Stefan Knapp

Stefan Knapp

SGC Frankfurt

Knapp

Biography

Prof Stefan Knapp studied Chemistry at the University of Marburg (Germany) and at the University of Illinois (USA). He did his PhD in protein crystallography at the Karolinska Institute in Stockholm (Sweden) (1996) and continued his career at the Karolinska Institute as a postdoctoral scientist (1996-1999). In 1999, he joined the Pharmacia Corporation as a principal research scientist in structural biology and biophysics. He left the company in 2004 to set up a research group at the Structural Genomics Consortium at Oxford University (SGC). From 2008 to 2015 he was a Professor of Structural Biology at the Nuffield Department of Clinical Medicine (NDM) at Oxford University (UK) and between 2012 and 2015 he was the Director for Chemical Biology at the Target Discovery Institute (TDI). He joined Frankfurt University (Germany) in 2015 as a Professor of Pharmaceutical Chemistry and the Buchmann Institute of Molecular Life Sciences. He remains associated to the SGC as a visiting Professor at Oxford and he is also adjunct Professor of the George Washington University. Since 2017 he is the CSO of the newly founded SGC node at the Goethe-University Frankfurt. His research interests are the rational design of selective inhibitors that target protein kinases as well as protein interactions modules that function as reader domains of the epigenetic code.

Research Areas

My laboratory is interested in understanding molecular mechanisms that regulate protein function of key signalling molecules and how these mechanisms can be utilized for the development of highly selective and potent inhibitors (chemical probes). As a basis for this work we have generated a comprehensive set of high resolution crystal structures that cover most members of the protein family of interest. We are particularly interested in protein interactions module of the bromodomain family that specifically recognize ε-N-lysine acetylation motifs, a key event in the reading process of epigenetic marks. This effort generated several highly selective chemical probes targeting bromodomains. A second research focus is on protein kinases. Our laboratory has solved a comprehensive set of crystal structure of this large protein family offering the opportunity to understand molecular mechanisms of their regulation and developing new strategies for their selective targeting. We developed for example a number of highly selective inhibitors by exploring unusual binding modes and allosteric binding sites. A particular focus of the laboratory is also to understand structural mechanisms leading to slow binding kinetics as part of the K4DD consortium.

2016

BET inhibition as a new strategy for the treatment of gastric cancer.

Montenegro RC, Clark PG, Howarth A, Wan X, Ceroni A, Siejka P, Nunez-Alonso GA, Monteiro O, Rogers C, Gamble V, Burbano R, Brennan PE, Tallant C, Ebner D, Fedorov O, O'Neill E, Knapp S, Dixon D, Müller S

Oncotarget. 2016-6-1 . .doi: 10.18632/oncotarget.9766

PMID: 27259267

Protein-protein interaction inhibition (2P2I)-oriented chemical library accelerates hit discovery.

Milhas S, Raux B, Betzi S, Derviaux C, Roche P, Restouin A, Basse MJ, Rebuffet E, Lugari A, Badol M, Kashyap R, Lissitzky JC, Eydoux C, Hamon V, Gourdel ME, Combes S, Zimmermann P, Aurrand-Lions M, Roux T, Rogers C, Müller S, Knapp S, Trinquet E, Collette Y, Guillemot JC, Morelli X

ACS Chem. Biol.. 2016-5-24 . .doi: 10.1021/acschembio.6b00286

PMID: 27219844

Mapping the chemical chromatin reactivation landscape identifies BRD4-TAF1 cross-talk.

Sdelci S, Lardeau CH, Tallant C, Klepsch F, Klaiber B, Bennett J, Rathert P, Schuster M, Penz T, Fedorov O, Superti-Furga G, Bock C, Zuber J, Huber KV, Knapp S, Müller S, Kubicek S

Nat. Chem. Biol.. 2016-5-9 . .doi: 10.1038/nchembio.2080

PMID: 27159579

Co-crystal structures of the protein kinase haspin with bisubstrate inhibitors.

Lavogina D, Kestav K, Chaikuad A, Heroven C, Knapp S, Uri A

Acta Crystallogr F Struct Biol Commun. 2016-5-1 . 72(Pt 5):339-45 .doi: 10.1107/S2053230X16004611

PMID: 27139824

Identification and development of 2,3-dihydropyrrolo[1,2-a]quinazolin-5(1H)-one inhibitors targeting bromodomains within the Switch/Sucrose Non-Fermenting complex.

Sutherell CL, Tallant C, Monteiro OP, Yapp C, Fuchs JE, Fedorov O, Siejka P, Müller S, Knapp S, Brenton JD, Brennan PE, Ley SV

J. Med. Chem.. 2016-4-27 . .doi: 10.1021/acs.jmedchem.5b01997

PMID: 27119626

Identification of a chemical probe for family VIII bromodomains through optimization of a fragment hit.

Gerstenberger BS, Trzupek JD, Tallant C, Fedorov O, Filippakopoulos P, Brennan PE, Fedele V, Martin S, Picaud S, Rogers CM, Parikh MD, Taylor A, Samas BM, O'Mahony A, Berg EL, Pallares G, Torrey AV, Treiber DK, Samardjiev IJ, Nasipak BT, Padilla-Benavides T, Wu Q, Imbalzano AN, Nickerson JA, Bunnage ME, Müller S, Knapp S, Owen DR

J. Med. Chem.. 2016-4-26 . .doi: 10.1021/acs.jmedchem.6b00012

PMID: 27115555

Discovery of pyrido[3,4-g]quinazoline derivatives as CMGC family protein kinase inhibitors: Design, synthesis, inhibitory potency and X-ray co-crystal structure.

Esvan YJ, Zeinyeh W, Boibessot T, Nauton L, Théry V, Knapp S, Chaikuad A, Loaëc N, Meijer L, Anizon F, Giraud F, Moreau P

Eur J Med Chem. 2016-4-5 . 118:170-177 .doi: 10.1016/j.ejmech.2016.04.004

PMID: 27128181

Quality control in oocytes by p63 is based on a spring-loaded activation mechanism on the molecular and cellular level.

Coutandin D, Osterburg C, Srivastav RK, Sumyk M, Kehrloesser S, Gebel J, Tuppi M, Hannewald J, Schäfer B, Salah E, Mathea S, Müller-Kuller U, Doutch J, Grez M, Knapp S, Dötsch V

Elife. 2016-3-29 . 5: .doi: 10.7554/eLife.13909

PMID: 27021569

Structure of the Human Protein Kinase ZAK in Complex with Vemurafenib.

Mathea S, Abdul Azeez KR, Salah E, Tallant C, Wolfreys F, Konietzny R, Fischer R, Lou HJ, Brennan PE, Schnapp G, Pautsch A, Kessler BM, Turk BE, Knapp S

ACS Chem. Biol.. 2016-3-21 . .doi: 10.1021/acschembio.6b00043

PMID: 26999302

Structure-based design of an in vivo active selective BRD9 inhibitor.

Martin LJ, Koegl M, Bader G, Cockcroft XL, Fedorov O, Fiegen D, Gerstberger T, Hofmann MH, Hohmann AF, Kessler D, Knapp S, Knesl P, Kornigg S, Müller S, Nar H, Rogers C, Rumpel K, Schaaf O, Steurer S, Tallant C, Vakoc CR, Zeeb M, Zoephel A, Pearson M, Boehmelt G, McConnell D

J. Med. Chem.. 2016-2-25 . .doi: 10.1021/acs.jmedchem.5b01865

PMID: 26914985