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Researcher profile

Xiaoliang Ma

Xiaoliang Ma contributes to research discovery and scholarly infrastructure.

ResearcherAffiliation not importedOpen to collaborate
BiomoleculesCell BehaviorComputer Vision

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Published work

5 published item(s)

preprint2026arXiv

Graph-based Semantic Calibration Network for Unaligned UAV RGBT Image Semantic Segmentation and A Large-scale Benchmark

Fine-grained RGBT image semantic segmentation is crucial for all-weather unmanned aerial vehicle (UAV) scene understanding. However, UAV RGBT image semantic segmentation faces two coupled challenges: cross-modal spatial misalignment caused by sensor parallax and platform vibration, and severe semantic confusion among fine-grained ground objects under top-down aerial views. To address these issues, we propose a Graph-based Semantic Calibration Network (GSCNet) for unaligned UAV RGBT image semantic segmentation. Specifically, we design a Feature Decoupling and Alignment Module (FDAM) that decouples each modality into shared structural and private perceptual components and performs deformable alignment in the shared subspace, enabling robust spatial correction with reduced modality appearance interference. Moreover, we propose a Semantic Graph Calibration Module (SGCM) that explicitly encodes the hierarchical taxonomy and co-occurrence regularities among ground-object categories in UAV scenes into a structured category graph, and incorporates these priors into graph-attention reasoning to calibrate predictions of visually similar and rare categories. In addition, we construct the Unaligned RGB-Thermal Fine-grained (URTF) benchmark, to the best of our knowledge, the largest and most fine-grained benchmark for unaligned UAV RGBT image semantic segmentation, containing over 25,000 image pairs across 61 semantic categories with realistic cross-modal misalignment. Extensive experiments on URTF demonstrate that GSCNet significantly outperforms state-of-the-art methods, with notable gains on fine-grained categories. The dataset is available at https://github.com/mmic-lcl/Datasets-and-benchmark-code.

0 citations0 reviewsNo code linkedOpen access
preprint2022arXiv

The low-entropy hydration shell at the binding site of spike RBD determines the contagiousness of SARS-CoV-2 variants

The infectivity of SARS-CoV-2 depends on the binding affinity of the receptor-binding domain (RBD) of the spike protein with the angiotensin converting enzyme 2 (ACE2) receptor. The calculated RBD-ACE2 binding energies indicate that the difference in transmission efficiency of SARS-CoV-2 variants cannot be fully explained by electrostatic interactions, hydrogen-bond interactions, van der Waals interactions, internal energy, and nonpolar solvation energies. Here, we demonstrate that low-entropy regions of hydration shells around proteins drive hydrophobic attraction between shape-matched low-entropy regions of the hydration shells, which essentially coordinates protein-protein binding in rotational-configurational space of mutual orientations and determines the binding affinity. An innovative method was used to identify the low-entropy regions of the hydration shells of the RBDs of multiple SARS-CoV-2 variants and the ACE2. We observed integral low-entropy regions of hydration shells covering the binding sites of the RBDs and matching in shape to the low-entropy region of hydration shell at the binding site of the ACE2. The RBD-ACE2 binding is thus found to be guided by hydrophobic collapse between the shape-matched low-entropy regions of the hydration shells. A measure of the low-entropy of the hydration shells can be obtained by counting the number of hydrophilic groups expressing hydrophilicity within the binding sites. The low-entropy level of hydration shells at the binding site of a spike protein is found to be an important indicator of the contagiousness of the coronavirus.

