REDRAW - Diagrammatic Reasoning System for Qualitative Structural Analysis

Author(s):  
S. Tessler ◽  
Y. Iwasaki ◽  
K.H. Law
1996 ◽  
Vol 25 (2-3) ◽  
pp. 149-159 ◽  
Author(s):  
Shirley Tessler ◽  
Yumi Iwasaki ◽  
Kincho H. Law

2001 ◽  
Vol 12 (3) ◽  
pp. 299-324 ◽  
Author(s):  
JOHN HOWSE ◽  
FERNANDO MOLINA ◽  
JOHN TAYLOR ◽  
STUART KENT ◽  
JOSEPH YOSSI GIL

2005 ◽  
Vol 8 ◽  
pp. 145-194 ◽  
Author(s):  
John Howse ◽  
Gem Stapleton ◽  
John Taylor

AbstractThe use of diagrams in mathematics has traditionally been restricted to guiding intuition and communication. With rare exceptions such as Peirce's alpha and beta systems, purely diagrammatic formal reasoning has not been in the mathematician's or logician's toolkit. This paper develops a purely diagrammatic reasoning system of “spider diagrams” that builds on Euler, Venn and Peirce diagrams. The system is known to be expressively equivalent to first-order monadic logic with equality. Two levels of diagrammatic syntax have been developed: an ‘abstract’ syntax that captures the structure of diagrams, and a ‘concrete’ syntax that captures topological properties of drawn diagrams. A number of simple diagrammatic transformation rules are given, and the resulting reasoning system is shown to be sound and complete.


2019 ◽  
Vol 42 ◽  
Author(s):  
Daniel J. Povinelli ◽  
Gabrielle C. Glorioso ◽  
Shannon L. Kuznar ◽  
Mateja Pavlic

Abstract Hoerl and McCormack demonstrate that although animals possess a sophisticated temporal updating system, there is no evidence that they also possess a temporal reasoning system. This important case study is directly related to the broader claim that although animals are manifestly capable of first-order (perceptually-based) relational reasoning, they lack the capacity for higher-order, role-based relational reasoning. We argue this distinction applies to all domains of cognition.


Author(s):  
W. H. Wu ◽  
R. M. Glaeser

Spirillum serpens possesses a surface layer protein which exhibits a regular hexagonal packing of the morphological subunits. A morphological model of the structure of the protein has been proposed at a resolution of about 25 Å, in which the morphological unit might be described as having the appearance of a flared-out, hollow cylinder with six ÅspokesÅ at the flared end. In order to understand the detailed association of the macromolecules, it is necessary to do a high resolution structural analysis. Large, single layered arrays of the surface layer protein have been obtained for this purpose by means of extensive heating in high CaCl2, a procedure derived from that of Buckmire and Murray. Low dose, low temperature electron microscopy has been applied to the large arrays.As a first step, the samples were negatively stained with neutralized phosphotungstic acid, and the specimens were imaged at 40,000 magnification by use of a high resolution cold stage on a JE0L 100B. Low dose images were recorded with exposures of 7-9 electrons/Å2. The micrographs obtained (Fig. 1) were examined by use of optical diffraction (Fig. 2) to tell what areas were especially well ordered.


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