Institution
Stony Brook University
Education•Stony Brook, New York, United States•
About: Stony Brook University is a education organization based out in Stony Brook, New York, United States. It is known for research contribution in the topics: Population & Poison control. The organization has 32534 authors who have published 68218 publications receiving 3035131 citations. The organization is also known as: State University of New York at Stony Brook & SUNY Stony Brook.
Papers published on a yearly basis
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TL;DR: A model in which regulated p53 tetramerization occludes its NES is proposed, thereby ensuring nuclear retention of the DNA‐binding form and suggesting that attenuation of p53 function involves the conversion of tetramers into monomers or dimers, in which the NES is exposed to the proteins which mediate their export to the cytoplasm.
Abstract: Appropriate subcellular localization is crucial for regulating p53 function. We show that p53 export is mediated by a highly conserved leucine-rich nuclear export signal (NES) located in its tetramerization domain. Mutation of NES residues prevented p53 export and hampered tetramer formation. Although the p53-binding protein MDM2 has an NES and has been proposed to mediate p53 export, we show that the intrinsic p53 NES is both necessary and sufficient for export. This report also demonstrates that the cytoplasmic localization of p53 in neuroblastoma cells is due to its hyperactive nuclear export: p53 in these cells can be trapped in the nucleus by the export-inhibiting drug leptomycin B or by binding a p53-tetramerization domain peptide that masks the NES. We propose a model in which regulated p53 tetramerization occludes its NES, thereby ensuring nuclear retention of the DNA-binding form. We suggest that attenuation of p53 function involves the conversion of tetramers into monomers or dimers, in which the NES is exposed to the proteins which mediate their export to the cytoplasm.
776 citations
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TL;DR: Evidence for a functional role for CD36 in lipoprotein/fatty acid metabolism that was previously underappreciated is provided.
774 citations
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TL;DR: The results have identified a function for Vav and define a mechanism in which engaged membrane receptors activate its signalling pathway, causing this GTPase to switch from its inactive to its active state.
Abstract: THE oncogenic protein Vav1,2 harbours a complex array of structural motifs, including leucine-rich, Dbl-homology, pleckstrin-homology, zinc-finger, SH2 and SH3 domains. Upon stimulation by antigens or mitogens, Vav becomes phosphorylated on key tyrosine residues3–5 and associates with other signalling proteins, including the mitogen receptors3,4 Zap-70 (ref. 6), Vap-1 (ref. 5) and Slp-76 (ref. 7). Disruption of the vav locus by homologous recombination causes severe defects in signalling by primary antigen receptors, leading to abnormal lymphocyte proliferation and lymphopenia8,9. Despite the importance of Vav cell signalling, the function of this protein remains unknown. Here we show that tyrosine-phosphorylated Vav, but not the non-phosphorylated protein, catalyses GDP/GTP exchange on Rac-1, a protein implicated in cell proliferation and cytoskeletal organization10,11, causing this GTPase to switch from its inactive to its active state. Transfection experiments also show that phosphorylation of Vav on tyrosine residues leads to nucleotide exchange on Rac-1 in vivo and stimulates c-Jun kinase, a downstream element in the signalling pathway involving this GTPase. Our results have identified a function for Vav and define a mechanism in which engaged membrane receptors activate its signalling pathway.
769 citations
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02 Dec 2019TL;DR: In this article, the authors present a series of tests for univariate normality with Censored data, including plots, probability plots and regression tests, as well as a robust estimation of location and scale.
Abstract: 1. Introduction Part 1: Testing for Univariate Normality 2. Plots, Probability Plots and Regression Tests 3. Test Using Moments 4. Other Tests for Univariate Normality 5. Goodness of Fit Tests 6. Tests for Outliers 7. Power Comparisons for Univariate Tests for Normality 8. Testing for Normality with Censored Data Part 2: Testing for Multivariate Normality 9. Assessing Multivariate Normality 10. Testing for Multivariate Outliers Part 3: Additional Topics 11. Testing for Normal Mixtures 12. Robust Estimation of Location and Scale 13. Computational Issues
768 citations
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University of Gothenburg1, University of California, San Francisco2, Universidade Estadual de Maringá3, University of Iowa4, University of California, Los Angeles5, University of Melbourne6, University of Texas Health Science Center at San Antonio7, Complutense University of Madrid8, University of Zurich9, University of Sydney10, Stony Brook University11, Seoul National University12, University of Michigan13, Katholieke Universiteit Leuven14, Kristianstad University College15, University of Bern16, Goethe University Frankfurt17, Columbia University18, University of Basel19
TL;DR: Case definitions in day-to-day clinical practice and in epidemiological or disease-surveillance studies for peri-implant health, peri"-implant mucositis, and peri'simplantitis were introduced.
Abstract: A classification for peri-implant diseases and conditions was presented. Focused questions on the characteristics of peri-implant health, peri-implant mucositis, peri-implantitis, and soft- and hard-tissue deficiencies were addressed. Peri-implant health is characterized by the absence of erythema, bleeding on probing, swelling, and suppuration. It is not possible to define a range of probing depths compatible with health; Peri-implant health can exist around implants with reduced bone support. The main clinical characteristic of peri-implant mucositis is bleeding on gentle probing. Erythema, swelling, and/or suppuration may also be present. An increase in probing depth is often observed in the presence of peri-implant mucositis due to swelling or decrease in probing resistance. There is strong evidence from animal and human experimental studies that plaque is the etiological factor for peri-implant mucositis. Peri-implantitis is a plaque-associated pathological condition occurring in tissues around dental implants, characterized by inflammation in the peri-implant mucosa and subsequent progressive loss of supporting bone. Peri-implantitis sites exhibit clinical signs of inflammation, bleeding on probing, and/or suppuration, increased probing depths and/or recession of the mucosal margin in addition to radiographic bone loss. The evidence is equivocal regarding the effect of keratinized mucosa on the long-term health of the peri-implant tissue. It appears, however, that keratinized mucosa may have advantages regarding patient comfort and ease of plaque removal. Case definitions in day-to-day clinical practice and in epidemiological or disease-surveillance studies for peri-implant health, peri-implant mucositis, and peri-implantitis were introduced. The proposed case definitions should be viewed within the context that there is no generic implant and that there are numerous implant designs with different surface characteristics, surgical and loading protocols. It is recommended that the clinician obtain baseline radiographic and probing measurements following the completion of the implant-supported prosthesis.
767 citations
Authors
Showing all 32829 results
Name | H-index | Papers | Citations |
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Zhong Lin Wang | 245 | 2529 | 259003 |
Dennis W. Dickson | 191 | 1243 | 148488 |
Hyun-Chul Kim | 176 | 4076 | 183227 |
David Baker | 173 | 1226 | 109377 |
J. N. Butler | 172 | 2525 | 175561 |
Roderick T. Bronson | 169 | 679 | 107702 |
Nora D. Volkow | 165 | 958 | 107463 |
Jovan Milosevic | 152 | 1433 | 106802 |
Thomas E. Starzl | 150 | 1625 | 91704 |
Paolo Boffetta | 148 | 1455 | 93876 |
Jacques Banchereau | 143 | 634 | 99261 |
Larry R. Squire | 143 | 472 | 85306 |
John D. E. Gabrieli | 142 | 480 | 68254 |
Alexander Milov | 142 | 1143 | 93374 |
Meenakshi Narain | 142 | 1805 | 147741 |