0 citations0 reviewsNo code linkedOpen access
preprint2021arXiv

Hydrophobic interaction determines docking affinity of SARS CoV 2 variants with antibodies

Preliminary epidemiologic, phylogenetic and clinical findings suggest that several novel severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants have increased transmissibility and decreased efficacy of several existing vaccines. Four mutations in the receptor-binding domain (RBD) of the spike protein that are reported to contribute to increased transmission. Understanding physical mechanism responsible for the affinity enhancement between the SARS-CoV-2 variants and ACE2 is the "urgent challenge" for developing blockers, vaccines and therapeutic antibodies against the coronavirus disease 2019 (COVID-19) pandemic. Based on a hydrophobic-interaction-based protein docking mechanism, this study reveals that the mutation N501Y obviously increased the hydrophobic attraction and decrease hydrophilic repulsion between the RBD and ACE2 that most likely caused the transmissibility increment of the variants. By analyzing the mutation-induced hydrophobic surface changes in the attraction and repulsion at the binding site of the complexes of the SARS-CoV-2 variants and antibodies, we found out that all the mutations of N501Y, E484K, K417N and L452R can selectively decrease or increase their binding affinity with some antibodies.

0 citations0 reviewsNo code linkedOpen access
preprint2020arXiv

A hydrophobic-interaction-based mechanism trigger docking between the SARS CoV 2 spike and angiotensin-converting enzyme 2

A recent experimental study found that the binding affinity between the cellular receptor human angiotensin converting enzyme 2 (ACE2) and receptor-binding domain (RBD) in spike (S) protein of novel severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is more than 10-fold higher than that of the original severe acute respiratory syndrome coronavirus (SARS-CoV). However, main-chain structures of the SARS-CoV-2 RBD are almost the same with that of the SARS-CoV RBD. Understanding physical mechanism responsible for the outstanding affinity between the SARS-CoV-2 S and ACE2 is the "urgent challenge" for developing blockers, vaccines and therapeutic antibodies against the coronavirus disease 2019 (COVID-19) pandemic. Considering the mechanisms of hydrophobic interaction, hydration shell, surface tension, and the shielding effect of water molecules, this study reveals a hydrophobic-interaction-based mechanism by means of which SARS-CoV-2 S and ACE2 bind together in an aqueous environment. The hydrophobic interaction between the SARS-CoV-2 S and ACE2 protein is found to be significantly greater than that between SARS-CoV S and ACE2. At the docking site, the hydrophobic portions of the hydrophilic side chains of SARS-CoV-2 S are found to be involved in the hydrophobic interaction between SARS-CoV-2 S and ACE2. We propose a method to design live attenuated viruses by mutating several key amino acid residues of the spike protein to decrease the hydrophobic surface areas at the docking site. Mutation of a small amount of residues can greatly reduce the hydrophobic binding of the coronavirus to the receptor, which may be significant reduce infectivity and transmissibility of the virus.

0 citations0 reviewsNo code linkedOpen access
preprint2020arXiv

The role of hydrophobic interactions in folding of $β$-sheets

Exploring the protein-folding problem has been a long-standing challenge in molecular biology. Protein folding is highly dependent on folding of secondary structures as the way to pave a native folding pathway. Here, we demonstrate that a feature of a large hydrophobic surface area covering most side-chains on one side or the other side of adjacent $β$-strands of a $β$-sheet is prevail in almost all experimentally determined $β$-sheets, indicating that folding of $β$-sheets is most likely triggered by multistage hydrophobic interactions among neighbored side-chains of unfolded polypeptides, enable $β$-sheets fold reproducibly following explicit physical folding codes in aqueous environments. $β$-turns often contain five types of residues characterized with relatively small exposed hydrophobic proportions of their side-chains, that is explained as these residues can block hydrophobic effect among neighbored side-chains in sequence. Temperature dependence of the folding of $β$-sheet is thus attributed to temperature dependence of the strength of the hydrophobicity. The hydrophobic-effect-based mechanism responsible for $β$-sheets folding is verified by bioinformatics analyses of thousands of results available from experiments. The folding codes in amino acid sequence that dictate formation of a $β$-hairpin can be deciphered through evaluating hydrophobic interaction among side-chains of an unfolded polypeptide from a $β$-strand-like thermodynamic metastable state.

0 citations0 reviewsNo code linkedOpen access