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, Poison control, Breast cancer, Receptor
Papers published on a yearly basis
Papers
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University of Toronto1, University of Turin2, Imperial College London3, Leicester General Hospital4, John Radcliffe Hospital5, Université de Montréal6, University of Washington7, LSU Health Sciences Center Shreveport8, Leiden University9, Columbia University10, Case Western Reserve University11, Mayo Clinic12, University of Amsterdam13, Vanderbilt University14, Western Infirmary15, German Cancer Research Center16, Johns Hopkins University17, St. Vincent's Health System18, Scott & White Hospital19, University of Florida20, University of North Carolina at Chapel Hill21, University of Alabama at Birmingham22, Jikei University School of Medicine23, The Chinese University of Hong Kong24, Nanjing University25, Austral University of Chile26, Juntendo University27, Peking University28, Erasmus University Rotterdam29, Wakayama Medical University30
TL;DR: In this article, a new classification for IgA nephropathy is presented by an international consensus working group and the goal of this new system was to identify specific pathological features that more accurately predict risk of progression of renal disease.
994 citations
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TL;DR: The first known small-molecule inhibitor of BMP signaling-dorsomorphin is described, which was identified in a screen for compounds that perturb dorsoventral axis formation in zebrafish and found that dorsomorphin selectively inhibits the BMP type I receptors ALK2, ALK3 and ALK6 and thus blocks BMP-mediated SMAD1/5/8 phosphorylation, target gene transcription and osteogenic differentiation.
Abstract: Bone morphogenetic protein (BMP) signals coordinate developmental patterning and have essential physiological roles in mature organisms. Here we describe the first known small-molecule inhibitor of BMP signaling—dorsomorphin, which we identified in a screen for compounds that perturb dorsoventral axis formation in zebrafish. We found that dorsomorphin selectively inhibits the BMP type I receptors ALK2, ALK3 and ALK6 and thus blocks BMP-mediated SMAD1/5/8 phosphorylation, target gene transcription and osteogenic differentiation. Using dorsomorphin, we examined the role of BMP signaling in iron homeostasis. In vitro, dorsomorphin inhibited BMP-, hemojuvelin- and interleukin 6–stimulated expression of the systemic iron regulator hepcidin, which suggests that BMP receptors regulate hepcidin induction by all of these stimuli. In vivo, systemic challenge with iron rapidly induced SMAD1/5/8 phosphorylation and hepcidin expression in the liver, whereas treatment with dorsomorphin blocked SMAD1/5/8 phosphorylation, normalized hepcidin expression and increased serum iron levels. These findings suggest an essential physiological role for hepatic BMP signaling in iron-hepcidin homeostasis.
994 citations
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TL;DR: It is found that maximal kinase activity of FAK immune complexes requires phosphorylation of both tyrosines 576 and 577, which indicates that phosphorylated by Src (or other Src family kinases) is an important step in the formation of an active signaling complex.
Abstract: Focal adhesion kinase (FAK) is a widely expressed nonreceptor protein-tyrosine kinase implicated in integrin-mediated signal transduction pathways and in the process of oncogenic transformation by v-Src. Elevation of FAK's phosphotyrosine content, following both cell adhesion to extracellular matrix substrata and cell transformation by Rous sarcoma virus, correlates directly with an increased kinase activity. To help elucidate the role of FAK phosphorylation in signal transduction events, we used a tryptic phosphopeptide mapping approach to identify tyrosine sites of phosphorylation responsive to both cell adhesion and Src transformation. We have identified four tyrosines, 397, 407, 576, and 577, which are phosphorylated in mouse BALB/3T3 fibroblasts in an adhesion-dependent manner. Tyrosine 397 has been previously recognized as the major site of FAK autophosphorylation. Phosphorylation of tyrosines 407, 576, and 577, which are previously unrecognized sites, is significantly elevated in the presence of c-Src in vitro and v-Src in vivo. Tyrosines 576 and 577 lie within catalytic subdomain VIII--a region recognized as a target for phosphorylation-mediated regulation of protein kinase activity. We found that maximal kinase activity of FAK immune complexes requires phosphorylation of both tyrosines 576 and 577. Our results indicate that phosphorylation of FAK by Src (or other Src family kinases) is an important step in the formation of an active signaling complex.
994 citations
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TL;DR: This genome-wide association study of gene expression resulted in the detection of more than 6,000 associations between SNP genotypes and liver gene expression traits, where many of the corresponding genes identified have already been implicated in a number of human diseases.
Abstract: Genetic variants that are associated with common human diseases do not lead directly to disease, but instead act on intermediate, molecular phenotypes that in turn induce changes in higher-order disease traits. Therefore, identifying the molecular phenotypes that vary in response to changes in DNA and that also associate with changes in disease traits has the potential to provide the functional information required to not only identify and validate the susceptibility genes that are directly affected by changes in DNA, but also to understand the molecular networks in which such genes operate and how changes in these networks lead to changes in disease traits. Toward that end, we profiled more than 39,000 transcripts and we genotyped 782,476 unique single nucleotide polymorphisms (SNPs) in more than 400 human liver samples to characterize the genetic architecture of gene expression in the human liver, a metabolically active tissue that is important in a number of common human diseases, including obesity, diabetes, and atherosclerosis. This genome-wide association study of gene expression resulted in the detection of more than 6,000 associations between SNP genotypes and liver gene expression traits, where many of the corresponding genes identified have already been implicated in a number of human diseases. The utility of these data for elucidating the causes of common human diseases is demonstrated by integrating them with genotypic and expression data from other human and mouse populations. This provides much-needed functional support for the candidate susceptibility genes being identified at a growing number of genetic loci that have been identified as key drivers of disease from genome-wide association studies of disease. By using an integrative genomics approach, we highlight how the gene RPS26 and not ERBB3 is supported by our data as the most likely susceptibility gene for a novel type 1 diabetes locus recently identified in a large-scale, genome-wide association study. We also identify SORT1 and CELSR2 as candidate susceptibility genes for a locus recently associated with coronary artery disease and plasma low-density lipoprotein cholesterol levels in the process.
992 citations
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TL;DR: The isolation, sequence and expression of a complementary DNA clone encoding the membrane form of guanylate cyclase from rat brain are reported, which represents a new class of mammalian cell-surface receptors which contain an extracellular ligand-binding domain and an intracellular guanyl cyclase catalytic domain.
Abstract: ATRIAL natriuretic peptide (ANP) is a polypeptide hormone whose effects include the induction of diuresis, natriuresis and vasorelaxation1. One of the earliest events following binding of ANP to receptors on target cells is an increase in cyclic GMP concentration, indicating that this nucleotide might act as a mediator of the physiological effects of the hormone2,3. Guanylate cyclase exists in at least two different molecular forms: a soluble haem-containing enzyme consisting of two summits4,5 and a non-haem-containing transmembrane protein having a single subunit6. It is the membrane form of guanylate cyclase that is activated following binding of ANP to target cells3,7,8. We report here the isolation, sequence and expression of a complementary DNA clone encoding the membrane form of guanylate cyclase from rat brain. Transfec-tion of this cDNA into cultured mammalian cells results in expression of guanylate cyclase activity and ANP-binding activity. The ANP receptor/guanylate cyclase represents a new class of mammalian cell-surface receptors which contain an extracellular ligand-binding domain and an intracellular guanylate cyclase catalytic domain.
991 citations
Authors
Showing all 45403 results
Name | H-index | Papers | Citations |
---|---|---|---|
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 |