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Good Night, Sleep Right — In a new publication in the journal Pediatrics, Dr.  Karen Bonuck discusses her finding that children with disrupted sleep patterns through five years of age were more likely to have special education needs (SEN) at eight years old.  Dr. Bonuck found that a prior history of sleep disordered breathing (SDB), coupled with behavioral sleep problems, were risk factors for SEN.  This extends her previous work, also published in Pediatrics earlier in 2012, which found children with SDB - which includes snoring, apnea, and open-mouth breathing - were more likely to have behavioral difficulties.  These reports contribute to the growing knowledge of the serious effects that sleep disorders can have on cognitive and emotional functions in children.  Dr. Bonuck is professor of family and social medicine and of obstetrics & gynecology and women’s health.

Wednesday, July 31, 2013
 

Stay Connected — The September 2012 issue of ICTR Connections is now available for viewing via the Einstein-Montefiore Institute for Clinical & Translational Research website.

Wednesday, July 31, 2013
 

Heavy Reality  In research published in the journal, Cancer, Dr. Joseph Sparano, found that just being overweight increases the risk of breast cancer recurrence. Dr. Sparano noted that the link between obesity and cancer remains regardless of treatment and that reducing weight may reduce risk of recurrence.

Wednesday, July 31, 2013
 

Growth Charting  The National Cancer Institute has awarded $1.7 million over five years to Dr. Steven Libutti and colleagues to support their investigation of tissue-specific cancer development. Dysfunctional tumor suppressor genes are known to cause cancer in some tissues but not others. Dr. Libutti’s team will intentionally disrupt the tumor suppressor gene Men1 in several tissue types and observe whether or not tumors result. By comparing the components of cells that develop tumors with the components of cells that don’t, they may discover unknown contributors to tumor growth, which may help identify potential targets for future intervention. Dr Libutti is associate director for clinical services at the Albert Einstein Cancer Center, vice chair of the department of surgery, and professor in the departments of surgery and genetics.

Wednesday, July 31, 2013
 

Antibody Therapeutics  Monoclonal antibodies (mAbs) that protect against toxins, or protective mAbs, have proven to be useful agents for treating infectious diseases caused by toxins in one’s system. Paradoxically, most of the antibodies that are generated to fight toxins are non-protective in nature. In seeking greater understanding of this role about which very little is known, researchers led by graduate student Siu-Kei Chow and his mentor Dr. Arturo Casadevall have shown that, compared to protective mAb treatment alone, a combination of protective and non-protective mAbs against anthrax toxin protective antigen (PA) leads to synergistic protection in mice challenged with anthrax toxin. The enhanced defense is driven by the formation of PA complexes that contain both types of antibodies, which results from the ability of each arm of the mAbs to bind to different targets. Through the demonstration of the protective potential of these mAbs, researchers may have promising new possibilities for antibody-based therapeutic study. The findings appear in the April 17 issue of Cell Host & Microbe. Dr. Casadevall is professor and chair of and microbiology & Immunology, as well as professor of medicine (infectious diseases). He also holds the Leo and Julia Forchheimer Chair in Microbiology & Immunology and is director of the Center for Immunological Sciences.

Wednesday, July 31, 2013
 

HIV-Susceptible Mice  In a May 2013 issue of PLoS ONE, Dr. Harris Goldstein and graduate student Kieran Seay report their development of a genetically engineered mouse that can be used to study HIV. Since a critical step in testing new drugs is to demonstrate effectiveness in mice; the researchers first had to overcome a critical obstacle: Mice cannot be infected by the virus. HIV infects by binding to and entering molecules via the proteins CD4 and CCR5, which are present on the cell surface of human immune cells. The virus then utilizes an internal protein, cyclin T1, to make copies of itself. The researchers were able to genetically engineer a mouse with the human copy of these critical genes, rendering the new mouse model susceptible to HIV infection. This “humanized” mouse model therefore provides a new way to conduct essential preclinical testing of HIV therapies to accelerate discovery of novel treatments. Dr. Goldstein is professor of pediatrics and of microbiology & immunology. He also is the Charles Michael Chair in Autoimmune Diseases and director of Einstein’s Center for AIDS Research.

