M. Zweckstetter

Publication List Details

Period

2002 - 2009

Number

79

Co-Authors

Structure of the human voltage-dependent anion channel (2008)

Bayrhuber, M., Meins, T., Habeck, M., Becker, S., Giller, K., Villinger, S., ...

The voltage-dependent anion channel (VDAC), also known as mitochondrial porin, is the most abundant protein in the mitochondrial outer membrane (MOM). VDAC is the channel known to guide the metabolic...

The "jaws" of the tau-microtubule interaction (2007)

Mukrasch, M. D., Von Bergen, M., Biernat, J., Fischer, D., Griesinger, C., Mandelkow, E., ...

Tau is the major microtubule-associated protein in neuronal axons. It aggregates into "neurofibrillary tangles" during the course of Alzheimer disease. Binding to microtubules and microtubule...

Highly populated turn conformations in natively unfolded tau protein identified from residual dipolar couplings and molecular simulation (2007)

Mukrasch, M. D., Markwick, P., Biernat, J., Von Bergen, M., Bernado, P., Griesinger, C., ...

Tau, a natively unstructured protein that regulates the organization of neuronal microtubules, is also found in high concentrations in neurofibrillary tangles of Alzheimer's disease and other...

Structural and microtubule binding properties of tau mutants of frontotemporal dementias (2007)

Fischer, D., Mukrasch, M. D., Von Bergen, M., Klos-Witkowska, A., Biernat, J., Griesinger, C., ...

Several mutations in the gene encoding the microtubule-associated protein tau are responsible for the formation of neurofibrillary inclusions in frontotemporal dementia with Parkinsonism linked to...

NMR in the SPINE Structural Proteomics project (2006)

Ab, E., Atkinson, A., Banci, L., Bertini, I., Ciofi-Baffoni, S., Brunner, Konrad, ...

This paper describes the developments, role and contributions of the NMR spectroscopy groups in the Structural Proteomics In Europe (SPINE) consortium. Focusing on the development of high-throughput...

Release of long-range tertiary interactions potentiates aggregation of natively unstructured α-synuclein (2005)

Bertoncini, C. W., Jung, Y. S., Fernandez, C. O., Hoyer, W., Griesinger, C., Jovin, T. M., ...

In idiopathic Parkinson’s disease, intracytoplasmic neuronal inclusions (Lewy bodies) containing aggregates of the protein α-synuclein (αS) are deposited in the pigmented nuclei of the brainstem....

Structural characterization of copper(II) binding to α-Synuclein: Insights into the bioinorganic chemistry of Parkinson's disease (2005)

Rasia, R. M., Bertoncini, C. W., Marsh, D., Hoyer, W., Cherny, D. I., Zweckstetter, M., ...

The aggregation of α -synuclein (AS) is characteristic of Parkinson’s disease and other neurodegenerative synucleinopathies. We demonstrate here that Cu(II) ions are effective in accelerating AS...

Familial mutants of α-synuclein with increased neurotoxicity have a destabilized conformation (2005)

Bertoncini, C. W., Fernandez, C. O., Griesinger, C., Jovin, T. M., Zweckstetter, M.

A30P and A53T mutations of the presynaptic protein α-synuclein are associated with familial forms of Parkinson’s disease. NMR spectroscopy demonstrates that Parkinsonism-linked mutations greatly...

NMR of α-synuclein-polyamine complexes elucidates the mechanism and kinetics of induced aggregation (2004)

Fernandez, C. O., Hoyer, W., Zweckstetter, M., Jares-Erijman, E. A., Subramaniam, V., Griesinger, C., ...

The aggregation of alpha-synuclein is characteristic of Parkinson’s disease (PD) and other neurodegenerative synucleinopathies. The 140-aa protein is natively unstructured; thus, ligands binding to...

Evaluation of uncertainty in alignment tensors obtained from dipolar couplings (2002)

Zweckstetter, M., Bax, A.

Residual dipolar couplings and their corresponding alignment tensors are useful for structural analysis of macromolecules. The error in an alignment tensor, derived from residual dipolar couplings on...

Structure of the IGF-binding domain of the insulin-like growth factor-binding protein-5 (IGFBP-5): implications for IGF and IGF-I receptor interactions.

Kalus, W, Zweckstetter, M, Renner, C, Sanchez, Y, Georgescu, J, Grol, M, ...

Binding proteins for insulin-like growth factors (IGFs) IGF-I and IGF-II, known as IGFBPs, control the distribution, function and activity of IGFs in various cell tissues and body fluids....

Structure of the IGF-binding domain of the insulin-like growth factor-binding protein-5 (IGFBP-5): implications for IGF and IGF-I receptor interactions.

Kalus, W, Zweckstetter, M, Renner, C, Sanchez, Y, Georgescu, J, Grol, M, ...

Binding proteins for insulin-like growth factors (IGFs) IGF-I and IGF-II, known as IGFBPs, control the distribution, function and activity of IGFs in various cell tissues and body fluids....