Ludmilla Morozova-Roche - Professor

Ordered protein aggregation known as amyloid formation has recently emerged as a universal phenomenon due to extensive research in protein folding and amyloid diseases. The amyloid is viewed as a generic structure characterized by cross-ß-sheet formation in its core, which implies that any polypeptide can adopt this conformation under amyloid-prone conditions. Amyloid deposits are involved in a wide range of human pathologies, including Alzheimer's and Parkinson's diseases, diabetes mellitus, systemic amyloidoses and others.

The amyloids represent also a new challenge to the industries which rely on proteinaceous products such as biopharmaceuticals. The potentially hazardous properties of amyloids demand the highest attention and in depth analysis in order to provide safe and sure products. Some other properties of amyloids, such as their remarkable physical stability, can be applied in nanotechnology for fabrication of novel nano-sized structures with controlled parameters. The cytotoxicity of proteinaceous complexes can also be used as a two edged sword, depending on the conditions either killing normal cells or inducing death of unwanted tumor. Our research interests are focused on the studies of the molecular and cellular mechanisms of amyloid formation of disease-related and de novo designed proteins. Specifically, we address the following questions:

1. Structural characterization of amyloid assemblies with particular focus on the early events in fibrillation process. Inhibition and reversal of amyloid formation. A state of the art atomic force microscopy (AFM), a range of biophysical and biochemical techniques are applied.
2. Revealing molecular and cellular mechanisms of amyloid toxicity, which involves identification of the toxic amyloid species and determination how they cause cell damage and death. Analysis of the apoptotic activity of proteinaceous complexes towards tumor cells.
3. Studies of ex vivo amyloids and evaluation of autoimmune responses to amyloids in biological fluids of patients with Parkinson's and Alzheimer's diseases.
4. Exploring amyloids as novel nanobiomaterials for nanobiotechnological applications.

The research is multidisciplinary involving the interface of structural biology, protein sciences, cell biology, immunology and neurobiological sciences.

Post-doctoral scientists, PhD students and project students are welcome to contact us via mail or in the laboratory. All letters will be answered promptly.

Popular description of our current research

Group:
Chao Wang
Alexei Klechikov

Publications

Author

Title

Year sorteringsordning

Fulltext

Clementi, Emily A.
Wilhelm, Kristina R.
Schleucher, Juergen; et al.

A Complex of Equine Lysozyme and Oleic Acid with Bactericidal Activity against Streptococcus pneumoniae
PLoS ONE, 8(11): Article Number: UNSP e80649-

2013

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Eremenko, Ekaterina
Ben-Zvi, Anat
Morozova-Roche, Ludmilla A.; et al.

Aggregation of Human S100A8 and S100A9 Amyloidogenic Proteins Perturbs Proteostasis in a Yeast Model
PLoS ONE, 8(3): e58218-

2013

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Xu, Weixin
Zhang, Ce
Morozova-Roche, Ludmilla; et al.

pH-dependent conformational ensemble and polymorphism of amyloid-β core fragment
Journal of Physical Chemistry B, 117(28): 8392-9

2013

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Gruden, Marina A.
Davidova, Tatiana V.
Yanamandra, Kiran; et al.

Nasal inoculation with a-synuclein aggregates evokes rigidity, locomotor deficits and immunity to such misfolded species as well as dopamine
Behavioural Brain Research, 243: 205-212

2013

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Vetri, Valeria
Leone, Maurizio
Morozova-Roche, Ludmilla A.; et al.

Unlocked Concanavalin A Forms Amyloid-like Fibrils from Coagulation of Long-lived "Crinkled'' Intermediates
PLoS ONE, 8(7): e68912-

2013

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Zhao, Li Na
Zhang, Tong
Zhang, Ce; et al.

S100A9 induces aggregation-prone conformation in Abeta peptides: a combined experimental and simulation study
RSC Advances, 3(46): 24081-24089

2013

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Botelho, Hugo M.
Leal, Sonia S.
Cardoso, Isabel; et al.

S100A6 Amyloid Fibril formation is Calcium-modulated and enhances Superoxide Dismutase-1 (SOD1) aggregation
Journal of Biological Chemistry, 287(50): 42233-42242

2012

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Bryan, Thomas
Luo, Xiliang
Forsgren, Lars; et al.

The robust electrochemical detection of a Parkinson's disease marker in whole blood sera
Chemical Science, 3(12): 3468-3473

2012

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Minkevich, N. I.
Rakitina, T. V.
Bogachuk, A. P.; et al.

Formation of amyloid-like fibrillar structures and destruction of fibroblasts of the Tenon's capsule in progressive myopia due to resistance of the pigment epithelium-derived factor to restricted proteolysis
Russian journal of bioorganic chemistry, 38(6): 605-612

2012

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Gruden, Marina A.
Yanamandra, Kiran
Kucheryanu, Valery G.; et al.

Correlation between Protective Immunity to alpha-Synuclein Aggregates, Oxidative Stress and Inflammation
Neuroimmunomodulation, 19(6): 334-342

2012

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Page Editor: Ludmilla Morozova-Roche
2012-10-10

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Ludmilla Morozova-Roche

Contact Information

Umeå University
Medical Biochemistry and Biophysics
SE-901 87 Umeå, SWEDEN 

Visiting Address
KBC-building, 6th floor

Tel:  +46 90 786 5283

Fax:  +46 90 786 9795

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