Search Results for: C. Erec Stebbins

C. Erec Stebbins awarded prestigious EUREKA grant

C. Erec Stebbins, associate professor at The Rockefeller University, has been awarded an inaugural EUREKA grant from the National Institutes of Health for a project aimed at exploiting a bacteria-based “nanosyringe” as a means of delivering proteins into specific cells for therapeutic purposes. The award, which provides $200,000 a year for three years, was announced by the NIH September 3. More »

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Scientists use Nature against Nature to develop an antibiotic with reduced resistance

Scientists at Rockefeller University and Astex Pharmaceuticals have discovered a new broad range antibiotic that kills a wide range of bacteria, including drug-resistant Staphylococcus (MRSA) bacteria that do not respond to traditional drugs, in mice. The antibiotic, Epimerox, targets weaknesses in bacteria that have long been exploited by viruses that attack them, known as phage.

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Proceedings of the National Academy of Sciences USA online: December 31, 2012

Proceedings of the National Academy of Sciences USA online: December 31, 2012 Solubility-based genetic screen identifies RING finger protein 126 as an E3 ligase for activation-induced cytidine deaminase Rebecca K. Delker, Yanjiao Zhou, Alexandros Strikoudis, C. Erec Stebbins and F. … More »

Bacterial protein mimics its host to disable a key enzyme

Bacteria use all sorts of cunning to trick hosts into doing their bidding. One con in their bag of tricks: the molecular mimic. In this ruse, bacteria or their agents look for all purposes like some native molecule in a cell, but then do not behave accordingly. Working with H. pylori, the bacterium responsible for gastric ulcers and cancer, researchers have revealed one way bacteria pull this off, deciphering the structure of a piece of CagA, a bacterial protein that impersonates a human protein in order to disable a key enzyme. More »

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New protein identified in bacterial arsenal

Virulence factors evolved nearly a billion years ago as opportunistic agents injected by bacteria to hijack the machinery of infected cells. Researchers at The Rockefeller University have discovered the molecular makeup of one such factor used by Salmonella — a ubiquitin ligase — that appears to take over a key process that regulates a wide range of cellular duties, from cell-cycle progression to cell death and even communication between cells. More »

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Structure of a virulent pathogen revealed

Certain mean strains of bacteria inject virulent teams of molecules into cells that prepare the way for bacteria to invade the cells and reproduce, spreading disease. Different types of these molecules, called virulence factors, wreak havoc in cells’ basic functioning in different ways. Now, using x-ray crystallography, researchers at The Rockefeller University have revealed the structure of one such molecule that has the especially damaging effect of arresting its host cells’ division. The finding offers clues as to how this bacterial weapon works and, potentially, how to defend against it or even use it to attack cancer. More »

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Structural study of anthrax yields new antibiotic target

By describing the structure of an enzyme involved in building an essential piece of the bacterium’s cell wall, Rockefeller University researchers have found a promising new drug target for anthrax and other bacteria. More »

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A wolf in sheep’s clothing: plague bacteria reveal one of their virulence tricks

The bacteria known as Yersinia, a family of pathogens that includes the plague, kill their host cells by — among other things — inserting proteins and other virulence factors that disrupt their normal structure. New research by Rockefeller University scientists shows at the atomic, cellular and organismal level that the cause of this disruption can be attributed largely to YpkA, a virulence factor that mimics proteins found in its host. More »

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Structural study shows how bacteria select their most virulent proteins

A diverse group of bacteria all rely on the same syringe-like system to infect their hosts. Rockefeller researchers have now uncovered a structural similarity shared by many of these virulent pathogens that may help direct future antibiotic research. More »

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Protein structure suggests bacteria may be more sophisticated than we thought

Rockefeller scientists say Pseudomonas syringae, a bacterial plant pathogen, evades a plant’s immune defenses by mimicking one of the plant’s own enzymes: an E3 ubiquitin ligase that had never before been seen in bacteria. More »

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Scientists say toxins use their shape to wreak havoc on cells

Last year, Rockefeller University scientists used X-ray crystallography to determine the structure of a widespread bacterial toxin called CDT. Now, the researchers have taken an even closer look at its configuration to gain a better understanding of what makes this potential carcinogen so effective. More »

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Molecular image of genotoxin reveal how bacteria damage human DNA

The three-dimensional structure of a DNA-damaging, bacterial toxin has been visualized by scientists at Rockefeller University. The molecular image of the toxin, published in the May 27 issue of the journal Nature, shows exactly how the toxin is put together at the molecular level and damages human DNA. The structure also could help scientists to design new drugs to fight the wide variety of bacteria that use this toxin. More »

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Salmonella bacterium uses potent molecular “staples” to change structure of cells it infects

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