ReviewBiochimica et biophysica acta2014
Selective transport by SecA2: an expanding family of customized motor proteins.
Review in Biochimica et biophysica acta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
44 citing papers in PubMed, 71 citations in OpenAlex.
- Oral streptococci utilize a Siglec-like domain of serine-rich repeat adhesins to preferentially target platelet sialoglycans in human blood.PLoS pathogens · 2014Trial
- Protein-Mediated Virulence in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026Review
- Genomic Characterization of the Honeybee-Probiotic StrainAnimals : an open access journal from MDPI · 2025Article
- Glycosylation of oral bacteria in modulating adhesion and biofilm formation.Journal of oral microbiology · 2025Review
- Sticking together: independent evolution of biofilm formation in different species of staphylococci has occurred multiple times via different pathways.BMC genomics · 2024Article
- Serine-rich repeat proteins: well-known yet little-understood bacterial adhesins.Journal of bacteriology · 2024Review
- Mycobacterium smegmatis: The Vanguard of Mycobacterial Research.Journal of bacteriology · 2023Review
- SecA2 Associates with Translating Ribosomes and Contributes to the Secretion of Potent IFN-β Inducing RNAs.International journal of molecular sciences · 2022Article
- Bacterial secretion systems: Networks of pathogenic regulation and adaptation in mycobacteria and beyond.PLoS pathogens · 2022Article
- Recent Advancements in Tracking Bacterial Effector Protein Translocation.Microorganisms · 2022Review
- A novel sialic acid-binding adhesin present in multiple species contributes to the pathogenesis of Infective endocarditis.PLoS pathogens · 2021Article
- Disease-associated gut microbiome and metabolome changes in patients with chronic obstructive pulmonary disease.Nature communications · 2020Article
- Selection of ImmunobioticMicroorganisms · 2020Article
- Mycobacteriosis and Infections with Non-tuberculous Mycobacteria in Aquatic Organisms: A Review.Microorganisms · 2020Review
- The Structure ofInternational journal of molecular sciences · 2020Article
- Spatial organization of Clostridium difficile S-layer biogenesis.Scientific reports · 2020Article
- Renibacterium salmoninarum and Mycobacterium spp.: two bacterial pathogens present at low levels in wild brown trout (Salmo trutta fario) populations in Austrian rivers.BMC veterinary research · 2020Article
- Functional and Genomic Characterization ofFrontiers in microbiology · 2020Article
- Serine-rich repeat proteins from gut microbes.Gut microbes · 2020Review
- Streptococcus oralis subsp.Infection and immunity · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The SecA2 proteins are a special class of transport-associated ATPases that are related to the SecA component of the general Sec system, and are found in an increasingly large number of Gram-positive bacterial species. The SecA2 substrates are typically linked to the cell wall, but may be lipid-linked, peptidoglycan-linked, or non-covalently associated S-layer proteins. These substrates can have a significant impact on virulence of pathogenic organisms, but may also aid colonization by commensals. The SecA2 orthologues range from being highly similar to their SecA paralogues, to being distinctly different in apparent structure and function. Two broad classes of SecA2 are evident. One transports multiple substrates, and may interact with the general Sec system, or with an as yet unidentified transmembrane channel. The second type transports a single substrate, and is a component of the accessory Sec system, which includes the SecY paralogue SecY2 along with the accessory Sec proteins Asp1-3. Recent studies indicate that the latter three proteins may have a unique role in coordinating post-translational modification of the substrate with transport by SecA2. Comparative functional and phylogenetic analyses suggest that each SecA2 may be uniquely adapted for a specific type of substrate. This article is part of a Special Issue entitled: Protein trafficking and secretion in bacteria. Guest Editors: Anastassios Economou and Ross Dalbey.
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What OpenQuestion holds
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.