Publications

Publications

Peer-reviewed publications:

  1. 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., (2022), accepted manuscript, preprint available via https://doi.org/10.1002/chem.202202565. Impact factor: 5.236
  2. 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. Impact factor: 4.634
  3. 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. Impact factor: yet unknown
  4. 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. Impact factor: 3,500
  5. 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. Impact factor: 15,336
  6. 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. Impact factor: 6.205
  7. 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
  8. 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. Impact factor: 4.614
  9. 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. Impact factor: 2.576
  10. 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. Impact factor: 2.576
  11. 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. Impact factor: 12.959
  12. 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. Impact factor: 5.387
  13. 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. Impact factor: 8.544
  14. 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. Impact factor: 2.802
  15. 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. Impact factor: 6.139
  16. 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. Impact factor: 6.054
  17. 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. Impact factor: 9.791
  18. 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. Impact factor: 4.122
  19. 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. Impact factor: 2.342
  20. 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. Impact factor: 6.259
  21. 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. Impact factor: 6.259
  22. 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. Impact factor: 11.994
  23. 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. Impact factor: 11.329
  24. 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. Impact factor: 2.218
  25. 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. Impact factor: 9.211

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.