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Keywords = cellular cryo-tomography (cryo-ET)

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13 pages, 3324 KiB  
Review
Zooming in and out: Exploring RNA Viral Infections with Multiscale Microscopic Methods
by Cheng-An Lyu, Yao Shen and Peijun Zhang
Viruses 2024, 16(9), 1504; https://doi.org/10.3390/v16091504 - 23 Sep 2024
Viewed by 1774
Abstract
RNA viruses, being submicroscopic organisms, have intriguing biological makeups and substantially impact human health. Microscopic methods have been utilized for studying RNA viruses at a variety of scales. In order of observation scale from large to small, fluorescence microscopy, cryo-soft X-ray tomography (cryo-SXT), [...] Read more.
RNA viruses, being submicroscopic organisms, have intriguing biological makeups and substantially impact human health. Microscopic methods have been utilized for studying RNA viruses at a variety of scales. In order of observation scale from large to small, fluorescence microscopy, cryo-soft X-ray tomography (cryo-SXT), serial cryo-focused ion beam/scanning electron microscopy (cryo-FIB/SEM) volume imaging, cryo-electron tomography (cryo-ET), and cryo-electron microscopy (cryo-EM) single-particle analysis (SPA) have been employed, enabling researchers to explore the intricate world of RNA viruses, their ultrastructure, dynamics, and interactions with host cells. These methods evolve to be combined to achieve a wide resolution range from atomic to sub-nano resolutions, making correlative microscopy an emerging trend. The developments in microscopic methods provide multi-fold and spatial information, advancing our understanding of viral infections and providing critical tools for developing novel antiviral strategies and rapid responses to emerging viral threats. Full article
(This article belongs to the Special Issue Microscopy Methods for Virus Research)
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14 pages, 5813 KiB  
Article
Cryo-Electron Tomography of Candida glabrata Plasma Membrane Proteins
by Cristina Jiménez-Ortigosa, Jennifer Jiang, Muyuan Chen, Xuyuan Kuang, Kelley R. Healey, Paul Castellano, Nikpreet Boparai, Steven J. Ludtke, David S. Perlin and Wei Dai
J. Fungi 2021, 7(2), 120; https://doi.org/10.3390/jof7020120 - 6 Feb 2021
Cited by 15 | Viewed by 7172 | Correction
Abstract
Fungal plasma membrane proteins have long been recognized as targets for the development of antifungal agents. Despite recent progress in experimental approaches and computational structural predictions, our knowledge of the structural dynamics and spatial distribution of these membrane proteins in the context of [...] Read more.
Fungal plasma membrane proteins have long been recognized as targets for the development of antifungal agents. Despite recent progress in experimental approaches and computational structural predictions, our knowledge of the structural dynamics and spatial distribution of these membrane proteins in the context of their native lipid environment remains limited. By applying cryo-electron tomography (cryoET) and subtomogram analysis, we aim to characterize the structural characteristics and spatial distribution of membrane proteins present in Candida glabrata plasma membranes. This study has resulted in the identification of the membrane-embedded structure of the fungal H+-ATPase, Pma1. Tomograms of the plasma membrane revealed that Pma1 complexes are heterogeneously distributed as hexamers that cluster into distinct membrane microdomains. This study characterizes fungal membrane proteins in the native cellular landscape and highlights the unique potential of cryoET to advance our understanding of cellular biology and biological systems. Full article
(This article belongs to the Special Issue The Application of Structural Biology in Antifungal Drug Discovery)
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18 pages, 10034 KiB  
Review
Cellular and Structural Studies of Eukaryotic Cells by Cryo-Electron Tomography
by Miriam Sarah Weber, Matthias Wojtynek and Ohad Medalia
Cells 2019, 8(1), 57; https://doi.org/10.3390/cells8010057 - 16 Jan 2019
Cited by 39 | Viewed by 19757
Abstract
The architecture of protein assemblies and their remodeling during physiological processes is fundamental to cells. Therefore, providing high-resolution snapshots of macromolecular complexes in their native environment is of major importance for understanding the molecular biology of the cell. Cellular structural biology by means [...] Read more.
The architecture of protein assemblies and their remodeling during physiological processes is fundamental to cells. Therefore, providing high-resolution snapshots of macromolecular complexes in their native environment is of major importance for understanding the molecular biology of the cell. Cellular structural biology by means of cryo-electron tomography (cryo-ET) offers unique insights into cellular processes at an unprecedented resolution. Recent technological advances have enabled the detection of single impinging electrons and improved the contrast of electron microscopic imaging, thereby significantly increasing the sensitivity and resolution. Moreover, various sample preparation approaches have paved the way to observe every part of a eukaryotic cell, and even multicellular specimens, under the electron beam. Imaging of macromolecular machineries at high resolution directly within their native environment is thereby becoming reality. In this review, we discuss several sample preparation and labeling techniques that allow the visualization and identification of macromolecular assemblies in situ, and demonstrate how these methods have been used to study eukaryotic cellular landscapes. Full article
(This article belongs to the Special Issue Development and Challenges in Microscopy for Cellular Imaging)
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