Publikationen von M. Zweckstetter
Alle Typen
Zeitschriftenartikel (285)
261.
Zeitschriftenartikel
102, 10.1073/pnas.0407881102, S. 4294 - 4299 (2005)
Structural characterization of copper(II) binding to α-Synuclein: Insights into the bioinorganic chemistry of Parkinson's disease. Proceedings of the National Academy of Sciences of the United States of America 262.
Zeitschriftenartikel
102 (5), S. 1430 - 1435 (2005)
Release of long-range tertiary interactions potentiates aggregation of natively unstructured α-synuclein. Proceedings of the National Academy of Sciences of the United States of America 263.
Zeitschriftenartikel
127 (51), S. 17968 - 17969 (2005)
Defining long-range order and local disorder in native α-synuclein using residual dipolar couplings. Journal of the American Chemical Society 264.
Zeitschriftenartikel
23 (18), S. 3632 - 3642 (2004)
Structure and DNA-binding properties of the cytolysin regulator CylR2 from Enterococcus faecalis. EMBO Journal 265.
Zeitschriftenartikel
30 (1), S. 11 - 23 (2004)
Mars - robust automatic backbone assignment of proteins. Journal of Biomolecular NMR 266.
Zeitschriftenartikel
30 (1), S. 25 - 35 (2004)
Backbone assignment of proteins with known structure using residual dipolar couplings. Journal of Biomolecular NMR 267.
Zeitschriftenartikel
86 (6), S. 3444 - 3460 (2004)
Prediction of charge-induced molecular alignment of biomolecules dissolved in dilute liquid-crystalline phases. Biophysical Journal 268.
Zeitschriftenartikel
23, doi:10.1038/sj.emboj.7600211, S. 2039 - 2046 (2004)
NMR of α-synuclein-polyamine complexes elucidates the mechanism and kinetics of induced aggregation. EMBO Journal 269.
Zeitschriftenartikel
60, S. 746 - 748 (2004)
Expression, purification, crystallization and preliminary crystallographic studies of the Enterococcus faecalis cytolysin repressor CylR2. Acta Crystallographica Section D-Biological Crystallography 270.
Zeitschriftenartikel
43 (26), S. 3479 - 3481 (2004)
Simultaneous assignment and structure determination of protein backbones by using NMR dipolar couplings. Angewandte Chemie-International Edition 271.
Zeitschriftenartikel
278 (40), S. 39185 - 39188 (2003)
The NMR structure of the sensory domain of the membranous two-component fumarate sensor (histidine protein kinase) DcuS of Escherichia coli. Journal of Biological Chemistry 272.
Zeitschriftenartikel
27 (1), S. 41 - 56 (2003)
Determination of molecular alignment tensors without backbone resonance assignment: Aid to rapid analysis of protein-protein interactions. Journal of Biomolecular NMR 273.
Zeitschriftenartikel
163 (2), S. 353 - 359 (2003)
Measurement of long range H,C couplings in natural products in orienting media: a tool for structure elucidation of natural products. Journal of Magnetic Resonance 274.
Zeitschriftenartikel
23 (2), S. 127 - 137 (2002)
Evaluation of uncertainty in alignment tensors obtained from dipolar couplings. Journal of Biomolecular NMR 275.
Zeitschriftenartikel
20 (4), S. 365 - 377 (2001)
Characterization of molecular alignment in aqueous suspensions of Pf1 bacteriophage. Journal of Biomolecular NMR 276.
Zeitschriftenartikel
20 (3), S. 340 - 349 (2001)
The extracellular human melanoma inhibitory activity (MIA) protein adopts an SH3 domain-like fold. EMBO Journal 277.
Zeitschriftenartikel
123 (38), S. 9490 - 9491 (2001)
Single-step determination of protein substructures using dipolar couplings: Aid to structural genomics. Journal of the American Chemical Society 278.
Zeitschriftenartikel
122 (15), S. 3791 - 3792 (2000)
Prediction of sterically induced alignment in a dilute liquid crystalline phase: Aid to protein structure determination by NMR. Journal of the American ChemicaL Society 279.
Zeitschriftenartikel
15 (4), S. 331 - 334 (1999)
Robust refocusing of 13C magnetization in multidimensional NMR experiments by adiabatic fast passage pulses. Journal of Biomolecular NMR 280.
Zeitschriftenartikel
38 (41), S. 13692 - 13698 (1999)
Structure of the active domain of the herpes simplex virus protein ICP47 in water/sodium dodecyl sulfate solution determined by nuclear magnetic resonance spectroscopy. Biochemistry