scispace - formally typeset
J

Jon T. Skare

Researcher at Texas A&M University

Publications -  40
Citations -  1960

Jon T. Skare is an academic researcher from Texas A&M University. The author has contributed to research in topics: Borrelia burgdorferi & Complement system. The author has an hindex of 22, co-authored 37 publications receiving 1685 citations. Previous affiliations of Jon T. Skare include Texas A&M Health Science Center College of Medicine & Washington State University.

Papers
More filters
Journal ArticleDOI

Escherichia coli TonB protein is exported from the cytoplasm without proteolytic cleavage of its amino terminus.

TL;DR: The amino terminus of TonB is uncleaved following its export from the cytoplasm and thatTonB is a membrane-associated protein, as determined by proteinase K accessibility experiments.
Journal ArticleDOI

The BosR regulatory protein of Borrelia burgdorferi interfaces with the RpoS regulatory pathway and modulates both the oxidative stress response and pathogenic properties of the Lyme disease spirochete.

TL;DR: Borrelia burgdorferi, the Lyme disease spirochete, adapts as it moves between the arthropod and mammalian hosts that it infects and it is hypothesized that BosR serves as a global regulator and provides a regulatory response that is necessary for B.
Journal ArticleDOI

A 9.0-kilobase-pair circular plasmid of Borrelia burgdorferi encodes an exported protein: evidence for expression only during infection.

TL;DR: The cloning, sequencing, and molecular analysis of a gene located on a 9.0-kbp circular plasmid of virulent Borrelia burgdorferi B31 designated eppA shows consistency with the idea that EppA is not peripherally associated with the outer membrane of E. coli but rather has an integral outer membrane association.
Journal ArticleDOI

Evidence for a TonB-dependent energy transduction complex in Escherichia coli.

TL;DR: The chemical half‐life of chromosomally encoded TonB in an exbB::Tn10 mutant was reduced at least 18‐fold, suggesting that TonB is a part of a cytoplasmic membrane complex that includes, at the minimum, ExbB.