4 cytosolic tails enables channel activation by physiological stimuli.
Proc. Nat. Acad. Sci. USA 110(23):9553-8.

Molecular Mechanisms of Microbial Communication

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Li, K.K., Cho, Y.I., Tran, M.A., Wiedemann, C., Koweek, R.S., Khánh Hoàng, N., Hamrick, G.S., Bowen, M.A., Koknona, B., Beld, J., Hellmich*, U.A., Charkoudian*, L. (2023) Strategic engineering unlocks in vitro type II polyketide biosynthesis. (*co-corresponding authors)
preprint available @ BioRxiv, doi: 10.1101/2023.08.02.551649v1

Wiedemann, C., Whittaker, J.J., Pérez Carrillo, V.H., Goretzki, B., Dajka, M., Tebbe, F., Harder, J.-M., T., Krajczy, P., Joseph, B., Hausch, F., Guskov, A., Hellmich, U.A. (2023) Legionella pneumophila macrophage infectivity potentiator protein appendage domains modulate protein dynamics and inhibitor binding.

Int. J. Biol. Macromol., accepted 


Deutscher, R., Karagöz, S., Purder, P., Kolos, J., Meyners, C., Sugiarto, W., Krajczy, P., Tebbe, F., Geiger, T., Ünal. C., Hellmich, U.A., Steinert, M., Hausch, F. (2023) [4.3.1] Bicyclic FKBP ligands inhibit Legionella pneumophila infection by LpMip-dependent and LpMip independent mechanisms.
ChemBioChem, accepted, doi: 10.1002/cbic.202300442 


Stallforth*, P., Mittag, M., Brakhage, A.A., Hertweck, C., Hellmich*, U.A. (2023) Functional Modulation of Chemical Mediators in Microbial Communities. (*corresponding authors) 

Trends Biochem. Sci., 48(1): 71-81 doi: 10.1016/j.tibs.2022.07.006 


Bando, Y., Hou, Y., Seyfarth, L., Probst, J., Götze, S., Bogacz, M., Hellmich, U.A., Stallforth, P., Mittag, M., Arndt, H.-D. (2022) Total Synthesis and Structural Correction of the Cyclic Lipodepsipeptide Orfamide A.
Chem. Eur. J.,  28(20): e202104417, doi: 10.1002/chem.202104417

Pérez Carrillo, V.H., Rose-Sperling, D., Tran, M.A., Wiedemann, C., Hellmich, U.A. (2022) Backbone NMR assignments of the nucleotide binding domain of the Bacillus subtilis ABC multidrug transporter BmrA in the post-hydrolysis state.
Biomol. NMR Assign., 16(1):81-86, doi:10.1007/s12104-021-10063-2

Hamdoun*, A., Hellmich*, U.A., Kuchler*, K., Szakacs*, G. (2021) The Incredible Diversity of Structures and Functions of ABC Transporters.
FEBS Lett.,  595(6):671-674. doi: 10.1002/1873-3468.14061 (invited editorial) (*corresponding authors)

Ford*, R. C., Hellmich*, U. A. (2020) What monomeric nucleotide binding domains can teach us about dimeric ABC proteins. 

FEBS Lett., 594(23):3857–3875. doi: 10.1002/1873-3468.13921 (*corresponding authors)

FEBS Letters Special Edition "Diversity of Structure and Function of ABC Transporters", Guest Editors: Amro Hamdoun, Ute A. Hellmich, Karl Kuchler, Gergely Szakacs

Rose-Sperling, D., Tran, M. A., Lauth, L.M., Goretzki, B., Hellmich, U.A. (2019) 19F NMR as a versatile tool to study membrane protein structure and dynamics.
Biol. Chem., 400(10):1277-1288. doi: 10.1515/hsz-2018-0473

Szöllösi, D., Rose-Sperling, D, Hellmich, U. A., Stockner, T. (2018) Comparison of mechanistic transport cycle models of ABC exporters.
Biochim. Biophys. Acta Biomembr. 1860(4):818-832. doi: 10.1016/j.bbamem.2017.10.028.

Hellmich*, U.A., McILwain*, B., Doshi*, R. (2018) Where do we go from here? Membrane protein research beyond the structure-function horizon. (invited editorial)
Biochim. Biophys. Acta Biomembr. 1860(4):801-803. doi: 10.1016/j.bbamem.2017.12.016. (*corresponding authors)

BBA Biomembranes Special Edition (2018) "Beyond the Structure-Function Horizon of Membrane Proteins", Guest Editors: Ute A. Hellmich, Rupak Doshi, Benjamin McIlwain

Neumann, J., Rose-Sperling, D. and Hellmich, U. A. (2017) Diverse relations between lipids and ABC transporters: an overview.

