The name "Sonic hedgehog" may conjure up images of Sega's blue videogame character, tumbling across a screen and collecting gold rings, but its namesake, the human gene Sonic hedgehog, encodes a protein (SHH) whose role in the body is anything but light entertainment.
Under a microscope in Ghana, deadly pathogens look beautiful. Little squiggles of green and blue highlight the cell nuclei of trypanosomes, the protozoa responsible for African sleeping sickness. For the past two weeks, 26 West African students learned skills and techniques that will help them conduct research on these and other infectious pathogens. The courses took place June 17- June 29, 2013, at the University of Ghana, a few miles outside Accra.
Cholera is changing the human genome, according to research published in Science Translational Medicine on Wednesday. The investigators scanned the genomes of individuals living in the Ganges Delta of Bangladesh and West Bengal in India, where cholera is prevalent. ScienceNow and the New York Times report that the researchers found 305 regions of the genome with changes due to cholera, evidence that natural selection made its mark on the genes over the past 5,000 to 30,000 years.
Tiny and seemingly simple organelles can cause big problems for an organism, if they get out of control. The centrosome, composed of just two barrel-shaped centrioles and a mass of proteins in human cells, forms the microtubule organizing center that regulates cell division (cytokinesis). During cell division, two centrosomes at opposite poles of the cell work together to position the mitotic spindle. An increase in the number of centrosomes is "a hallmark of human tumors," according to Véronique Marthiens and Renata Basto at the Curie Institute in Paris who report in Nature Cell Biology on their surprising results in mice after adding extra centrosomes in the cells of the developing central nervous system (CNS).
RNA interference (RNAi) is a Nobel Prize-winning discovery first published in 1998 by Andrew Fire and Craig Mello. The potential of RNAi technology to silence genes involved in disease was apparent from the beginning, at least in theory. These theoretical RNAi therapies would switch off genes upregulated in diseased cells, such as in cancer or Huntington's disease. However, delivering RNAi treatments to deep tissues within the body posed enormous challenges until now.
A foundation created by a Slovakian-born microbiologist who helped shape a monoclonal antibody into a clinically effective tumor necrosis factor (TNF) blocker will once again award three $35,000 no-strings cash prizes to young immigrant scientists who demonstrate "exceptional" records of early career achievement in the life sciences.
The year 1953 is generally considered the year zero for molecular cell biology with the publication of Watson and Crick's celebrated Nature paper on the structure of DNA. But there was another big paper in 1953 by Yves Clermont and Charles Leblond of McGill University that appeared in the American Journal of Anatomy.
With the death from brain cancer of Senator Ted Kennedy in 2009, gliobastoma multiforme (GBM), made a brief but frightening appearance in the news. GBM is a bitter diagnosis with a poor prognosis. More than half the patients will die within one year and the five-year survival rate is approximately 5%. Why is this cancer so deadly?
Actin's role in the nucleus comes packed in its very own black box. The cell nucleus is a very small and complex place but given how much is known about actin in the cytoplasm, it can be startling to hear how little agreement there is about actin in the nucleus.
The mad cow disease, or bovine spongiform encephalopathy (BSE), outbreak that burst into the news in the United Kingdom in the late 1980s is caused by a harmful version of the prion protein. In affected cows, the misfolded prion protein results in the degeneration of the nervous system and eventual death. Alarmingly, the incidence of the human version of BSE, known as Creutzfeld-Jakob Disease (CJD), increased following the bovine epidemic, indicating that the disease could transfer from one species to another. How the misfolded version of the prion protein causes these neurodegenerative diseases is currently not understood.