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Latest Chaperone Stories

2012-03-09 01:43:43

Max Planck scientists identify key player of protein folding Proteins are the molecular building blocks and machinery of cells and involved in practically all biological processes. To fulfil their tasks, they need to be folded into a complicated three-dimensional structure. Scientists from the Max Planck Institute of Biochemistry (MPIB) in Martinsried near Munich, Germany, have now analysed one of the key players of this folding process: the molecular chaperone DnaK. “The...

2012-03-02 01:17:19

Mayo Clinic researchers have gained insights into the function of a member of a family of specialized proteins called histone chaperones. Using nuclear magnetic resonance (NMR) spectroscopy and X-ray crystallography, they have determined the 3-D structure and interactions of the histone chaperone Rtt106 down to the atomic details. "The interactions we described are important for gene silencing and the DNA damage response," says senior author Georges Mer, Ph.D., a Mayo Clinic structural...

2012-01-23 22:13:55

Targeting a single protein can help fight both breast cancers and leukemias, according to two reports published online on January 23 in the Journal of Experimental Medicine (http://www.jem.org). The single protein is HSP90, which acts as a chaperone to protect other proteins in the cell. A team led by Ute Moll at the University of Göttingen in Germany found that blocking HSP90 activity rendered normally protected proteins vulnerable to attack and destruction. One of these...

2012-01-23 21:51:13

A group of researchers led by the Institute of Biotechnology and Biomedicine (IBB) and Universitat Autònoma de Barcelona (UAB) have achieved to quantify with precision the effect of protein aggregation on cell aging processes using as models the Escherichia coli bacteria and the molecule which triggers Alzheimer's disease. Scientists demonstrated that the effect can be predicted before it occurs. Protein aggregation is related to several diseases, including neurodegenerative...

2012-01-14 01:38:57

Large conformational changes without ATP consummation A special group of proteins, the so-called chaperons, helps other proteins to obtain their correct conformation. Until now scientists supposed that hydrolyzing ATP provides the energy for the large conformational changes of chaperon Hsp90. Now a research team from the Nanosystems Initiative Munich could prove that Hsp90 utilizes thermal fluctuations as the driving force for its conformational changes. The renowned journal PNAS reports...

2011-12-22 15:36:45

A research team led by biochemist Scott Garman at the University of Massachusetts Amherst has discovered a key interaction at the heart of a promising new treatment for a rare childhood metabolic disorder known as Fabry disease. The discovery will help understanding of other protein-folding disorders such as Alzheimer's, Parkinson's and Huntington's diseases, as well. Findings are featured as the cover story in the current issue of Chemistry & Biology. People born with Fabry disease...

2011-12-16 12:24:07

Access to clean water is a necessity often taken for granted. However UNICEF estimates that 900 million people across the world do not have access to safe drinking water. New research published in BioMed Central's open access journal BMC Biotechnology shows that an enteric virus-binding protein (EVBP), isolated from bacteria found in activated sludge, is able to capture viruses often present in contaminated water. One of the difficulties in measuring viral contamination in water is that...

2011-09-07 13:48:10

The protein p53 plays an essential role in the prevention of cancer by initiating the controlled death of a cell with damaged genes which is in danger to transform into a cancerous cell. The heat shock protein Hsp90, in turn, activates and stabilizes p53. Now scientists of the Technische Universität München (TUM) have discovered both the site where the two proteins interact and the interaction mechanism. The results of their work are reported in the current...

2011-09-01 15:24:41

Researchers have found that a protein variation linked by some genetic studies to Alzheimer's disease is consistently present in the brains of people with Alzheimer's. In further biochemical and cell culture investigations, they have shown that this protein, known as ubiquilin-1, performs a critical Alzheimer's-related function: it "chaperones" the formation of amyloid precursor protein, a molecule whose malformation has been directly tied to Alzheimer's pathology. "What we saw here is...

2011-08-25 21:34:14

Study finds KN1 trafficking through tiny channels called plasmodesmata cannot occur without chaperonins Like all living things, plants depend for their growth and sustenance on elaborate signaling networks to maintain stem cells, cells that have an almost magical regenerative capacity. The signals sent through these networks convey an incredible diversity of instructions, which make it possible for plants to follow genetic and cellular programs regulating growth, shape, and energy...


Word of the Day
glogg
  • Scandinavian punch made of claret and aquavit with spices and raisins and orange peel and sugar.
This word comes from the Swedish 'glogg,' which is an alteration of 'glodgat,' mulled (wine).
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