Institution
Vanderbilt University
Education•Nashville, Tennessee, United States•
About: Vanderbilt University is a education organization based out in Nashville, Tennessee, United States. It is known for research contribution in the topics: Population & Cancer. The organization has 45066 authors who have published 106528 publications receiving 5435039 citations. The organization is also known as: Vandy.
Topics: Population, Cancer, Receptor, Health care, Poison control
Papers published on a yearly basis
Papers
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TL;DR: Modern evolutionary theory is informing more models, emphasizing that expressions are directed at a receiver, that the interests of sender and receiver can conflict, that there are many determinants of sending an expression in addition to emotion, that expressions influence the receiver in a variety of ways, and that the receiver's response is more than simply decoding a message.
Abstract: A flurry of theoretical and empirical work concerning the production of and response to facial and vocal expressions has occurred in the past decade. That emotional expressions express emotions is a tautology but may not be a fact. Debates have centered on universality, the nature of emotion, and the link between emotions and expressions. Modern evolutionary theory is informing more models, emphasizing that expressions are directed at a receiver, that the interests of sender and receiver can conflict, that there are many determinants of sending an expression in addition to emotion, that expressions influence the receiver in a variety of ways, and that the receiver's response is more than simply decoding a message.
722 citations
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TL;DR: It is proposed that regulation of matrilysin production by β-catenin accumulation is a contributing factor to intestinal tumorigenesis.
Abstract: Matrilysin is a matrix metalloproteinase expressed in the tumor cells of greater than 80% of intestinal adenomas. The majority of these intestinal tumors are associated with the accumulation of β-catenin, a component of the cadherin adhesion complex and, through its association with the T Cell Factor (Tcf) DNA binding proteins, a regulator in the Wnt signal transduction pathway. In murine intestinal tumors, matrilysin transcripts show striking overlap with the accumulation of β-catenin protein. The matrilysin promoter is upregulated as much as 12-fold by β-catenin in colon tumor cell lines in a manner inversely proportional to the endogenous levels of β-catenin/Tcf complex and is dependent upon a single optimal Tcf-4 recognition site. Coexpression of the E-cadherin cytoplasmic domain blocked this induction and reduced basal promoter activity in every colon cancer cell line tested. Inactivation of the Tcf binding site increased promoter activity and overexpression of the Tcf factor, LEF-1, significantly downregulated matrilysin promoter activity, suggesting that β-catenin transactivates the matrilysin promoter by virtue of its ability to abrogate Tcf-mediated repression. Because genetic ablation of matrilysin decreases tumor formation in multiple intestinal neoplasia (Min) mice, we propose that regulation of matrilysin production by β-catenin accumulation is a contributing factor to intestinal tumorigenesis.
722 citations
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TL;DR: The results suggest a novel mechanism by which metalloproteinases can influence invasion, as indicated by induction of invasion into collagen type I and inhibition of E-cadherin-dependent cell aggregation.
Abstract: The function of many transmembrane molecules can be altered by cleavage and subsequent release of their ectodomains. We have investigated ectodomain cleavage of the cell-cell adhesion and signal-transducing molecule E-cadherin. The E-cadherin ectodomain is constitutively shed from the surface of MCF-7 and MDCKts.srcC12 cells in culture. Release of the 80 kDa soluble E-cadherin fragment is stimulated by phorbol-12-myristate-13-acetate and is inhibited by overexpression of the tissue inhibitor of metalloproteinases-2. The metalloproteinases matrilysin and stromelysin-1 both cleave E-cadherin at the cell surface and release sE-CAD into the medium. The soluble E-cadherin fragment thus released inhibits E-cadherin functions in a paracrine way, as indicated by induction of invasion into collagen type I and inhibition of E-cadherin-dependent cell aggregation. Our results, therefore, suggest a novel mechanism by which metalloproteinases can influence invasion.
722 citations
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TL;DR: It is reported that this G protein specifically activates the β1 isozyme, but not the γ1 and δ1 isozymes of phospholipase C and it is shown that this protein is related to the Gq class of G protein α subunits12.
Abstract: MANY hormones, neurotransmitters and growth factors, on binding to G protein-coupled receptors or receptors possessing tyrosine kinase activity, increase intracellular levels of the second messengers inositol 1,4,5-trisphosphate and 1,2-diacylglycerol. This is due to activation of phosphoinositide-specific phospho-lipase(s) C (PLC), the isozymes of which are classified into groups, α, β, γ and δ (refs 1, 2). The β, γ and δ groups themselves contain PLC isozymes which have both common and unique structural domains3. Only the γl isozyme has been implicated in a signal transduction mechanism4. This involves association with, and tyrosine phosporylation by, the ligand-bound epidermal growth factor and platelet-derived growth factor receptors5–7, probably by means of the PLC-γl-specific src homology (SH2) domain8. Because EGF receptor-mediated tyrosine phosphorylation of PLC-γ1 stimulates catalytic activity in vitro9 and G proteins have been implicated in the activation of PLC10, we investigated which PLC isozymes are subject to G protein regulation. We have purified11 an activated G protein α subunit that stimulates partially purified phospholipase C and now report that this G protein specifically activates the β1 isozyme, but not the γ1 and δ1 isozymes of phospholipase C. We also show that this protein is related to the Gq class of G protein α subunits12.
720 citations
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TL;DR: A fully-fledged particle-flow reconstruction algorithm tuned to the CMS detector was developed and has been consistently used in physics analyses for the first time at a hadron collider as mentioned in this paper.
Abstract: The CMS apparatus was identified, a few years before the start of the LHC operation at CERN, to feature properties well suited to particle-flow (PF) reconstruction: a highly-segmented tracker, a fine-grained electromagnetic calorimeter, a hermetic hadron calorimeter, a strong magnetic field, and an excellent muon spectrometer. A fully-fledged PF reconstruction algorithm tuned to the CMS detector was therefore developed and has been consistently used in physics analyses for the first time at a hadron collider. For each collision, the comprehensive list of final-state particles identified and reconstructed by the algorithm provides a global event description that leads to unprecedented CMS performance for jet and hadronic τ decay reconstruction, missing transverse momentum determination, and electron and muon identification. This approach also allows particles from pileup interactions to be identified and enables efficient pileup mitigation methods. The data collected by CMS at a centre-of-mass energy of 8\TeV show excellent agreement with the simulation and confirm the superior PF performance at least up to an average of 20 pileup interactions.
719 citations
Authors
Showing all 45403 results
Name | H-index | Papers | Citations |
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Walter C. Willett | 334 | 2399 | 413322 |
Meir J. Stampfer | 277 | 1414 | 283776 |
John Q. Trojanowski | 226 | 1467 | 213948 |
Robert M. Califf | 196 | 1561 | 167961 |
Matthew Meyerson | 194 | 553 | 243726 |
Scott M. Grundy | 187 | 841 | 231821 |
Tony Hunter | 175 | 593 | 124726 |
David R. Jacobs | 165 | 1262 | 113892 |
Donald E. Ingber | 164 | 610 | 100682 |
L. Joseph Melton | 161 | 531 | 97861 |
Ralph A. DeFronzo | 160 | 759 | 132993 |
David W. Bates | 159 | 1239 | 116698 |
Charles N. Serhan | 158 | 728 | 84810 |
David Cella | 156 | 1258 | 106402 |
Jay Hauser | 155 | 2145 | 132683 |