AV
Alex J. Vecchio
University at Buffalo, State University of New York, University of Nebraska–Lincoln
Research areas: Biochemistry, Genetics and Molecular Biology · Structural Biology · Enzyme Structure and Function · Barrier Structure and Function Studies · Inflammatory mediators and NSAID effects
Employment
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University at Buffalo, State University of New York Associate Professor2023 - Present
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University of Nebraska-Lincoln Assistant Professor2018 - 2023
Education
Education history is unavailable.
Projects & Funding
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RII Track-4:NSF: Structures of Membrane Protein Assemblies Resolved by Cryogenic Electron Microscopy Office of the Director2022 - 2024
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Impact of CLDN1 inhibition on chemoresistance and metastasis of colon cancer National Cancer Institute2021 - 2026
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Structure and assembly of membrane proteins at tight junctions National Institute of General Medical Sciences2020 - 2025
Publications (16)
- Cryo-EM structures of a synthetic antibody against 22 kDa claudin-4 reveal its complex withClostridium perfringensenterotoxin Save
- Identification and characterization of a first-generation inhibitor of claudin-1 in colon cancer progression and metastasis. Save
- Development, structure, and mechanism of synthetic antibodies that target claudin and Clostridium perfringens enterotoxin complexes Save
- Disruption of Claudin-Made Tight Junction Barriers by Clostridium perfringens Enterotoxin: Insights from Structural Biology Save
- Development, Structure, and Mechanism of Synthetic Antibodies that Target Claudin and Clostridium perfringens Enterotoxin Complexes Save
- Claudin-1-Targeted Nanoparticles for Delivery to Aging-Induced Alterations in the Blood-Brain Barrier. Save
- Structural basis for Clostridium perfringens enterotoxin targeting of claudins at tight junctions in mammalian gut Save
- Highlighting membrane protein structure and function: A celebration of the Protein Data Bank. Save
- Claudin-9 structures reveal mechanism for toxin-induced gut barrier breakdown Save
- High-Throughput Nano-Scale Characterization of Membrane Proteins Using Fluorescence-Detection Size-Exclusion Chromatography. Save
- Crystal Structure of Aspirin-Acetylated Human Cyclooxygenase-2: Insight into the Formation of Products with Reversed Stereochemistry. Save
- Investigating substrate promiscuity in cyclooxygenase-2: the role of Arg-120 and residues lining the hydrophobic groove. Save
- The structure of NS-398 bound to cyclooxygenase-2. Save
- The structural basis of endocannabinoid oxygenation by cyclooxygenase-2. Save
- Human cyclooxygenase-2 is a sequence homodimer that functions as a conformational heterodimer. Save
- Structural basis of fatty acid substrate binding to cyclooxygenase-2. Save