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Institution

Indiana University

EducationBloomington, Indiana, United States
About: Indiana University is a education organization based out in Bloomington, Indiana, United States. It is known for research contribution in the topics: Population & Poison control. The organization has 64480 authors who have published 150058 publications receiving 6392902 citations. The organization is also known as: Indiana University system & indiana.edu.


Papers
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Journal ArticleDOI
26 Jan 2001-Science
TL;DR: The scope of mental development includes cognitive, behavioral, emotional, and all other mental capabilities that are exhibited by humans, higher animals, and artificial systems as discussed by the authors, which is a fundamental change from the traditional paradigm for constructing intelligent machines.
Abstract: The scope of mental development includes cognitive, behavioral, emotional, and all other mental capabilities that are exhibited by humans, higher animals, and artificial systems. Computational principles of autonomous mental development in humans and the synthesis of developmental programs for robots and other artificial systems are beginning to be actively studied. Robots that develop their mental skills autonomously represent a fundamental change from the traditional paradigm for constructing intelligent machines. Support for this new field should lead to advances in science, engineering, economy, and understanding of the mind.

629 citations

Journal ArticleDOI
TL;DR: A new and more robust evolutionary synthesis is emerging that attempts to explain macroevolution as well as microevolutionary events, and the morphogenetic field is seen as a major unit of ontogeny whose changes bring about changes in evolution.

629 citations

Journal ArticleDOI
01 Mar 1983-Vacuum
TL;DR: In this article, the relative sensitivities of a Bayard-alpert ionization gauge for various organic molecules have been measured and a good correlation with total ionization cross section at 75 eV was found.

628 citations

Journal ArticleDOI
Joseph Adams1, C. Adler2, Madan M. Aggarwal3, Zubayer Ahammed4  +364 moreInstitutions (39)
TL;DR: High statistics measurements of inclusive charged hadron production in Au+Au and p+p collisions at sqrt[s(NN)]=200 GeV report no evidence of p(T)-dependent suppression, which may be expected from models incorporating jet attenuation in cold nuclear matter or scattering of fragmentation hadrons.
Abstract: We report high statistics measurements of inclusive charged hadron production in Au+Au and p+p collisions at rootS(NN)=200 GeV. A large, approximately constant hadron suppression is observed in central Au+Au collisions for 5

628 citations

Journal ArticleDOI
TL;DR: Variable activity of these P450s, brought about by genetic polymorphisms and drug interactions, may alter the balance of TAM effects in vivo.
Abstract: We performed comprehensive kinetic, inhibition, and correlation analyses in human liver microsomes and experiments in expressed human cytochromes P450 (P450s) to identify primary and secondary metabolic routes of tamoxifen (TAM) and the P450s catalyzing these reactions at therapeutically relevant concentrations. N-Desmethyl-TAM formation catalyzed by CYP3A4/5 was quantitatively the major primary metabolite of TAM; 4-hydroxy-TAM formation catalyzed by CYP2D6 (and other P450s) represents a minor route. Other minor primary metabolites include alpha -, 3-, and 4'-hydroxyTAM and one unidentified metabolite (M-I) and were primarily catalyzed by CYP3A4, CYP3A5, CYP2B6/2C19, and CYP3A4, respectively. TAM secondary metabolism was examined using N-desmethyl- and 4-hydroxy-TAM as intermediate substrates. N-Desmethyl-TAM was predominantly biotransformed to alpha-hydroxy N-desmethyl-, N-didesmethyl-, and 4-hydroxy N-desmethyl-TAM (endoxifen), whereas 4-hydroxy-TAM was converted to 3,4-dihydroxyTAM and endoxifen. Except for the biotransformation of N-desmethyl-TAM to endoxifen, which was exclusively catalyzed by CYP2D6, all other routes of N-desmethyl- and 4-hydroxy-TAM biotransformation were catalyzed predominantly by the CYP3A subfamily. TAM and its primary metabolites undergo extensive oxidation, principally by CYP3A and CYP2D6 to metabolites that exhibit a range of pharmacological effects. Variable activity of these P450s, brought about by genetic polymorphisms and drug interactions, may alter the balance of TAM effects in vivo.

628 citations


Authors

Showing all 64884 results

NameH-indexPapersCitations
Frank B. Hu2501675253464
Stuart H. Orkin186715112182
Bruce M. Spiegelman179434158009
David R. Williams1782034138789
D. M. Strom1763167194314
Markus Antonietti1761068127235
Lei Jiang1702244135205
Brenda W.J.H. Penninx1701139119082
Nahum Sonenberg167647104053
Carl W. Cotman165809105323
Yang Yang1642704144071
Jaakko Kaprio1631532126320
Ralph A. DeFronzo160759132993
Gavin Davies1592036149835
Tyler Jacks158463115172
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Performance
Metrics
No. of papers from the Institution in previous years
YearPapers
2023127
2022694
20217,273
20207,310
20196,943
20186,496