Enhancing LGMD-based model for collision prediction via binocular structure.

Introduction: Lobular giant motion detector (LGMD) neurons, renowned for their distinctive response to looming stimuli, inspire the development of visual neural network models for collision prediction. However, the existing LGMD-based models could not yet incorporate the invaluable feature of depth distance and still suffer from the following two primary drawbacks. Firstly, they struggle to effectively distinguish the three fundamental motion patterns of approaching, receding, and translating, in contrast to the natural abilities of LGMD neurons. Secondly, due to their reliance on a general determination process employing an activation function and fixed threshold for output, these models exhibit dramatic fluctuations in prediction effectiveness across different scenarios. Methods: To address these issues, we propose a novel LGMD-based model with a binocular structure (Bi-LGMD). The depth distance of the moving object is extracted by calculating the binocular disparity facilitating a clear differentiation of the motion patterns, after obtaining the moving object's contour through the basic components of the LGMD network. In addition, we introduce a self-adaptive warning depth-distance, enhancing the model's robustness in various motion scenarios. Results: The effectiveness of the proposed model is verified using computer-simulated and real-world videos. Discussion: Furthermore, the experimental results demonstrate that the proposed model is robust to contrast and noise.

Indolent mucinous tubular and spindle cell carcinoma of the kidney: A case report and review of the literature.

Mucinous tubular and spindle cell carcinoma of the kidney (MTSCC) is a rare subtype of renal cancer. It consists of tubules separated by mucus stroma and a spindle cell. Few cases have been reported; thus, the imaging features of MTSCC are not well characterized. An MTSCC in the left kidney of a 65-year-old woman was incidentally discovered during a medical checkup. A review of the patient's medical history revealed that this kidney lump had an indolent growth process. The current study presented this case and reviewed the pathological features, imaging findings and treatment options of MTSCC to strengthen the recognition of this rare renal neoplasm by radiologists.

Efficient Degradation of Tetracycline Antibiotics by Engineered Myoglobin with High Peroxidase Activity.

Tetracyclines are one class of widely used antibiotics. Meanwhile, due to abuse and improper disposal, they are often detected in wastewater, which causes a series of environmental problems and poses a threat to human health and safety. As an efficient and environmentally friendly method, enzymatic catalysis has attracted much attention. In previous studies, we have designed an efficient peroxidase (F43Y/P88W/F138W Mb, termed YWW Mb) based on the protein scaffold of myoglobin (Mb), an O2 carrier, by modifying the heme active center and introducing two Trp residues. In this study, we further applied it to degrade the tetracycline antibiotics. Both UV-Vis and HPLC studies showed that the triple mutant YWW Mb was able to catalyze the degradation of tetracycline, oxytetracycline, doxycycline, and chlortetracycline effectively, with a degradation rate of ~100%, ~98%, ~94%, and ~90%, respectively, within 5 min by using H2O2 as an oxidant. These activities are much higher than those of wild-type Mb and other heme enzymes such as manganese peroxidase. As further analyzed by UPLC-ESI-MS, we identified multiple degradation products and thus proposed possible degradation mechanisms. In addition, the toxicity of the products was analyzed by using in vitro antibacterial experiments of E. coli. Therefore, this study indicates that the engineered heme enzyme has potential applications for environmental remediation by degradation of tetracycline antibiotics.

Calcium-dependent conformational transition of calmodulin determined by Fourier transform infrared spectroscopy.

The Ca(2+)-induced conformational changes in calmodulin (CaM) were monitored by Fourier transform infrared spectroscopy (FT-IR) at different molar ratios of Ca(2+) to CaM. The results show that these changes occur in two distinctive transitions. The first transition involves significant changes in the overall secondary structure with a small gain in solvent accessibility, and is completed after the second Ca(2+) binds to both EF-hands of its C-terminal domain. The second transition is accompanied by CaM folding into a tighter, less hydrogen-exchangeable structure, and is completed by the addition of the fourth Ca(2+) to have four Ca(2+) per molecule. Particularly, α-helices in CaM-nCa(2+)(n=0, 1, 2) are less stable than those in CaM-nCa(2+)(n=3, 4).

Calcium-induced changes in calmodulin structural dynamics and thermodynamics.

The thermodynamics of the interaction between Ca(2+) and calmodulin (CaM) was examined using isothermal titration calorimetry (ITC). The chemical denaturation of calmodulin was monitored spectroscopically to determine the stability of Ca(2+)-free (apo) and Ca(2+)-loaded (holo) CaMs. We explored the conformational and structural dynamics of CaM using amide hydrogen-deuterium (H-D) exchange coupled with Fourier transform infrared (FT-IR) spectroscopy. The results of H-D exchange and FT-IR suggest that CaM activation by Ca(2+) binding involves significant conformational changes. The results have also revealed that while the overall conformation of holo-CaM is more stable than that of the apo-CaM, some part of its α-helix structures, most likely the EF-hand domain region, has more solvent exposure, thus, has a faster H-D exchange rate than that of the apo-CaM. The ITC method provides a new strategy for obtaining site-specific Ca(2+) binding properties and a better estimation of the cooperativity and conformational change contributions of coupled EF-hand proteins.

Roles of hinge region, loops 3 and 4 in the activation of Escherichia coli cyclic AMP receptor protein.

The cAMP receptor protein (CRP) requires cAMP for an allosteric change and regulates more than 150 genes in Escherichia coli. In this study, the modular half of cAMP receptor protein was used to investigate the allosteric signal transmission pathway induced by cAMP binding. The activation of CRP upon cAMP binding is indicated to be realignment of the two subunits within the CRP dimer. The interaction of loop 3 and Phe136 do not involve in signal transmission.

The conformational change of rabbit muscle pyruvate kinase induced by activating cations and its substrates.

Catalysis by rabbit muscle pyruvate kinase involves domain movements and conformational changes induced by activating cations and its substrates. Fluorescence acrylamide quenching analyses reveal that interactions with Mg(2+) and K(+) lead to a more exposed active site of PK while interactions with PEP and ADP decrease solvent accessibility of the active site.