Publications

Publications

Peer-reviewed publications:

  1. Development of a fluorescent ligand for the intracellular allosteric binding site of the neurotensin receptor 1. H. Vogt, P. Shinkwin, M.E. Huber, N. Staffen, H. Hübner, P. Gmeiner, M. Schiedel, Dorothee Weikert. ACS Pharmacol. Transl. Sci. (2024), accepted article. https://pubs.acs.org/doi/10.1021/acsptsci.4c00086. Impact factor: 6.000

  2. Development and initial characterization of the first 18F-CXCR2-targeting radiotracer for PET imaging of neutrophils. P. Spatz, X. Chen, K. Reichau, M.E. Huber, S. Mühlig, Y. Matsusaka, M. Schiedel, T. Higuchi, M. Decker.  J. Med. Chem. (2024), accepted article. https://doi.org/10.1021/acs.jmedchem.3c02285.
  3. Small molecule ligands of the BET-like bromodomain, SmBRD3, affect Schistosoma mansoni survival, oviposition, and development. M. Schiedel*, D. McArdle*, G. Padalino*, A.K.N. Chan, J. Forde-Thomas, M. McDonough, H. Whitel, M. Beckmann, R. Cookson, K.F. Hoffmann, S.J. Conway. J. Med. Chem. (2023), accepted manuscript, preprint available via https://doi.org/10.1021/acs.jmedchem.3c01321 [*shared first authorship].
  4. Development of first-in-class dual Sirt2/HDAC6 inhibitors as molecular tools for dual inhibition of tubulin deacetylation. L. Sinatra, A. Vogelmann, F. Friedrich, M.A. Tararina, E. Neuwirt, A. Colcerasa, P. König, L. Toy, T.Z. Yesiloglu, S. Hilscher, L. Gaitzsch, N. Papenkordt, S. Zhai, Zhang, C. Romier, O. Einsle, W. Sippl, M. Schutkowski, O. Groß, G. Bendas, D. Christianson, F. Hansen, M. Jung, M. Schiedel. J. Med. Chem. 66 (2023), 14787-14814. https://doi.org/10.1021/acs.jmedchem.3c01385.
  5. Mutate and conjugate: A method to enable rapid in-cell target validation. A.M. Thomas, M. Serafini, E.K. Grant, E.A.J. Coombs, J.P. Bluck, Schiedel, M.A. McDonough, J.K. Reynolds, B. Lee, M. Platt, V. Sharlandjieva, P.C. Biggin, F. Duarte, T.A. Milne, J.T. Bush, S.J. Conway. ACS Chem. Biol. 18 (2023), 2405-2417. https://doi.org/10.1021/acschembio.3c00437.
  6. Fluorescent ligands enable target engagement studies for the intracellular allosteric binding site of the chemokine receptor CXCR2. E. Huber, S. Wurnig, L. Toy, C. Weiler, N. Merten, E. Kostenis#, F.K. Hansen#, M. Schiedel#. J. Med. Chem. 66 (2023), 9916–9933 [#shared corresponding authorship]. https://doi.org/10.1021/acs.jmedchem.3c00769.
  7. Back in person: Frontiers in Medicinal Chemistry 2023. Gehringer, F. Pape, M. Méndez, P. Barbie, A. Unzue Lopez, J. Lefranc, F.-M. Klingler, G. Hessler, T. Langer, E. Diamanti#, M. Schiedel#. ChemMedChem (2023), e202300344 [#shared corresponding authorship]. https://doi.org/10.1002/cmdc.202300344.
  8. Small molecule tools to study cellular target engagement for the intracellular allosteric binding site of GPCRs. E. Huber, L. Toy, M.F. Schmidt, D. Weikert, M. Schiedel. Chem. Eur. J., 29 (2023), e202202565. https://doi.org/10.1002/chem.202202565.
  9. Fluorescent ligands targeting the intracellular allosteric binding site of the chemokine receptor CCR2. L. Toy, M.E. Huber, M.F. Schmidt, D. Weikert, M. Schiedel. ACS Chem. Biol., 17 (2022), 2142-22152. https://pubs.acs.org/doi/10.1021/acschembio.2c00263.
