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Lulu Jiang

Publications and source records attributed to Lulu Jiang.

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Modeling Spatially Obfuscated Street-Crime Data using Log-Gaussian Cox Processes on Metric Graphs

We develop a log-Gaussian Cox process framework for modelling street-level crime data observed on a road network when the released event locations are spatially obfuscated. Motivated by UK Police street-level crime data, where published coordinates are anonymised proxy locations rather than exact event locations, we address the resulting support mismatch by representing each observation through an aggregated support on the street network. The latent log-intensity is modelled as a Whittle--Mat\'ern Gaussian field defined on a metric graph through an SPDE representation, allowing the crime intensity to vary continuously along streets while respecting the geometry of the road network. We compare the proposed metric-graph aggregated model with two alternatives: a planar point model that treats the released locations as exact points, and a planar aggregated model that accounts for spatial aggregation but ignores the network support. In a simulation study where data are generated on a street network, the metric-graph model provides more accurate parameter recovery and better overall fit than the planar alternative. In the City of London application, the metric-graph model also achieves the best fit across several crime types, including theft from the person, robbery, drugs, and bicycle theft. The results further suggest that the relationship between environmental amenities and crime risk varies by crime type, with supermarkets showing the most consistent positive associations. The proposed framework provides a principled approach for analysing network-constrained spatial event data with privacy-protected and imprecise locations.

stat.AP

Label-free Imaging of Single-Biomolecule Structure and Interaction by Stimulated Raman Photothermal Encoded Scattering

Current single molecule methods either rely on fluorescence or lack chemical information. Here we report stimulated Raman photothermal encoded scattering (SRPSCAT) microscopy for quantitative bond-selective imaging of single-biomolecule structures and interactions in native environments. In this approach, scattering of the target molecule is modulated by the deposited energy from stimulated Raman gain and loss processes, thereby encoding vibrational spectroscopic information. Leveraging single-molecule sensitivity of interferometric scattering, SRPSCAT can map single proteins with chemical specificity, determine their mass, and distinguish protein secondary structures based on their Raman fingerprints. Furthermore, single protein binding kinetics are quantified and the conformational dynamics of single de novo designed allosteric proteins are observed. Together, these results highlight the potential of SRPSCAT for label-free structural, functional and dynamic analysis at the single-molecule level.

physics.bio-ph

Mid-infrared Chemical Imaging of Intracellular Tau Fibrils using Fluorescence-guided Computational Photothermal Microscopy

Amyloid proteins are associated with a broad spectrum of neurodegenerative diseases. However, it remains a grand challenge to extract molecular structure information from intracellular amyloid proteins in their native cellular environment. To address this challenge, we developed a computational chemical microscope integrating 3D mid-infrared photothermal imaging with fluorescence imaging, termed Fluorescence-guided Bond-Selective Intensity Diffraction Tomography (FBS-IDT). Based on a low-cost and simple optical design, FBS-IDT enables chemical-specific volumetric imaging and 3D site-specific mid-IR fingerprint spectroscopic analysis of tau fibrils, an important type of amyloid protein aggregates, in their intracellular environment. Label-free volumetric chemical imaging of human cells with/without seeded tau fibrils is demonstrated to show the potential correlation between lipid accumulation and tau aggregate formation. Depth-resolved mid-infrared fingerprint spectroscopy is performed to reveal the protein secondary structure of the intracellular tau fibrils. 3D visualization of the \b{eta}-sheet for tau fibril structure is achieved.

physics.optics