Biochim. Biophys. Acta Biomembr.  1859(4):605-618.

 

Hellmich*, U.A., Mönkemeyer, L., Velamakanni, S., van Veen, H.W., Glaubitz*, C. (2015) Effects of nucleotide binding to LmrA: A combined MAS-NMR and solution NMR study. 

Biochim. Biophys. Acta Biomembr. 1848(12):3158-65. (*corresponding authors)


Hacker, C., Christ, N. A., Duchardt-Ferner, E., Korn, S., Göbl, C., Berninger, L., Düsterhus, S., Hellmich, U. A., Madl, T., Kötter, P., Entian, K., Wöhnert, J. (2015) The solution structure of the lantibiotic immunity protein NisI and its interactions with nisin.
J. Biol. Chem.290(48):28869-86.

Mörs, K., Hellmich, U.A., Basting, D., Marchand, P., Wurm, J.P., Haase, W. and Glaubitz, C. (2013) A lipid-dependent link between activity and oligomerization state of the M. tuberculosis SMR protein Tbsmr.
Biochim. Biophys. Acta Biomembr. 1828(2):561-7.

Christ, N.A., Bochmann, S., Gottstein, D., Duchardt-Ferner, E., Hellmich, U.A., Düsterhus, S., Kötter, P., Güntert, P., Entian, K.D. and Wöhnert, J. (2012) The first structure of a LanI protein, SpaI: The protein conferring autoimmunity against the lantibiotic subtilin in Bacillus subtilis reveals a novel fold. 
J. Biol. Chem. 287(42):35286-98.

Hellmich*, U.A., Lyubenova*, S., Kaltenborn, E., Doshi, R., van Veen, H. W., Prisner, T.F. and Glaubitz, C. (2012) Probing the ATP hydrolysis cycle of the ABC multidrug transporter LmrA by pulsed EPR Spectroscopy.
J. Am. Chem. Soc., 134(13):5857-62.(*contributed equally)

Hellmich, U.A., Duchardt-Ferner, E., Glaubitz, C. and Wöhnert, J. (2012) Backbone NMR resonance assignments of the nucleotide binding domain of the ABC multidrug transporter LmrA from Lactococcus lactis in its ADP-bound state.
Biomol. NMR Assign. 6(1):69-73.

Ullrich*, S.J., Hellmich*, U.A., Ullrich, S. and Glaubitz, C. (2011) Interfacial enzyme kinetics of a membrane bound kinase analyzed by real-time MAS-NMR.
Nature Chem. Biol. 7(5):263-70. (*contributed equally)

Zutz, A., Hoffman, J., Hellmich, U.A., Glaubitz, C., Ludwig, B., Brutschy, B. and Tampé, R. (2011) Asymmetric ATP hydrolysis cycle of the heterodimeric multidrug ABC complex TmrAB from Thermus thermophiles.
J. Biol. Chem. 286(9):7104-15

Hellmich*, U.A. and Glaubitz, C. (2009) NMR and EPR on membrane transporters.
Biol. Chem. 390(8), 815-34. Invited Review (*corresponding author)

Pfleger, N., Wörner, A. C., Yang, J., Shastri, S., Hellmich, U.A., Aslimovska, L., Maier, M. S. M. and Glaubitz, C. (2009) Solid-state NMR and functional studies on Proteorhodopsin.
Biochim. Biophys. Acta Bioenerg. 1787(6), 697-705

Hellmich*, U.A., Pfleger*, N. and Glaubitz, C. (2009) 19F NMR on Proteorhodopsin: enhanced protocol for labeling for general application on membrane proteins.
Photochem. Photobiol. 85(2), 535-539 (*contributed equally)

Hellmich, U.A., Haase, W., Velamakanni, S., van Veen, H. W. and Glaubitz, C. (2008) Caught in the Act: ATP hydrolysis of an ABC multidrug transporter by real-time MAS NMR.
FEBS Lett. 23(23-24), 3557-3562

Siarheyeva, A., Lopez, J. J., Lehner, I., Hellmich, U.A., van Veen, H. W. and Glaubitz, C. (2007) Probing the Molecular Dynamics of the ABC Multidrug Transporter LmrA by Deuterium Solid-State Nuclear Magnetic Resonance.
Biochemistry 46(11); 3075-3083 

Neglected Tropical Diseases & Host/Pathogen Interactions

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Wiedemann, C., Whittaker, J.J., Pérez Carrillo, V.H., Goretzki, B., Dajka, M., Tebbe, F., Harder, J.-M., T., Krajczy, P., Joseph, B., Hausch, F., Guskov, A., Hellmich, U.A. (2023) Legionella pneumophila macrophage infectivity potentiator protein appendage domains modulate protein dynamics and inhibitor binding.

