Chicago Ridge, IL, United States

Loyola University Chicago
Chicago Ridge, IL, United States

Loyola University Chicago is a private Jesuit university located in Chicago, Illinois. It was founded by the Roman Catholic Society of Jesus in 1870 under the name of "St. Ignatius College", and has grown to be the largest Jesuit university in the United States with a total enrollment of 15,068 and over 150,000 alumni.Loyola University has six campuses throughout the Chicago metropolitan area, and it also has a permanent overseas campus in Rome, Italy and guest programs in Beijing, China and Ho Chi Minh City, Vietnam. Loyola has twelve undergraduate, graduate, and professional schools offering 71 undergraduate degrees, 85 master's degrees, 31 doctoral degrees, and 26 graduate-level certificate programs.The main campus, the Lake Shore Campus, is located in the Rogers Park and Edgewater neighborhoods of the City of Chicago, located along the shore of Lake Michigan. Loyola University Chicago's intercollegiate sports teams, commonly called the "Loyola Ramblers", compete in National Collegiate Athletic Association Division I and the Missouri Valley Conference. As of 2013, Loyola University is still the only Division I school in the State of Illinois to win a national championship in men's basketball. Wikipedia.

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Loyola University Chicago, Marquette University and The University Of Texas System | Date: 2015-08-12

Indoline sulfonamide compounds that can inhibit DapE and/or bacterial metallo--lactamases (MBLs), such as NDM-1, are disclosed. Also disclosed are methods of treating an individual suffering from a bacterial infection using the indoline sulfonamide compounds disclosed herein.

Loyola University Chicago, Marquette University and The University Of Texas System | Date: 2017-06-21

Indoline sulfonamide compounds that can inhibit DapE and/or bacterial metallo-- lactamases (MBLs), such as NDM-1, are disclosed. Also disclosed are methods of treating an individual suffering from a bacterial infection using the indoline sulfonamide compounds disclosed herein.

Methods for modulating T-type calcium channel activity without directly targeting the T-type calcium channels are provided that include modulating kelch-like protein 1 (KLHL1) levels in a subject by providing a small hairpin RNA (shRNA) that targets a KLHL1 gene, and then administering the shRNA to the subject in an amount sufficient to modulate KLHL1 gene expression. The KLHL1 level directly effects current activity in T-type calcium channels and therefore modulation of KLHL1 gene expression indirectly modulates current activity in T-type calcium channels. The methods may be implemented with, for example, an shRNA molecule suitable for modulating a KLHL1 level in the subject which may be provided as a plasmid encoding the shRNA molecule or an adeno-associated virus vector encoding the shRNA molecule. Methods of identifying compounds that modulate current activity in T-type calcium channels by determining an effect of the compound on KLHL1 gene expression are also provided.

Huntsinger J.R.,Loyola University Chicago
Journal of Experimental Psychology: General | Year: 2012

The current research challenges the common view that positive affect and negative affect generate a broadened or narrowed attentional focus, respectively. Contrary to this view, two studies found that the link between affect and attentional focus as measured by a traditional flanker task (Study 1) and a modified flanker task (Study 2) reflects whatever focus is momentarily dominant. Further, in these studies when neither focus was dominant, the link between affect and attentional focus vanished. These results demonstrate that, like reward, positive affect and negative affect are not dedicated to a particular broadened or narrowed attentional scope but rather provide embodied information about the value of currently accessible attentional orientations. © 2012 American Psychological Association.

Campbell E.M.,Loyola University Chicago | Hope T.J.,Northwestern University
Nature Reviews Microbiology | Year: 2015

In a mature, infectious HIV-1 virion, the viral genome is housed within a conical capsid core made from the viral capsid (CA) protein. The CA protein and the structure into which it assembles facilitate virtually every step of infection through a series of interactions with multiple host cell factors. This Review describes our understanding of the interactions between the viral capsid core and several cellular factors that enable efficient HIV-1 genome replication, timely core disassembly, nuclear import and the integration of the viral genome into the genome of the target cell. We then discuss how elucidating these interactions can reveal new targets for therapeutic interactions against HIV-1. © 2015 Macmillan Publishers Limited. All rights reserved.

