A5074839515- Heat shock proteins research
- Protein Structure and Dynamics
- Enzyme Structure and Function
- Monoclonal and Polyclonal Antibodies Research
- Toxin Mechanisms and Immunotoxins
- Endoplasmic Reticulum Stress and Disease
- thermodynamics and calorimetric analyses
- Glycosylation and Glycoproteins Research
- ATP Synthase and ATPases Research
- Connexins and lens biology
- Protein purification and stability
- Signaling Pathways in Disease
- Cancer-related Molecular Pathways
- Galectins and Cancer Biology
- Amyloidosis: Diagnosis, Treatment, Outcomes
- RNA and protein synthesis mechanisms
- Computational Drug Discovery Methods
- Plant biochemistry and biosynthesis
- Genetics, Aging, and Longevity in Model Organisms
- Mitochondrial Function and Pathology
- Viral Infectious Diseases and Gene Expression in Insects
- Radiomics and Machine Learning in Medical Imaging
- Biochemical effects in animals
- Fungal and yeast genetics research
- Transgenic Plants and Applications
Technical University of Munich
2016-2025
Center for Integrated Protein Science Munich
2014-2024
Ashland (United States)
2023-2024
University of Illinois Chicago
2023-2024
Council of Science Editors
2022-2024
Cezanne (Italy)
2019-2024
Robert Koch Institute
2013-2024
Walter de Gruyter (Germany)
2013-2024
National Agricultural Library
2024
Baidu (China)
2024
Small heat shock proteins (sHsp) with a molecular mass of 15-30 kDa are ubiquitous and conserved. Up to now their function has remained enigmatic. Increased expression under conditions protective effect on cell viability at elevated temperatures suggest that they may have in the formation or maintenance native conformation cytosolic proteins. To test this hypothesis we studied influence murine Hsp25, human Hsp27, bovine alpha-B-crystallin (an eye lens protein homologous sHsps) unfolding...
The small heat shock proteins (sHsps) from human (Hsp27) and mouse (Hsp25) form large oligomers which can act as molecular chaperones in vitro protect cells oxidative stress when overexpressed. In addition, mammalian sHsps are rapidly phosphorylated by MAPKAP kinase 2/3 at two or three serine residues response to various extracellular stresses. Here we analyze the effect of sHsp phosphorylation on its quaternary structure, chaperone function, protection against stress. We show that...
The molecular chaperone GroE facilitates correct protein folding in vivo and vitro. mode of action was investigated by using refolding citrate synthase as a model system. In vitro denaturation this dimeric is almost irreversible, since the polypeptide chains aggregate rapidly, shown directly strong, concentration-dependent increase light scattering. yields reactivated were strongly increased upon addition MgATP. inhibits aggregation reactions that compete with folding, indicated specific...
Molecular chaperones are a set of conserved protein families that share the remarkable ability to recognize and selectively bind nonnative proteins under physiological stress conditions. Thus, they prevent irreversible aggregation reactions keep on productive folding pathway. Evidence suggests cell has developed several functionally distinct chaperone support folding. The importance molecular conditions is highlighted by finding all major heat shock (Hsp104, Hsp90, Hsp70, Hsp60/GroEL, small...
The Hsp90 heat shock protein of eukaryotic cells regulates the activity proteins involved in signal transduction pathways and may direct intracellular folding general. performs at least part its function a complex with specific set partner that include members prolyl isomerase family. properties major components were examined through use vitro assays. Two components, FKBP52 p23, functioned as mechanistically distinct molecular chaperones. These results suggest existence super-chaperone cytosol cells.