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1.
Niu, Z. et al.: Structural insight into IAPP-derived amyloid inhibitors and their mechanism of action. Angew. Chem.-Int. Edit. 59, 2-13 (2020)
2.
Ščupáková, K.* ; Dewez, F.* ; Walch, A.K. ; Heeren, R.M.A.* & Balluff, B.*: Morphometric cell classification for single-Cell MALDI-mass spectrometry imaging. Angew. Chem.-Int. Edit. 132, 17600-17603 (2020)
3.
Jagtap, P.K.A.* et al.: Selective inhibitors of FKBP51 employ conformational selection of dynamic invisible states (vol 58, pg 9429, 2019). Angew. Chem.-Int. Edit., DOI: 10.1002/anie.201908888 (2019)
4.
Jagtap, P.K.A.* et al.: Selective inhibitors of FKBP51 employ conformational selection of dynamic invisible states. Angew. Chem.-Int. Edit. 58, 9429-9433 (2019)
5.
Kirsch, V.C.* et al.: The cytotoxic natural product vioprolide A targets nucleolar protein 14 essential for ribosome biogenesis. Angew. Chem.-Int. Edit. 59, 1595-1600 (2019)
6.
Xue, K. ; Mühlbauer, M. ; Mamone, S.* ; Sarkar, R. & Reif, B.: Accurate determination of H-1-N-15 dipolar couplings using inaccurate settings of the magic angle in solid-state NMR spectroscopy. Angew. Chem.-Int. Edit. 58, 4286-4290 (2019)
7.
Asami, S.* et al.: Ultrashort broadband cooperative pulses for multidimensional bio-molecular NMR experiments. Angew. Chem.-Int. Edit. 57, 14498-14502 (2018)
8.
Jürjens, G. et al.: Total synthesis and structural revision of the antibiotic tetrapeptide GE81112A. Angew. Chem.-Int. Edit. 57, 12157-12161 (2018)
9.
Supekar, S.* et al.: Conformational selection of dimethylarginine recognition by the survival motor neuron tudor domain. Angew. Chem.-Int. Edit. 57, 486-490 (2018)
10.
Tošner, Z.* et al.: Overcoming volume selectivity of dipolar recoupling in biological solid-state NMR spectroscopy Angew. Chem.-Int. Edit. 130, 14722-14726 (2018)
11.
Plettenburg, O.: What do reactive fragments actually do in cells? Angew. Chem.-Int. Edit. 56, 446-448 (2017)
12.
Sonntag, M. et al.: Segmental, domain-selective perdeuteration and small-angle neutron scattering for structural analysis of multi-domain proteins. Angew. Chem.-Int. Edit. 56, 9322-9325 (2017)
13.
Göbl, C. et al.: Increasing the chemical-shift dispersion of unstructured proteins with a covalent lanthanide shift reagent. Angew. Chem.-Int. Edit. 55, 14847-14851 (2016)
14.
Hartlmüller, C. ; Göbl, C. & Madl, T.: Prediction of protein structure using surface accessibility data. Angew. Chem.-Int. Edit. 55, 11970-11974 (2016)
15.
Aichler, M. et al.: Spatially resolved quantification of Gadolinium(III)-based magnetic resonance agents in tissue by MALDI imaging mass spectrometry after in vivo MRI. Angew. Chem.-Int. Edit. 54, 4279-4283 (2015)
16.
Andreetto, E.* et al.: A hot-segment-based approach for the design of cross-amyloid interaction surface mimics as inhibitors of amyloid self-assembly. Angew. Chem.-Int. Edit. 54, 13095-13100 (2015)
17.
Schilling, F.* et al.: Next-generation heteronuclear decoupling for high-field biomolecular NMR spectroscopy. Angew. Chem.-Int. Edit. 53, 4475-4479 (2014)
18.
Zierer, B.K.* et al.: Artificial accelerators of the molecular chaperone Hsp90 facilitate rate-limiting conformational transitions. Angew. Chem.-Int. Edit. 53, 12257-12262 (2014)
19.
Asami, S. ; Rakwalska-Bange, M.* ; Carlomagno, T.* & Reif, B.: Protein-RNA interfaces probed by 1H-detected MAS solid-state NMR spectroscopy. Angew. Chem.-Int. Edit. 52, 2345-2349 (2013)
20.
Dallmann, A. et al.: Efficient detection of hydrogen bonds in dynamic regions of RNA by sensitivity-optimized NMR pulse sequences. Angew. Chem.-Int. Edit. 52, 10487-10490 (2013)