Jiali Li
Affiliation confirmed via AI analysis of OpenAlex, ORCID, and web sources.
Professor
Also affiliated: Rutgers, The State University of New Jersey (2009–2010); Harvard University (2002–2004); Scripps Institution of Oceanography (2011); Daqing Oilfield General Hospital (2021); Scripps (United States) (2011); Ulsan National Institute of Science and Technology (2017); Yangzhou University (2021)
Faculty Researcher
Research Areas
Biomedical Subjects
Links
Biography and Research Information
OverviewAI-generated summary
Jiali Li's research focuses on the application of nanotechnology, particularly solid-state nanopore sensors, for characterizing biomolecules. Her work investigates the size and shape of protein oligomers in solution, including alpha-synuclein and beta-lactoglobulin, contributing to the understanding of protein aggregation mechanisms relevant to various diseases. Li also studies the aggregation and conformational changes of tau and tubulin proteins using nanopore methods in conjunction with atomic force microscopy. Her lab has developed and functionally characterized immortalized rabbit dermal papilla cell lines. Further research explores the amplification mechanisms of bent DNA sensors through all-atom molecular dynamics simulations and the sensing of RNA stability using silicon nitride nanopore devices.
Metrics
- h-index: 25
- Publications: 62
- Citations: 5,360
Selected Publications
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Tracking single-molecule ferritin reassembly and disassembly using polymer-coated nanopores (2025)
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Understanding the Mechanism of Bent DNA Amplifying Sensors Using All-Atom Molecular Dynamics Simulations (2025)
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BPS2025 - Sensing RNA stability by a silicon nitride nanopore device (2025)
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Dependence of protein shape and stability on electric field strength and solution environment (2024)
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Probing heat shock protein-coding RNA of Sulfolobus solfataricus P2 through a solid-state nanopore under different pH and temperature (2024)
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Aggregation and Oligomerization Characterization of ß-Lactoglobulin Protein Using a Solid-State Nanopore Sensor (2023)
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Detecting DNA-Binding Sites of Regulation Proteins with Ion Beam Sculpted Silicon Nitride Nanopores (2023)
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Simultaneous Determination of the Size and Shape of Single α-Synuclein Oligomers in Solution (2023)
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Aggregation and Oligomerization Characterization of ß-lactoglobulin Protein by a Solid State Nanopore Sensor (2023)
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Tau and tubulin protein aggregation characterization by solid-state nanopore method and atomic force microscopy (2023)
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Simultaneous Determination of the Size and Shape of Single α-Synuclein Oligomers in Solution (2023)
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Fluid surface coatings for solid-state nanopores: comparison of phospholipid bilayers and archaea-inspired lipid monolayers (2019)
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Estimation of Shape, Volume, and Dipole Moment of Individual Proteins Freely Transiting a Synthetic Nanopore (2019)
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Estimating RNA Polymerase Protein Binding Sites on λ DNA Using Solid-State Nanopores (2018)
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A tip-attached tuning fork sensor for the control of DNA translocation through a nanopore (2017)
Collaboration Network
Top Collaborators
- Detecting DNA-Binding Sites of Regulation Proteins with Ion Beam Sculpted Silicon Nitride Nanopores
- Probing heat shock protein-coding RNA of Sulfolobus solfataricus P2 through a solid-state nanopore under different pH and temperature
- Dependence of protein shape and stability on electric field strength and solution environment
- BPS2025 - Sensing RNA stability by a silicon nitride nanopore device
- Simultaneous Determination of the Size and Shape of Single α-Synuclein Oligomers in Solution
- Tracking single-molecule ferritin reassembly and disassembly using polymer-coated nanopores
- Simultaneous Determination of the Size and Shape of Single α-Synuclein Oligomers in Solution
- Tau and tubulin protein aggregation characterization by solid-state nanopore method and atomic force microscopy
- Aggregation and Oligomerization Characterization of ß-Lactoglobulin Protein Using a Solid-State Nanopore Sensor
- Aggregation and Oligomerization Characterization of ß-lactoglobulin Protein by a Solid State Nanopore Sensor
- Probing heat shock protein-coding RNA of Sulfolobus solfataricus P2 through a solid-state nanopore under different pH and temperature
- Dependence of protein shape and stability on electric field strength and solution environment
- BPS2025 - Sensing RNA stability by a silicon nitride nanopore device
- Probing heat shock protein-coding RNA of Sulfolobus solfataricus P2 through a solid-state nanopore under different pH and temperature
- Dependence of protein shape and stability on electric field strength and solution environment
- BPS2025 - Sensing RNA stability by a silicon nitride nanopore device
- Simultaneous Determination of the Size and Shape of Single α-Synuclein Oligomers in Solution
- Simultaneous Determination of the Size and Shape of Single α-Synuclein Oligomers in Solution
- Simultaneous Determination of the Size and Shape of Single α-Synuclein Oligomers in Solution
- Simultaneous Determination of the Size and Shape of Single α-Synuclein Oligomers in Solution
- Aggregation and Oligomerization Characterization of ß-Lactoglobulin Protein Using a Solid-State Nanopore Sensor
- Aggregation and Oligomerization Characterization of ß-lactoglobulin Protein by a Solid State Nanopore Sensor
- Aggregation and Oligomerization Characterization of ß-Lactoglobulin Protein Using a Solid-State Nanopore Sensor
- Aggregation and Oligomerization Characterization of ß-lactoglobulin Protein by a Solid State Nanopore Sensor
- Aggregation and Oligomerization Characterization of ß-Lactoglobulin Protein Using a Solid-State Nanopore Sensor
- Aggregation and Oligomerization Characterization of ß-lactoglobulin Protein by a Solid State Nanopore Sensor
- Aggregation and Oligomerization Characterization of ß-Lactoglobulin Protein Using a Solid-State Nanopore Sensor
- Aggregation and Oligomerization Characterization of ß-lactoglobulin Protein by a Solid State Nanopore Sensor
- Aggregation and Oligomerization Characterization of ß-Lactoglobulin Protein Using a Solid-State Nanopore Sensor
- Aggregation and Oligomerization Characterization of ß-lactoglobulin Protein by a Solid State Nanopore Sensor
- Aggregation and Oligomerization Characterization of ß-Lactoglobulin Protein Using a Solid-State Nanopore Sensor
- Aggregation and Oligomerization Characterization of ß-lactoglobulin Protein by a Solid State Nanopore Sensor
- Detecting DNA-Binding Sites of Regulation Proteins with Ion Beam Sculpted Silicon Nitride Nanopores
- Dependence of protein shape and stability on electric field strength and solution environment
- Probing heat shock protein-coding RNA of Sulfolobus solfataricus P2 through a solid-state nanopore under different pH and temperature
- BPS2025 - Sensing RNA stability by a silicon nitride nanopore device
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