  10. Development of a NanoBRET assay to validate dual inhibitors of Sirt2-mediated lysine deacetylation and defatty-acylation that block prostate cancer cell migration. A. Vogelmann, M. Schiedel, N. Wössner, A. Merz, D. Herp, S. Hammelmann, A. Colcerasa, G. Komaniecki, J.Y. Hong, M. Sum, E. Metzger, E. Neuwirt, L. Zhang, O. Einsle, O. Groß, R. Schüle, H. Lin, W. Sippl, M. Jung. RSC Chem. Biol. 3 (2022), 468-485. https://doi.org/10.1039/D1CB00244A.
  11. Comparison of cellular target engagement methods for the tubulin deacetylases Sirt2 and HDAC6: NanoBRET, CETSA, tubulin acetylation, and PROTACs. A. Vogelmann, M. Jung, F.K. Hansen, M. Schiedel. ACS Pharmacol. Transl. Sci. 5 (2022), 138-140. https://doi.org/10.1021/acsptsci.2c00004.
  12. A chemical biology toolbox targeting the intracellular binding site of CCR9: Fluorescent ligands, new drug leads and PROTACs. E. Huber, L. Toy, M.F. Schmidt, H. Vogt, J. Budzinski, M.F.J. Wiefhoff, N. Merten, E. Kostenis, D. Weikert, M. Schiedel. Angew. Chem. Int. Ed., 61 (2022), e202116782. https://doi.org/10.1002/anie.202116782. Angew. Chem., 134 (2022), e202116782. https://doi.org/10.1002/ange.202116782.
  13. Controlling Intramolecular Interactions in the Design of Selective, High-Affinity, Ligands for the CREBBP Bromodomain. M. Brand, J. Clayton, M. Moroglu, M. Schiedel, S. Picaud, J. Bluck, A. Skwarska, H. Bolland, A.K.N. Chan, C.M.C. Laurin, A.R. Scorah, L. See, T.P.C. Rooney, K.H. Andrews, O. Fedorov, G, Perell, P. Kalra, K.B. Vinh, W.A. Cortopassi, P. Heitel, K.E. Christensen, R.I. Cooper, R.S. Paton, W.C.K. Pomerantz, P.C. Biggin, E.M. Hammond, P. Filippakopoulos, S.J Conway. J. Med. Chem. 64 (2021), 10102-10123. https://doi.org/10.1021/acs.jmedchem.1c00348.
  14. Call for Papers: “Epigenetics 2.0”—A Joint Virtual Special Issue on Epigenetics. Bhatia#, F.K. Hansen#, M. Schiedel#. ACS Pharmacol. Transl. Sci. 4 (2021), 1262-1263. https://doi.org/10.1021/acsptsci.1c00156 [#shared corresponding authorship]. Impact factor: 3,500
  15. Fragment-based identification of ligands for bromodomain-containing factor 3 of Trypanosoma cruzi. C. Laurin, J. Bluck, A. Chan, M. Keller, A. Boczek, A. Scorah, K.F. See, L. Jennings, D. Hewings, F. Woodhouse, J. Reynolds, M. Schiedel, P. Humphreys, P. Biggin, S. Conway,  ACS Infect. Dis. 7 (2021), 2238-2249. https://doi.org/10.1021/acsinfecdis.0c00618.
  16. HaloTag-targeted Sirtuin rearranging ligand (SirReal) for the development of proteolysis targeting chimeras (PROTACs) against the lysine deacetylase Sirtuin 2 (Sirt2). M. Schiedel, A. Lehotzky, S. Szunyogh, J. Oláh, S. Hammelmann, N. Wössner, D. Robaa, O. Einsle, W. Sippl, J. Ovádi, M. Jung. ChemBioChem 21 (2020), 3371-3376. https://doi.org/10.1002/cbic.202000351.
  17. Validation of slow off-kinetics of sirtuin rearranging ligands (SirReals) by means of the label-free electrically switchable nanolever technology. M. Schiedel*, H. Daub*, A. Itzen, M. Jung [*contributed equally]. ChemBioChem 21 (2020), 1161-1166. https://doi.org/10.1002/cbic.201900527.