Gerding D.N.,Loyola University Chicago
Discovery Medicine | Year: 2013

We are in the midst of a resurgence of Clostridium difficile infection (CDI) in North America and Europe for which morbidity and mortality are higher than ever seen. C. difficile has risen in frequency to become the most common healthcare-associated infection pathogen, exceeding methicillin-resistant Staphylococcus aureus in many hospitals. Protection against CDI is thought to be mediated first by the normal bacterial microbiota, supplemented by an adaptive immune antibody response directed primarily at C. difficile toxins. Treatment of CDI is with antimicrobials that also further disrupt the protective bacterial microbiota leaving the patient susceptible to recurrent CDI. In addition, patients most susceptible to CDI, the advanced elderly, may already have a limited immune response and fail to increase their adaptive immune response with infection. The importance of both of these protective modalities has been demonstrated by 1) the success of fecal microbiota to restore "colonization resistance" for patients with multiple recurrences of CDI, and 2) the marked reduction in CDI recurrences with the use of intravenous monoclonal antibodies directed against toxin A and toxin B as an adjunct to antimicrobial treatment. Anti-toxin vaccines, passive monoclonal anti-toxin antibodies, and non-toxigenic C. difficile (to restore colonization resistance) are already undergoing patient clinical trials. The opportunity to prevent CDI is compelling and future research should focus on understanding the critical elements of the microbiota needed to restore colonization resistance and on development of novel immunologic strategies that include systemic and mucosal vaccines and passive immune modulators. © 2013, Discovery Medicine.

Wolfe A.J.,Loyola University Chicago
Current Opinion in Microbiology | Year: 2010

Recent reports support the long-standing hypothesis that acetyl phosphate, a physiologically relevant small molecule, can serve as a phosphoryl donor to a subset of two-component response regulators that regulate diverse cellular processes. Since acetyl phosphate is a central metabolite, this ability would link nutritional status to global signaling. This review will first introduce acetyl phosphate and its pathway. It will then summarize the most compelling evidence supporting the hypothesis and list predicted properties of an acetyl phosphate-sensitive pathway. Next, it will describe emerging evidence that acetyl phosphate and/or its pathway can influence diverse cellular processes across a broad spectrum of bacteria. Finally, the review will explore the possibility that other metabolites can function in a capacity similar to acetyl phosphate. © 2010 Elsevier Ltd. All rights reserved.

Marchese A.,Loyola University Chicago
Current Opinion in Cell Biology | Year: 2014

Chemokine receptors belong to the super family of G protein-coupled receptors (GPCRs). The cognate ligands for chemokine receptors are small circulating proteins known as chemokines. Upon binding to their cognate chemokines, receptors are rapidly desensitized, internalized onto early endosomes and sorted either into a recycling pathway or degradative pathway. Chemokine receptor trafficking is essential because it limits the magnitude and duration of signaling by removing receptors from the cell surface thereby limiting access to their ligands, but it also delivers bound chemokines to lysosomes for degradation. Receptor sorting into the recycling pathway contributes to resensitization of receptor signaling, whereas sorting into the degradative pathway leads to long-term attenuation of signaling. Recent studies have revealed some key information regarding the molecular determinants mediating chemokine receptor internalization and have shed light on the mechanisms dictating sorting into either the recycling or degradative pathways. Here I discuss our current understanding of the mechanisms mediating chemokine receptor trafficking with a focus primarily on recent findings for the chemokine receptor CXCR4. © 2013.