Int. J. Biol. Macromol., accepted 


Deutscher, R., Karagöz, S., Purder, P., Kolos, J., Meyners, C., Sugiarto, W., Krajczy, P., Tebbe, F., Geiger, T., Ünal. C., Hellmich, U.A., Steinert, M., Hausch, F. (2023) [4.3.1] Bicyclic FKBP ligands inhibit Legionella pneumophila infection by LpMip-dependent and LpMip independent mechanisms.
ChemBioChem, accepted, doi: 10.1002/cbic.202300442 


Maus, H., Hammerschmidt, S.J., Hinze, G., Barthels, F., Pérez Carrillo, V.H., Hellmich, U.A., Basché, T., Schirmeister, T. (2023) The effects of allosteric and competitive inhibitors on ZIKV protease conformational dynamics explored through smFRET, nanoDSF, DSF, and 19F-NMR.
Eur. J. Med. Chem., 258: 115573, doi: 10.1016/j.ejmech.2023.115573


Previti, S., Ettari, R., Di Chio, C., Ravichandran, R., Bogacz, M., Hellmich, U.A., Schirmeister, T., Cosconati, S., Zappalà. M. (2022) Development of Reduced Peptide Bond Pseudopeptide Michael Acceptors for the Treatment of Human African Trypanosomiasis.

Molecules. 27(12):3765. doi: 10.3390/molecules27123765


Jung, S., Fuchs, N., Grathwohl, C., Hellmich, U.A., Wagner, A., Diehl, E., Willmes, T., Sotriffer, C., Schirmeister, T. (2022) New peptidomimetic rhodesain inhibitors with improved selectivity towards human cathepsins.

Eur. J. Med. Chem., 238: 114460, doi: 10.1016/j.ejmech.2022.114460 


Di Chio, C., Previti, S., Amendola, G., Ravichandran, R., Wagner, A., Cosconati, S., Hellmich, U.A., Schirmeister, T., Zappalà, M., Ettari, R. (2022) Development of novel dipeptide nitriles as inhibitors of rhodesain of Trypanosoma brucei rhodesiense.
Eur. J. Med. Chem.,  236: 114328, doi: 10.1016/j.ejmech.2022.114328 

 

Johé, P., Jaenicke, E., Neuweiler, H., Schirmeister, T., Kersten, C., Hellmich, U.A (2021) Structure, interdomain dynamics and pH-dependent autoactivation of pro-rhodesain, the main lysosomal cysteine protease from African trypanosomes.

J. Biol. Chem., 296:100565, doi: 10.1016/j.jbc.2021.100565 


Jung, S., Fuchs, N., Johé, P., Wagner, A., Diehl, E., Yuliani, T., Zimmer, C., Barthels, F., Klein, P., Opatz, T., Tenzer, S., Distler, U., Räder, H.-J., Weil, T., Kersten, C., Hellmich, U.A., Klein, J., Schirmeister, T. (2021) Fluorovinylsulfones and -sulfonates as potent covalent reversible inhibitors of the trypanosomal cysteine protease rhodesain: SAR, inhibition mechanism, metabolism and in vivo studies.

J. Med. Chem., 64(16):12322-12358, doi: 10.1021/acs.jmedchem.1c01002


Götz, C., Hinze, G., Gellert, A., Maus, H., von Hammerstein, F., Hammerschmidt, S., Lauth, L.M., Hellmich, U.A., Schirmeister, T., Basché, T. (2021) Conformational Dynamics of the Dengue Virus Protease revealed by Fluorescence Correlation and Single-Molecule FRET studies.
J. Phys. Chem. B,  125(25): 6837–6846, doi: 10.1021/acs.jpcb.1c01797


Johé, P., Jung, S., Endres, E., Kersten, C., Zimmer, C., Ye, W., Sönnichsen, C., Hellmich, U.A., Sotriffer, C., Schirmeister, T., Neuweiler, H. (2021) Warhead reactivity limits the speed of inhibition of the cysteine protease rhodesain.
ACS Chem. Biol., 16(4):661–670, doi: 10.1021/acschembio.0c00911

