Institution
University of Vermont
Education•Burlington, Vermont, United States•
About: University of Vermont is a education organization based out in Burlington, Vermont, United States. It is known for research contribution in the topics: Population & Poison control. The organization has 17592 authors who have published 38251 publications receiving 1609874 citations. The organization is also known as: UVM & University of Vermont and State Agricultural College.
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TL;DR: Results from this study indicate that the use of EAF steel slag in constructed wetlands or filter beds is a promising solution for P removal via adsorption and precipitation mechanisms.
263 citations
TL;DR: This goal was to determine whether resistance training would improve walking endurance and lower-limb strength in nondisabled, community-dwelling elderly persons and whether this would result in increased measures of physical performance and corresponding increases in muscle strength, size, and short-course walking speed.
Abstract: Objective: To determine the effect of a resistance-training program on walking endurance in a healthy, community-dwelling elderly population. Design: 12-week randomized, controlled trial comparing ...
263 citations
TL;DR: An overview of short patch base excision repair in humans is provided and current knowledge of defects in base excison repair in mouse models and functional studies on shortPatch base excisions repair germ line polymorphisms and their relationship to cancer are summarized.
263 citations
TL;DR: In this article, the authors focus on developing a method for selecting sites for PES where the main interest is to bundle biodiversity with other ecosystem services, and assess the opportunities for bundling biodiversity conservation with carbon and water services at the national scale and identify where using PES to protect these areas of multiple benefits would be most cost effective and efficient.
263 citations
TL;DR: Unphosphorylated myosin acts as a load to slow down the rate at which actin is moved by the faster cycling phosphorylated cross-bridges, and the observed modulation of actin velocity as a function of copolymer composition can be accounted for by a model based on mechanical interactions between cross- bridges.
Abstract: Although it is generally believed that phosphorylation of the regulatory light chain of myosin is required before smooth muscle can develop force, it is not known if the overall degree of phosphorylation can also modulate the rate at which cross-bridges cycle. To address this question, an in vitro motility assay was used to observe the motion of single actin filaments interacting with smooth muscle myosin copolymers composed of varying ratios of phosphorylated and unphosphorylated myosin. The results suggest that unphosphorylated myosin acts as a load to slow down the rate at which actin is moved by the faster cycling phosphorylated cross-bridges. Myosin that was chemically modified to generate a noncycling analogue of the "weakly" bound conformation was similarly able to slow down phosphorylated myosin. The observed modulation of actin velocity as a function of copolymer composition can be accounted for by a model based on mechanical interactions between cross-bridges.
263 citations
Authors
Showing all 17727 results
| Name | H-index | Papers | Citations |
|---|---|---|---|
| Albert Hofman | 267 | 2530 | 321405 |
| Ralph B. D'Agostino | 226 | 1287 | 229636 |
| George Davey Smith | 224 | 2540 | 248373 |
| Stephen V. Faraone | 188 | 1427 | 140298 |
| Valentin Fuster | 179 | 1462 | 185164 |
| Dennis J. Selkoe | 177 | 607 | 145825 |
| Anders Björklund | 165 | 769 | 84268 |
| Alfred L. Goldberg | 156 | 474 | 88296 |
| Christopher P. Cannon | 151 | 1118 | 108906 |
| Debbie A Lawlor | 147 | 1114 | 101123 |
| Roger J. Davis | 147 | 498 | 103478 |
| Andrew S. Levey | 144 | 600 | 156845 |
| Jonathan G. Seidman | 137 | 563 | 89782 |
| Yu Huang | 136 | 1492 | 89209 |
| Christine E. Seidman | 134 | 519 | 67895 |