Publications
2022
Grethe C, Schmidt M, Kipka GM, O'Dea R, Gallant K, Janning P, Gersch M,
"Structural basis for specific inhibition of the deubiquitinase UCHL1"
Nat Commun., 2022, 13(1), 5950. doi.org/10.1038/s41467-022-33559-4
2021
Ruiz EJ, Pinto-Fernandez A, Turnbull AP, Lan L, Charlton TM, Scott HC, Damianou A, Vere G, Riising EM, Da Costa C, Krajewski WW, Guerin D, Kearns JD, Ioannidis S, Katz M, McKinnon C, O'Connell J, Moncaut N, Rosewell I, Nye E, Jones N, Heride C, Gersch M, Wu M, Dinsmore CJ, Hammonds TR, Kim S, Komander D, Urbe S, Clague MJ, Kessler BM, Behrens A,
"USP28 deletion and small-molecule inhibition destabilizes c-MYC and elicits regression of squamous cell lung carcinoma"
Elife, 2021, 10, e71596. doi.org/10.7554/eLife.71596
2020
Rusilowicz-Jones EV, Jardine J, Kallinos A, Pinto-Fernandez A, Guenther F, Giurrandino M, Barone FG, McCarron K, Burke CJ, Murad A, Martinez A, Marcassa E, Gersch M, Buckmelter AJ, Kayser-Bricker KJ, Lamoliatte F, Gajbhiye A, Davis S, Scott HC, Murphy E, England K, Mortiboys H, Komander D, Trost M, Kessler BM, Ioannidis S, Ahlijanian MK, Urbé S, Clague MJ,
"USP30 sets a trigger threshold for PINK1-PARKIN amplification of mitochondrial ubiquitylation"
Life Sci Alliance ,2020, 3(8), e202000768. doi.org/10.26508/lsa.202000768
2019
Gersch M, Wagstaff JL, Toms AV, Graves B, Freund SMV, Komander D,
“Distinct USP25 and USP28 Oligomerization States Regulate Deubiquitinating
Activity”
Mol Cell, 2019, 74(3), 436–451. doi.org/10.1016/j.molcel.2019.02.030
2018
Stahl M, Korotkov VS, Balogh D, Kick LM, Gersch M, Pahl A, Kielkowski P, Richter K, Schneider S, Sieber SA,
“Selective Activation of Human Caseinolytic Protease P (ClpP)”
Angew Chem Int Ed, 2018, 57(44), 14602-14607. doi.org/10.1002/anie.201808189
2017
Turnbull AP, Ioannidis S, Krajewski WW, Pinto-Fernandez A, Heride C, Martin ACL, Tonkin LM, Townsend EC, Buker SM, Lancia DR, Caravella JA, Toms AV, Charlton TM, Lahdenranta J, Wilker E, Follows BC, Evans NJ, Stead L, Alli C, Zarayskiy VV, Talbot AC, Buckmelter AJ, Wang M, McKinnon CL, Saab F, McGouran JF, Century H, Gersch M, Pittman MS, Marshall CG, Raynham TM, Simcox M, Stewart LMD, McLoughlin SB, Escobedo JA, Bair KW, Dinsmore CJ, Hammonds TR, Kim S, Urbé S, Clague MJ, Kessler BM, Komander D,
“Molecular basis of USP7 inhibition by selective small-molecule inhibitors”
Nature, 2017, 550, 481–486. doi.org/10.1038/nature24451
Gersch M, Gladkova C, Schubert A, Michel M, Maslen S, Komander D,
“Mechanism and regulation of the Lys6-selective deubiquitinase USP30”
Nat Struct Mol Biol, 2017, 24(11), 920–930. (Also highlighted in Nat Chem Biol). doi.org/10.1038/nsmb.3475
Hundshammer C, Düwel S, Köcher S, Gersch M, Feuerecker B, Scheurer C, Haase A, Glaser SJ, Schwaiger M, Schilling F,
“Deuteration of hyperpolarized 13C-labeled zymonic acid enables sensitivity-enhanced dynamic MRI of pH”