Maiorana, S., Ettari, R., Previti, S., Amendola, G., Wagner, A., Cosconati, S., Hellmich, U.A., Schirmeister, T., Zappalà, M. (2020) Peptidyl vinyl ketone irreversible inhibitors of rhodesain: modifications of the P2 fragment.
ChemMedChem, 15(16):1552-1561. doi: 10.1002/cmdc.202000360


Dietschreit, J.C.B., Wagner, A., Le, T.A., Klein, P., Schindelin, H., Opatz, T., Engels, B., Hellmich*, U.A., Ochsenfeld*, C. (2020) Predicting 19F NMR Chemical Shifts: A Combined Computational and Experimental Study of a Trypanosomal Oxidoreductase-Inhibitor Complex.
Angew. Chem. Int. Ed. Engl., 59(31):12669-12673 doi: 10.1002/anie.202000539 (*corresponding authors)

Klein, P., Barthels, F., Johé, P., Wagner, A., Tenzer, S., Distler, U., Le, T.A., Schmid, P., Engel, V., Engels, B., Hellmich, U.A., Opatz, T., Schirmeister, T.  (2020) Naphthoquinones as inhibitors of cysteine proteases.
Molecules, 25(9):2064. doi: 10.3390/molecules25092064

Klein, P., Johé, P., Wagner, A., Jung, S., Kühlborn, J., Tenzer, S., Distler, U., Waigel, W., Engels, B., Hellmich, U.A., Opatz, T., Schirmeister, T. (2020) New Cysteine Protease Inhibitors: Electrophilic (Het)arenes and unexpected Prodrug Identification.
Molecules, 25(6):1451. doi: 10.3390/molecules25061451

Millies, B., von Hammerstein, F., Gellert, A., Hammerschmidt, S., Barthels, F., Göppel, U., Immerheiser, M., Elgner, F., Jung, N., Basic, M., Kersten, C., Kiefer, W., Bodem, J., Hildt, E., Windbergs, M., Hellmich*, U.A., Schirmeister*, T. (2019) Proline-based allosteric inhibitors of Zika and Dengue virus NS2B/NS3 proteases.

J. Med. Chem. 62(24):11359-11382. doi: 10.1021/acs.jmedchem.9b01697 (*corresponding authors)

Ettari, R., Previti, S., Maiorana, S., Amendola, G., Wagner, A., Cosconati, S., Schirmeister, T., Hellmich, U.A., Zappalà, M. (2019) Optimization strategy of novel peptide-based Michael acceptors for the treatment of Human African Trypanosomiasis.
J. Med. Chem. 62(23):10617-10629. doi: 10.1021/acs.jmedchem.9b00908

von Hammerstein*, F., Lauth*, L. M., Hammerschmidt, S., Wagner, A., Schirmeister, T., Hellmich, U.A. (2019) Cis autocatalytic cleavage of glycine‐linked Zika virus NS2B‐NS3 protease constructs.

FEBS Lett. 593(16):2204-2213. doi: 10.1002/1873-3468.13507. (*shared first authors)


Wagner, A., Le, T.A., Brennich, M., Klein, P., Bader, N., Diehl, E., Paszek, D., Weickhmann, A.K., Dirdjaja, N., Krauth-Siegel, R.L., Engels, B., Opatz, T., Schindelin, H., Hellmich, U.A. (2019) Inhibitor-Induced Dimerization of an Essential Oxidoreductase from African Trypanosomes.

Angewandte Chemie Int. Ed. 58(11):3640-3644. doi: 10.1002/anie.201810470


Wagner, A., Le, T. A., Brennich, M., Klein, P., Bader, N., Diehl, E., Paszek, D., Weickhmann, A. K., Dirdjaja, N., Krauth-Siegel, R. L., Engels, B., Opatz, T., Schindelin, H., Hellmich, U.A. (2019) Inhibitor-induzierte Dimerisierung einer essentiellen Oxidoreduktase aus Afrikanischen Trypanosomen. doi: 10.1002/ange.201810470
Angewandte Chemie, 131(11):3679-3683


Preveti, S., Ettari, R., Cosconati, S., Amendola, G., Chouchene, K., Wagner, A., Hellmich, U.A., Ulrich, K., Krauth-Siegel, R.L., Wich, P.R., Schmid, I., Schirmeister, T., Gut, J., Rosenthal, P.J., Grasso, S., Zappalà, M. (2017) Development of novel peptide-based Michael acceptors targeting rhodesain and falcipain-2 for the treatment of Neglected Tropical Diseases (NTDs).

