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Biology subjects

Denny, E.

Publications and source records attributed to Denny, E..

2 recordsLinked to original sources

PhenoVision: A framework for automating and delivering research-ready plant phenology data from field images

Plant phenology plays a fundamental role in shaping ecosystems, and global change-induced shifts in phenology have cascading impacts on species interactions and ecosystem structure and function. Detailed, high-quality observations of when plants undergo seasonal transitions such as leaf-out, flowering, and fruiting are critical for tracking causes and consequences of phenology shifts, but these data are often sparse and biased globally. These data gaps limit broader generalizations and forecasting improvements in the face of continuing disturbance. One solution to closing such gaps is to document phenology on field images taken by public participants. iNaturalist, in particular, provides global scale research-grade data and is expanding rapidly. Here we utilize over 53 million field images of plants and millions of human annotations from iNaturalist - data spanning all angiosperms and drawn from across the globe - to train a computer vision model (PhenoVision) to detect the presence of fruits and flowers. PhenoVision utilizes a vision transformer architecture pretrained with a masked autoencoder to improve classification success, and it achieves high accuracy for flower (98.5%) and fruit presence (95%). Key to producing research-ready phenology data is post-calibration tuning and validation focused on reducing noise inherent in field photographs, and maximizing the true positive rate. We also develop a standardized set of quality metrics and metadata so that results can be used effectively by the community. Finally, we showcase how this effort vastly increases phenology data coverage, including regions of the globe where data have been limited before. Our end products are tuned models, new data resources, and an application streamlining discovery and use of those data for the broader research and management community. We close by discussing next steps, including automating phenology annotations, adding new phenology targets, e.g., leaf phenology, and further integration with other resources to form a global central database integrating all in-situ plant phenology resources.

ecology↗

t-Darpp is an elongated monomer that binds to calcium and is phosphorylated by cyclin-dependent kinases 1 and 5

t-Darpp is a protein encoded by the PPP1R1B gene and is expressed in breast, colon, esophageal, gastric, and prostate cancers, as well as in normal adult brain striatal cells. Overexpression of t-Darpp in cultured cells leads to increased protein kinase A activity and increased phosphorylation of AKT (protein kinase B). In HER2+ breast cancer cells t-Darpp confers resistance to the chemotherapeutic agent trastuzumab. To shed light on t-Darpp function, we studied its secondary structure, oligomerization status, metal-binding properties, and phosphorylation by cyclin dependent kinases 1 and 5. t-Darpp exhibits 12% alpha helix, 29% beta strand, 24% beta turn and 35% random coil structures. t-Darpp binds to calcium, but not to other metals commonly found in biological systems. The T39 site, critical for t-Darpp activation of the AKT signaling pathway, is a substrate for phosphorylation by cyclin-dependent kinase 1 (CDK1) and cyclin-dependent kinase 5 (CDK5). Gel filtration chromatography, sedimentation equilibrium analysis, blue native gel electrophoresis, and glutaraldehyde-mediated crosslinking experiments demonstrate that the majority of t-Darpp exists as a monomer, but forms low levels (< 3%) of hetero-oligomers with its longer isoform Darpp-32. t-Darpp has a large Stokes radius of 4.4 nm relative to its mass of 19 kDa, indicating that it has an elongated structure.

biochemistry↗