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Publications by C. Karanian

TprC/D (Tp0117/131), a Trimeric, Pore-Forming Rare Outer Membrane Protein of Treponema Pallidum, Has a Bipartite Domain Structure

Journal of Bacteriology
MicrobiologyMolecular Biology
2012English

Related publications

Porin Activity and Sequence Analysis of a 31-Kilodalton Treponema Pallidum Subsp. Pallidum Rare Outer Membrane Protein (Tromp1).

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The Major Outer Sheath Protein (Msp) of Treponema Denticola Has a Bipartite Domain Architecture and Exists as Periplasmic and Outer Membrane-Spanning Conformers

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Selective Release of the Treponema Pallidum Outer Membrane and Associated Polypeptides With Triton X-114.

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1988English

Characterization of a Manganese-Dependent Regulatory Protein, TroR, From Treponema Pallidum

Proceedings of the National Academy of Sciences of the United States of America
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Outer Membrane Antigens of Oral Treponema Species

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Topographic Labelling of Pore-Forming Proteins From the Outer Membrane ofEscherichia Coli

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1986English

Tom40, the Pore-Forming Component of the Protein-Conducting Tom Channel in the Outer Membrane of Mitochondria

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Unfolding Study of a Trimeric Membrane Protein AcrB

Protein Science
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2014English

The Molecular Epidemiology of Treponema Pallidum Subspecies Pallidum

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