Spatial Localization in Infancy: Position Constancy in a Square and Circular Room with and without a Landmark

1986 ◽  
Vol 57 (1) ◽  
pp. 115 ◽  
Author(s):  
M. B. Keating ◽  
B. E. McKenzie ◽  
R. H. Day
Keyword(s):  
Spatial Localization ◽  
Position Constancy

The Nature of Oxide Surfaces: Topographic and Electronic Structure

1993 ◽  
Vol 51 ◽  
pp. 966-967
Author(s):  
Dawn A. Bonnell ◽  
Yong Liang
Keyword(s):  
Transition Metal Oxides ◽  
Electronic Structures ◽  
Recent Progress ◽  
Spatial Localization ◽  
Level Of Detail ◽  
Scanning Tunneling ◽  
Oxide Surfaces ◽  
Tunneling Microscopy ◽  
Considerable Effort ◽  
Complete Understanding

Recent progress in the application of scanning tunneling microscopy (STM) and tunneling spectroscopy (STS) to oxide surfaces has allowed issues of image formation mechanism and spatial resolution limitations to be addressed. As the STM analyses of oxide surfaces continues, it is becoming clear that the geometric and electronic structures of these surfaces are intrinsically complex. Since STM requires conductivity, the oxides in question are transition metal oxides that accommodate aliovalent dopants or nonstoichiometry to produce mobile carriers. To date, considerable effort has been directed toward probing the structures and reactivities of ZnO polar and nonpolar surfaces, TiO2 (110) and (001) surfaces and the SrTiO3 (001) surface, with a view towards integrating these results with the vast amount of previous surface analysis (LEED and photoemission) to build a more complete understanding of these surfaces. However, the spatial localization of the STM/STS provides a level of detail that leads to conclusions somewhat different from those made earlier.

Spatial localization of unknown proteins in the endoplasmic reticulum predicts functions

2007 ◽  
Vol 30 (4) ◽  
pp. 84
Author(s):  
Michael D. Jain ◽  
Hisao Nagaya ◽  
Annalyn Gilchrist ◽  
Miroslaw Cygler ◽  
John J.M. Bergeron
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Folding ◽  
Protein Synthesis ◽  
Protein Function ◽  
Protein Translocation ◽  
Spatial Localization ◽  
Predict Protein Function ◽  
Insight Into ◽  
Soluble Fractions ◽  
Er Membrane

Protein synthesis, folding and degradation functions are spatially segregated in the endoplasmic reticulum (ER) with respect to the membrane and the ribosome (rough and smooth ER). Interrogation of a proteomics resource characterizing rough and smooth ER membranes subfractionated into cytosolic, membrane, and soluble fractions gives a spatial map of known proteins involved in ER function. The spatial localization of 224 identified unknown proteins in the ER is predicted to give insight into their function. Here we provide evidence that the proteomics resource accurately predicts the function of new proteins involved in protein synthesis (nudilin), protein translocation across the ER membrane (nicalin), co-translational protein folding (stexin), and distal protein folding in the lumen of the ER (erlin-1, TMX2). Proteomics provides the spatial localization of proteins and can be used to accurately predict protein function.

scholarly journals A Four-point three-dimensional spatial localization algorithm based on RSSI

2020 ◽  
Vol 1550 ◽  
pp. 032022
Author(s):  
Li Ma ◽  
Ning Cao ◽  
Minghe Mao ◽  
Jianping Zhang
Keyword(s):  
Three Dimensional ◽  
Spatial Localization ◽  
Localization Algorithm

(VS-107)POSITION CONSTANCY, ACCOMMODATION, AND APPARENT DISTANCE

2000 ◽  
Vol 77 (SUPPLEMENT) ◽  
pp. 235
Author(s):  
Kay Fisher ◽  
Glen McCormack
Keyword(s):  
Apparent Distance ◽  
Position Constancy

Aging and Spatial Localization during Feature Search

Gerontology ◽  
2000 ◽  
Vol 46 (6) ◽  
pp. 300-305 ◽  
Author(s):  
Cynthia Owsley ◽  
Kerri Burton-Danner ◽  
Gregory R. Jackson
Keyword(s):  
Spatial Localization ◽  
Feature Search
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