  18. Chemical epigenetics: the impact of chemical- and chemical biology techniques on bromodomain target validation. M. Schiedel, M. Moroglu, D.M.H. Ascough, A.E.R. Chamberlain, J.J.A.G. Kamps, A.R. Sekirnik, S.J. Conway. Angew. Chem. Int. Ed. 58 (2019), 17930-17952. https://doi.org/10.1002/anie.201812164. Chemische Epigenetik: der Einfluss chemischer und chemo‐biologischer Techniken auf die Zielstruktur‐Validierung von Bromodomänen. Angew. Chem. 131 (2019), 18096-18120. https://doi.org/10.1002/ange.201812164.
  19. Opening the selectivity pocket in the human lysine deacetylase sirtuin 2 – New opportunities, new questions. Robaa, D. Monaldi, N. Wössner, N. Kudo, T. Rumpf, M. Schiedel, M. Yoshida, M. Jung. Chem. Rec. 18 (2018), 1701-1707. https://doi.org/10.1002/tcr.201800044.
  20. Small molecules as tools to study the chemical epigenetics of lysine acetylation. M. Schiedel#, S.J. Conway# [#shared corresponding authorship]. Curr. Opin. Chem. Biol. 45 (2018), 166-178. https://doi.org/10.1016/j.cbpa.2018.06.015.
  21. BET bromodomain ligands: Probing the WPF shelf to improve BRD4 bromodomain affinity and metabolic stability. L.E. Jennings*, M. Schiedel*, D.S. Hewings, S. Picaud, C.M.C. Laurin, P.A. Bruno, J.P. Bluck, A.R. Scorah, L. See, J.K. Reynolds, M. Moroglu, I.N. Mistry, A. Hicks, P. Guzanov, J. Clayton, C.N.G. Evans, G. Stazi, P.C. Biggin, A.K. Mapp, E.M. Hammond, P.G. Humphreys, P. Filippakopoulos, S.J. Conway [*contributed equally]. Bioorg. Med. Chem. 26 (2018), 2937-2957. https://doi.org/10.1016/j.bmc.2018.05.003.
  22. New chemical tools for probing activity and inhibition of the NAD+ dependent lysine deacylase sirtuin 2. S. Swyter*, M. Schiedel*, D. Monaldi, S. Szunyogh, A. Lehotzky, T. Rumpf, J. Ovádi, W. Sippl, M. Jung [*contributed equally]. Phil. Trans. R. Soc. B 373 (2018), 20170083. https://doi.org/10.1098/rstb.2017.0083.
  23. Chemically induced degradation of sirtuin 2 (Sirt2) by a proteolysis targeting chimera (PROTAC) based on sirtuin rearranging ligands (SirReals). M. Schiedel, D. Herp, S. Hammelmann, S. Swyter, A. Lehotzky, D. Robaa, J. Olah, J. Ovádi, W. Sippl, M. Jung. J. Med. Chem. 61 (2018), 482-491. https://doi.org/10.1021/acs.jmedchem.6b01872. 
  24. The current state of NAD+-dependent histone deacetylases (sirtuins) as novel therapeutic targets. M.  Schiedel, D, Robaa, T. Rumpf, W. Sippl, M. Jung. Med. Res. Rev. 38 (2018), 147-200. https://doi.org/10.1002/med.21436.
  25. Modulation of microtubule acetylation by the interplay of TPPP/p25, SIRT2 and new anticancer agents with anti-SIRT2 potency. A. Szabó, J. Oláh, S. Szunyogh, A. Lehotzky, T. Szénási, M. Csaplár, M. Schiedel, P. Lőw, M. Jung, J. Ovádi. Sci. Rep. 7 (2017), 17070. https://doi.org/10.1038/s41598-017-17381-3.
  26. Synthesis and biological evaluation of 8-hydroxy-2,7-naphthyridin-2-ium salts as novel inhibitors of acetylcholinesterase (AChE) and butyrylcholinesterase (BChE). M. Schiedel, A. Fallarero, C. Luise, W. Sippl, P. Vuorela, M. Jung. MedChemComm 8 (2017), 465-470. https://doi.org/10.1039/C6MD00647G.
