Scientific cooperation between Italy and Israel: A perspective looking to the future

Mario Pagliaro

Affiliation: Istituto per lo Studio dei Materiali Nanostrutturati, Palermo, Italy

DOI: 10.17160/josha.4.2.294

From renewable energy through neuroscience, from chemistry to nanotechnology, the scientific cooperation between Italy and Israel touches many fields and involves hundreds of scholars and students in both countries. We identify the main research policy factors that led to this successful outcome, and those that might drive forthcoming cooperation between these two Mediterranean countries whose science linkages have a long and significant history.


Characterization of the AZF region of the Y chromosome in Native American haplogroup Q

Evguenia Alechine, Werner Schempp, Daniel Corach

Affiliation: University of Buenos Aires

DOI: 10.17160/josha.3.4.219

The Y chromosome is a genomic niche for genes involved in male gamete production. The existence of an azoospermia factor (AZF) in its long arm is a key genetic determinant for spermatogenesis since its deletion is associated with infertility. Deletions in the AZFc region are the most frequent known genetic cause of male infertility. This region contains eight gene families involved in spermatogenesis, including Deleted in Azoospermia (DAZ) and the Chromodomain Protein Y (CDY) genes. AZFc displays significant variation across the male population; nonetheless, the phenotypical consequences of some of these variants remain unclear. Many Y-chromosome geographically differentiated haplogroups have been defined in the human population. However, the information available on the Y chromosome sequence in GenBank belongs only to the European haplogroup R. Recent studies have shown that high mutation rates have driven extensive structural polymorphism among human Y chromosomes.


Assembly and disassembly of Rad51 filaments on single-stranded DNA: A novel assay to study the dynamics of protein-ssDNA interactions at the single-molecule level

Mariella Franker

DOI: 10.17160/josha.3.3.198

Eukaryotic recombinase protein Rad51 is the key player in homologous recombination, an essential DNA repair mechanism used for the repair of double-strand breaks. Double-strand breaks can lead to chromosome fragmentation and are particularly hazardous during and shortly after DNA replication. The mechanism of homologous recombination is highly conserved between species and recombinase proteins are expressed in a wide range of prokaryotic and eukaryotic cells. The primary event in homologous recombination is the formation of a helical nucleoprotein filament on single- stranded DNA overhangs around double-strand breaks. The nucleoprotein filament mediates all subsequent steps of homologous recombination and is capable of performing strand exchange reactions unassisted in vitro. Dynamic assembly and disassembly interactions between the nucleoprotein filament and its DNA substrate are essential for strand exchange.


Homologous recombination: Single-molecule experiments and their lessons for the in vivo situation

Mariella Franker

DOI: 10.17160/josha.3.3.197

Homologous recombination is an essential DNA repair mechanism in both prokaryotes and eukaryotes. It especially plays an important role in the repair of broken or stalled replication forks and is vital for proper chromosome segregation and immunoglobulin diversity. The main event in homologous recombination is the formation of a nucleoprotein filament by RecA-like proteins. Assembly of this filament is the rate-limiting step in recombination and it mediates subsequent stages of repair. Single-molecule experiments have given great insights into the physical mechanism and function of the nucleoprotein filament. In vivo, however, many recombination mediators are involved in the processes and various complex pathways are activated. INSTITUTION: VU University Amsterdam, Faculty of Sciences, Department of Physics and Astronomy, Physics of Living Systems


Bioinformatic Studies on Buffalo Prolactin Derived Anti-Angiogenic Peptide

Pulak P. Kumar, Pratishtha Singh

Affiliation: Student

DOI: 10.17160/josha.3.3.193

A 14-amino acid sequence within the buffalo prolactin (buPRL) protein has been identified by BLAST search as similar to that of somatostatin, the gold standard for determining anti-angiogenic activity. A synthetic peptide with the same sequence has been shown to exhibit powerful anti-angiogenic activity, possibly by functioning as a kallikrein-kinin system (KKS) antagonist. In order to further study this peptide’s anti-angiogenic nature, bioinformatics tools were used to analyze its interaction with the bradykinin B1 receptor, which is a component of the KKS. Molecular docking studies were conducted in silico using structures of bradykinin B1 receptor obtained by homology modeling using SWISS-MODEL via the EXPASY web server, as well as a structure of the synthetic peptide that was modeled by the PEP-FOLD de novo modeling server.


