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

Protonography, a powerful tool for analyzing the activity and the oligomeric state of the γ-carbonic anhydrase identified in the genome of Porphyromonas gingivalis

11 Apr 2015

Abstract excerpt

No abstract is available from the source.

Read the complete abstract on PubMed

Topics

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

Share to Cholinesterase and Neurodegenerative Diseases
Share to Enzyme function and inhibition
Share to Polyamine Metabolism and Applications

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Source

Identifiers

PMID: 25910585
DOI: 10.1016/j.bmc.2015.03.080

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 23 Oct 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Protonography, a powerful tool for analyzing the activity and the oligomeric state of the γ-carbonic anhydrase identified in the genome of Porphyromonas gingivalisPMID 25910585Read ↗

Carbonic Anhydrase from Porphyromonas Gingivalis as a Drug TargetSemantic proximity Read ↗

An Overview of the Carbonic Anhydrases from Two Pathogens of the Oral Cavity: Streptococcus mutans and Porphyromonas gingivalisSemantic proximity Read ↗

Biochemical characterization of recombinant β-carbonic anhydrase (PgiCAb) identified in the genome of the oral pathogenic bacteriumPorphyromonas gingivalisSemantic proximity Read ↗

Biochemical, structural, and computational studies of a γ-carbonic anhydrase from the pathogenic bacterium Burkholderia pseudomalleiSemantic proximity Read ↗

Discovery of a new family of carbonic anhydrases in the malaria pathogen Plasmodium falciparum—The η-carbonic anhydrasesSemantic proximity Read ↗

Identification and characterization of the α-CA in the outer membrane vesicles produced by Helicobacter pyloriSemantic proximity Read ↗

Identification of a Novel Cobamide Remodeling Enzyme in the Beneficial Human Gut Bacterium Akkermansia muciniphilaSemantic proximity Read ↗

New light on bacterial carbonic anhydrases phylogeny based on the analysis of signal peptide sequencesSemantic proximity Read ↗

Exploring Local Flexibility/Rigidity in Psychrophilic and Mesophilic Carbonic AnhydrasesSemantic proximity Read ↗

The zinc coordination pattern in the η-carbonic anhydrase from Plasmodium falciparum is different from all other carbonic anhydrase genetic familiesSemantic proximity Read ↗

Crystal structure of PhnH: an essential component of carbon-phosphorus lyase in Escherichia coli.Semantic proximity Read ↗

Bacterial ι-carbonic anhydrase: a new active class of carbonic anhydrase identified in the genome of the Gram-negative bacterium Burkholderia territoriiSemantic proximity Read ↗

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