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Institution

University of Iowa

EducationIowa City, Iowa, United States
About: University of Iowa is a education organization based out in Iowa City, Iowa, United States. It is known for research contribution in the topics: Population & Poison control. The organization has 49229 authors who have published 109171 publications receiving 5021465 citations. The organization is also known as: UI & The University of Iowa.


Papers
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Journal ArticleDOI
TL;DR: In this article, a controlled experimental study was conducted to compare the performance on a brainstorming task between groups composed of all Anglo-Americans with groups ofAnglo-, Asian, African, and Hispanic Americans.
Abstract: There is a growing belief among managers that ethnic diversity, when well managed, can provide organizations with certain competitive advantages. But the belief in this value-inl diversity hypothesis rests largely on anecdotal rather than empirical evidence. Results are reported ofa controlled experimental study that compares the performance on a brainstorm ing task between groups composed of all Anglo-Americans with groups composed ofAnglo-, Asian, African, and Hispanic Americans. The particular brainstorming task used-The Tourist Problem-was chosenfor its relevancefordiversity along the dimension of ethnicity. The ideas produced by the ethnically diverse groups were judged to be of higher quality-more effective andfeasible-than the ideas produced by the homogeneous groups. Members of homogeneous groups reported marginally more attraction to their groups than did members of diverse oroups. Directions for future research with respect to the degree of diversity, the nature of the task, and group process ar...

745 citations

Journal ArticleDOI
Joseph Piven1, Pat Palmer1, Dinah Jacobi1, Debra Childress1, Stephan Arndt1 
TL;DR: Higher rates of social and communication deficits and stereotyped behaviors were found in the relatives in the families with multiple-incidence autism, suggesting that this broader autism phenotype should be included in some future genetic analyses of this disorder.
Abstract: Objective: Studies of families ascertained through a single autistic proband suggest that the genetic liability for autism may be expressed in nonautistic relatives in a phenotype that is milder but qualitatively similar to the defining features of autism. The objective of this study was to examine behaviors that may define this broader phenotype in relatives ascertained through two autistic siblings. Method: The authors used a semistructured family history interview to compare the rates of social and communication deficits and stereotyped behaviors in relatives ascertained through two autistic siblings (families with multiple-incidence autism; 25 families) with the rates in relatives of Down syndrome probands (30 families). Results: Higher rates of social and communication deficits and stereotyped behaviors were found in the relatives in the families with multiple-incidence autism. Conclusions: These data suggest that further studies should be undertaken to delineate the boundaries of the broader autism phenotype and that this broader phenotype should be included in some future genetic analyses of this disorder. (Am J Psychiatry 1997; 154:185‐190)

745 citations

Journal ArticleDOI
01 Sep 1982-Cell

741 citations

Journal ArticleDOI
26 Sep 2002-Nature
TL;DR: The POH1 (also known as Rpn11 in yeast) subunit of the 19S complex is responsible for substrate deubiquitination during proteasomal degradation and appears to be a Zn2+-dependent protease.
Abstract: The 26S proteasome is responsible for most intracellular proteolysis in eukaryotes. Efficient substrate recognition relies on conjugation of substrates with multiple ubiquitin molecules and recognition of the polyubiquitin moiety by the 19S regulatory complex--a multisubunit assembly that is bound to either end of the cylindrical 20S proteasome core. Only unfolded proteins can pass through narrow axial channels into the central proteolytic chamber of the 20S core, so the attached polyubiquitin chain must be released to allow full translocation of the substrate polypeptide. Whereas unfolding is rate-limiting for the degradation of some substrates and appears to involve chaperone-like activities associated with the proteasome, the importance and mechanism of degradation-associated deubiquitination has remained unclear. Here we report that the POH1 (also known as Rpn11 in yeast) subunit of the 19S complex is responsible for substrate deubiquitination during proteasomal degradation. The inability to remove ubiquitin can be rate-limiting for degradation in vitro and is lethal to yeast. Unlike all other known deubiquitinating enzymes (DUBs) that are cysteine proteases, POH1 appears to be a Zn(2+)-dependent protease.

741 citations


Authors

Showing all 49661 results

NameH-indexPapersCitations
Stephen V. Faraone1881427140298
Jie Zhang1784857221720
D. M. Strom1763167194314
Bradley T. Hyman169765136098
John H. Seinfeld165921114911
David Jonathan Hofman1591407140442
Stephen J. O'Brien153106293025
John T. Cacioppo147477110223
Mark Raymond Adams1471187135038
E. L. Barberio1431605115709
Andrew Ivanov142181297390
Stephen J. Lippard141120189269
Russell Richard Betts140132395678
Barry Blumenfeld1401909105694
Marcus Hohlmann140135694739
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Performance
Metrics
No. of papers from the Institution in previous years
YearPapers
2023154
2022727
20214,129
20203,902
20193,763
20183,659