ArticleCurrent microbiology2011
Recognition of host proteins by Helicobacter cysteine-rich protein C.
Article in Current microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
8 citing papers in PubMed, 9 citations in OpenAlex.
- Live Attenuated Measles Virus Vaccine ExpressingMolecular therapy oncolytics · 2020Article
- Comprehensive mapping of the Helicobacter pylori NikR regulon provides new insights in bacterial nickel responses.Scientific reports · 2017Article
- Identification and Characterization of msf, a Novel Virulence Factor in Haemophilus influenzae.PloS one · 2016Article
- Article
- Structural and functional aspects of the Helicobacter pylori secretome.World journal of gastroenterology · 2014Review
- Refining the plasmid-encoded type IV secretion system substrate repertoire of Coxiella burnetii.Journal of bacteriology · 2013Article
- Robustness of Helicobacter pylori infection conferred by context-variable redundancy among cysteine-rich paralogs.PloS one · 2013Article
- Sequence divergence and conservation in genomes of Helicobacter cetorum strains from a dolphin and a whale.PloS one · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tetratricopeptide- and sel1-like repeat (SLR) proteins modulate various cellular activities, ranging from transcription regulation to cell-fate control. Helicobacter cysteine-rich proteins (Hcp) consist of several SLRs that are cross-linked by disulfide bridges and have been implicated in host/pathogen interactions. Using pull-down proteomics, several human proteins including Nek9, Hsp90, and Hsc71 have been identified as putative human interaction partners for HcpC. The interaction between the NimA-like protein kinase Nek9 and HcpC has been validated by ELISA and surface plasmon resonance. Recombinant Nek9 is recognized by HcpC with a dissociation constant in the lower micromolar range. This interaction is formed either directly between Nek9 and HcpC or via the formation of a complex with Hsc71. The HcpC homologue HcpA possesses no affinity for Nek9, suggesting that the reported interaction is rather specific for HcpC. These results are consistent with previous observations where Nek9 was targeted upon bacterial or viral invasion. However, further experiments will be required to show that the reported interactions also occur in vivo.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.