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

Journal of Bacteriology - United States
doi 10.1128/jb.00101-12
Full Text
Abstract

Available in full text

Date
Authors
Publisher

American Society for Microbiology

Related search

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

Journal of Bacteriology
MicrobiologyMolecular Biology
1995English

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

Journal of Bacteriology
MicrobiologyMolecular Biology
2013English

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

Journal of Bacteriology
MicrobiologyMolecular Biology
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
Multidisciplinary
1999English

Outer Membrane Antigens of Oral Treponema Species

Journal of Medical Microbiology
MedicineMicrobiology
1994English

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

Biochemical Journal
BiochemistryCell BiologyMolecular Biology
1986English

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

Journal of Cell Biology
MedicineCell Biology
2001English

Unfolding Study of a Trimeric Membrane Protein AcrB

Protein Science
BiochemistryMedicineMolecular Biology
2014English

The Molecular Epidemiology of Treponema Pallidum Subspecies Pallidum

Sexual Health
EnvironmentalPublic HealthInfectious DiseasesOccupational Health
2015English

Amanote Research

Note-taking for researchers

Follow Amanote

© 2024 Amaplex Software S.P.R.L. All rights reserved.

Privacy PolicyRefund Policy