Year |
Citation |
Score |
2024 |
Knödlstorfer S, Schiavina M, Rodella MA, Ledolter K, Konrat R, Pierattelli R, Felli IC. Disentangling the Complexity in Protein Complexes Using Complementary Isotope-Labeling and Multiple-Receiver NMR Spectroscopy. Journal of the American Chemical Society. PMID 39374115 DOI: 10.1021/jacs.4c09176 |
0.301 |
|
2023 |
Platzer G, Ptaszek AL, Böttcher J, Fuchs JE, Geist L, Braun D, McConnell DB, Konrat R, Sánchez-Murcia PA, Mayer M. Ligand H NMR Chemical Shifts as Accurate Reporters for Protein-Ligand Binding Interfaces in Solution. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. e202300636. PMID 37955910 DOI: 10.1002/cphc.202300636 |
0.302 |
|
2023 |
Schiavina M, Konrat R, Ceccolini I, Mateos B, Konrat R, Felli IC, Pierattelli R. Studies of proline conformational dynamics in IDPs by C-detected cross-correlated NMR relaxation. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 354: 107539. PMID 37632987 DOI: 10.1016/j.jmr.2023.107539 |
0.308 |
|
2022 |
Feichtinger M, Beier A, Migotti M, Schmid M, Bokhovchuk F, Chène P, Konrat R. Long-range structural preformation in yes-associated protein precedes encounter complex formation with TEAD. Iscience. 25: 104099. PMID 35378854 DOI: 10.1016/j.isci.2022.104099 |
0.382 |
|
2021 |
Mateos B, Holzinger J, Conrad-Billroth C, Platzer G, Żerko S, Sealey-Cardona M, Anrather D, Koźmiński W, Konrat R. Hyperphosphorylation of Human Osteopontin and Its Impact on Structural Dynamics and Molecular Recognition. Biochemistry. 60: 1347-1355. PMID 33876640 DOI: 10.1021/acs.biochem.1c00050 |
0.322 |
|
2020 |
Kauffmann C, Zawadzka-Kazimierczuk A, Kontaxis G, Konrat R. Using Cross-Correlated Spin Relaxation to Characterize Backbone Dihedral Angle Distributions of Flexible Protein Segments. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. 22: 18-28. PMID 33119214 DOI: 10.1002/cphc.202000789 |
0.376 |
|
2020 |
Kauffmann C, Kazimierczuk K, Schwarz TC, Konrat R, Zawadzka-Kazimierczuk A. A novel high-dimensional NMR experiment for resolving protein backbone dihedral angle ambiguities. Journal of Biomolecular Nmr. 74: 257-265. PMID 32239382 DOI: 10.1007/s10858-020-00308-y |
0.404 |
|
2020 |
Olsen GL, Szekely O, Mateos B, Kadeřávek P, Ferrage F, Konrat R, Pierattelli R, Felli IC, Bodenhausen G, Kurzbach D, Frydman L. Sensitivity-enhanced three-dimensional and carbon-detected two-dimensional NMR of proteins using hyperpolarized water. Journal of Biomolecular Nmr. PMID 32040802 DOI: 10.1007/S10858-020-00301-5 |
0.315 |
|
2019 |
Mateos B, Conrad-Billroth C, Schiavina M, Beier A, Kontaxis G, Konrat R, Felli IC, Pierattelli R. The Ambivalent Role of Proline Residues in an Intrinsically Disordered Protein: From Disorder Promoters to Compaction Facilitators. Journal of Molecular Biology. 432: 3093-3111. PMID 31794728 DOI: 10.1016/j.jmb.2019.11.015 |
0.392 |
|
2019 |
Somlyay M, Ledolter K, Kitzler M, Cobb SL, Sandford G, Konrat R. 19F NMR tagging and PRE-based conformational analysis of intrinsically disordered protein complexes. Chembiochem : a European Journal of Chemical Biology. PMID 31529763 DOI: 10.1002/Cbic.201900453 |
0.318 |
|
2018 |
Mateos B, Konrat R, Pierattelli R, Felli IC. NMR Characterization of Long-Range Contacts in Intrinsically Disordered Proteins from Paramagnetic Relaxation Enhancement in C Direct-Detection Experiments. Chembiochem : a European Journal of Chemical Biology. 20: 335-339. PMID 30407719 DOI: 10.1002/cbic.201800539 |