Wednesday, July 31, 2013
 

HIV Intervention  Dr. Betsy Herold and her colleagues have been awarded $12 million over five years from the National Institute of Allergy and Infectious Diseases for their novel approach to HIV prevention. Effective HIV preventatives have remained elusive due to difficulties with adherence and biological differences in how drugs are distributed to sites of HIV acquisition. Dr. Herold has proposed that drug development begin with extensive assessments of these factor using animal models and clinical samples. The investigators will then apply their findings to further optimize an intra-vaginal ring that delivers a more potent combination of drugs than current gel products and ensures appropriate dosage and targeting of tissues, while also overcoming issues of patient adherence to strict dosing regimens. Dr. Herold is professor of pediatrics (infectious diseases), of microbiology & immunology and of obstetrics & gynecology and women’s health. Co-investigators at Einstein include Dr. Marla Keller and Pedro Mesquita. The Einstein team will work with collaborators at other institutions, including the University of Utah, Northwestern University, Johns Hopkins, the Centers for Disease Control and Prevention, University of Washington, and Kenyatta National Hospital in Nairobi, Kenya.

Wednesday, July 31, 2013
 

All in the Family  In the May 7, 2013 issue of the journal StructureDr. Andras Fiser , Dr. Steve Almo and former graduate student Dr. Rotem Rubenstein describe the brotherhood algorithm, a new computational method that groups proteins into functionally related families.  Based on the principle that “if my brother is your brother then we must also be brothers,” the method identifies and clusters families of proteins by shared similar proteins between any two candidates.  Using this method, they identified and, through experiments,  subsequently verified new members of the nectin/nectin-like protein family, which have key roles in mediating the immune response. The brotherhood algorithm can be used to discover new functional relationships among cell surface-attached immunoglobulin proteins; these proteins are common therapeutic targets for developing treatments for infectious diseases, cancer, and autoimmune diseases.  Dr. Fiser is professor of systems and computation biology and of biochemistry; Dr. Almo is professor of biochemistry and of physiology & biophysics

Wednesday, July 31, 2013
 

Mutant G Proteins and Human Disease  This week's New England Journal of Medicine (NEJM) published an editorial on G proteins written by Dr. Allen M. Spiegel, Einstein's Marilyn and Stanley M. Katz Dean. Members of the G protein family couple activation of a class of transmembrane receptors termed GPCRs to signaling pathways that regulate key cellular processes. GPCRs are activated by a diverse array of extracellular signals including hormones, neurotransmitters and photons of light. Dr. Spiegel's editorial accompanied the publication of a research paper and letter reporting that mutations that inactivate or activate a particular G protein cause hypercalcemic and hypocalcemic disorders, respectively. Previous studies had shown that these disorders can also result from mutations in the gene encoding a GPCR activated by extracellular calcium. Dr. Spiegel noted that the present work expands the list of diseases caused by mutant G proteins beyond those originally described by his and other labs. (Subscription may be required)

Wednesday, July 31, 2013
 

Structurally Sound  In the June 4 issue of Structure, Drs. Vern Schramm, Steven Almo and Antti Haapalainen report their use of crystallography – a method used to determine molecular structures by examining them in crystalline form – to identify novel inhibitors of a key enzyme of the bacteria Salmonella enterica.  This enzyme, called MTAN (MTA/SAH nucleosidase), is responsible for metabolism of the amino acid methionine and is only expressed by bacteria, making it an ideal target for developing antibiotics.  Drs. Schramm and Almo analyzed the crystal structure of MTAN and used this structural information to develop rational design of inhibitors that bind to the enzyme very strongly, identifying new possible antibiotics against S. enterica as well as a method that can be used to develop inhibitors of other bacterial targets. Dr. Schramm is professor and chair of biochemistry and the Ruth Merns Chair in Biochemistry; Dr. Almo is professor of biochemistry and holds the Wollowick Family Foundation Chair in Multiple Sclerosis and Immunology; Dr. Haapalainen is a postdoctoral fellow in the Schramm lab.

Wednesday, July 31, 2013
 
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