Computer-aided methods for 3-D visualization of serial sections and thick biological specimens

1992 ◽  
Vol 50 (2) ◽  
pp. 1060-1061
Author(s):  
Mark Ellisman ◽  
Maryann Martone ◽  
Gabriel Soto ◽  
Eleizer Masliah ◽  
David Hessler ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Three Dimensional ◽  
Neuritic Plaque ◽  
Dimensional Structure ◽  
Data Sets ◽  
Molecular Physiology ◽  
Research Activities ◽  
Computer Aided ◽  
Dimensional Reconstruction

Structurally-oriented biologists examine cells, tissues, organelles and macromolecules in order to gain insight into cellular and molecular physiology by relating structure to function. The understanding of these structures can be greatly enhanced by the use of techniques for the visualization and quantitative analysis of three-dimensional structure. Three projects from current research activities will be presented in order to illustrate both the present capabilities of computer aided techniques as well as their limitations and future possibilities.The first project concerns the three-dimensional reconstruction of the neuritic plaques found in the brains of patients with Alzheimer's disease. We have developed a software package “Synu” for investigation of 3D data sets which has been used in conjunction with laser confocal light microscopy to study the structure of the neuritic plaque. Tissue sections of autopsy samples from patients with Alzheimer's disease were double-labeled for tau, a cytoskeletal marker for abnormal neurites, and synaptophysin, a marker of presynaptic terminals.

scholarly journals Identification of biomolecules for Alzheimer's disease using docking analysis of tau protein

2021 ◽  
pp. 192-203
Author(s):  
Mansi Agrahari ◽  
Kanu Megha ◽  
Kajal Dahiya ◽  
Ila Sharma ◽  
Ankur Sharma ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Tau Protein ◽  
Active Site ◽  
Protein A ◽  
Three Dimensional ◽  
Docking Studies ◽  
Dimensional Structure ◽  
Docking Analysis ◽  
Bioinformatic Tools

Objective: In-silico methods to find and characterize the ligands against the active site of tau protein which could assist in the therapeutics of Alzheimer's disease. Methods: The aid of various bioinformatic tools such as phylogenetic analysis, homology modeling, and active site prediction led to the molecular docking analysis of the major malefactor for Alzheimer’s disease ‘microtubule- associated tau protein’. A three-dimensional structure of microtubule-related tau protein was created, and the Ramachandran plot was acquired for quality appraisal. Results: Procheck showed 62.95 of residues in the most preferred region with 20% residues in the additional allowed region and 5.7 % in the disallowed region of microtubule-associated tau protein. Screenings of the particles were done dependent on Lipinski's standard of five. Conclusion: Genistein, Hesperidin, and epigallocatechin-3 are the potential ligands in regulating microtubule-related tau protein and Epigallocatechin-3 gallate is the most potent among them and the most elevated negative free vitality of official with the maximum interacting surface territory throughout docking studies.

P-105: Three-dimensional reconstruction of histological sections and correlations with MRI from transgenic models of Alzheimer's disease

2007 ◽  
Vol 3 (3S_Part_2) ◽  
pp. S132-S132
Author(s):  
M. Mallar Chakravarty ◽  
Barry J. Bedell ◽  
Simone P. Zehntner ◽  
Kurt Hemmings ◽  
Edith Hamel ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Three Dimensional ◽  
Transgenic Models ◽  
Three Dimensional Reconstruction ◽  
Histological Sections ◽  
Dimensional Reconstruction

scholarly journals ALZHEIMER’S DISEASE THERAPEUTIC APPROACHES

2018 ◽  
Vol 11 (7) ◽  
pp. 17
Author(s):  
Sandhya A ◽  
Gomathi Kannayiram
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Protein Misfolding ◽  
Amyloid Fibrils ◽  
Adult Population ◽  
Three Dimensional ◽  
Lewy Bodies ◽  
Cerebral Hypoperfusion ◽  
Dimensional Structure ◽  
Islet Amyloid

A protein is a large biomolecule which consists of one or more chains of amino acid residues. Proteins exhibit a biological phenomenon in which, they are misfolded as aggregates (i.e., accumulate and clump together) either intra- or extracellularly. This process plays a central role in the pathogenesis of Alzheimer’s disease (AD) and diabetes mellitus (DM) - 2 and common for many degenerative diseases. In this case, the histopathological consequences of protein misfolding such as sensile plaques and neurofibrillary tangles in AD and lewy bodies in Parkinson’s disease occur. 8–10% of adult population shares risk factors with AD. Amyloid fibrils which build up in tissue as an abnormal protein form Amyloidosis. Conformational change in three-dimensional structure forms amyloid fibrils. Type 2 DM is characterized by the deposition of islet amyloid polypeptide within beta cells of the pancreas which leads to chronic cerebral hypoperfusion that result in degeneration of neuroglial cells.

