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Jon Ladd

Researcher at Fred Hutchinson Cancer Research Center

Publications -  28
Citations -  2399

Jon Ladd is an academic researcher from Fred Hutchinson Cancer Research Center. The author has contributed to research in topics: Autoantibody & Cancer. The author has an hindex of 20, co-authored 28 publications receiving 2115 citations. Previous affiliations of Jon Ladd include University of Washington & Academy of Sciences of the Czech Republic.

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Zwitterionic polymers exhibiting high resistance to nonspecific protein adsorption from human serum and plasma

TL;DR: The zwitterionic polymer surface based on carboxybetaine methacrylate (CBMA) also incorporates functional groups for protein immobilization in the nonfouling background, making it a strong candidate for many applications such as in diagnostics and drug delivery.
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Quantitative and simultaneous detection of four foodborne bacterial pathogens with a multi-channel SPR sensor.

TL;DR: The quantitative and simultaneous detection of four species of bacteria, Escherichia coli O157:H7, Salmonella choleraesuis serotype typhimurium, Listeria monocytogenes, and Campylobacter jejuni, using an eight-channel surface plasmon resonance (SPR) sensor based on wavelength division multiplexing is reported.
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DNA directed protein immobilization on mixed ssDNA/oligo(ethylene glycol) self-assembled monolayers for sensitive biosensors.

TL;DR: The specificity, sensitivity, and convenience of using protein-DNA conjugates to convert a DNA/OEG SAM surface into a biosensor surface is demonstrated and this platform is applied to the detection of human chorionic gonadotropin using surface plasmon resonance.
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DNA-Directed Protein Immobilization for Simultaneous Detection of Multiple Analytes by Surface Plasmon Resonance Biosensor

TL;DR: This work employs DNA-directed protein immobilization to functionalize a multichannel biosensor, which was used for the simultaneous detection of a set of three fertility hormones: human chorionic gonadotropin, human luteinizing hormone, and follicle stimulating hormone by surface plasmon resonance sensor.
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DNA-Directed Protein Immobilization on Mixed Self-Assembled Monolayers via a Streptavidin Bridge

TL;DR: This work presents a simple approach for the functionalization of sensor surfaces suitable for multichannel detection by utilizing self-assembled monolayer (SAM) chemistry to create a nonfouling, functional sensor platform based on biotinylated single-stranded DNA immobilized via a streptavidin bridge to a mixed SAM of biOTinylated alkanethiol and oligo(ethylene glycol).