J. Med. Chem. 60(16):6911-6923.

Wagner, A., Diehl, E., Krauth-Siegel, R.L., Hellmich, U. A. (2017) Backbone NMR assignments of tryparedoxin, the central protein in the hydroperoxide detoxification cascade of African trypanosomes, in the oxidized and reduced form.
Biomol. NMR Assign. 11(2):193-196.

Latorre, A., Schirmeister, T., Kesselring, J., Jung, S., Johé, P., Hellmich, U. A., Heilos, A., Engels, B., Krauth-Siegel, R. L., Dirdjaja, N., Bou-Iserte, L., Rodríguez, S., González, F. V. (2016) Dipeptidyl Nitroalkenes as Potent Reversible Inhibitors of Cysteine Proteases Rhodesain and Cruzain.

ACS Med. Chem. Lett. 7(12):1073-1076.

Schirmeister, T., Kesselring, J., Jung, S., Schneider, T., Weickert, A., Becker, J., Lee, W., Bamberger, D., Wich, P. R., Distler, U., Tenzer, S., Johé, P., Hellmich, U. A., Engels, B. (2016) Quantum chemical-based Protocol for the rational Design of covalent Inhibitors.
J. Am. Chem. Soc., 138(27):8332-5.

Other topics

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Bothe, S., Hänzelmann, P., Boehler, S., Kehrein, J., Zehe., M., Wiedemann, C., Hellmich, U.A., Brenk, R., Schindelin, H., Sotriffer, C. (2022) Fragment screening using biolayer interferometry reveals ligands targeting the SHP-motif binding site of the AAA+ ATPase p97. 

Commun. Chem. 5,  169, doi:  10.1038/s42004-022-00782-5 

 
Zengerling, L., Kemper. B., Hellmich, U.A., Besenius, P. (2021) Synthesis and Structural Stability of α-Helical Au(I)-Metallopeptides. 

Synlett, 32:344-349, doi: 10.1055/a-1290-8412

Wesenberg, L., Diehl, E., Zähringer, T.B., Dörr, C., Schollmeyer, D., Shimizu, A., Yoshida, J., Hellmich, U.A., Waldvogel, S.R. (2020) Metal-free Twofold Electrochemical C-H Amination of Activated Arenes: Application to Medicinally Relevant Precursor Syntheses.

Chem. Eur. J., 26(72):17574-17580. doi: 10.1002/chem.202003852

Jungglas, B., Orru, R., Axt, A., Siebenaller, C., Steinchen, W., Heidrich, J., Hellmich, U.A., Hellmann, N., Wolf, E., Weber, S.L., Schneider, D. (2020) IM30 IDPs form a membrane protective carpet upon super-complex disassembly.
Commun. Biol., 3(1):595. doi: 10.1038/s42003-020-01314-4


Goretzki, B., Heiby, J., Hacker, C. Neuweiler, H., Hellmich, U.A. (2020) NMR assignments of a dynamically perturbed and dimerization inhibited N-terminal domain variant of a spider silk protein from E. australis.

Biomol NMR Assign. 14:67–71. doi: 10.1007/s12104-019-09922-w.

Steiert, E., Ewald, J., Wagner, A., Hellmich, U.A., Frey, H., Wich, P.R. (2020) pH-Responsive Protein Nanoparticles via Conjugation of Degradable PEG to the Surface of Cytochrome c.
Polymer Chem. 11:551-559. doi: 10.1039/C9PY01162E

Heiby*, J., Goretzki*, B., Johnson, C., Hellmich#, U.A., Neuweiler#, H. (2019) Methionine in a protein hydrophobic core drives tight interactions required for assembly of spider silk.

Nature Commun. 10(1):4378.  doi: 10.1038/s41467-019-12365-5. (*shared first authors, #corresponding authors)


Hellmich, U.A., Weis, B.L., Luitikov, A., Wurm, J.P., Christ, N.A., Hantke, K., Kötter, P., Entian, K.D., Schleiff, E. and Wöhnert, J. (2013) Essential ribosome assembly factor Fap7 regulates a hierarchy of RNA-protein interactions during small ribosomal subunit biogenesis.

Proc. Nat. Acad. Sci. USA 110(38):15253-8.

Hellmich, U.A. and Wöhnert, J. (2013) Backbone resonance assignments for a homolog of the essential ribosome biogenesis factor Fap7 from P. horikoshii in its nucleotide-free and -bound forms.
Biomol. NMR Assign. 7(2):261-5.