0.324 |
|
2018 |
Beier A, Schwarz TC, Kurzbach D, Platzer G, Tribuzio F, Konrat R. Modulation of Correlated Segment Fluctuations in IDPs upon Complex Formation as an Allosteric Regulatory Mechanism. Journal of Molecular Biology. 430: 2439-2452. PMID 29733855 DOI: 10.1016/j.jmb.2018.04.035 |
0.324 |
|
2018 |
Feichtinger M, Sára T, Platzer G, Mateos B, Bokhovchuk F, Chène P, Konrat R. H, C, N resonance assignment of human YAP 50-171 fragment. Biomolecular Nmr Assignments. 12: 179-182. PMID 29372459 DOI: 10.1007/s12104-018-9805-8 |
0.342 |
|
2017 |
Geist L, Mayer M, Cockcroft XL, Wolkerstorfer B, Kessler D, Engelhardt H, McConnell DB, Konrat R. Direct NMR Probing of Hydration Shells of Protein Ligand Interfaces and its Application to Drug Design. Journal of Medicinal Chemistry. PMID 28910100 DOI: 10.1021/acs.jmedchem.7b00845 |
0.319 |
|
2017 |
Kurzbach D, Beier A, Vanas A, Flamm AG, Platzer G, Schwarz TC, Konrat R. NMR probing and visualization of correlated structural fluctuations in intrinsically disordered proteins. Physical Chemistry Chemical Physics : Pccp. PMID 28397898 DOI: 10.1039/c7cp00430c |
0.381 |
|
2016 |
Żerko S, Byrski P, Włodarczyk-Pruszyński P, Górka M, Ledolter K, Masliah E, Konrat R, Koźmiński W. Five and four dimensional experiments for robust backbone resonance assignment of large intrinsically disordered proteins: application to Tau3x protein. Journal of Biomolecular Nmr. PMID 27430223 DOI: 10.1007/S10858-016-0048-7 |
0.328 |
|
2015 |
Kurzbach D, Kontaxis G, Coudevylle N, Konrat R. NMR Spectroscopic Studies of the Conformational Ensembles of Intrinsically Disordered Proteins. Advances in Experimental Medicine and Biology. 870: 149-85. PMID 26387102 DOI: 10.1007/978-3-319-20164-1_5 |
0.388 |
|
2014 |
Sára T, Schwarz TC, Kurzbach D, Wunderlich CH, Kreutz C, Konrat R. Magnetic resonance access to transiently formed protein complexes. Chemistryopen. 3: 115-23. PMID 25050230 DOI: 10.1002/open.201402008 |
0.307 |
|
2014 |
Konrat R. NMR contributions to structural dynamics studies of intrinsically disordered proteins. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 241: 74-85. PMID 24656082 DOI: 10.1016/j.jmr.2013.11.011 |
0.363 |
|
2014 |
Kurzbach D, Schwarz TC, Platzer G, Höfler S, Hinderberger D, Konrat R. Compensatory adaptations of structural dynamics in an intrinsically disordered protein complex. Angewandte Chemie (International Ed. in English). 53: 3840-3. PMID 24604825 DOI: 10.1002/anie.201308389 |
0.358 |
|
2014 |
Orbán-Németh Z, Henen MA, Geist L, Żerko S, Saxena S, Stanek J, Koźmiński W, Propst F, Konrat R. Backbone and partial side chain assignment of the microtubule binding domain of the MAP1B light chain. Biomolecular Nmr Assignments. 8: 123-7. PMID 23339032 DOI: 10.1007/s12104-013-9466-6 |
0.499 |
|
2013 |
Stanek J, Saxena S, Geist L, Konrat R, Ko?mi?ski W. Probing Local Backbone Geometries in Intrinsically Disordered Proteins by Cross-Correlated NMR Relaxation. Angewandte Chemie (Weinheim An Der Bergstrasse, Germany). 125: 4702-4704. PMID 25821254 DOI: 10.1002/ange.201210005 |
0.313 |
|
2013 |
Kurzbach D, Platzer G, Schwarz TC, Henen MA, Konrat R, Hinderberger D. Cooperative unfolding of compact conformations of the intrinsically disordered protein osteopontin. Biochemistry. 52: 5167-75. PMID 23848319 DOI: 10.1021/bi400502c |
0.568 |
|
2013 |
