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New York City, NY, United States

Yeshiva University is a private university in New York City, with four campuses in New York City. Founded in 1886, it is a research university.The university's undergraduate schools—Yeshiva College, Stern College for Women, and Syms School of Business— offer a dual curriculum inspired by Modern-Centrist-Orthodox Judaism's hashkafa of Torah Umadda combining academic education with the study of Torah. Yeshiva is perhaps best known for its secular, highly selective graduate schools, the Albert Einstein College of Medicine and the Benjamin N. Cardozo School of Law. The Forward announced on May 27, 2014 that Yeshiva would be shedding the financial burden of Albert Einstein College of Medicine by initiating an arrangement with Montefiore Hospital.Yeshiva University is an independent institution chartered by New York State. It is accredited by the Commission on Higher Education of the Middle States Association of Colleges and Schools and by several professional agencies. Wikipedia.


Frangogiannis N.G.,Yeshiva University
Circulation Research | Year: 2012

Myocardial necrosis triggers an inflammatory reaction that clears the wound from dead cells and matrix debris, while activating reparative pathways necessary for scar formation. A growing body of evidence suggests that accentuation, prolongation, or expansion of the postinfarction inflammatory response results in worse remodeling and dysfunction following myocardial infarction. This review manuscript discusses the cellular effectors and endogenous molecular signals implicated in suppression and containment of the inflammatory response in the infarcted heart. Clearance of apoptotic neutrophils, recruitment of inhibitory monocyte subsets and regulatory T cells, macrophage differentiation and pericyte/endothelial interactions may play an active role in restraining postinfarction inflammation. Multiple molecular signals may be involved in suppressing the inflammatory cascade. Negative regulation of toll-like receptor signaling, downmodulation of cytokine responses, and termination of chemokine signals may be mediated through the concerted action of multiple suppressive pathways that prevent extension of injury and protect from adverse remodeling. Expression of soluble endogenous antagonists, decoy receptors, and posttranslational processing of bioactive molecules may limit cytokine and chemokine actions. Interleukin-10, members of the transforming growth factor-β family, and proresolving lipid mediators (such as lipoxins, resolvins, and protectins) may suppress proinflammatory signaling. In human patients with myocardial infarction, defective suppression, and impaired resolution of inflammation may be important mechanisms in the pathogenesis of remodeling and in progression to heart failure. Understanding of inhibitory and proresolving signals in the infarcted heart and identification of patients with uncontrolled postinfarction inflammation and defective cardiac repair is needed to design novel therapeutic strategies. © 2011 American Heart Association, Inc. Source


Schramm V.L.,Yeshiva University
Annual Review of Biochemistry | Year: 2011

Experimental analysis of enzymatic transition-state structures uses kinetic isotope effects (KIEs) to report on bonding and geometry differences between reactants and the transition state. Computational correlation of experimental values with chemical models permits three-dimensional geometric and electrostatic assignment of transition states formed at enzymatic catalytic sites. The combination of experimental and computational access to transition-state information permits (a) the design of transition-state analogs as powerful enzymatic inhibitors, (b) exploration of protein features linked to transition-state structure, (c) analysis of ensemble atomic motions involved in achieving the transition state, (d) transition-state lifetimes, and (e) separation of ground-state (Michaelis complexes) from transition-state effects. Transition-state analogs with picomolar dissociation constants have been achieved for several enzymatic targets. Transition states of closely related isozymes indicate that the protein's dynamic architecture is linked to transition-state structure. Fast dynamic motions in catalytic sites are linked to transition-state generation. Enzymatic transition states have lifetimes of femtoseconds, the lifetime of bond vibrations. Binding isotope effects (BIEs) reveal relative reactant and transition-state analog binding distortion for comparison with actual transition states. © 2011 by Annual Reviews. All rights reserved. Source


Frangogiannis N.G.,Yeshiva University
Physiological Reviews | Year: 2012

The term matricellular proteins describes a family of structurally unrelated extracellular macromolecules that, unlike structural matrix proteins, do not play a primary role in tissue architecture, but are induced following injury and modulate cell-cell and cell-matrix interactions. When released to the matrix, matricellular proteins associate with growth factors, cytokines, and other bioactive effectors and bind to cell surface receptors transducing signaling cascades. Matricellular proteins are upregulated in the injured and remodeling heart and play an important role in regulation of inflammatory, reparative, fibrotic and angiogenic pathways. Thrombospondin (TSP)-1, -2, and -4 as well as tenascin-C and -X secreted protein acidic and rich in cysteine (SPARC), osteopontin, periostin, and members of the CCN family (including CCN1 and CCN2/connective tissue growth factor) are involved in a variety of cardiac pathophysiological conditions, including myocardial infarction, cardiac hypertrophy and fibrosis, aging-associated myocardial remodeling, myocarditis, diabetic cardiomyopathy, and valvular disease. This review discusses the properties and characteristics of the matricellular proteins and presents our current knowledge on their role in cardiac adaptation and disease. Understanding the role of matricellular proteins in myocardial pathophysiology and identification of the functional domains responsible for their actions may lead to design of peptides with therapeutic potential for patients with heart disease. © 2012 by the American Physiological Society. Source


Extended X-ray absorption fine structure (EXAFS) spectroscopy has been used to study short range order in heterometallic alloys for almost four decades. In this critical review, experimental, theoretical and data analytical approaches are revisited to examine their power, and limitations, in studies of bimetallic nanocatalysts. This article covers the basics of EXAFS experiments, data analysis, and modelling of nanoscale clusters. It demonstrates that, in the best case scenario, quantitative information about the nanocatalyst's size, shape, details of core-shell architecture, as well as static and dynamic disorder in metal-metal bond lengths can be obtained. The article also emphasizes the main challenge accompanying such insights: the need to account for the statistical nature of the EXAFS technique, and discusses corrective strategies. © 2012 The Royal Society of Chemistry. Source


Patent
Yeshiva University | Date: 2015-03-24

Methods are disclosed for therapy of radiation-induced lung injury and other lung diseases using R-spondin

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