Agency: NSF | Branch: Standard Grant | Program: | Phase: ENVIRONMENTAL ENGINEERING | Award Amount: 600.00K | Year: 2016

Accumulation of man-made trash in the oceans has received much public attention. Human trash includes plastic, fishing debris, and metal, which have negative effects on marine resources. For example, some trash can be ingested by organisms including birds and turtles, and plastic can break down into small particles that have unique toxic properties. The study of the origins, movement, and consumption of trash in the ocean has provided information about ocean currents and food webs. Research by this investigator has shown that trash in rivers can reach similar densities as in the oceans. However, the sources, movements, and influences on biological systems of human trash in rivers are unknown, and are needed to develop efficient prevention strategies and policies. Also, studying the ecology of trash in rivers may reveal previously unexplored controls on ecosystem structure and function. This study will be conducted in Chicago- and Baltimore-area rivers, and include students from high school, undergraduate, and graduate levels. Trash removal will be used by student teachers to develop lessons for teaching the scientific method across grade levels.

This research will examine the ecosystem role of anthropogenic litter (AL) in 3 size classes by adapting fundamental tools used to measure communities of organisms and movement of organic matter. First, the role of large AL will be measured. Urban rivers typically have reduced channel complexity due to straightening and flood management. Large AL may act as an ?artificial reef,? providing habitat complexity and organic matter retention that is otherwise lacking, and thereby enhance biodiversity. Researchers will measure stream organism abundance at naturally occurring debris dams (i.e., wood) and at those generated by large AL. Next, this research will quantify interactions between AL and microbes. Bacteria, fungi, and algae carry out important biological activities in rivers, removing excess nutrients and providing food for insects and fish. Initial studies showed AL has unique microbial communities compared to natural surfaces. Experiments will test how microbes are affected by the structural and chemical properties of AL surfaces. Last, movement of intermediate-sized (e.g., shopping bags), and small AL (e.g., microplastic) will be examined. Initial research showed that AL in rivers is abundant and mobile, with some portion always moving downstream. Because AL attracts common toxic chemicals, its movement may be an overlooked pathway for delivery of toxins downstream and into food webs. This work will quantify inputs, outputs, and re-distribution of toxins on litter surfaces in urban streams.

Agency: NSF | Branch: Standard Grant | Program: | Phase: Molecular Biophysics | Award Amount: 640.00K | Year: 2016

ADP-glucose pyrophosphorylase is central to starch synthesis in plants and glycogen synthesis in bacteria and other organisms, serving as carbon storage polymers. It is a common biotechnology target and an informed understanding of its regulation has implications for starch/glycogen synthesis in a host of organisms. Allosteric control of ADP-glucose pyrophosphorylase activity is an important but poorly understood regulatory mechanism. Presently it is unclear how the enzyme is allosterically activated and how that activation signal is transmitted structurally within the enzyme. The goal of this project is to perform computational, structural and biochemical studies to understand and characterize the allosteric signals and the interaction of the allosteric effectors on ADP-glucose pyrophosphorylase activity in bacteria as a model for plants. The PIs predict the presence of a common structural element that works as a switch but also the presence of an alternative allosteric signal binding site. This project will also contribute to education by training undergraduate and graduate students, establish international collaborations, and foster participation of underrepresented minorities in research by supporting programs such as McNair-SROP. This project will also support an international course on protein science that includes elements of the research, providing a unique training opportunity for undergraduate and graduate students.

Plant starch and bacterial glycogen biosynthetic pathways provide models for the structure and evolution of allosteric regulatory functions of the enzyme ADP-glucose pyrophosphorylase. Despite the importance of these pathways, the allosteric mechanism that controls the activity of this enzyme is largely unknown. The project comprises computational, structural, and biochemical studies to understand and characterize the transmission of the allosteric signal and the interaction of the allosteric effectors in the ADP-glucose pyrophosphorylase family. It is predicted there is both a common structural element that works as a switch and an alternative allosteric signal guided by a secondary site. Three main research objectives will be pursued: 1) screen several enzyme forms from diverse branches of the phylogenetic tree for the presence of a dual allosteric mechanism; 2) obtain crystal structures of allosteric mutants (switched off) in several different conditions with different ligands to test the hypothesis that certain residues form a conserved allosteric switch in ADP-glucose pyrophosphorylases; and 3) perform computational studies (molecular dynamics, correlated movement analysis, and network pathway analysis) to predict the signaling pathways of activation from each putative allosteric site.

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