Geist L, Henen MA, Haiderer S, Schwarz TC, Kurzbach D, Zawadzka-Kazimierczuk A, Saxena S, Zerko S, Koźmiński W, Hinderberger D, Konrat R. Protonation-dependent conformational variability of intrinsically disordered proteins. Protein Science : a Publication of the Protein Society. 22: 1196-205. PMID 23821606 DOI: 10.1002/pro.2304 |
0.543 |
|
2013 |
Stanek J, Saxena S, Geist L, Konrat R, Koźmiński W. Probing local backbone geometries in intrinsically disordered proteins by cross-correlated NMR relaxation. Angewandte Chemie (International Ed. in English). 52: 4604-6. PMID 23520002 DOI: 10.1002/anie.201210005 |
0.313 |
|
2013 |
Solyom Z, Schwarten M, Geist L, Konrat R, Willbold D, Brutscher B. BEST-TROSY experiments for time-efficient sequential resonance assignment of large disordered proteins. Journal of Biomolecular Nmr. 55: 311-21. PMID 23435576 DOI: 10.1007/s10858-013-9715-0 |
0.311 |
|
2012 |
Henen MA, Coudevylle N, Geist L, Konrat R. Toward rational fragment-based lead design without 3D structures. Journal of Medicinal Chemistry. 55: 7909-19. PMID 22889313 DOI: 10.1021/jm301016m |
0.525 |
|
2011 |
Naranjo Y, Pons M, Konrat R. Meta-structure correlation in protein space unveils different selection rules for folded and intrinsically disordered proteins. Molecular Biosystems. 8: 411-6. PMID 22108787 DOI: 10.1039/c1mb05367a |
0.312 |
|
2011 |
Platzer G, Schedlbauer A, Chemelli A, Ozdowy P, Coudevylle N, Auer R, Kontaxis G, Hartl M, Miles AJ, Wallace BA, Glatter O, Bister K, Konrat R. The metastasis-associated extracellular matrix protein osteopontin forms transient structure in ligand interaction sites. Biochemistry. 50: 6113-24. PMID 21609000 DOI: 10.1021/bi200291e |
0.323 |
|
2010 |
Konrat R. The meandering of disordered proteins in conformational space. Structure (London, England : 1993). 18: 416-9. PMID 20399178 DOI: 10.1016/j.str.2010.03.003 |
0.312 |
|
2010 |
Brüschweiler S, Schanda P, Kloiber K, Brutscher B, Kontaxis G, Konrat R, Tollinger M. Direct observation of the dynamic process underlying allosteric signal transmission. Journal of the American Chemical Society. 131: 3063-8. PMID 19203263 DOI: 10.1021/ja809947w |
0.302 |
|
2009 |
Schedlbauer A, Coudevylle N, Auer R, Kloiber K, Tollinger M, Konrat R. Autocorrelation analysis of NOESY data provides residue compactness for folded and unfolded proteins. Journal of the American Chemical Society. 131: 6038-9. PMID 19364097 DOI: 10.1021/ja8074067 |
0.362 |
|
2008 |
Schedlbauer A, Auer R, Ledolter K, Tollinger M, Kloiber K, Lichtenecker R, Ruedisser S, Hommel U, Schmid W, Konrat R, Kontaxis G. Direct methods and residue type specific isotope labeling in NMR structure determination and model-driven sequential assignment. Journal of Biomolecular Nmr. 42: 111-27. PMID 18762865 DOI: 10.1007/S10858-008-9268-9 |
0.326 |
|
2006 |
Tollinger M, Kloiber K, Agoston B, Dorigoni C, Lichtenecker R, Schmid W, Konrat R. An isolated helix persists in a sparsely populated form of KIX under native conditions. Biochemistry. 45: 8885-93. PMID 16846231 DOI: 10.1021/Bi0607305 |
0.31 |
|
2005 |
Hoffmann B, Eichmüller C, Steinhauser O, Konrat R. Rapid assessment of protein structural stability and fold validation via NMR. Methods in Enzymology. 394: 142-75. PMID 15808220 DOI: 10.1016/S0076-6879(05)94006-8 |
0.35 |
|
2004 |
Ludwiczek ML, Baminger B, Konrat R. NMR probing of protein-protein interactions using reporter ligands and affinity tags. Journal of the American Chemical Society. 126: 1636-7. PMID 14871086 DOI: 10.1021/ja039149b |
0.321 |
|
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