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Kenyon College: Digital Kenyon - Research, Scholarship, and Creative Exchange
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    The Impact of Increasing Salinity on Phaseolus vulgaris

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    Effect of nitrogen fertlisation on Sorghum bicolor

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    Human Proximity Has No Significant Influence on Pika (Ochotona princeps) Gut Microbiome Diversity In Glacier National Park

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    Effect of pH on the Pulse Rate of Lumbriculus variegatus

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    Kenyon Collegian - September 11, 2025

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    https://digital.kenyon.edu/collegian/3661/thumbnail.jp

    Regarding Chinese Conceptual Art (Essay)

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    This is an essay, titled On Conceptual Art in China, written by the Paris-based art critic about the origin and state of Chinese Conceptual Art. The corresponding document is an abstract of the essay written by Zhou Yan. (Nicole Wang \u2726).https://digital.kenyon.edu/zhoudocs/1508/thumbnail.jp

    Blue Mosque, Interior

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    https://digital.kenyon.edu/arthistorystudycollection/2738/thumbnail.jp

    Blue Mosque

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    https://digital.kenyon.edu/arthistorystudycollection/2748/thumbnail.jp

    Miliaresion of Romanos III

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    The obverse of this coin depicts a full-length, standing portrait of the Virgin turned slightly to the right. She is nimbate (haloed) and wearing a tunic and maphorion (veil). The Virgin also stands on a dais. In her left arm she is holding the infant Christ, who raises his right hand in the benediction. The infant holds a scroll in his left hand. The Virgin’s right hand rests on her breast. The figures are surrounded by an inscription of Greek letters and a decorative border. The reverse of this coin depicts a full-length portrait of the emperor Romanos III standing on a round cushion, bearded, wearing a crown with a cross and pendilia (gemmed pendants). He also wears a modified loros (long decorated scarf). In his right hand, Romanos holds a long patriarchal cross, and in his left hand, a globe surmounted by a cross. The same decorative border as on the obverse encircles him. Sonia Suben 2025https://digital.kenyon.edu/arthistorystudycollection/2711/thumbnail.jp

    Characterization of functionally important residues in the transport mechanism of Aedes aegypti cation chloride cotransporter 2 (aeCCC2)

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    Aedes aegypti cation chloride cotransporter 2 (aeCCC2) belongs to a family of Na+-dependent cation chloride cotransporters which includes Na+-K+-2Cl- (NKCC) cotransporters (Duong et al. 2022). Despite high sequence similarity to the electroneutral NKCCs, aeCCC2 transports ions electrogenically, suggesting a transport mechanism that has differentiated from the NKCCs (Kalsi et al. 2019). In this thesis, we use site-directed mutagenesis and a Xenopus laevis expression system to explore residue-specific contributions to the transport properties of aeCCC2 in order to further investigate its transport mechanism. We found that aeCCC2-mediated transport saturated at low extracellular ion concentrations. Furthermore, single mutations at ion-binding residues L155 or W158 decreased ion affinity three to four-fold, while constructs carrying mutations at both L155 and W158 had a ten-fold decrease in ion affinity. aeCCC2 mutants had decreased Li+ uptake rates and increased Rb+ uptake rates in comparison to aeCCC2 WT. In fact, the Li+:Rb+ uptake rate ratio was roughly two to four-fold lower than aeCCC2 WT in aeCCC2 mutants. To explore the effects of hypotonic activation on aeCCC2-mediated transport, we measured the ion affinity of aeCCC2 in response to hypotonic stimulation, as well as the Li+ transport rate of aeCCC2 constructs carrying mutations at the predicted SPS/Ste20 proline-alanine-rich kinase (SPAK)-binding site. Hypotonic activation does not alter the ion affinity of aeCCC2, and aeCCC2-mediated Li+ uptake is abolished in kinase-binding mutants. Altogether, these results suggest a carrier-like mechanism of aeCCC2-mediated transport that is dependent on basal activation by the with no lysine (WNK)/SPAK kinase complex, where L155 and W158 both contribute to ion binding and may contribute to ion selectivity

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    Kenyon College: Digital Kenyon - Research, Scholarship, and Creative Exchange
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