ArticlePloS one2015
NMR Structure and Dynamics of the Resuscitation Promoting Factor RpfC Catalytic Domain.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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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.
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Who cites it
15 citing papers in PubMed, 21 citations in OpenAlex.
- Exploring the multifaceted roles of resuscitation-promoting factors in tuberculosis: Implications for diagnosis, vaccine development, and drug targeting.Biotechnology reports (Amsterdam, Netherlands) · 2025Review
- Resuscitation-promoting factor (Rpf) terminates dormancy among diverse soil bacteria.mSystems · 2025Article
- Excavation of resources ofFrontiers in microbiology · 2025Article
- Resuscitation Promotion Factor: A Pronounced Bacterial Cytokine in Propelling Bacterial Resuscitation.Microorganisms · 2024Review
- Virulence Factors inBiomolecules · 2023Article
- A Structural View at Vaccine Development againstCells · 2023Review
- Structure based design of effective HtpG-derived vaccine antigens againstFrontiers in molecular biosciences · 2022Article
- Small RNA F6 ProvidesInternational journal of molecular sciences · 2021Article
- The Cell Wall Hydrolytic NlpC/P60 Endopeptidases in Mycobacterial Cytokinesis: A Structural Perspective.Cells · 2019Review
- Article
- Characterising resuscitation promoting factor fluorescent-fusions in mycobacteria.BMC microbiology · 2018Article
- A structural overview of mycobacterial adhesins: Key biomarkers for diagnostics and therapeutics.Protein science : a publication of the Protein Society · 2018Review
- Solution NMR Studies of Mycobacterium tuberculosis Proteins for Antibiotic Target Discovery.Molecules (Basel, Switzerland) · 2017Review
- Structure and dynamics of the multi-domain resuscitation promoting factor RpfB from Mycobacterium tuberculosis.Journal of biomolecular structure & dynamics · 2017Article
- Sub-minimum inhibitory concentration of rifampin: a potential risk factor for resuscitation ofAntimicrobial resistance and infection control · 2017Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mycobacterium tuberculosis latent infection is maintained for years with no clinical symptoms and no adverse effects for the host. The mechanism through which dormant M. tuberculosis resuscitates and enters the cell cycle leading to tuberculosis is attracting much interest. The RPF family of proteins has been found to be responsible for bacteria resuscitation and normal proliferation. This family of proteins in M. tuberculosis is composed by five homologues (named RpfA-E) and understanding their conformational, structural and functional peculiarities is crucial to the design of therapeutic strategies.Therefore, we report the structural and dynamics characterization of the catalytic domain of RpfC from M. tubercolosis by combining Nuclear Magnetic Resonance, Circular Dichroism and Molecular Dynamics data. We also show how the formation of a disulfide bridge, highly conserved among the homologues, is likely to modulate the shape of the RpfC hydrophobic catalytic cleft. This might result in a protein function regulation via a "conformational editing" through a disulfide bond formation.
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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.