Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Study of the Protein Complex, Pore Diameter, and Pore-forming Activity of the Borrelia burgdorferi P13 Porin

14 May 2014

Abstract excerpt

P13 is one of the major outer membrane proteins of Borrelia burgdorferi. Previous studies described P13 as a porin. In the present study some structure and function aspects of P13 were studied. P13 showed according to lipid bilayer studies a channel-forming activity of 0.6 nanosiemens in 1 m KCl. Single channel and selectivity measurements demonstrated that P13 had no preference for either cations or anions and...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Clostridium difficile and Clostridium perfringens research
Share to Toxin Mechanisms and Immunotoxins
Share to Vector-borne infectious diseases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 24825899
DOI: 10.1074/jbc.m113.539528

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Study of the Protein Complex, Pore Diameter, and Pore-forming Activity of the Borrelia burgdorferi P13 PorinPMID 24825899Read ↗

Characterization of Multiprotein Complexes of the <i>Borrelia burgdorferi</i> Outer Membrane VesiclesSemantic proximity Read ↗

Elimination of channel-forming activity by insertional inactivation of the p66 gene in Borrelia burgdorferi.Semantic proximity Read ↗

Crystal structures explain functional properties of two E. coli porins.Semantic proximity Read ↗

An RND-Type Efflux System in Borrelia burgdorferi Is Involved in Virulence and Resistance to Antimicrobial CompoundsSemantic proximity Read ↗

The Major Outer Membrane Protein ofChlamydia psittaciFunctions as a Porin-Like Ion ChannelSemantic proximity Read ↗

Genotype-specific differences in structural features of hepatitis C virus (HCV) p7 membrane protein.Semantic proximity Read ↗

In vivo and in vitro studies of transmembrane beta-strand deletion, insertion or substitution mutants of the Escherichia coli K-12 maltoporin.Semantic proximity Read ↗

BB0323 and Novel Virulence Determinant BB0238:Borrelia burgdorferiProteins That Interact With and Stabilize Each Other and Are Critical for InfectivitySemantic proximity Read ↗

Structural and Biophysical Characterization of the Yersinia Type Three Secretion System ATPase YscNSemantic proximity Read ↗

Structural and Functional Properties of the Hepatitis C Virus p7 ViroporinSemantic proximity Read ↗

Direct in situ structural analysis of recombinant outer membrane porins expressed in an OmpA-deficient mutant Escherichia coli strain.Semantic proximity Read ↗

Surface expression, single-channel analysis and membrane topology of recombinant Chlamydia trachomatis Major Outer Membrane Protein.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.