KU ScholarWorks is the digital repository of the University of Kansas. It contains scholarly work created by KU faculty, staff and students, as well as material from the University Archives. KU ScholarWorks makes important research and historical items available to a wider audience and helps assure their long-term preservation.
On February 11, 2010 the KU Faculty Senate passed a revised Open Access policy granting the University permission to deposit a copy of their scholarly work in an open access repository-- KU ScholarWorks. For more about the policy, "how to" documents, Q&A, addenda and more, please visit Open Access @ KU.
For information about submitting to KU ScholarWorks please contact Marianne Reed, mreed@ku.edu. For information about KU ScholarWorks in general, please email kuscholarworks@ku.edu.
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un/reliable reflections: The burden of reliability and the refuge of unreliability
(2018-10)Under the umbrella title “un/reliable reflections,” the two parts address burnout by comparing expectations for the reliability of computing and of data librarians. The first part, “The Burden of Reliability,” invokes ... -
HuR-targeted small molecule inhibitor exhibits cytotoxicity towards human lung cancer cells
(Nature Research, 2017-08-30)Human antigen (Hu) R is an RNA-binding protein whose overexpression in human cancer correlates with aggressive disease, drug resistance, and poor prognosis. HuR inhibition has profound anticancer activity. Pharmacologic ... -
Human oncoprotein Musashi-2 N-terminal RNA recognition motif backbone assignment and identification of RNA-binding pocket
(Impact Journals, 2017-11-20)RNA-binding protein Musashi-2 (MSI2) is a key regulator in stem cells, it is over-expressed in a variety of cancers and its higher expression is associated with poor prognosis. Like Musashi-1, it contains two N-terminal ... -
Transformational dynamics of BZO and BHO nanorods imposed by Y2O3 nanoparticles for improved isotropic pinning in YBa2Cu3O7−δ thin films
(AIP Publishing, 2017)An elastic strain model was applied to evaluate the rigidity of the c-axis aligned one-dimensional artificial pinning centers (1D-APCs) in YBa2Cu3O7-δ matrix films. Higher rigidity was predicted for BaZrO3 1D-APCs than ... -
High-Definition Mapping of Four Spatially Distinct Neutralizing Epitope Clusters on RiVax, a Candidate Ricin Toxin Subunit Vaccine
(American Society for Microbiology, 2017-10-18)RiVax is a promising recombinant ricin toxin A subunit (RTA) vaccine antigen that has been shown to be safe and immunogenic in humans and effective at protecting rhesus macaques against lethal-dose aerosolized toxin exposure. ...
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