ChemPhysChem, 2017, 18, 2422–2425. doi.org/10.1002/cphc.201700779
Düwel S, Hundshammer C, Gersch M, Feuerecker B, Steiger K, Buck A, Walch A, Haase A, Glaser SJ, Schwaiger M, Schilling F,
“Imaging of pH in vivo using hyperpolarized 13C-labelled zymonic acid”
Nat Commun, 2017, 8, 15126. doi.org/10.1038/ncomms15126
Balogh D, Dahmen M, Stahl M, Poreba M, Gersch M, Drag M, Sieber SA,
“Insights into ClpXP proteolysis: heterooligomerization and partial deactivation enhance chaperone affinity and substrate turnover in Listeria monocytogenes”
Chem Sci, 2017, 8, 1592–1600. doi.org/10.1039/C6SC03438A
2016
Mevissen TE, Kulathu Y, Mulder MP, Geurink PP, Maslen SL, Gersch M, Elliott PR, Burke JE, van Tol BD, Akutsu M, El Oualid F, Kawasaki M, Freund SM, Ovaa H, Komander D,
“Molecular basis of Lys11-polyubiquitin specificity in the deubiquitinase Cezanne”
Nature, 2016, 538(7625), 402–405. doi.org/10.1038/nature19836
Gersch M, Stahl M, Poreba M, Dahmen M, Dziedzic A, Drag M, Sieber SA
“Barrel-shaped ClpP proteases display attenuated cleavage specificities”
ACS Chem Biol, 2016, 19(11), 389–399. doi.org/10.1021/acschembio.5b00757
2015
Gersch M, Hackl M, Dubiella C, Dobrinevski A, Groll M, Sieber SA,
“Intact protein mass spectrometry of 20S proteasomes reveals complex integrity, phosphorylation stoichiometry and inhibitor specificity”
Chem Biol, 2015, 22(3), 404–411. doi.org/10.1016/j.chembiol.2015.01.004
Gersch M, Famulla K, Dahmen M, Goebl C, Malik I, Richter K, Korotkov VS, Sass P, Ruebsamen-Schaeff H, Madl T, Broetz-Oesterhelt H, Sieber SA,
“AAA+ chaperones and acyldepsipeptides activate the ClpP protease via conformational control”
Nat Commun, 2015, 19(6), 6320. doi.org/10.1038/ncomms7320
Wauer T, Swatek KN, Wagstaff JL, Gladkova C, Pruneda JN, Michel MA, Gersch M, Johnson CM, Freund SM, Komander D,
“Ubiquitin Ser65 phosphorylation affects ubiquitin structure, chain assembly and hydrolysis”
EMBO J, 2015, 34(3), 307–325. doi.org/10.15252/embj.201489847
2014
Gersch M, Sieber SA,
“Modulation of ClpP Protease Activity: from Antibiotics to Antivirulence”
In: Concepts and Case Studies in Chemical Biology, 2014, Wiley-VCH, Weinheim.
Dubiella C, Cui H, Gersch M, Brouwer A, Sieber SA, Krüger A, Liskamp RM, Groll M,
“Selective immunoproteasome inhibition by ligand-induced active site crosslinking”
Angew Chem Int Ed, 2014, 53(44), 11969–11973. doi.org/10.1002/anie.201406964
Gersch M, Kolb R, Alte F, Groll M, Sieber SA,
"Disruption of oligomerization and dehydroalanine formation as mechanisms for ClpP protease inhibition"
J Am Chem Soc, 2014, 136(4),1360–1366. doi.org/10.1021/ja4082793
Schilling F, Glaser SJ, Düwel S, Gersch M,
“pH-biosensors based on compounds produced from pyruvic acid for magnetic resonance imaging and spectroscopy and their uses”
European patent EP3058375, filed: 15.10.2014, granted: 26.12.2018.
