ReviewMicrobiologyOpen2013
Topological mapping methods for α-helical bacterial membrane proteins--an update and a guide.
Review in MicrobiologyOpen, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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.
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Who cites it
11 citing papers in PubMed.
- Non-invasive tools for analysis of plasma membrane protein topology in living cells.Methods (San Diego, Calif.) · 2025Article
- Article
- Defining Membrane Protein Topology Using pho-lac Reporter Fusions.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Exploring Uniform, Dual, and Dynamic Topologies of Membrane Proteins by Substituted Cysteine Accessibility Method (SCAM™).Methods in molecular biology (Clifton, N.J.) · 2024Article
- Modulation of bacterial multicellularity via spatio-specific polysaccharide secretion.PLoS biology · 2020Article
- Evidence to Suggest Bacterial Lipoprotein Diacylglyceryl Transferase (Lgt) is a Weakly Associated Inner Membrane Protein.The Journal of membrane biology · 2019Article
- Mutation of a Salmonella serogroup-C1-specific gene abrogates O7-antigen biosynthesis and triggers NaCl-dependent motility deficiency.PloS one · 2014Article
- Conserved-residue mutations in Wzy affect O-antigen polymerization and Wzz-mediated chain-length regulation in Pseudomonas aeruginosa PAO1.Scientific reports · 2013Article
- Structure-function analysis of MurJ reveals a solvent-exposed cavity containing residues essential for peptidoglycan biogenesis in Escherichia coli.Journal of bacteriology · 2013Article
- The D3 bacteriophage α-polymerase inhibitor (Iap) peptide disrupts O-antigen biosynthesis through mimicry of the chain length regulator Wzz in Pseudomonas aeruginosa.Journal of bacteriology · 2013Article
- Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Integral membrane proteins with α-helical transmembrane segments (TMS) are known to play important and diverse roles in prokaryotic cell physiology. The net hydrophobicity of TMS directly corresponds to the observed difficulties in expressing and purifying these proteins, let alone producing sufficient yields for structural studies using two-/three-dimensional (2D/3D) crystallographic or nuclear magnetic resonance methods. To gain insight into the function of these integral membrane proteins, topological mapping has become an important tool to identify exposed and membrane-embedded protein domains. This approach has led to the discovery of protein tracts of functional importance and to the proposition of novel mechanistic hypotheses. In this review, we synthesize the various methods available for topological mapping of α-helical integral membrane proteins to provide investigators with a comprehensive reference for choosing techniques suited to their particular topological queries and available resources.
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Registered trials
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