Marianna Tatarek‐Nossol

发表

Selectively N-methylated soluble IAPP mimics as potent IAPP receptor agonists and nanomolar inhibitors of cytotoxic self-assembly of both IAPP and Aβ40.

G. Rammes, B. Göke, M. Storr, 2013, Angewandte Chemie.

Peptide Inhibitors of the amyloidogenesis of IAPP: verification of the hairpin‐binding geometry hypothesis

N. Andersen, A. Kapurniotu, Marianna Tatarek‐Nossol, 2016, FEBS letters.

An amphipathic helix in Brl1 is required for nuclear pore complex biogenesis in S. cerevisiae

E. Dultz, O. Medalia, E. Noor, 2022, eLife.

New motifs in Ndc1 mediating interaction with the Nup84 complex and nuclear membranes

W. Antonin, B. Brügger, Johannes Schwarz, 2022, bioRxiv.

Design of a mimic of nonamyloidogenic and bioactive human islet amyloid polypeptide (IAPP) as nanomolar affinity inhibitor of IAPP cytotoxic fibrillogenesis

A. Kapurniotu, Aphrodite Kapurniotu, Li-Mei Yan, 2006, Proceedings of the National Academy of Sciences of the United States of America.

IAPP mimic blocks Abeta cytotoxic self-assembly: cross-suppression of amyloid toxicity of Abeta and IAPP suggests a molecular link between Alzheimer's disease and type II diabetes.

A. Kapurniotu, E. Andreetto, Li-mei Yan, 2007, Angewandte Chemie.

Inhibition of hIAPP amyloid-fibril formation and apoptotic cell death by a designed hIAPP amyloid- core-containing hexapeptide.

G. Westermark, A. Kapurniotu, Aphrodite Kapurniotu, 2005, Chemistry & biology.

Development of accessible peptidic tool compounds to study the phosphatase PTP1B in intact cells.

J. Bernhagen, M. Wilmanns, M. Köhn, 2014, ACS chemical biology.

An amphipathic helix in Brl1 is required for membrane fusion during nuclear pore complex biogenesis in S. cerevisiae

E. Dultz, O. Medalia, E. Noor, 2022, bioRxiv.

Cytotoxicity of insulin within its self-assembly and amyloidogenic pathways.

H. Rehage, R. Winter, A. Kapurniotu, 2007, Journal of molecular biology.

A self-inhibitory interaction within Nup155 and membrane binding are required for nuclear pore complex formation

M. Dewor, W. Antonin, P. De Magistris, 2018, Journal of Cell Science.

Conformational Restriction via Cyclization in β-Amyloid Peptide Aβ(1-28) Leads to an Inhibitor of Aβ(1-28) Amyloidogenesis and Cytotoxicity

J. Bernhagen, A. Kapurniotu, T. Hirsch, 2003 .

Blocking inflammasome activation caused by β-amyloid peptide (Aβ) and islet amyloid polypeptide (IAPP) through an IAPP mimic.

E. Latz, C. Beyer, A. Kapurniotu, 2019, ACS chemical neuroscience.

Exploiting cross-amyloid interactions to inhibit protein aggregation but not function: nanomolar affinity inhibition of insulin aggregation by an IAPP mimic.

A. Kapurniotu, E. Andreetto, Aleksandra Velkova, 2008, Angewandte Chemie.