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.

2013

Mechanism and consequence of the autoactivation of p38α mitogen-activated protein kinase promoted by TAB1.

De Nicola GF, Martin ED, Chaikuad A, Bassi R, Clark J, Martino L, Verma S, Sicard P, Tata R, Atkinson RA, Knapp S, Conte MR, Marber MS

Nat. Struct. Mol. Biol.. 2013-9-15 . 20(10):1182-1190 .doi: 10.1038/nsmb.2668

PMID: 24037507

Topical anti-angiogenic SRPK1 inhibitors reduce choroidal neovascularization in rodent models of exudative-AMD.

Gammons MV, Federov O, Ivison D, Du C, Clark TL, Hopkins C, Hagiwara M, Dick AD, Cox RJ, Harper SJ, Hancox JC, Knapp S, Bates DO

Invest. Ophthalmol. Vis. Sci.. 2013-7-25 . .doi: 10.1167/iovs.13-12422

PMID: 23887803

Effect of single amino Acid substitution observed in cancer on pim-1 kinase thermodynamic stability and structure.

Lori C, Lantella A, Pasquo A, Alexander LT, Knapp S, Chiaraluce R, Consalvi V

PLoS ONE. 2013-6-5 . 8(6):e64824 .doi: 10.1371/journal.pone.0064824

PMID: 23755147

Structures of Down Syndrome Kinases, DYRKs, Reveal Mechanisms of Kinase Activation and Substrate Recognition.

Soundararajan M, Roos AK, Savitsky P, Filippakopoulos P, Kettenbach AN, Olsen JV, Gerber SA, Eswaran J, Knapp S, Elkins JM

Structure. 2013-6-4 . 21(6):986-96 .doi: 10.1016/j.str.2013.03.012

PMID: 23665168

PFI-1, a Highly Selective Protein Interaction Inhibitor, Targeting BET Bromodomains.

Picaud S, Da Costa D, Thanasopoulou A, Filippakopoulos P, Fish PV, Philpott M, Fedorov O, Brennan P, Bunnage ME, Owen DR, Bradner JE, Taniere P, O'Sullivan B, Müller S, Schwaller J, Stankovic T, Knapp S

Cancer Res.. 2013-6-1 . 73(11):3336-3346 .doi: 10.1158/0008-5472.CAN-12-3292

PMID: 23576556

X-ray Crystal Structure of ERK5 (MAPK7) in Complex with a Specific Inhibitor.

Elkins JM, Wang J, Deng X, Pattison MJ, Arthur JS, Erazo T, Gomez N, Lizcano JM, Gray NS, Knapp S

J. Med. Chem.. 2013-5-17 . .doi: 10.1021/jm4000837

PMID: 23656407

Restoring p53 Function in Human Melanoma Cells by Inhibiting MDM2 and Cyclin B1/CDK1-Phosphorylated Nuclear iASPP.

Lu M, Breyssens H, Salter V, Zhong S, Hu Y, Baer C, Ratnayaka I, Sullivan A, Brown NR, Endicott J, Knapp S, Kessler BM, Middleton MR, Siebold C, Jones EY, Sviderskaya EV, Cebon J, John T, Caballero OL, Goding CR, Lu X

Cancer Cell. 2013-5-13 . 23(5):618-33 .doi: 10.1016/j.ccr.2013.03.013

PMID: 23623661

Selective Bisubstrate Inhibitors with Sub-nanomolar Affinity for Protein Kinase Pim-1.

Ekambaram R, Enkvist E, Vaasa A, Kasari M, Raidaru G, Knapp S, Uri A

ChemMedChem. 2013-4-24 . 8(6):909-13 .doi: 10.1002/cmdc.201300042

PMID: 23616352

Construction of human activity-based phosphorylation networks.

Newman RH, Hu J, Rho HS, Xie Z, Woodard C, Neiswinger J, Cooper C, Shirley M, Clark HM, Hu S, Hwang W, Jeong JS, Wu G, Lin J, Gao X, Ni Q, Goel R, Xia S, Ji H, Dalby KN, Birnbaum MJ, Cole PA, Knapp S, Ryazanov AG, Zack DJ, Blackshaw S, Pawson T, Gingras AC, Desiderio S, Pandey A, Turk BE, Zhang J, Zhu H, Qian J

Mol. Syst. Biol.. 2013-4-4 . 9:655 .doi: 10.1038/msb.2013.12

PMID: 23549483