2013
Zeiler E, List A, Alte F, Gersch M, Wachtel R, Poreba M, Drag M, Groll M, Sieber SA,
"Structural and functional insights into caseinolytic proteases reveal an unprecedented regulation principle of their catalytic triad“
Proc Natl Acad Sci USA, 2013, 110(28), 11302–11307. doi.org/10.1073/pnas.1219125110
Gersch M, Gut F, Korotkov V, Lehmann J, Böttcher T, Rusch M, Hedberg C, Waldmann H, Klebe G, Sieber SA,
"The Mechanism of ClpP Inhibition",
Angew Chem Int Ed, 2013, 52(10), 3009–3014. doi.org/10.1002/anie.201204690
2012
Gersch M, Kreuzer J, Sieber SA,
"Electrophilic natural products and their biological targets",
Nat Prod Rep, 2012, 29, 659–682. doi.org/10.1039/C2NP20012K
Gersch M, List A, Groll M, Sieber SA,
"Insights into the structural network responsible for oligomerization and activity of the bacterial virulence regulator caseinolytic protease P (ClpP)"
J Biol Chem, 2012, 287(12), 9484–9494. doi.org/10.1074/jbc.M111.336222
2011
Shen A, Lupardus PJ, Gersch M, Puri AW, Albrow VE, Garcia KC, Bogyo M,
"Defining an allosteric circuit in the cysteine protease domain of Clostridium difficile toxins"
Nat Struct Mol Biol, 2011, 18(3), 364–371. doi.org/10.1038/nsmb.1990
2010
Gersch M, Sieber SA,
"Disarming Clostridium difficile"
Chem Biol, 2010, 17, 1165–1166. doi.org/10.1016/j.chembiol.2010.11.003
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Location & approach
The campus of TU Dortmund University is located close to interstate junction Dortmund West, where the Sauerlandlinie A 45 (Frankfurt-Dortmund) crosses the Ruhrschnellweg B 1 / A 40. The best interstate exit to take from A 45 is "Dortmund-Eichlinghofen" (closer to Campus Süd), and from B 1 / A 40 "Dortmund-Dorstfeld" (closer to Campus Nord). Signs for the university are located at both exits. Also, there is a new exit before you pass over the B 1-bridge leading into Dortmund.
To get from Campus Nord to Campus Süd by car, there is the connection via Vogelpothsweg/Baroper Straße. We recommend you leave your car on one of the parking lots at Campus Nord and use the H-Bahn (suspended monorail system), which conveniently connects the two campuses.
TU Dortmund University has its own train station ("Dortmund Universität"). From there, suburban trains (S-Bahn) leave for Dortmund main station ("Dortmund Hauptbahnhof") and Düsseldorf main station via the "Düsseldorf Airport Train Station" (take S-Bahn number 1, which leaves every 20 or 30 minutes). The university is easily reached from Bochum, Essen, Mülheim an der Ruhr and Duisburg.
You can also take the bus or subway train from Dortmund city to the university: From Dortmund main station, you can take any train bound for the Station "Stadtgarten", usually lines U41, U45, U 47 and U49. At "Stadtgarten" you switch trains and get on line U42 towards "Hombruch". Look out for the Station "An der Palmweide". From the bus stop just across the road, busses bound for TU Dortmund University leave every ten minutes (445, 447 and 462). Another option is to take the subway routes U41, U45, U47 and U49 from Dortmund main station to the stop "Dortmund Kampstraße". From there, take U43 or U44 to the stop "Dortmund Wittener Straße". Switch to bus line 447 and get off at "Dortmund Universität S".
The H-Bahn is one of the hallmarks of TU Dortmund University. There are two stations on Campus Nord. One ("Dortmund Universität S") is directly located at the suburban train stop, which connects the university directly with the city of Dortmund and the rest of the Ruhr Area. Also from this station, there are connections to the "Technologiepark" and (via Campus Süd) Eichlinghofen. The other station is located at the dining hall at Campus Nord and offers a direct connection to Campus Süd every five minutes.
The AirportExpress is a fast and convenient means of transport from Dortmund Airport (DTM) to Dortmund Central Station, taking you there in little more than 20 minutes. From Dortmund Central Station, you can continue to the university campus by interurban railway (S-Bahn). A larger range of international flight connections is offered at Düsseldorf Airport (DUS), which is about 60 kilometres away and can be directly reached by S-Bahn from the university station.
The facilities of TU Dortmund University are spread over two campuses, the larger Campus North and the smaller Campus South. Additionally, some areas of the university are located in the adjacent "Technologiepark".
Site Map of TU Dortmund University (Second Page in English).