Macrophage+: a Game With a Purpose for Applying Human Intelligence in Control Mechanisms

2020 ◽  
Vol 0 (0) ◽  
pp. 0-0
Author(s):  
Ali Tarihi ◽  
Hassan Haghighi ◽  
Fereidoon Shams Aliee ◽  
Amirmehdi Setarenejad
2001 ◽  
Vol 120 (5) ◽  
pp. A502-A502
Author(s):  
R GAUTHIER ◽  
J DROLET ◽  
J REED ◽  
A VEZINA ◽  
P VACHON

1973 ◽  
Vol 18 (9) ◽  
pp. 416-417
Author(s):  
MARJORIE P. HONZIK
Keyword(s):  

1966 ◽  
Vol 11 (6) ◽  
pp. 317-317
Author(s):  
No authorship indicated
Keyword(s):  

2011 ◽  
Author(s):  
Frederick Verbruggen ◽  
Rachel Adams ◽  
Chris Chambers

1966 ◽  
Vol 05 (03) ◽  
pp. 142-146
Author(s):  
A. Kent ◽  
P. J. Vinken

A joint center has been established by the University of Pittsburgh and the Excerpta Medica Foundation. The basic objective of the Center is to seek ways in which the health sciences community may achieve increasingly convenient and economical access to scientific findings. The research center will make use of facilities and resources of both participating institutions. Cooperating from the University of Pittsburgh will be the School of Medicine, the Computation and Data Processing Center, and the Knowledge Availability Systems (KAS) Center. The KAS Center is an interdisciplinary organization engaging in research, operations, and teaching in the information sciences.Excerpta Medica Foundation, which is the largest international medical abstracting service in the world, with offices in Amsterdam, New York, London, Milan, Tokyo and Buenos Aires, will draw on its permanent medical staff of 54 specialists in charge of the 35 abstracting journals and other reference works prepared and published by the Foundation, the 700 eminent clinicians and researchers represented on its International Editorial Boards, and the 6,000 physicians who participate in its abstracting programs throughout the world. Excerpta Medica will also make available to the Center its long experience in the field, as well as its extensive resources of medical information accumulated during the Foundation’s twenty years of existence. These consist of over 1,300,000 English-language _abstract of the world’s biomedical literature, indexes to its abstracting journals, and the microfilm library in which complete original texts of all the 3,000 primary biomedical journals, monitored by Excerpta Medica in Amsterdam are stored since 1960.The objectives of the program of the combined Center include: (1) establishing a firm base of user relevance data; (2) developing improved vocabulary control mechanisms; (3) developing means of determining confidence limits of vocabulary control mechanisms in terms of user relevance data; 4. developing and field testing of new or improved media for providing medical literature to users; 5. developing methods for determining the relationship between learning and relevance in medical information storage and retrieval systems’; and (6) exploring automatic methods for retrospective searching of the specialized indexes of Excerpta Medica.The priority projects to be undertaken by the Center are (1) the investigation of the information needs of medical scientists, and (2) the development of a highly detailed Master List of Biomedical Indexing Terms. Excerpta Medica has already been at work on the latter project for several years.


1986 ◽  
Vol 56 (02) ◽  
pp. 151-154 ◽  
Author(s):  
Christina A Mitchell ◽  
Lena Hau ◽  
Hatem H Salem

SummaryThrombin has been shown to cleave the vitamin K dependent cofactor protein S with subsequent loss of its cofactor activity. This study examines the control mechanisms for thrombin cleavage of protein S.The anticoagulant activity of activated protein C (APC) is enhanced fourteen fold by the addition of protein S. Thrombin cleaved protein S is seven fold less efficient than the native protein, and this loss of activity is due to reduced affinity of cleaved protein S for APC or the lipid surface compared to the intact protein.In the absence of Ca++, protein S is very sensitive to minimal concentrations of thrombin. As little as 1.5 nM thrombin results in complete cleavage of 20 nM protein S in 10 min and loss of cofactor activity. Ca++, in concentrations greater than 0.5 mM, will inhibit this cleavage and in the presence of physiological Ca++ concentrations, no cleavage of protein S could be demonstrated in spite of high concentrations of thrombin (up to 1 μM) and prolonged incubations (up to two hours). The endothelial surface protein thrombomodulin is very efficient in inhibiting the cleavage of protein S by thrombin suggesting that any thrombin formed on the endothelial cell surface is unlikely to cleave protein S, thus allowing the intact protein to act as a cofactor to APC.We conclude that the inhibitory effects of Ca++ and thrombomodulin on thrombin mediated cleavage of protein S imply that this event, by itself, is unlikely to represent a physiological control of the activity of protein S.


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