Grutsch S, Fuchs JE, Ahammer L,  Kamenik AS, Liedl KR*, Tollinger M*.
        Conformational flexibility differentiates naturally occurring Bet v 1 isoforms.
        Int J Mol Sci 2017 (18) 1192. (open access)
        doi: 10.3390/ijms18061192


Ahammer L, Grutsch S, Kamenik AS, Liedl KR, Tollinger M*.
        Structure of the major apple allergen Mal d 1.
        J Agricult Food Chem 2017 (65): 1606-1612. (open access)
        doi: 10.1021/acs.jafc.6b05752


Ahammer L, Grutsch S, Wallner M, Ferreira F, Tollinger M*.
        NMR resonance assignments of a hypoallergenic isoform of the major birch pollen allergen Bet v 1.
        Biomol NMR Assign 2017 (18): accepted for publication.


Nussbaumer F, Juen M, Gasser C, Kremser J, Mueller T, Tollinger M, Kreutz CK*.
        Synthesis and incorporation of 13C-labeled DNA building blocks to probe structural dynamics of DNA by NMR.
        Nucleic Acids Res 2017 (45): accepted for publication. (open access)
        doi: 10.1002/nar/gkx592


Moschen T, Grutsch S, Juen, MA, Wunderlich CH, Kreutz C*, Tollinger M*.
        Measurement of ligand-target residence times by 1H relaxation dispersion NMR spectroscopy.
        J Med Chem 2016 (59): 10788-10793. (open access)
        doi: 10.1021/acs.jmedchem.6b01110


Juen MA, Wunderlich CH, Nussbaumer F, Tollinger M, Kontaxis G, Konrat R, Hansen DF*, Kreutz CK*.
        Excited states of nucleic acids probed by proton relaxation dispersion NMR spectroscopy. 
        Angew Chem Intl Ed Engl 2016 (55): 12008-12012. (open access)
        doi: 10.1002/anie.201605870


Ahammer L, Grutsch STollinger M*.
        NMR resonance assignments of the major apple allergen Mal d 1. 
        Biomol NMR Assign 2016 (10): 287-290. (open access) 
        doi: 10.1007/s12104-016-9685-8


Grutsch SBrüschweiler STollinger M*.
        NMR methods to study dynamic allostery. 
        PLoS Comput Biol 2016 (12): e1004620. (open access) 
        doi: 10.1371/journal.pcbi.1004620


Machado Y, Freier R, Scheiblhofer S, Thalhamer T, Mayr M, Briza P, Grutsch SAhammer L, Fuchs J, Wallnöfer H, Isakovic A, Kohlbauer V, Hinterholzer A, Steiner M, Danzer M, Horejs-Hoeck J, Ferreira F, Liedl KR, Tollinger M, Lackner P, Johnson CM, Brandstetter H, Thalhamer J & Weiss R*.
        Fold-stability during endolysosomal acidification is a key factor for allergenicity and immunogenicity of the major birch pollen allergen.
        Journal of Allergy and Clinical Immunology 2016 (137): 1525-1534. (open access)
        doi: 10.1016/j.jaci.2015.09.026 


Kaderavek P, Grutsch S, Salvi N, Tollinger M, Zidek L, Bodenhausen G & Ferrage F*.
        Cross-correlated relaxation measurements under adiabatic sweeps: determination of local order in proteins. 
        J Biomol NMR 2015 (63): 353-365. (open access)
        doi: 10.1007/s10858-015-9994-8


Moschen T, Wunderlich C, Kreutz C, Tollinger M*.
        NMR resonance assignments of the archaeal ribosomal protein L7Ae in the apo form and bound to a 25 nt RNA.
        Biomol NMR Assign 2015 (9): 177-180. (open access)
        doi: 10.1007/s12104-014-9569-8


