Katrin Weise
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Katrin Weise has a total of 30 co-authors. Here are the top co-authors by number of shared publications:
- Roland Winter
Physical Chemistry I, Biophysical Chemistry, Faculty of Chemistry and Chemical Biology, TU Dortmund University, Dortmund, Germany
8 shared publications Shobhna Kapoor
Chemical Biology, TU Dortmund University, Dortmund, Germany; Department of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany
4 shared publications- Herbert Waldmann
Department of Chemical Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
3 shared publications Simone Möbitz
Physical Chemistry I - Biophysical Chemistry, TU Dortmund University, Dortmund, Germany
3 shared publications- Alfred Wittinghofer
Structural Biology Group, Max Planck Institute of Molecular Physiology, Dortmund, Germany
2 shared publications Benjamin Sperlich
Physical Chemistry I - Biophysical Chemistry, TU Dortmund University, Dortmund, Germany
2 shared publications
Latest Publications
- 1 July 2016
- Published by Elsevier in Biophysical Journal
- Vol. 111 (1) , 113-122
Regulation of K-Ras4B Membrane Binding by Calmodulin
- 1 July 2016
- Published by Elsevier in Biophysical Journal
- Vol. 111 (1) , 113-122
Regulation of K-Ras4B Membrane Binding by Calmodulin
- 1 October 2015
- Published by Elsevier in Biophysical Journal
- Vol. 109 (8) , 1619-1629
Effect of the N-Terminal Helix and Nucleotide Loading on the Membrane and Effector Binding of Arl2/3
- 1 October 2015
- Published by Elsevier in Biophysical Journal
- Vol. 109 (8) , 1619-1629
Effect of the N-Terminal Helix and Nucleotide Loading on the Membrane and Effector Binding of Arl2/3
- 12 February 2015
- Published by Royal Society of Chemistry (RSC) in Physical Chemistry Chemical Physics
- Vol. 17 (11) , 7507-7513
Exploring the structure and phase behavior of plasma membrane vesicles under extreme environmental conditions
A protocol was developed to generate GPMVs showing phase separation under ambient conditions and theirp,T-dependent phase behavior was studied.
- 12 February 2015
- Published by Royal Society of Chemistry (RSC) in Physical Chemistry Chemical Physics
- Vol. 17 (11) , 7507-7513
Exploring the structure and phase behavior of plasma membrane vesicles under extreme environmental conditions
A protocol was developed to generate GPMVs showing phase separation under ambient conditions and theirp,T-dependent phase behavior was studied.
- 1 January 2015
- Published by Elsevier in Biophysical Journal
- Vol. 108 (2) , 381a
The Difference in Arl2 and Arl3 Membrane Binding and Localization
- 1 January 2015
- Published by Elsevier in Biophysical Journal
- Vol. 108 (2) , 381a
The Difference in Arl2 and Arl3 Membrane Binding and Localization
- 1 January 2015
- Published by Elsevier in Biophysical Journal
- Vol. 108 (2) , 381a
Regulation of K-Ras Membrane Association: Calmodulin Versus PDEδ
- 1 January 2015
- Published by Elsevier in Biophysical Journal
- Vol. 108 (2) , 381a
Regulation of K-Ras Membrane Association: Calmodulin Versus PDEδ
- 1 December 2011
- Published by Wiley in Angewandte Chemie
- Vol. 124 (3) , 703-707
Cross‐Amyloid Interaction of Aβ and IAPP at Lipid Membranes
- 1 December 2011
- Published by Wiley in Angewandte Chemie
- Vol. 124 (3) , 703-707
Cross‐Amyloid Interaction of Aβ and IAPP at Lipid Membranes
- 1 February 2011
- Published by Elsevier in Biophysical Journal
- Vol. 100 (3) , 89a
Membrane-Mediated Induction and Sorting of K-Ras Microdomain Signaling Platforms
- 1 February 2011
- Published by Elsevier in Biophysical Journal
- Vol. 100 (3) , 89a
Membrane-Mediated Induction and Sorting of K-Ras Microdomain Signaling Platforms
- 7 June 2010
- Published by Wiley in ChemBioChem
- Vol. 11 (9) , 1280-1290
Interaction of hIAPP with Model Raft Membranes and Pancreatic β‐Cells: Cytotoxicity of hIAPP Oligomers
Type II diabetes mellitus (T2DM) is associated with β‐cell failure, which correlates with the formation of pancreatic islet amyloid deposits. The human islet amyloid polypeptide (hIAPP) is the major component of islet amyloid and undergoes structural changes followed by self‐association and pathological tissue deposition during aggregation in T2DM. There is clear evidence that the aggregation process is accelerated in the presence of particular lipid membranes. Whereas hIAPP aggregation has been extensively studied in homogeneous model membrane systems, especially negatively charged lipid bilayers, information on the interaction of hIAPP with heterogeneous model raft membranes has been missing until now. In the present study, we focus on the principles of aggregation and amyloid formation of hIAPP in the presence of model raft membranes. Time‐lapse tapping mode AFM and confocal fluorescence microscopy experiments followed membrane permeabilization and localization of hIAPP in the raft membrane. Together with the ThT and WST‐1 assay, the data revealed elevated cytotoxicity of hIAPP oligomers on INS‐1E cells.
- 7 June 2010
- Published by Wiley in ChemBioChem
- Vol. 11 (9) , 1280-1290
Interaction of hIAPP with Model Raft Membranes and Pancreatic β‐Cells: Cytotoxicity of hIAPP Oligomers
Type II diabetes mellitus (T2DM) is associated with β‐cell failure, which correlates with the formation of pancreatic islet amyloid deposits. The human islet amyloid polypeptide (hIAPP) is the major component of islet amyloid and undergoes structural changes followed by self‐association and pathological tissue deposition during aggregation in T2DM. There is clear evidence that the aggregation process is accelerated in the presence of particular lipid membranes. Whereas hIAPP aggregation has been extensively studied in homogeneous model membrane systems, especially negatively charged lipid bilayers, information on the interaction of hIAPP with heterogeneous model raft membranes has been missing until now. In the present study, we focus on the principles of aggregation and amyloid formation of hIAPP in the presence of model raft membranes. Time‐lapse tapping mode AFM and confocal fluorescence microscopy experiments followed membrane permeabilization and localization of hIAPP in the raft membrane. Together with the ThT and WST‐1 assay, the data revealed elevated cytotoxicity of hIAPP oligomers on INS‐1E cells.