Reviews, Editorials and Special Editions

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Hellmich, U.A. (2023) Dynamic ion channel defies dogma.
Nature, doi: d41586-023-02486-9

  •  invited News and Views Article for paper by the Scheuring lab on the first pentameric TRP channel structure 
  • Read their paper here: Lansky et al (2023) A pentameric TRPV3 channel with a dilated pore. Nature, https://doi.org/10.1038/s41586-023-06470-1 


Stallforth*, P., Mittag, M., Brakhage, A.A., Hertweck, C., Hellmich*, U.A. (2023) Functional Modulation of Chemical Mediators in Microbial Communities. (*corresponding authors) 

Trends Biochem. Sci., 48(1): 71-81, doi: 10.1016/j.tibs.2022.07.006 


Hellmich*, U.A., Delemotte, L. (2022) TRP channels: branching out into the fungal kingdom

Structure, 30(4): 2-4, doi.org/10.1016/j.str.2021.12.006  (*corr. author)

  • invited preview for paper by the Moiseenkova-Bell lab on the first fungal TRP channel structure 
  • Read their paper here: Ahmed et al (2021) Structure of the ancient TRPY1 channel from Saccharomyces cerevisiae reveals mechanisms of modulation by lipids and calcium. Structure, S0969-2126(21)00298-7. 


Goretzki, B., Guhl, C., Tebbe, F., Harder, J.-M., Hellmich, U.A. (2021) Unstructural Biology of TRP Ion Channels: The Role of Intrinsically Disordered Regions in Channel Function and Regulation.
J. Mol. Biol., 166931, doi:10.1016/j.jmb.2021.166931

Hamdoun*, A., Hellmich*, U.A., Kuchler*, K., Szakacs*, G. (2021) The Incredible Diversity of Structures and Functions of ABC Transporters.
FEBS Lett.,  595(6):671-674. doi: 10.1002/1873-3468.14061 (invited editorial) (*corresponding authors)

Ford*, R. C., Hellmich*, U. A. (2020) What monomeric nucleotide binding domains can teach us about dimeric ABC proteins. 

FEBS Lett., 594(23):3857–3875. doi: 10.1002/1873-3468.13921 (*corresponding authors)

FEBS Letters Special Edition (2021) "Diversity of Structure and Function of ABC Transporters", Guest Editors: Amro Hamdoun, Ute A. Hellmich, Karl Kuchler, Gergely Szakacs

Rose-Sperling, D., Tran, M. A., Lauth, L.M., Goretzki, B., Hellmich, U.A. (2019) 19F NMR as a versatile tool to study membrane protein structure and dynamics.
Biol. Chem., 400(10):1277-1288. doi: 10.1515/hsz-2018-0473

Howard*, R.J., Carnevale*, V., Delemotte*, L., Hellmich*, U. A., Rothberg*, B. (2018) Permeating disciplines: overcoming barriers between molecular simulations and classical structure-function approaches in biological ion transport.
Biochim. Biophys. Acta Biomembr. 1860(4):927-942. doi: 10.1016/j.bbamem.2017.12.013. Front Cover. (*corresponding authors)

Szöllösi, D., Rose-Sperling, D, Hellmich, U. A., Stockner, T. (2018) Comparison of mechanistic transport cycle models of ABC exporters.
Biochim. Biophys. Acta Biomembr. 1860(4):818-832. doi: 10.1016/j.bbamem.2017.10.028.

Hellmich*, U.A., McILwain*, B., Doshi*, R. (2018) Where do we go from here? Membrane protein research beyond the structure-function horizon. (invited editorial)
Biochim. Biophys. Acta Biomembr. 1860(4):801-803. doi: 10.1016/j.bbamem.2017.12.016. (*corresponding authors)

BBA Biomembranes Special Edition (2018) "Beyond the Structure-Function Horizon of Membrane Proteins", Guest Editors: Ute A. Hellmich, Rupak Doshi, Benjamin McIlwain

Neumann, J., Rose-Sperling, D. and Hellmich, U. A. (2017) Diverse relations between lipids and ABC transporters: an overview.
Biochim. Biophys. Acta Biomembr.  1859(4):605-618.  doi: 10.1016/j.bbamem.2016.09.023

Hellmich*, U.A. and Gaudet*, R. (2014) High-resolution views of TRPV1 and their implications for the TRP channel superfamily. In Mammalian Transient Receptor Potential (TRP) cation channels, B. Nilius, and V. Flockerzi, eds. (Heidelberg, Germany: Springer DE). 
Handb. Exp. Pharmacol. 223:991-1004.  (*corresponding authors)