Pummer BG*, Budke C, Augustin-Bauditz S, Niedermeier D, Felgitsch L, Kampf CJ, Huber RG, Liedl KR, Loerting T, Moschen T, Schauperl M, Tollinger M, Morris CE, Wex H, Grothe H, Pöschl U, Koop T, Fröhlich-Nowoisky J.
        Ice nucleation by water-soluble macromolecules. 
        Athmos Chem Phys 2015 (15): 4077-4091. (open access)
        doi: 10.5194/acp-15-4077-2015


Moschen T, Wunderlich CH, Spitzer R, Levic J, Micura R, Tollinger M*, Kreutz C*.
        Ligand-detected relaxation dispersion NMR spectroscopy: dynamics of preQ1-RNA binding.
        Angew Chem Intl Ed Engl 2015 (54): 560-563.
        doi: 10.1002/anie.201409779


Grutsch S, Fuchs JE, Freier R, Kofler S, Bibi M, Asam C, Wallner M, Ferreira F, Brandstetter H, Liedl KR, Tollinger M*.
        Ligand binding modulates structural dynamics and compactness of the major birch pollen allergen Bet v 1.0101. 
        Biophys J 2014 (107): 2963-2972. (open access)
        doi: 10.1016/j.bpj.2014.10.062


Morin S, Linnet TE, Lescanne M, Schanda P, Thompson G, Tollinger M, Teilum K, Gagne S, Marion D, Griesinger C, Blackledge M, d´Auvergne E*.
        Relax: the analysis of biomolecular kinetics and thermodynamics using NMR relaxation dispersion data. 
        Bioinformatics 2014 (30): 2219-2220. (open access)
        doi: 10.1093/bioinformatics/btu166


Moschen TTollinger M*.
        A kinetic study of domain swapping in Protein L. 
        Phys Chem Chem Phys 2014 (16): 6383-6390.
        doi: 10.1039/C3CP54126F


Palazzesi F, Barducci A, Tollinger M, Parrinello M*.
        The allosteric communication pathways in the KIX domain. 
        Proc Natl Acad Sci USA 2013 (110): 14237-14242. (open access)
        doi: 10.1073/pnas.1313548110


Brüschweiler S, Konrat R, Tollinger M*.
        Allosteric communication in the KIX domain proceeds through dynamic re-packing of the hydrophobic core. 
        ACS Chem Biol 2013 (8): 1600-1610. (open access)
        doi: 10.1021/cb4002188


Tollinger M, Sivertsen A, Meier B, Ernst M, Schanda P*.
        Site-resolved measurement of microsecond to millisecond conformational-exchange processes in proteins by solid-state NMR spectroscopy.
        J Am Chem Soc 2012 (134): 14800-14807. (open access)
        doi: 10.1021/ja303591y


Wunderlich C, Spitzer R, Santner T, Fauster K, Tollinger M, Kreutz C*.
        Synthesis of 6-13C-pyrimidine nucleotides as spin labels for RNA dynamics.
        J Am Chem Soc 2012 (134): 7558-7569.
        doi:10.1021/ja302148g


Kloiber K, Spitzer R, Grutsch S, Kreutz C, Tollinger M*.
        Longitudinal exchange: an alternative strategy towards quantification of dynamics parameters in ZZ exchange spectroscopy.
        J Biomol NMR 2011 (51): 123-129.
        doi: 10.1007/s10858-011-9547-8


Spitzer R, Kloiber K, Tollinger M, Kreutz C*.
        Kinetics of DNA refolding via longitudinal exchange NMR spectroscopy.
        ChemBioChem 2011 (12): 2007-2010.
        doi: 10.1002/cbic.201100318


Auer R, Tollinger M, Kuprov I, Konrat R, Kloiber K*.
        Mathematical treatment of adiabatic fast passage pulses for the computation of nuclear spin relaxation rates in proteins with conformational exchange.
        J Biomol NMR 2011 (51): 35-47. (open access)
        doi: 10.1007/s10858-011-9539-8


