Stefan Krimmer
Associate Research Scientist in Pharmacology
Research & Publications
Biography
Coauthors
Selected Publications
- Cryo-EM analyses of KIT and oncogenic mutants reveal structural oncogenic plasticity and a target for therapeutic interventionKrimmer S, Bertoletti N, Suzuki Y, Katic L, Mohanty J, Shu S, Lee S, Lax I, Mi W, Schlessinger J. Cryo-EM analyses of KIT and oncogenic mutants reveal structural oncogenic plasticity and a target for therapeutic intervention. Proceedings Of The National Academy Of Sciences Of The United States Of America 2023, 120: e2300054120. PMID: 36943885, PMCID: PMC10068818, DOI: 10.1073/pnas.2300054120.
- Unveiling molecular insights into the mechanism of activation of oncogenic phosphoinositide 3-kinase mutantsKrimmer S, Schlessinger J. Unveiling molecular insights into the mechanism of activation of oncogenic phosphoinositide 3-kinase mutants. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 119: e2218237119. PMID: 36475945, PMCID: PMC9897451, DOI: 10.1073/pnas.2218237119.
- Insights on JAK2 Modulation by Potent, Selective, and Cell-Permeable Pseudokinase-Domain LigandsLiosi ME, Ippolito JA, Henry SP, Krimmer SG, Newton AS, Cutrona KJ, Olivarez RA, Mohanty J, Schlessinger J, Jorgensen WL. Insights on JAK2 Modulation by Potent, Selective, and Cell-Permeable Pseudokinase-Domain Ligands. Journal Of Medicinal Chemistry 2022, 65: 8380-8400. PMID: 35653642, PMCID: PMC9939005, DOI: 10.1021/acs.jmedchem.2c00283.
- Conversion of a False Virtual Screen Hit into Selective JAK2 JH2 Domain Binders Using Convergent Design StrategiesHenry SP, Liosi ME, Ippolito JA, Cutrona KJ, Krimmer SG, Newton AS, Schlessinger J, Jorgensen WL. Conversion of a False Virtual Screen Hit into Selective JAK2 JH2 Domain Binders Using Convergent Design Strategies. ACS Medicinal Chemistry Letters 2022, 13: 819-826. PMID: 35586418, PMCID: PMC9109162, DOI: 10.1021/acsmedchemlett.2c00051.
- Structural basis for ligand reception by anaplastic lymphoma kinaseLi T, Stayrook SE, Tsutsui Y, Zhang J, Wang Y, Li H, Proffitt A, Krimmer SG, Ahmed M, Belliveau O, Walker IX, Mudumbi KC, Suzuki Y, Lax I, Alvarado D, Lemmon MA, Schlessinger J, Klein DE. Structural basis for ligand reception by anaplastic lymphoma kinase. Nature 2021, 600: 148-152. PMID: 34819665, PMCID: PMC8639777, DOI: 10.1038/s41586-021-04141-7.
- Indoloxytriazines as binding molecules for the JAK2 JH2 pseudokinase domain and its V617F variantNewton AS, Liosi ME, Henry SP, Deiana L, Faver JC, Krimmer SG, Puleo DE, Schlessinger J, Jorgensen WL. Indoloxytriazines as binding molecules for the JAK2 JH2 pseudokinase domain and its V617F variant. Tetrahedron Letters 2021, 77: 153248. PMID: 34393283, PMCID: PMC8357305, DOI: 10.1016/j.tetlet.2021.153248.
- Metadynamics as a Postprocessing Method for Virtual Screening with Application to the Pseudokinase Domain of JAK2Cutrona KJ, Newton AS, Krimmer SG, Tirado-Rives J, Jorgensen WL. Metadynamics as a Postprocessing Method for Virtual Screening with Application to the Pseudokinase Domain of JAK2. Journal Of Chemical Information And Modeling 2020, 60: 4403-4415. PMID: 32383599, PMCID: PMC7927942, DOI: 10.1021/acs.jcim.0c00276.
- Selective Janus Kinase 2 (JAK2) Pseudokinase Ligands with a Diaminotriazole CoreLiosi ME, Krimmer SG, Newton AS, Dawson T, Puleo DE, Cutrona KJ, Suzuki Y, Schlessinger J, Jorgensen WL. Selective Janus Kinase 2 (JAK2) Pseudokinase Ligands with a Diaminotriazole Core. Journal Of Medicinal Chemistry 2020, 63: 5324-5340. PMID: 32329617, PMCID: PMC7949251, DOI: 10.1021/acs.jmedchem.0c00192.
