Institution
Rocky Mountain Laboratories
About: Rocky Mountain Laboratories is a based out in . It is known for research contribution in the topics: Virus & Borrelia burgdorferi. The organization has 715 authors who have published 906 publications receiving 62623 citations. The organization is also known as: RML & Rocky Mountain Laboratory.
Topics: Virus, Borrelia burgdorferi, Scrapie, Viral replication, Gene
Papers published on a yearly basis
Papers
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TL;DR: In this article, three classes of GFP mutants having single excitation maxima around 488 nm are shown to be brighter than wild-type GFP following 488-nm excitation.
3,093 citations
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TL;DR: It is concluded that CD4 and CCR5 directly or indirectly interact in a concentration-dependent manner within a pathway that is essential for infection by macrophagetropic HIV-1 and that the requirements for each are increased when the other component is present in a limiting amount.
Abstract: It has been proposed that changes in cell surface concentrations of coreceptors may control infections by human immunodeficiency virus type 1 (HIV-1), but the mechanisms of coreceptor function and the concentration dependencies of their activities are unknown. To study these issues and to generate stable clones of adherent cells able to efficiently titer diverse isolates of HIV-1, we generated two panels of HeLa-CD4/CCR5 cells in which individual clones express either large or small quantities of CD4 and distinct amounts of CCR5. The panels were made by transducing parental HeLa-CD4 cells with the retroviral vector SFF-CCR5. Derivative clones expressed a wide range of CCR5 quantities which were between 7.0 x 10(2) and 1.3 x 10(5) molecules/cell as measured by binding antibodies specific for CCR5 and the chemokine [125I]MIP1beta. CCR5 was mobile in the membranes, as indicated by antibody-induced patching. In cells with a large amount of CD4, an unexpectedly low trace of CCR5 (between 7 x 10(2) and 2.0 x 10(3) molecules/cell) was sufficient for maximal susceptibility to all tested HIV-1, including primary patient macrophagetropic and T-cell-tropic isolates. Indeed, the titers as indicated by immunoperoxidase staining of infected foci were as high as the tissue culture infectious doses measured in human peripheral blood mononuclear cells. In contrast, cells with a small amount of CD4 required a much larger quantity of CCR5 for maximal infection by macrophagetropic HIV-1 (ca. 1.0 x 10(4) to 2.0 x 10(4) molecules/cell). Cells that expressed low and high amounts of CD4 were infected with equal efficiencies when CCR5 concentrations were above threshold levels for maximal infection. Our results suggest that the concentrations of CD4 and CCR5 required for efficient infections by macrophagetropic HIV-1 are interdependent and that the requirements for each are increased when the other component is present in a limiting amount. We conclude that CD4 and CCR5 directly or indirectly interact in a concentration-dependent manner within a pathway that is essential for infection by macrophagetropic HIV-1. In addition, our results suggest that multivalent virus-receptor bonds and diffusion in the membrane contribute to HIV-1 infections.
1,222 citations
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TL;DR: A quantitative mass spectrometry-based phosphoproteomics survey of SARS-CoV-2 infection in Vero E6 cells reveals dramatic rewiring of phosphorylation on host and viral proteins, revealing potential COVID-19 therapies.
723 citations
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TL;DR: This study has found that fusion of the endoplasmic reticulum (ER) with the macrophage plasmalemma, underneath phagocytic cups, is a source of membrane for phagosome formation in macrophages.
683 citations
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TL;DR: It is proposed that PrPTME conformation could play a role in targeting TME strains to different neuron populations in which strain-specific formation occurs and is consistent with the idea thatPrPTME protein structure determines the molecular basis of strain variation.
Abstract: The molecular basis of strain variation in scrapie diseases is unknown. The only identified component of the agent is the posttranslationally modified host prion protein (PrPSc). The biochemical and physical properties of PrP from two strains of transmissible mink encephalopathy (TME), called hyper (HY) and drowsy (DY), were compared to investigate if PrP heterogeneity could account for strain diversity. The degradation rate of PrPTME digested with proteinase K was found to be strain specific and correlated with inactivation of the TME titer. Edman protein sequencing revealed that the major N-terminal end of HY PrPTME commenced at least 10 amino acid residues prior to that of DY PrPTME after digestion with proteinase K. Analysis of the brain distribution of PrPTME exhibited a strain-specific pattern and localization of PrPTME to the perikarya of specific neuron populations. Our findings are consistent with HY and DY PrPTME having distinct protein conformations and/or strain-specific ligand interactions that influence PrPTME properties. We propose that PrPTME conformation could play a role in targeting TME strains to different neuron populations in which strain-specific formation occurs. These data are consistent with the idea that PrPTME protein structure determines the molecular basis of strain variation. Images
657 citations
Authors
Showing all 715 results
Name | H-index | Papers | Citations |
---|---|---|---|
Eliezer Masliah | 170 | 982 | 127818 |
Richard O. Hynes | 143 | 442 | 97442 |
Stanley Falkow | 134 | 349 | 62461 |
Michael B. A. Oldstone | 123 | 670 | 54675 |
James M. Musser | 113 | 461 | 42030 |
Michael Otto | 105 | 490 | 39622 |
José M. C. Ribeiro | 95 | 489 | 33417 |
Clifton E. Barry | 95 | 314 | 38051 |
Heinz Feldmann | 92 | 468 | 31199 |
Katherine L. Nathanson | 92 | 394 | 31586 |
Alan G. Barbour | 91 | 308 | 27997 |
Frank R. DeLeo | 86 | 206 | 26462 |
Peter T. Lansbury | 83 | 203 | 39882 |
Byron Caughey | 77 | 236 | 22590 |
Alan D. Michelson | 74 | 287 | 20705 |