Coudevylle N, Geist L, Hoetzinger M, Tollinger M, Konrat R*.
        Siderocalin Q83 exhibits differential slow dynamics upon ligand binding.
        J Biomol NMR 2011 (51): 83-88.
        doi: 10.1007/s10858-011-9543-z


Kloiber K, Spitzer R, Tollinger M, Konrat R, Kreutz C*.
        Probing RNA dynamics via longitudinal exchange and CPMG relaxation dispersion NMR spectroscopy using a sensitive 13C-methyl label.
        Nucleic Acids Res 2011 (39): 4340-4351. (open access)
        doi: 10.1093/nar/gkq1361


Breuker K*, Brüschweiler STollinger M.
        Electrostatic stabilization of native protein structure in the gas phase. 
        Angew Chem Intl Ed Engl 2011 (50): 873-877. (open access)
        doi: 10.1002/ange.201005112
        Discussed in: Barran PE: Angew Chem Intl Ed Engl 2011 (50): 3120-3122.


Brüschweiler S, Schanda P, Kloiber K, Brutscher B, Kontaxis G, Konrat R, Tollinger M*.
        Direct observation of the dynamic process underlying allosteric signal transmission. 
        J Am Chem Soc 2009 (131): 3063-3068.
        doi: 10.1021/ja809947w


Schedlbauer A, Coudevylle N, Auer R, Kloiber K, Tollinger M, Konrat R*.
        Auto-correlation analysis of NOESY data provides residue compactness for folded and unfolded proteins. 
        J Am Chem Soc 2009 (131): 6038-6039.
        doi: 10.1021/ja8074067


Schedlbauer A, Auer R, Ledolter K, Tollinger M, Kloiber K, Lichtenecker R, Rüdisser 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. 
        J Biomol NMR 2008 (42): 111-127.
        doi: 10.1007/s10858-008-9268-9


Schanda P, Brutscher B, Konrat R, Tollinger M*.
        Folding of the KIX domain: characterization of the equilibrium analog of a folding intermediate using 15N/13C relaxation dispersion and fast 1H/2H amide exchange NMR spectroscopy. 
        J Mol Biol 2008 (380): 726-741.
        doi: 10.1016/j.jmb.2008.05.040


Marsh JA, Baker JM, Tollinger M, Forman-Kay JD*.
        Calculation of residual dipolar couplings from disordered state ensembles using local alignment.
        J Am Chem Soc 2008 (130): 7804-7805.
        doi: 10.1021/ja802220c


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 2006 (45): 8885-8893.
        doi: 10.1021/bi0607305


Tollinger M, Neale C, Kay LE, Forman-Kay JD*.
        Characterization of the hydrodynamic properties of the folding transition state of an SH3 domain by magnetization transfer NMR spectroscopy.
        Biochemistry 2006 (45): 6434-6445.
        doi: 10.1021/bi060268o


Tollinger M*, Kay LE, Forman-Kay JD.
        Measuring pK(a) values in protein folding transition state ensembles by NMR spectroscopy.
        J Am Chem Soc 2005 (127): 8904-8905.
        doi: 10.1021/ja051942c


Bezsonova I, Singer A, Choy WY, Tollinger M, Forman-Kay JD*.
        Structural comparison of the unstable drkN SH3 domain and a stable mutant.
        Biochemistry 2005 (44): 15550-15560.
        doi: 10.1021/bi0512795


Tollinger M, Crowhurst KA, Kay LE, Forman-Kay JD*.
        Site-specific contributions to the pH dependence of protein stability.
        Proc Natl Acad Sci USA 2003 (100): 4545-4550.
        doi: 10.1073􏰓pnas.0736600100


Crowhurst KA, Tollinger M, Forman-Kay JD*.
        Cooperative interactions and a non-native buried Trp in the unfolded state of an SH3 domain.
        J Mol Biol 2002 (322): 163-178.
        doi: 10.1016/S0022-2836(02)00741-6


