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Latest Heat shock proteins Stories

2012-06-05 22:20:50

LAUSANNE, Switzerland, June 6, 2012 /PRNewswire/ -- Debiopharm Group(TM) (Debiopharm), a Swiss-based global biopharmaceutical group of companies with a focus on the development of prescription drugs that target unmet medical needs and companion diagnostics, presented results of a Phase I open-label dose-escalation study with Debio 0932, an oral Heat Shock Protein 90 (HSP90) inhibitor in clinical development as an anti-cancer agent. The study was designed to determine the...

2012-03-17 00:00:51

Additional study identifies 224 new genetic interactors for key protein in Candida albicans Scientists at the University of Toronto have found a molecular mechanism that plays a key role in the transition of Candida albicans yeast into disease-causing fungus–one of the leading causes of hospital-acquired infection. The finding highlights the importance of heat in fungal growth, and provides a new target for drug therapies to counter Candida albicans infection. Candida albicans is...

2012-02-16 06:00:00

LAUSANNE, Switzerland and LEXINGTON, Massachusetts, February 16, 2012 /PRNewswire/ -- Curis, Inc. (NASDAQ: CRIS), a drug development company seeking to develop proprietary targeted medicines for cancer treatment, and Debiopharm Group (Debiopharm), a group of companies with a focus on the development of prescription drugs that target unmet medical needs, today announced that Debiopharm has begun treating patients in a Phase Ib clinical trial of Heat Shock Protein 90 (HSP90)...

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 13:29:45

Research team with RUB involvement reports in Genes and Development The same mechanism that stabilizes the DNA in the cell nucleus is also important for the structure and function of vertebrate muscle cells. This has been established by RUB-researchers led by Prof. Dr. Wolfgang Linke (Institute of Physiology) in cooperation with American and German colleagues. An enzyme attaches a methyl group to the protein Hsp90, which then forms a complex with the muscle protein titin. When the...

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...

2011-12-02 12:41:50

New research reports on new method that reveals complete set of aberrant signaling pathways that give rise to cancers One major obstacle in the fight against cancer is that anticancer drugs often affect normal cells in addition to tumor cells, resulting in significant side effects. Yet research into development of less harmful treatments geared toward the targeting of specific cancer-causing mechanisms is hampered by lack of knowledge of the molecular pathways that drive cancers in...

2011-09-28 11:37:39

Breast cancer cells that mutate to resist drug treatment survive by establishing tiny pumps on their surface that reject the drugs as they penetrate the cell membrane — making the cancer insensitive to chemotherapy drugs even after repeated use. Researchers have found a new way to break that resistance and shut off the pumps by genetically altering those breast cancer cells to forcibly activate a heat-shock protein called Hsp27. This protein regulates several others, including the...

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...

2011-08-23 21:33:41

New Findings Could Have Important Implications for Current Cancer Treatments In a joint research effort with researchers at St. Jude Children´s Research Hospital, and with help from scientists at The University of Pennsylvania, The University of Minnesota, and the National Institutes of Health, investigators from the Florida campus of The Scripps Research Institute have defined a specific protein complex that allows cells to rid themselves of damaged mitochondria, which are the energy...