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Fabry, M.

Publications and source records attributed to Fabry, M..

2 recordsLinked to original sources

Semi-automated identification of southern right whales from drone imagery by classical image matching methods

Individual southern right whales (Eubalaena australis) can be identified from the callosity pattern on the head, a stable pattern of roughened keratinized patches. Manual comparison of drone images with large catalogs, however, is time-consuming. For southern right whales, automated photo-identification approaches typically require substantial training data or retraining when new individuals are added. Here we evaluate two classical image-similarity methods for individual identification from standardized dorsal head images: histograms of oriented gradients (HOG), and symmetric log-chamfer distance. We tested 375 query images from 198 known whales with recurrent sightings against 411 reference images, one for each individual whale. HOG ranked the correct whale first in 361 of 375 cases (96.3%), whereas log-chamfer ranked the correct whale first in 355 cases (94.7%). All incorrect rank-1 matches could be identified by a high risk score computed from query-reference distance distributions. A combined rule selecting the first-ranked candidate from the method with the lower risk score increased rank-1 accuracy to 368 cases (98.1%). These results show that classical registered image matching provides a practical tool for southern right whale photo-identification.

ecology↗

N-glycosylation blocks and simultaneously fosters different receptor-ligand binding sites: the chameleonic CD44-hyaluronan interaction

While DNA encodes protein structure, glycans provide a complementary layer of information to protein function. As a prime example of the significance of glycans, the ability of the cell surface receptor CD44 to bind its ligand, hyaluronan, is modulated by N-glycosylation. However, the details of this modulation remain unclear. Based on atomistic simulations and NMR, we provide evidence that CD44 has multiple distinct binding sites for hyaluronan, and that N-glycosylation modulates their respective roles. We find that non-glycosylated CD44 favors the canonical sub-micromolar binding site, while glycosylated CD44 binds hyaluronan with an entirely different micromolar binding site. Our findings show (for the first time) how glycosylation can alter receptor affinity by shielding specific regions of the host protein, thereby promoting weaker binding modes. The mechanism revealed in this work emphasizes the importance of glycosylation in protein function and poses a challenge for protein structure determination where glycosylation is usually neglected.

molecular biology↗