Recovering three-dimensional velocity and establishing stereo correspondence from binocular image flows

1995 ◽  
Vol 34 (7) ◽  
pp. 2157 ◽  
Author(s):  
Lingxiao Li
Keyword(s):  
Three Dimensional ◽  
Stereo Correspondence

scholarly journals Disparity processing in primary visual cortex

2016 ◽  
Vol 371 (1697) ◽  
pp. 20150255 ◽  
Author(s):  
Sid Henriksen ◽  
Seiji Tanabe ◽  
Bruce Cumming
Keyword(s):  
Visual Cortex ◽  
Primary Visual Cortex ◽  
Striate Cortex ◽  
Three Dimensional ◽  
Empirical Support ◽  
Energy Model ◽  
Correspondence Problem ◽  
Stereo Correspondence ◽  
V1 Neurons ◽  
The Right

The first step in binocular stereopsis is to match features on the left retina with the correct features on the right retina, discarding ‘false’ matches. The physiological processing of these signals starts in the primary visual cortex, where the binocular energy model has been a powerful framework for understanding the underlying computation. For this reason, it is often used when thinking about how binocular matching might be performed beyond striate cortex. But this step depends critically on the accuracy of the model, and real V1 neurons show several properties that suggest they may be less sensitive to false matches than the energy model predicts. Several recent studies provide empirical support for an extended version of the energy model, in which the same principles are used, but the responses of single neurons are described as the sum of several subunits, each of which follows the principles of the energy model. These studies have significantly improved our understanding of the role played by striate cortex in the stereo correspondence problem. This article is part of the themed issue ‘Vision in our three-dimensional world’.

Computational studies of the extraction of visual spatial information from binocular and motion cues

1988 ◽  
Vol 66 (4) ◽  
pp. 464-477 ◽  
Author(s):  
Ellen C. Hildreth
Keyword(s):  
Computational Models ◽  
Spatial Information ◽  
Experimental Studies ◽  
Three Dimensional ◽  
Stereo Correspondence ◽  
Motion Cues ◽  
Visual Spatial ◽  
Binocular Stereo ◽  
Dimensional Shape ◽  
Three Dimensional Shape

This paper reviews some of the contributions that work in computational vision has made to the study of biological vision systems. We concentrate on two areas where there has been strong interaction between computational and experimental studies: the use of binocular stereo to recover the distances to surfaces in space, and the recovery of the three-dimensional shape of objects from relative motion in the image. With regard to stereo, we consider models proposed for solving the stereo correspondence problem, focussing on the way in which physical properties of the world constrain possible methods of solution. We also show how critical observations regarding human stereo vision have helped to shape these models. With regard to the recovery of structure from motion, we focus on how the constraint of object rigidity has been used in computational models of this process.

The orbit of Pluto over a long interval of time

1966 ◽  
Vol 25 ◽  
pp. 227-229 ◽  
Author(s):  
D. Brouwer
Keyword(s):  
Periodic Orbit ◽  
Numerical Integration ◽  
Restricted Problem ◽  
Three Dimensional ◽  
The Third ◽  
Circular Restricted Problem ◽  
Resonance Relation

The paper presents a summary of the results obtained by C. J. Cohen and E. C. Hubbard, who established by numerical integration that a resonance relation exists between the orbits of Neptune and Pluto. The problem may be explored further by approximating the motion of Pluto by that of a particle with negligible mass in the three-dimensional (circular) restricted problem. The mass of Pluto and the eccentricity of Neptune's orbit are ignored in this approximation. Significant features of the problem appear to be the presence of two critical arguments and the possibility that the orbit may be related to a periodic orbit of the third kind.