- Bayesian analysis of isothermal titration calorimetry for binding thermodynamicsNguyen T, Rustenburg A, Krimmer S, Zhang H, Clark J, Novick P, Branson K, Pande V, Chodera J, Minh D. Bayesian analysis of isothermal titration calorimetry for binding thermodynamics. PLOS ONE 2018, 13: e0203224. PMID: 30212471, PMCID: PMC6136728, DOI: 10.1371/journal.pone.0203224.
- Optimization of Pyrazoles as Phenol Surrogates to Yield Potent Inhibitors of Macrophage Migration Inhibitory FactorTrivediāParmar V, Robertson MJ, Cisneros J, Krimmer SG, Jorgensen WL. Optimization of Pyrazoles as Phenol Surrogates to Yield Potent Inhibitors of Macrophage Migration Inhibitory Factor. ChemMedChem 2018, 13: 1092-1097. PMID: 29575754, PMCID: PMC5990473, DOI: 10.1002/cmdc.201800158.
- Adding a Hydrogen Bond May Not Help: Naphthyridinone vs Quinoline Inhibitors of Macrophage Migration Inhibitory FactorDawson TK, Dziedzic P, Robertson MJ, Cisneros J, Krimmer SG, Newton AS, Tirado-Rives J, Jorgensen WL. Adding a Hydrogen Bond May Not Help: Naphthyridinone vs Quinoline Inhibitors of Macrophage Migration Inhibitory Factor. ACS Medicinal Chemistry Letters 2017, 8: 1287-1291. PMID: 29259749, PMCID: PMC5733268, DOI: 10.1021/acsmedchemlett.7b00384.
- How Nothing Boosts Affinity: Hydrophobic Ligand Binding to the Virtually Vacated S1ā² Pocket of ThermolysinKrimmer S, Cramer J, Schiebel J, Heine A, Klebe G. How Nothing Boosts Affinity: Hydrophobic Ligand Binding to the Virtually Vacated S1ā² Pocket of Thermolysin. Journal Of The American Chemical Society 2017, 139: 10419-10431. PMID: 28696673, DOI: 10.1021/jacs.7b05028.
- Paying the Price of Desolvation in Solvent-Exposed Protein Pockets: Impact of Distal Solubilizing Groups on Affinity and Binding Thermodynamics in a Series of Thermolysin InhibitorsCramer J, Krimmer S, Heine A, Klebe G. Paying the Price of Desolvation in Solvent-Exposed Protein Pockets: Impact of Distal Solubilizing Groups on Affinity and Binding Thermodynamics in a Series of Thermolysin Inhibitors. Journal Of Medicinal Chemistry 2017, 60: 5791-5799. PMID: 28590130, DOI: 10.1021/acs.jmedchem.7b00490.
- Elucidating the Origin of Long Residence Time Binding for Inhibitors of the Metalloprotease ThermolysinCramer J, Krimmer S, Fridh V, Wulsdorf T, Karlsson R, Heine A, Klebe G. Elucidating the Origin of Long Residence Time Binding for Inhibitors of the Metalloprotease Thermolysin. ACS Chemical Biology 2016, 12: 225-233. PMID: 27959500, DOI: 10.1021/acschembio.6b00979.
- Rational Design of Thermodynamic and Kinetic Binding Profiles by Optimizing Surface Water Networks Coating Protein-Bound LigandsKrimmer S, Cramer J, Betz M, Fridh V, Karlsson R, Heine A, Klebe G. Rational Design of Thermodynamic and Kinetic Binding Profiles by Optimizing Surface Water Networks Coating Protein-Bound Ligands. Journal Of Medicinal Chemistry 2016, 59: 10530-10548. PMID: 27933956, DOI: 10.1021/acs.jmedchem.6b00998.
