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Publications

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

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).