  27. Aminothiazoles as potent and selective Sirt2 inhibitors: A structure-activity relationship study. M. Schiedel, T. Rumpf, B. Karaman, A. Lehotzky, J. Oláh, S. Gerhardt, J. Ovádi, W. Sippl, O. Einsle, M. Jung. J. Med. Chem. 59 (2016), 1599-1612. https://doi.org/10.1021/acs.jmedchem.5b01517.
  28. A continuous, fluorogenic sirtuin 2 deacylase assay: substrate screening and inhibitor evaluation. I. Galleano, M. Schiedel, M. Jung, A.S. Madsen, C.A. Olsen. J. Med. Chem. 59 (2016), 1021-1031. https://doi.org/10.1021/acs.jmedchem.5b01532.
  29. Structure-based development of an affinity probe for sirtuin 2. M. Schiedel, T. Rumpf, B. Karaman, A. Lehotzky, S. Gerhardt, J. Ovádi, W. Sippl, O. Einsle, M. Jung. Angew. Chem. Int. Ed. 55 (2016), 2252-2256. https://doi.org/10.1002/anie.201509843. Strukturbasierte Entwicklung einer Affinitätssonde für Sirtuin 2. Angew. Chem. 128 (2016), 2293-2297. https://doi.org/10.1002/ange.201509843.
  30. Selective Sirt2 inhibition by ligand-induced rearrangement of the active site. T. Rumpf, M. Schiedel, B. Karaman, C. Roessler, B.J. North, A. Lehotzky, J. Oláh, K.I. Ladwein, K. Schmidtkunz, M. Gajer, M. Pannek, C. Steegborn, D.A. Sinclair, S. Gerhardt, J. Ovádi, M. Schutkowski, W. Sippl, O. Einsle, M Jung. Nat. Commun. 6 (2015), 6263. https://doi.org/10.1038/ncomms7263.
  31. Fluorescence-based screening assays for the NAD⁺-dependent histone deacetylase smSirt2 from Schistosoma mansoni. M. Schiedel, M. Marek, J. Lancelot, B. Karaman, I. Almlöf, J. Schultz, W. Sippl, R.J. Pierce, C. Romier, M. Jung. J. Biomol. Screen. 20 (2015), 112-121. https://doi.org/10.1177/1087057114555307.
  32. Chromo-pharmacophores: photochromic diarylmaleimide inhibitors for sirtuins. Falenczyk, M. Schiedel, B. Karaman, T. Rumpf, N. Kuzmanovic, M. Grøtli, W. Sippl, M. Jung, B. König. Chem. Sci. 5 (2014), 4794-4799. https://doi.org/10.1039/C4SC01346H. 

Other publications:

  1. Introducing Matthias Schiedel, Angew. Chem. Int. Ed., 61 (2021), e202200131. https://doi.org/10.1002/anie.202200131.
  2. Front Cover: Validation of the Slow Off-Kinetics of Sirtuin-Rearranging Ligands (SirReals) by Means of Label-Free Electrically Switchable Nanolever Technology. ChemBioChem 21 (2020), 8, https://doi.org/10.1002/cbic.202000190.
  3. Epigenetiker treffen sich in Freiburg. [Epigeneticists meet up in Freiburg.] M. Schiedel, M. Jung, Nachr. Chem. 64 (2016), 904. https://doi.org/10.1002/nadc.20164054947.
  4. Epigenetische Wirkstoffforschung. [Epigenetic drug discovery.] M. Schiedel, M. Jung, Nachr. Chem. 62 (2014), 302-306. https://doi.org/10.1002/nadc.201490087.
  5. Resveratrol ist zurück! [Resveratrol is back!] M. Schiedel, M. Jung, Pharmakon. 1 (2013), 446‑448.
  6. Fehlregulation der Histon‐Acetylierung als molekulare Grundlage der Demenzentwicklung. [Dysregulation of histone acetylation as a molecular basis for the development of dementia.] M. Schiedel, M. Jung, Pharm. Unserer Zeit 40 (2011), 297-299. https://doi.org/10.1002/pauz.201190039.
  7. HIV‐1‐Eradikation durch “shock & kill”‐ [HIV-1 eradication with the “shock and kill” strategy.] M. Schiedel, Pharm. Unserer Zeit 39 (2010), 171-173. https://doi.org/10.1002/pauz.201090026.