An Ran
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
An Ran has a total of 10 co-authors. Here are the top co-authors by number of shared publications:
- Anup Kollanoor Johny
Department of Animal Science, University of Minnesota, Saint Paul, MN 55108, USA
1 shared publication - Chunlai Zhang
State Key Laboratory of Earth Surface Processes and Disaster Risk Reduction Engineering Center of Desertification and Blown‐Sand Control of Ministry of Education Faculty of Geographical Science Beijing Normal University Beijing China
1 shared publication - Jiaqiong Zhang
State Key Laboratory of Soil and Water Conservation and Desertification Control, The Research Center of Soil and Water Conservation and Ecological Environment, Chinese Academy of Sciences and Ministry of Education, Xianyang 712100, China
1 shared publication - Jirui Gong
State Key Laboratory of Earth Surface Processes and Disaster Risk Reduction, Faculty of Geographical Science, MOE Engineering Research Center of Desertification and Blown-Sand Control, Faculty of Geographical Science, Beijing Normal University, Beijing, China
1 shared publication - Juan E. Abrahante
Research Informatics, Minnesota Supercomputing Institute, University of Minnesota, Minneapolis, USA
1 shared publication - Kent M. Reed
Department of Veterinary and Biomedical Sciences, University of Minnesota, St. Paul, MN, United States
1 shared publication
Latest Publications
- Open Access
Transcriptional Profiling and Molecular Characterization of the yccT Mutant Link: A Novel STY1099 Protein with the Peroxide Stress Response and Cell Division of Salmonella enterica Serovar Enteritidis
Uncharacterized protein STY1099, encoded by the yccT gene, was previously identified as the most altered (i.e., upregulated) protein among the ZnO nanoparticle (NP) stimulon of Salmonella enterica serovar Enteritidis. Here we combined various stress response-related assays with functional genetics, global transcriptomic and proteomic analyses to characterize the yccT gene and its STY1099 product. Exposure of S. enterica Enteritidis to H2O2 (i.e., hydrogen peroxide) resulted in a significant (p < 0.0001) upregulation of the yccT gene, whereas exposure to paraquat (i.e., superoxide) did not alter the expression of the yccT gene. The ∆yccT mutant of S. enterica Enteritidis exposed to 0.75 mM H2O2, showed significantly reduced (p < 0.05) viability compared to the wild type strain. Further, comparative transcriptome analyses supported by Co-immunoprecipitation (Co-IP) assay revealed that STY1099 protein plays a role in redox homeostasis during the peroxide stress assault via involvement in the processes of respiratory nitrate reductase, oxidoreductase activities, cellular uptake and stress response. In addition, we found that the STY1099 protein has the monopolar subcellular location and that it interacts with key cell division proteins, MinD, and FtsH, as well as with a rod shape-determining protein MerB.
Open AccessTranscriptional Profiling and Molecular Characterization of the yccT Mutant Link: A Novel STY1099 Protein with the Peroxide Stress Response and Cell Division of Salmonella enterica Serovar Enteritidis
Uncharacterized protein STY1099, encoded by the yccT gene, was previously identified as the most altered (i.e., upregulated) protein among the ZnO nanoparticle (NP) stimulon of Salmonella enterica serovar Enteritidis. Here we combined various stress response-related assays with functional genetics, global transcriptomic and proteomic analyses to characterize the yccT gene and its STY1099 product. Exposure of S. enterica Enteritidis to H2O2 (i.e., hydrogen peroxide) resulted in a significant (p < 0.0001) upregulation of the yccT gene, whereas exposure to paraquat (i.e., superoxide) did not alter the expression of the yccT gene. The ∆yccT mutant of S. enterica Enteritidis exposed to 0.75 mM H2O2, showed significantly reduced (p < 0.05) viability compared to the wild type strain. Further, comparative transcriptome analyses supported by Co-immunoprecipitation (Co-IP) assay revealed that STY1099 protein plays a role in redox homeostasis during the peroxide stress assault via involvement in the processes of respiratory nitrate reductase, oxidoreductase activities, cellular uptake and stress response. In addition, we found that the STY1099 protein has the monopolar subcellular location and that it interacts with key cell division proteins, MinD, and FtsH, as well as with a rod shape-determining protein MerB.
- Open Access
Ecophysiological Responses of Three Tree Species to a High-Altitude Environment in the Southeastern Tibetan Plateau
This paper measured the ecophysiological responses of Populus cathayana Rehd., Salix longistamina C. Wang et P. Y. Fu., and Ulmus pumila L. to high altitude in the Tibetan Plateau based on changes in water relations, gas exchange, and chlorophyll fluorescence. P. cathayana and U. pumila have higher survival rates than S. longistamina, but the latter has highest biomass. S. longistamina has higher water-use efficiency (WUE), lower transpiration rates (E), higher water potential (Ψ), highest light saturation point (LSP) and higher photosystem II (PSII) photochemistry efficiency (Fv’/Fm’) and non-photochemistry quenching (NPQ) than the other species, and is thus adapted to its habitat for afforestation. U. pumila has lower E, light compensation point (LCP), dark respiration (Rd), Fv’/Fm’ and electron transport rate (ETR), with higher Ψ, apparent quantum yield (AQY), net photosynthetic rate (Pn) and non-photochemical quenching (NPQ), which helps it maintain water balance and utilize weak light to survive at high altitude. Relative low WUE, Ψ, Rd, NPQ, with high E, Pn, Fv’/Fm’ and biomass, imply that P. cathayana is more suitable for shelterbelt forests than for a semi-arid habitat. These three species can adapt to high-altitude conditions by different physiological mechanisms and morphological characteristics, which can provide a theoretical basis for afforestation and forest management in the Qinghai Tibetan Plateau.
Open AccessEcophysiological Responses of Three Tree Species to a High-Altitude Environment in the Southeastern Tibetan Plateau
This paper measured the ecophysiological responses of Populus cathayana Rehd., Salix longistamina C. Wang et P. Y. Fu., and Ulmus pumila L. to high altitude in the Tibetan Plateau based on changes in water relations, gas exchange, and chlorophyll fluorescence. P. cathayana and U. pumila have higher survival rates than S. longistamina, but the latter has highest biomass. S. longistamina has higher water-use efficiency (WUE), lower transpiration rates (E), higher water potential (Ψ), highest light saturation point (LSP) and higher photosystem II (PSII) photochemistry efficiency (Fv’/Fm’) and non-photochemistry quenching (NPQ) than the other species, and is thus adapted to its habitat for afforestation. U. pumila has lower E, light compensation point (LCP), dark respiration (Rd), Fv’/Fm’ and electron transport rate (ETR), with higher Ψ, apparent quantum yield (AQY), net photosynthetic rate (Pn) and non-photochemical quenching (NPQ), which helps it maintain water balance and utilize weak light to survive at high altitude. Relative low WUE, Ψ, Rd, NPQ, with high E, Pn, Fv’/Fm’ and biomass, imply that P. cathayana is more suitable for shelterbelt forests than for a semi-arid habitat. These three species can adapt to high-altitude conditions by different physiological mechanisms and morphological characteristics, which can provide a theoretical basis for afforestation and forest management in the Qinghai Tibetan Plateau.