Conformation of Ribosomes from Escherichia Coli

1974 ◽  
Vol 32 ◽  
pp. 210-211
Author(s):  
M. Boublik ◽  
W. Hellmann ◽  
F. Jenkins
Keyword(s):  
Binding Sites ◽  
Ribosomal Proteins ◽  
Fluorescent Dyes ◽  
Protein Biosynthesis ◽  
Three Dimensional ◽  
Spatial Arrangement ◽  
Dimensional Structure ◽  
Complete Understanding ◽  
And Function

The present knowledge of the three-dimensional structure of ribosomes is far too limited to enable a complete understanding of the various roles which ribosomes play in protein biosynthesis. The spatial arrangement of proteins and ribonuclec acids in ribosomes can be analysed in many ways. Determination of binding sites for individual proteins on ribonuclec acid and locations of the mutual positions of proteins on the ribosome using labeling with fluorescent dyes, cross-linking reagents, neutron-diffraction or antibodies against ribosomal proteins seem to be most successful approaches. Structure and function of ribosomes can be correlated be depleting the complete ribosomes of some proteins to the functionally inactive core and by subsequent partial reconstitution in order to regain active ribosomal particles.

Ultrastructural Investigations of the Contractile Filaments of Amoebae

1974 ◽  
Vol 32 ◽  
pp. 188-189
Author(s):  
P.L. Moore
Keyword(s):  
Cytoplasmic Streaming ◽  
Three Dimensional ◽  
Freeze Fracture ◽  
Amoeboid Movement ◽  
Different Types ◽  
Chemical Conditions ◽  
Complete Interpretation

Previous freeze fracture results on the intact giant, amoeba Chaos carolinensis indicated the presence of a fibrillar arrangement of filaments within the cytoplasm. A complete interpretation of the three dimensional ultrastructure of these structures, and their possible role in amoeboid movement was not possible, since comparable results could not be obtained with conventional fixation of intact amoebae. Progress in interpreting the freeze fracture images of amoebae required a more thorough understanding of the different types of filaments present in amoebae, and of the ways in which they could be organized while remaining functional.The recent development of a calcium sensitive, demembranated, amoeboid model of Chaos carolinensis has made it possible to achieve a better understanding of such functional arrangements of amoeboid filaments. In these models the motility of demembranated cytoplasm can be controlled in vitro, and the chemical conditions necessary for contractility, and cytoplasmic streaming can be investigated. It is clear from these studies that “fibrils” exist in amoeboid models, and that they are capable of contracting along their length under conditions similar to those which cause contraction in vertebrate muscles.

Structural organization of escherichia coli ribosomes as determined by immuno electron microscopy

1978 ◽  
Vol 36 (2) ◽  
pp. 166-167 ◽  
Author(s):  
G. Stöffler ◽  
R.W. Bald ◽  
J. Dieckhoff ◽  
H. Eckhard ◽  
R. Lührmann ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Escherichia Coli ◽  
Ribosomal Proteins ◽  
Structural Organization ◽  
Three Dimensional ◽  
Ribosomal Subunit ◽  
Spatial Arrangement ◽  
Small Subunit ◽  
Antibody Binding ◽  
Immuno Electron Microscopy

A central step towards an understanding of the structure and function of the Escherichia coli ribosome, a large multicomponent assembly, is the elucidation of the spatial arrangement of its 54 proteins and its three rRNA molecules. The structural organization of ribosomal components has been investigated by a number of experimental approaches. Specific antibodies directed against each of the 54 ribosomal proteins of Escherichia coli have been performed to examine antibody-subunit complexes by electron microscopy. The position of the bound antibody, specific for a particular protein, can be determined; it indicates the location of the corresponding protein on the ribosomal surface.The three-dimensional distribution of each of the 21 small subunit proteins on the ribosomal surface has been determined by immuno electron microscopy: the 21 proteins have been found exposed with altogether 43 antibody binding sites. Each one of 12 proteins showed antibody binding at remote positions on the subunit surface, indicating highly extended conformations of the proteins concerned within the 30S ribosomal subunit; the remaining proteins are, however, not necessarily globular in shape (Fig. 1).

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