Hellmich*, U.A. and Gaudet*, R. (2014) Structural Biology of TRP Channels. In Mammalian Transient Receptor Potential (TRP) cation channels, B. Nilius, and V. Flockerzi, eds. (Heidelberg, Germany: Springer DE).
Handb. Exp. Pharmacol. 223:963-90. (*corresponding authors)

Hellmich*, U.A. and Glaubitz, C. (2009) NMR and EPR on membrane transporters.
Biol. Chem. 390(8), 815-34. Invited Review (*corresponding author)

Publications with undergraduate researchers

Undergraduate authors (Diploma/MSc/BSc/Intern) in italics

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In our opinion, exposure to real scientific problems and participation in actual research cannot start early enough in the undergraduate education. We take great pride in planning and carrying out diverse projects with undergraduates during their BSc/MSc theses or internships.
Below you will find the results already published, but make sure you check in from time to time to see the newest updates!

Li, K.K., Cho, Y.I., Tran, M.A., Wiedemann, C., Koweek, R.S., Khánh Hoàng, N., Hamrick, G.S., Bowen, M.A., Koknona, B., Beld, J., Hellmich*, U.A., Charkoudian*, L. (2023) Strategic engineering unlocks in vitro type II polyketide biosynthesis. (*co-corresponding authors) 

preprint available @ BioRxiv, doi: 10.1101/2023.08.02.551649v1 

Goretzki, B., Wiedemann, C., McCray, B.A., Schäfer, S.L., Jansen, J., Tebbe, F., Mitrovic, S.A., Nöth, J.,  Claveras Cabezudo, A., Donohue, J., Jeffries, J.M., Steinchen, W., Stengel, F., Sumner, C.J., Hummer, G., Hellmich, U.A. (2023) Crosstalk between regulatory elements in the disordered TRPV4 N-terminus modulates lipid-dependent channel activity.
Nature Commun. 14: 4165, doi: 10.1038/s41467-023-39808-4

  • Press release from FSU Jena
  • Selected as a featured article in the Editors’ Highlights on "Structural biology, biochemistry and biophysics" in Nature Communications


Wiedemann, C., Goretzki, B., Merz, Z.N., Tebbe, F., Schmitt, P., Hellmich, U.A. (2022) Extent of intrinsic disorder and NMR chemical shift assignments of the distal N-termini from human TRPV1, TRPV2 and TRPV3 ion channels.

Biomol. NMR Assign., 16: 289–296, doi: 10.1007/s12104-022-10093-4


Goretzki, B., Tebbe, F., Mitrovic, S.-A., Hellmich, U.A. (2022) Backbone NMR assignments of the extensive human and chicken TRPV4 N-terminal intrinsically disordered regions as important players in ion channel regulation.

Biomol. NMR Assign., 16: 205–212, doi: 10.1007/s12104-022-10080-9 


Götz, C., Hinze, G., Gellert, A., Maus, H., von Hammerstein, F., Hammerschmidt, S., Lauth, L.M., Hellmich, U.A., Schirmeister, T., Basché, T. (2021) Conformational Dynamics of the Dengue Virus Protease revealed by Fluorescence Correlation and Single-Molecule FRET studies.

J. Phys. Chem. B,  125(25): 6837–6846, doi: 10.1021/acs.jpcb.1c01797


Goretzki, B., Guhl, C., Tebbe, F., Harder, J.-M., Hellmich, U.A. (2021) Unstructural Biology of TRP Ion Channels: The Role of Intrinsically Disordered Regions in Channel Function and Regulation.

J. Mol. Biol., 166931, doi:10.1016/j.jmb.2021.166931

Wesenberg, L., Diehl, E., Zähringer, T.B., Dörr, C., Schollmeyer, D., Shimizu, A., Yoshida, J., Hellmich, U.A., Waldvogel, S.R. (2020) Metal-free Twofold Electrochemical C-H Amination of Activated Arenes: Application to Medicinally Relevant Precursor Syntheses.

Chem. Eur. J., 26(72):17574-17580. doi: 10.1002/chem.202003852

Millies, B., von Hammerstein, F., Gellert, A., Hammerschmidt, S., Barthels, F., Göppel, U., Immerheiser, M., Elgner, F., Jung, N., Basic, M., Kersten, C., Kiefer, W., Bodem, J., Hildt, E., Windbergs, M., Hellmich*, U.A., Schirmeister*, T. (2019) Proline-based allosteric inhibitors of Zika and Dengue virus NS2B/NS3 proteases.
J. Med. Chem. 62(24):11359-11382. doi: 10.1021/acs.jmedchem.9b01697 (*corresponding authors)

von Hammerstein*, F., Lauth*, L. M., Hammerschmidt, S., Wagner, A., Schirmeister, T., Hellmich, U.A. (2019) Cis autocatalytic cleavage of glycine‐linked Zika virus NS2B‐NS3 protease constructs.