IMBS Winter School, Freiburg September 2016 - January 2017

Christoph Borner

DOI: 10.17160/josha.3.2.117

The University of Freiburg offers The Winter School in Biomedical Sciences, which is a 5 months program. The students will receive a Diploma of Advanced Studies in Biomedical Sciences (DAS) upon successfully completing the program, consisting of 30 Credit Points in the European Credit Transfer System (ECTS). This international program is designed as an intensive time of studies and research with a specific and practical training that qualifies for success in academia or the private sector. The modules focus on the following topics: Pharmacology and Toxicology, Materials and Microsystems, Molecular Medicine, Immunology, Pathology, Molecular Oncology, Genetics of Disease and Cancer, Molecular and Cellular Biology, Statistical Bioinformatics and Bioethics. Participants are encouraged to choose a personal research project which involves experimental work, data analysis and a scientific research publication.


IMBS Class 2017-19 Application Now Open

Evguenia Alechine, Christoph Borner, Marta Mollerach, Cristina Arranz et al.

Affiliation: University of Buenos Aires

DOI: 10.17160/josha.3.2.109

The International Master in Biomedical Sciences (IMBS) is pleased to announce that the application for the class 2017-2019 is now open. The IMBS program was established in 2008 as a joint program between the School of Medicine of Albert-Ludwigs-University of Freiburg (ALU), Germany, and the Schools of Medicine and Pharmacy and Biochemistry of the University of Buenos Aires (UBA), Argentina. The aim of this program is to train prospective researchers in scientific knowledge and state-of-the-art experimental experience in current and emerging biomedical research areas with a focus on translational research and development. It is also meant to foster teaching and research cooperation between the two Universities and to contribute to the cultural exchange on the master, PhD, and academic levels.


International Conference PHILOSOPHY AND CANCER (IHPST Paris) April 28,2016

Thomas Pradeu , Lucie Laplane

DOI: 10.17160/josha.3.2.106

International Conference PHILOSOPHY AND CANCER APRIL 28TH, 2016 Institute for the History and Philosophy of Science and Technology (IHPST) 13 rue du Four 75006 Paris Second Floor, conference room 9:30 – 18:00 Organized by Lucie Laplane (CNRS IHPST & UMR 1170) and Thomas Pradeu (CNRS & University of Bordeaux). Funded by IHPST, University Paris I Panthéon-Sorbonne (BQR), and University of Bordeaux (IDEX Chair Thomas Pradeu) This timely and important international conference on Philosophy and Cancer addresses novel concepts of understanding cancer and cancer treatment. Stimulating communication and interaction between scientists, doctors and philosophers should contribute to identify priorities and innovative concepts for further research. In the attached pdf you will find the program and the abstracts of all contributions.


Brief history of the German-Argentine Academic and Scientific Cooperation and the Future of Science

Ruben Villaverde

DOI: 10.17160/josha.3.1.95

In this article the history of German-Argentine collaboration is discussed as well as implications for the future of science in general. Rubén Alejandro Villaverde is the Founding President of the Centro de Observaciones Astronómicas de Mar del Plata, COAM, where he has pursued astronomical research for more than 20 years. His research encompasses various astronomical topics such as black holes, white holes and the supersymetrical universum as well as philosophical concepts, the“Filosofía Cuántica Comparativa” which combines traditional philosophy and quantum physics. Villaverde has contributed to more than 700 Conferences and Seminars at the Universidad Nacional de Mar Plata and the Universidad de Belgrano in Buenos Aires, Argentina.


The NMR View of Proteins

Kurt Wüthrich

DOI: 10.17160/josha.2.7.84

Nobel Prize laureate Kurt Wüthrich is the Cecil H. and Ida M. Green Professor of Structural Biology at The Scripps Research Institute, La Jolla, CA, USA, and Professor of Biophysics at the ETH Zürich, Zürich, Switzerland. He also directs research groups at the Universidad Federal do Rio de Janeiro in Brazil and at the iHuman Institute of ShanghaiTech University in China. His research interests are in molecular structural biology and structural genomics. His specialty is nuclear magnetic resonance (NMR) spectroscopy with biological macromolecules, where he contributed the NMR method of three-dimensional structure determination of proteins and nucleic acids in solution. The Wüthrich groups have determined a large number of macromolecular NMR structures, including the immunosuppression system cyclophilin A–cyclosporin A, the homeodomain–operator DNA transcriptional regulatory system, and prion proteins from humans, cattle and a variety of other species.