- Active Site Mapping of an Aspartic Protease by Multiple Fragment Crystal Structures: Versatile Warheads To Address a Catalytic DyadRadeva N, Schiebel J, Wang X, Krimmer S, Fu K, Stieler M, Ehrmann F, Metz A, Rickmeyer T, Betz M, Winquist J, Park A, Huschmann F, Weiss M, Mueller U, Heine A, Klebe G. Active Site Mapping of an Aspartic Protease by Multiple Fragment Crystal Structures: Versatile Warheads To Address a Catalytic Dyad. Journal Of Medicinal Chemistry 2016, 59: 9743-9759. PMID: 27726357, DOI: 10.1021/acs.jmedchem.6b01195.
- Experimental Active-Site Mapping by Fragments: Hot Spots Remote from the Catalytic Center of EndothiapepsinRadeva N, Krimmer S, Stieler M, Fu K, Wang X, Ehrmann F, Metz A, Huschmann F, Weiss M, Mueller U, Schiebel J, Heine A, Klebe G. Experimental Active-Site Mapping by Fragments: Hot Spots Remote from the Catalytic Center of Endothiapepsin. Journal Of Medicinal Chemistry 2016, 59: 7561-7575. PMID: 27463859, DOI: 10.1021/acs.jmedchem.6b00645.
- High-Throughput Crystallography: Reliable and Efficient Identification of Fragment HitsSchiebel J, Krimmer S, Rƶwer K, Knƶrlein A, Wang X, Park A, Stieler M, Ehrmann F, Fu K, Radeva N, Krug M, Huschmann F, Glƶckner S, Weiss M, Mueller U, Klebe G, Heine A. High-Throughput Crystallography: Reliable and Efficient Identification of Fragment Hits. Structure 2016, 24: 1398-1409. PMID: 27452405, DOI: 10.1016/j.str.2016.06.010.
- Six Biophysical Screening Methods Miss a Large Proportion of Crystallographically Discovered Fragment Hits: A Case StudySchiebel J, Radeva N, Krimmer S, Wang X, Stieler M, Ehrmann F, Fu K, Metz A, Huschmann F, Weiss M, Mueller U, Heine A, Klebe G. Six Biophysical Screening Methods Miss a Large Proportion of Crystallographically Discovered Fragment Hits: A Case Study. ACS Chemical Biology 2016, 11: 1693-1701. PMID: 27028906, DOI: 10.1021/acschembio.5b01034.
- Impact of Surface Water Layers on ProteināLigand Binding: How Well Are Experimental Data Reproduced by Molecular Dynamics Simulations in a Thermolysin Test Case?Betz M, Wulsdorf T, Krimmer S, Klebe G. Impact of Surface Water Layers on ProteināLigand Binding: How Well Are Experimental Data Reproduced by Molecular Dynamics Simulations in a Thermolysin Test Case? Journal Of Chemical Information And Modeling 2016, 56: 223-233. PMID: 26691064, DOI: 10.1021/acs.jcim.5b00621.
- Thermodynamics of proteināligand interactions as a reference for computational analysis: how to assess accuracy, reliability and relevance of experimental dataKrimmer S, Klebe G. Thermodynamics of proteināligand interactions as a reference for computational analysis: how to assess accuracy, reliability and relevance of experimental data. Journal Of Computer-Aided Molecular Design 2015, 29: 867-883. PMID: 26376645, DOI: 10.1007/s10822-015-9867-y.
- Methyl, Ethyl, Propyl, Butyl: Futile But Not for Water, as the Correlation of Structure and Thermodynamic Signature Shows in a Congeneric Series of Thermolysin InhibitorsKrimmer S, Betz M, Heine A, Klebe G. Methyl, Ethyl, Propyl, Butyl: Futile But Not for Water, as the Correlation of Structure and Thermodynamic Signature Shows in a Congeneric Series of Thermolysin Inhibitors. ChemMedChem 2014, 9: 833-846. PMID: 24623396, DOI: 10.1002/cmdc.201400013.
- Synthesis and Characterization of Poly(Īµācaprolactone)āblockāpoly[Nā(2āhydroxypropyl)methacrylamide] Micelles for Drug DeliveryKrimmer S, Pan H, Liu J, Yang J, KopeÄek J. Synthesis and Characterization of Poly(Īµācaprolactone)āblockāpoly[Nā(2āhydroxypropyl)methacrylamide] Micelles for Drug Delivery. Macromolecular Bioscience 2011, 11: 1041-1051. PMID: 21567954, PMCID: PMC4598047, DOI: 10.1002/mabi.201100019.