Tollinger M, Forman-Kay JD, Kay LE*.
        Measurement of side-chain carboxyl pK(a) values of glutamate and aspartate residues in an unfolded protein by multinuclear NMR spectroscopy.
        J Am Chem Soc 2002 (124): 5714-5717.
        doi: 10.1021/ja020066p


Tollinger M, Skrynnikov NR, Mulder FA, Forman-Kay JD, Kay LE*.
        Slow dynamics in folded and unfolded states of an SH3 domain.
        J Am Chem Soc 2001 (123): 11341-11352.
        doi: 10.1021/ja011300z


Choy WY, Tollinger M, Mueller GA, Kay LE*.
        Direct structure refinement of high molecular weight proteins against residual dipolar couplings and carbonyl chemical shift changes upon alignment: an application to maltose binding protein.
        J Biomol NMR 2001 (21): 31-40.
        doi: 10.1023/A:1011933020122


Hoffmann B, Tollinger M, Konrat R, Huhta M, Marsh EN, Kräutler B*.
        A protein pre-organized to trap the nucleotide moiety of coenzyme B12: refined solution structure of the B12-binding subunit of glutamate mutase from Clostridium tetanomorphum.
        Chembiochem 2001 (2): 643-655.
        doi: 10.1002/1439-7633(20010903)2:9<643::AID-CBIC643>3.0.CO;2-J


Eichmüller C, Tollinger M, Kräutler B, Konrat R*.
        Mapping the ligand binding site at protein side-chains in protein-ligand complexes through NOE difference spectroscopy.
        J Biomol NMR 2001 (20): 195-202.
        doi: 10.1023/A:1011299009214


Tollinger M, Eichmüller C, Konrat R, Huhta MS, Marsh EN, Kräutler B*.
        The B12-binding subunit of glutamate mutase from Clostridium tetanomorphum traps the nucleotide moiety of coenzyme B12.
        J Mol Biol 2001 (309): 777-791.
        doi: 10.1023/A:1011299009214


Konrat R*, Tollinger M.
        Heteronuclear relaxation in time-dependent spin systems: 15N T1-rho dispersion during adiabatic fast passage.
        J Biomol NMR 1999 (13): 213-221.
        doi: 10.1023/A:1008324721356


Tollinger M, Konrat R, & Kräutler B*. 
        The structure of methylcob(II)alamin in aqueous solution - a water molecule as structuring element of the nucleotide loop.
        Helv Chim Acta 1999 (82): 1596-1609.
        doi: 10.1002/(SICI)1522-2675(19991006)82:10<1596::AID-HLCA1596>3.0.CO;2-K


Kontaxis G, Riether D, Hannak R, Tollinger M, Kräutler, B*.
        Electrochemical synthesis and structure analysis of neocoenzyme B12 - an epimer of coenzyme B12 with a remarkably flexible organometallic group.
        Helv Chim Acta 1999 (82): 848-869.
        doi: 10.1002/(SICI)1522-2675(19990609)82:6<848::AID-HLCA848>3.0.CO;2-L


Zieger G, Sterk H, Bermel W, Konrat R, Tollinger M, Kräutler B, Werbelow, L.* 
        Relaxation-induced polarization transfer and determination of methyl group 13C chemical shielding anisotropy.
        J Phys Chem A 1999 (103): 5253-5258.
        doi: 10.1021/jp990409e


Tollinger M, Konrat R, Hilbert BH, Marsh EN, Kräutler B*.
        How a protein prepares for B12 binding: structure and dynamics of the B12-binding subunit of glutamate mutase from Clostridium tetanomorphum.
        Structure 1998 (6): 1021-1033.
        doi: 10.1016/S0969-2126(98)00103-8


Konrat R, Tollinger M, Kräutler B*. 
        New NMR structural and dynamical probes of organometallic B12-derivatives. 
        in: Vitamin B12 and B12-binding Proteins, Verlag Wiley-VCH Weinheim, Germany 1998, pp. 349-368