Electron microscopy and image analysis reveal common principles of organization in two large protein complexes: groEL-Type proteins and proteasomes

1990 ◽  
Vol 103 (3) ◽  
pp. 197-203 ◽  
Author(s):  
Peter Zwickl ◽  
Günter Pfeifer ◽  
Friedrich Lottspeich ◽  
Friedrich Kopp ◽  
Burkhardt Dahlmann ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Image Analysis ◽  
Protein Complexes ◽  
Large Protein

Electron Microscopy and image analysis of nucleo-protein complexes

1994 ◽  
Vol 52 ◽  
pp. 88-89
Author(s):  
E. H. Egelman ◽  
X. Yu
Keyword(s):  
Electron Microscopy ◽  
Image Analysis ◽  
Normal Cell ◽  
Genetic Recombination ◽  
Protein Complexes ◽  
Chromosomal Rearrangements ◽  
Reca Protein ◽  
E Coli ◽  
Helical Polymer ◽  
Specific Protease

The RecA protein of E. coli has been shown to mediate genetic recombination, regulate its own synthesis, control the expression of other genes, act as a specific protease, form a helical polymer and have an ATPase activity, among other observed properties. The unusual filament formed by the RecA protein on DNA has not previously been shown to exist outside of bacteria. Within this filament, the 36 Å pitch of B-form DNA is extended to about 95 Å, the pitch of the RecA helix. We have now establishedthat similar nucleo-protein complexes are formed by bacteriophage and yeast proteins, and availableevidence suggests that this structure is universal across all of biology, including humans. Thus, understanding the function of the RecA protein will reveal basic mechanisms, in existence inall organisms, that are at the foundation of general genetic recombination and repair.Recombination at this moment is assuming an importance far greater than just pure biology. The association between chromosomal rearrangements and neoplasms has become stronger and stronger, and these rearrangements are most likely products of the recombinatory apparatus of the normal cell. Further, damage to DNA appears to be a major cause of cancer.

Electron microscopy of decorated crystals for the determination of crystallographic rotation and translation parameters in large protein complexes

1992 ◽  
Vol 225 (4) ◽  
pp. 1065-1073 ◽  
Author(s):  
Adelbert Bacher ◽  
Sevil Weinkauf ◽  
Luis Bachmann ◽  
Karl Ritsert ◽  
Wolfgang Baumeister ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Protein Complexes ◽  
Large Protein

Morphometric analysis of cellular interactions with the endothelium during the development of arterial lesions using Scanning Electron Microscopy and digital image analysis

1987 ◽  
Vol 45 ◽  
pp. 918-919
Author(s):  
M.E. Rosenfeld ◽  
C. Karboski ◽  
M.F. Prescott ◽  
P. Goodwin ◽  
R. Ross
Keyword(s):  
Electron Microscopy ◽  
Image Analysis ◽  
Quantitative Data ◽  
Digital Image Analysis ◽  
Lower Cost ◽  
Matched Control ◽  
Digital Analysis ◽  
Cellular Interactions ◽  
Arterial Lesions ◽  
Scanning Electron

Previous research documenting the chronology of the cellular interactions that occur on or below the surface of the endothelium during the initiation and progression of arterial lesions, primarily consisted of descriptive studies. The recent development of lower cost image analysis hardware and software has facilitated the collection of high resolution quantitative data from microscopic images. In this report we present preliminary quantitative data on the sequence of cellular interactions that occur on the endothelium during the initiation of atherosclerosis or vasculitis utilizing digital analysis of images obtained directly from the scanning electron microscope. Segments of both atherosclerotic and normal arteries were obtained from either diet-induced or endogenously (WHHL) hypercholesterolemic rabbits following 1-4 months duration of hypercholesterolemia and age matched control rabbits. Vasculitis was induced in rats following placement of an endotoxin soaked thread adjacent to the adventitial surface of arteries.

Applications of CCEM to Environmental Health Problems

1985 ◽  
Vol 43 ◽  
pp. 102-103
Author(s):  
R. J. Lee ◽  
J. S. Walker
Keyword(s):  
Electron Microscopy ◽  
Image Analysis ◽  
Environmental Health ◽  
Computer Control ◽  
External Agent ◽  
External Agents ◽  
Computer Controlled ◽  
Primitive State ◽  
Textural Changes ◽  
General Aspects

Electron microscopy (EM), with the advent of computer control and image analysis techniques, is rapidly evolving from an interpretative science into a quantitative technique. Electron microscopy is potentially of value in two general aspects of environmental health: exposure and diagnosis.In diagnosis, electron microscopy is essentially an extension of optical microscopy. The goal is to characterize cellular changes induced by external agents. The external agent could be any foreign material, chemicals, or even stress. The use of electron microscopy as a diagnostic tool is well- developed, but computer-controlled electron microscopy (CCEM) has had only limited impact, mainly because it is fairly new and many institutions lack the resources to acquire the capability. In addition, major contributions to diagnosis will come from CCEM only when image analysis (IA) and processing algorithms are developed which allow the morphological and textural changes recognized by experienced medical practioners to be quantified. The application of IA techniques to compare cellular structure is still in a primitive state.

scholarly journals Application of Cryo-Electron Microscopy on Drug Discovery

2021 ◽  
Vol 27 (S1) ◽  
pp. 3250-3250
Author(s):  
Viswanath Vittaladevaram ◽  
Kranthi Kuruti
Keyword(s):  
Electron Microscopy ◽  
Protein Complexes ◽  
Lead Discovery ◽  
Biologically Relevant ◽  
Biological Targets ◽  
3 Dimensional ◽  
Drug Molecules ◽  
Cryo Electron Microscopy ◽  
Therapeutic Molecules ◽  
Novel Drug

AbstractThe key aspect for development of novel drug molecules is to perform structural determination of target molecule associated with its ligand. One such tool that provides insights towards structure of molecule is Cryo-electron microscopy which covers biological targets that are intractable. Examination of proteins can be carried out in native state, as the samples are frozen at -175 degree Celsius i.e. cryogenic temperatures. In addition to this, there were no limits for molecular and functional structures of proteins that can be imagined in 3-dimensional form. This includes ligands which unravel mechanisms that are biologically relevant. This will enable to better understand the mechanisms that are used for development of new therapeutics. Application of Cryo-electron microscopy is not limited to protein complexes and is considered as non-specific. Intervention of Cryo-EM would allow to analyse the structures and also able to dissect the interaction with therapeutic molecules. The study determines the usage of cryo-EM for providing resolutions that are acceptable for lead discovery. It also provides support for lead optimization and also for discovery of vaccines and therapeutics.

scholarly journals Tafazzins from Drosophila and mammalian cells assemble in large protein complexes with a short half-life

Mitochondrion ◽  
2015 ◽  
Vol 21 ◽  
pp. 27-32 ◽  
Author(s):  
Yang Xu ◽  
Ashim Malhotra ◽  
Steven M. Claypool ◽  
Mindong Ren ◽  
Michael Schlame
Keyword(s):  
Half Life ◽  
Mammalian Cells ◽  
Protein Complexes ◽  
Large Protein ◽  
Short Half Life

The structure of grease via electron microscopy and image analysis

1991 ◽  
Vol 4 (1) ◽  
pp. 35-50 ◽  
Author(s):  
P. J. Shuff ◽  
L. J. Clarke
Keyword(s):  
Electron Microscopy ◽  
Image Analysis
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