November 20th 2008, 4 pm, large lecture hall at MedILS
Natural substances may interact with numerous target proteins in human cells. For the flavonoid quercetin a method has been developed which allows the identification of unknown target proteins. The target proteins that have been of particular interest to us include the cytoskeletal proteins actin and tubulin and their associated motor proteins. New inhibitors for these proteins have been identified and the effect of the inhibitors studied in various cellular test systems. Possible medical applications will be discussed.
Interaction of natural substances with cellular target proteins (prof. dr. Herwig Gutzeit, TU Dresden, Germany)
October 9th 2008, 10 am, large lecture hall at MedILS
Skeletogenesis and hematopoietic development (prof. dr. Leonardo Aguila, University of Connecticut Health Center, USA)
07.10.2008, 9 am, MedILS, large lecture hall
The phenomenon referred as «mucilage of Northern Adriatic» has been observed infrequently over the past three centuries but more recently its intensity and frequency of occurrence has increased dramatically. The phenomenon manifests itself in rapid production of enormous amounts of gelatinous matter in the water column and covering the sea surface at a scale observable from the satellite. The mucilage phenomenon has attracted attention of many scientists worldwide and research is performed by oceanographers, biologists and chemists. Current views leave no doubt on phytosynthetic production of long chain polysaccharide molecules by unicellular marine algae, as a proximal source constituting the gel network, but the basic mechanism of mucilage events is still not understood.
Studies of supramolecular organization of organic molecules in seawater into vesicles and microgels have revealed that the macroscopic phenomena, such as mucilage events are governed by biological and abiotic transformations at the micro- and nano- scales.
Discovery of AFM (Atomic Force Microscopy) has made possible the masurements of atomic forces for imaging living and non-living organic structures at molecular and sub-molecular resolution under ambient conditions.
I shall describe here how we applied AFM imaging to reveal the process of marine gel formation at the nanoscale, starting from extracellular production of polysaccharide chains by a living diatom cell, to gradual and multiple entanglement of polysaccharide molecules into the polysaccharide gel networks which reached macroscopic dimensions during the mucilage event.
Mucilage phenomenon at the nanoscale (dr. Vesna Svetličić, Institute Ruđer Bošković, Zagreb)
Why our proteins have to die so we shall live
A lecture for the general public
Aaron Ciechanover, Nobel Prize winner
Cancer and Vascular Biology Research Center, Faculty of Medicine,
Technion-Israel Institute of Technology, Haifa, Israel
Faculty of Economics, Split, Large Amphiteather, Tuesday, September 16th 2008, 6pm
Proteins are the machines that drive our body. They are responsible for all our activities such as walking, seeing, hearing, heart beeping, digestion, respiration, secretion of waste materials. Unlike the items that surround us and that we use daily, like furniture and our clothes, the body proteins are in a dynamic state, they are being destroyed and renewed all the time and in an extensive manner. We are destroying daily up to 10% of our proteins and generating new ones instead. The obvious questions are (i) why this occurs, (ii) what is the mechanism that carries out this function, (iii) what are the diseases that result if the mechanism does not work properly, and (iv) how can we cure these disease. In the lecture we shall try to shed light on these problems, and understand the value of basic research for the development of drugs to target many diseases that affect us in the Western world - cancer and neurodegenerative disorders like Alzheimer’s disease, for example. No doubt research of the system will yield practical implications to diseases of the developing world as well – infectious diseases, for example, but researchers need proper investment to explore these new venues.
Why our proteins have to die so we shall live (Aaron Ciechanover, Nobel Prize winner, Technion, Israel)
The Ubiquitin Proteolytic System: From Basic Mechanisms through Human Diseases and onto Drug Targeting (Aaron Ciechanover, Nobel Prize winner, Technion, Israel)
The Ubiquitin Proteolytic System: From Basic Mechanisms through Human Diseases and onto Drug Targeting (Aaron Ciechanover, Nobel Prize winner, Technion, Israel)
Retrograde transport of proteins across the endoplasmic reticulum membrane (Kristina Oresic, Mount Sinai School of Medicine, USA)
Retrograde transport of proteins across the endoplasmic reticulum membrane
(Kristina Oresic)
Department of Microbiology, Mount Sinai School of Medicine, New York, NY
Monday, August 18, 2008, 10-11 am.
Interaction of a-conotoxin OmIA with acetylcholine binding protein (Zoran Radic, UCSD)
“Interaction of a-conotoxin OmIA with acetylcholine binding protein”
Zoran Radic, UCSD
Skaggs School of Pharmacy, University of California San Diego
Tuesday, July 1st, 2008, 11.30 – 12.30 am
Genomic principles for feedback regulation of metabolism (dr. Nick Luscombe, European Bioinformatics Institute)
Nick Luscombe, PhD
European Bioinformatics Institute
Wellcome Trust Genome Campus
Cambridge, UK
MedILS, big lecture hall, June 17th 2008, 4 pm
Dr. Ikeda’s lecture on ubiquitin and ubiquitin like molecules in the regulation of signaling
Ubiquitin is a small molecule, so-named for its extraordinary wide distribution from yeast to man. The covalent ubiquitylation of proteins is a widespread regulatory post-translational modification, as like protein phosphorylation. Early interest in ubiquitylation centered on the role of polyubiquitin chains in targeting proteins for degradation. However, ubiquitin is now revealed to be involved in many biological functions.
MedILS, September 17th 2007