scholarly journals Orexin A peptidergic system: Comparative physiology, morphology and population between brains of nomal and Alzheimer’s disease mice

2021 ◽  
Author(s):  
Peng Zhao ◽  
Yaqian You ◽  
Zhe Wang ◽  
Yanjun Zhou ◽  
Gaoshang Chai ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Three Dimensional ◽  
Amyloid Β ◽  
Nrem Sleep ◽  
Poor Sleep ◽  
Anterior Fontanelle ◽  
Orexin A ◽  
Innovative Methods ◽  
Dimensional Reconstruction

Abstract Sleep disturbance is common in patients with Alzheimer’s disease (AD), and orexin A is a pivotal neurotransmitter for bidirectional regulating the amyloid-β (Aβ) deposition of AD brain and poor sleep. In the present study, we examined the characteristic of sleep-wake architecture in APPswe/PSldE9 (APP/PS1) and Aβ-treated mice using electroencephalogram (EEG) and electromyographic (EMG) analysis. We compared the expression of orexin A, distribution, and morphology of the corresponding orexin A neurons using innovative methods including three-dimensional reconstruction and brain tissue clearing between Wild type (WT) and APP/PS1 mice. Results from our study demonstrated that increased wakefulness and reduced NREM sleep were seen in APP/PS1 and Aβ treated mice while the expression of orexin A was significantly upregulated. Higher density and distribution of orexin A activated neurons were seen in APP/PS1 mice, with a location of 1.06 mm to 2.30 mm away from the anterior fontanelle compared to 1.34 mm to 2.18 mm away from the anterior fontanelle in WT mice. These results suggested that the population and distribution of orexin A may play an important role in the progression of AD.

Computer-aided image analysis and graphics in biological microscopy at higher voltages

1991 ◽  
Vol 49 ◽  
pp. 438-439
Author(s):  
B. Carragher ◽  
D. F. Hessler ◽  
J. E. Hinshaw ◽  
M. Martone ◽  
R. A. Milligan ◽  
...  
Keyword(s):  
Biological Sciences ◽  
Imaging Techniques ◽  
Three Dimensional ◽  
Molecular Physiology ◽  
The Past ◽  
Software Packages ◽  
Wide Range ◽  
Computer Aided ◽  
Dimensional Reconstruction ◽  
Insight Into

The range of problems accessible to study using high voltage microscopy encompasses structures that span a wide range of dimensions from Angstroms to tens of microns. Structurally oriented cell biologists and neurobiologists examine cells, tissues, organelles and macromolecules in order to gain insight into cellular and molecular physiology by relating structure to function. Comprehension of these structures can be greatly enhanced by the application of computer aided three dimensional reconstruction and analysis techniques.The past decade has seen an explosive growth in the capabilities for the digital acquisition of images. At the same time, the availability of relatively inexpensive graphics workstations and sophisticated image processing and analysis software packages has made graphics and imaging techniques accessible to most research laboratories. However, the complexity of problems studied in the biological sciences has always presented a challenge to the techniques used in the analysis, and methods based on computer graphics are certainly no exception to this rule.

Three-Dimensional Reconstruction Using Stereo Pairs from Serial Thick Sections

1977 ◽  
Vol 35 ◽  
pp. 562-563
Author(s):  
Robert Glaeser ◽  
Thomas Bauer ◽  
David Grano
Keyword(s):  
Three Dimensional ◽  
Dimensional Structure ◽  
Serial Sections ◽  
Thin Sections ◽  
3 Dimensional ◽  
Transmission Electron ◽  
Freeze Dried ◽  
Dimensional Reconstruction ◽  
Stereo Imagery ◽  
Whole Mounts

In transmission electron microscopy, the 3-dimensional structure of an object is usually obtained in one of two ways. For objects which can be included in one specimen, as for example with elements included in freeze- dried whole mounts and examined with a high voltage microscope, stereo pairs can be obtained which exhibit the 3-D structure of the element. For objects which can not be included in one specimen, the 3-D shape is obtained by reconstruction from serial sections. However, without stereo imagery, only detail which remains constant within the thickness of the section can be used in the reconstruction; consequently, the choice is between a low resolution reconstruction using a few thick sections and a better resolution reconstruction using many thin sections, generally a tedious chore. This paper describes an approach to 3-D reconstruction which uses stereo images of serial thick sections to reconstruct an object including detail which changes within the depth of an individual thick section.

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