Institution
University of Iowa
Education•Iowa 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.
Topics: Population, Poison control, Large Hadron Collider, Health care, Gene
Papers published on a yearly basis
Papers
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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
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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
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743 citations
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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
Name | H-index | Papers | Citations |
---|---|---|---|
Stephen V. Faraone | 188 | 1427 | 140298 |
Jie Zhang | 178 | 4857 | 221720 |
D. M. Strom | 176 | 3167 | 194314 |
Bradley T. Hyman | 169 | 765 | 136098 |
John H. Seinfeld | 165 | 921 | 114911 |
David Jonathan Hofman | 159 | 1407 | 140442 |
Stephen J. O'Brien | 153 | 1062 | 93025 |
John T. Cacioppo | 147 | 477 | 110223 |
Mark Raymond Adams | 147 | 1187 | 135038 |
E. L. Barberio | 143 | 1605 | 115709 |
Andrew Ivanov | 142 | 1812 | 97390 |
Stephen J. Lippard | 141 | 1201 | 89269 |
Russell Richard Betts | 140 | 1323 | 95678 |
Barry Blumenfeld | 140 | 1909 | 105694 |
Marcus Hohlmann | 140 | 1356 | 94739 |