FEBS Lett. 593(16):2204-2213. doi: 10.1002/1873-3468.13507. (*shared first authors)


Viet*, K.K., Wagner*, A., Schwickert*, K., Hellwig, N., Brennich, M., Bader, N., Schirmeister, T., Morgner, N., Schindelin, H., Hellmich, U.A. (2019) Structure of the human TRPML2 ion channel extracytosolic/lumenal domain.
Structure, 27(8):1246-1257. doi: 10.1016/j.str.2019.04.016. (*shared first authors) 


Rose-Sperling, D., Tran, M. A., Lauth, L.M., Goretzki, B., Hellmich, U.A. (2019) 19F NMR as a versatile tool to study membrane protein structure and dynamics.
Biol. Chem., 400(10):1277-1288. doi: 10.1515/hsz-2018-0473

Wagner, A., Le, T.A., Brennich, M., Klein, P., Bader, N., Diehl, E., Paszek, D., Weickhmann, A.K., Dirdjaja, N., Krauth-Siegel, R.L., Engels, B., Opatz, T., Schindelin, H., Hellmich, U.A. (2019) Inhibitor-Induced Dimerization of an Essential Oxidoreductase from African Trypanosomes.
Angewandte Chemie Int. Ed. 58(11):3640-3644. doi: 10.1002/anie.201810470


Wagner, A., Le, T. A., Brennich, M., Klein, P., Bader, N., Diehl, E., Paszek, D., Weickhmann, A. K., Dirdjaja, N., Krauth-Siegel, R. L., Engels, B., Opatz, T., Schindelin, H., Hellmich, U.A. (2019) Inhibitor-induzierte Dimerisierung einer essentiellen Oxidoreduktase aus Afrikanischen Trypanosomen. doi: 10.1002/ange.201810470
Angewandte Chemie, 131(11):3679-3683


Goretzki*, B., Glogowski*, N.A., Diehl, E., Duchardt-Ferner, E., Hacker, C., Gaudet, R., Hellmich, U. A. (2018) Structural basis of TRPV4 N-terminus interaction with Syndapin/PACSIN1-3 and PIP2.

Structure, 26(12):1583-1593. doi: 10.1016/j.str.2018.08.002 (*shared first authors) 


Wagner, A., Diehl, E., Krauth-Siegel, R.L., Hellmich, U. A. (2017) Backbone NMR assignments of tryparedoxin, the central protein in the hydroperoxide detoxification cascade of African trypanosomes, in the oxidized and reduced form.

Biomol. NMR Assign. 11(2):193-196.

Hellmich*, U.A., Mönkemeyer, L., Velamakanni, S., van Veen, H.W., Glaubitz*, C. (2015) Effects of nucleotide binding to LmrA: A combined MAS-NMR and solution NMR study. 

Biochim. Biophys. Acta Biomembr. 1848(12):3158-65. (*corresponding authors)


Hellmich, U.A., Weis, B.L., Luitikov, A., Wurm, J.P., Christ, N.A., Hantke, K., Kötter, P., Entian, K.D., Schleiff, E. and Wöhnert, J. (2013) Essential ribosome assembly factor Fap7 regulates a hierarchy of RNA-protein interactions during small ribosomal subunit biogenesis.

Proc. Nat. Acad. Sci. USA 110(38):15253-8.

Mörs, K., Hellmich, U.A., Basting, D., Marchand, P., Wurm, J.P., Haase, W. and Glaubitz, C. (2013) A lipid-dependent link between activity and oligomerization state of the M. tuberculosis SMR protein Tbsmr.

Biochim. Biophys. Acta Biomembr. 1828(2):561-7.

Hellmich*, U.A., Lyubenova*, S., Kaltenborn, E., Doshi, R., van Veen, H. W., Prisner, T.F. and Glaubitz, C. (2012) Probing the ATP hydrolysis cycle of the ABC multidrug transporter LmrA by pulsed EPR Spectroscopy.

J. Am. Chem. Soc., 134(13):5857-62.(*contributed equally)

Pfleger, N., Wörner, A. C., Yang, J., Shastri, S., Hellmich, U.A., Aslimovska, L., Maier, M. S. M. and Glaubitz, C. (2009) Solid-state NMR and functional studies on Proteorhodopsin.

Biochim. Biophys. Acta Bioenerg. 1787(6), 697-70