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Bacterial Protein Secretion Systems

Overview of attention for book
Cover of 'Bacterial Protein Secretion Systems'

Table of Contents

  1. Altmetric Badge
    Book Overview
  2. Altmetric Badge
    Chapter 1 Identification of Protein Secretion Systems in Bacterial Genomes Using MacSyFinder
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    Chapter 2 Protein Sorting Prediction
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    Chapter 3 Cell Fractionation
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    Chapter 4 Defining Lipoprotein Localisation by Fluorescence Microscopy
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    Chapter 5 Identification of Lipoproteins Using Globomycin and Radioactive Palmitate
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    Chapter 6 Defining Membrane Protein Localization by Isopycnic Density Gradients
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    Chapter 7 Cell Surface Exposure
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    Chapter 8 Probing Inner Membrane Protein Topology by Proteolysis
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    Chapter 9 Mapping of Membrane Protein Topology by Substituted Cysteine Accessibility Method (SCAM™)
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    Chapter 10 Defining Membrane Protein Topology Using pho-lac Reporter Fusions
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    Chapter 11 In Vivo and In Vitro Protein–Peptidoglycan Interactions
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    Chapter 12 Measure of Peptidoglycan Hydrolase Activity
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    Chapter 13 Protein–Protein Interaction: Bacterial Two-Hybrid
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    Chapter 14 Protein–Protein Interactions: Yeast Two-Hybrid System
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    Chapter 15 Protein–Protein Interactions: Cytology Two-Hybrid
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    Chapter 16 Fusion Reporter Approaches to Monitoring Transmembrane Helix Interactions in Bacterial Membranes
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    Chapter 17 Protein–Protein Interactions: Co-Immunoprecipitation
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    Chapter 18 Protein–Protein Interaction: Tandem Affinity Purification in Bacteria
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    Chapter 19 Site-Directed and Time-Resolved Photocrosslinking in Cells Metabolically Labeled with Radioisotopes
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    Chapter 20 Protein–Protein Interactions: Pull-Down Assays
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    Chapter 21 Protein–Protein Interactions: Surface Plasmon Resonance
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    Chapter 22 Assessing Energy-Dependent Protein Conformational Changes in the TonB System
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    Chapter 23 Defining Assembly Pathways by Fluorescence Microscopy
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    Chapter 24 Large Complexes: Cloning Strategy, Production, and Purification
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    Chapter 25 Shearing and Enrichment of Extracellular Type IV Pili
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    Chapter 26 Blue Native PAGE Analysis of Bacterial Secretion Complexes
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    Chapter 27 In Situ Imaging of Bacterial Secretion Systems by Electron Cryotomography
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    Chapter 28 Structural Analysis of Protein Complexes by Cryo Electron Microscopy
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    Chapter 29 Bacterial Filamentous Appendages Investigated by Solid-State NMR Spectroscopy
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    Chapter 30 Energy Requirements for Protein Secretion via the Flagellar Type III Secretion System
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    Chapter 31 Identification of Effectors: Precipitation of Supernatant Material
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    Chapter 32 Screening for Secretion of the Type VI Secretion System Protein Hcp by Enzyme-Linked Immunosorbent Assay and Colony Blot
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    Chapter 33 Effector Translocation: Cya Reporter Assay
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    Chapter 34 Monitoring Effector Translocation using the TEM-1 Beta-Lactamase Reporter System
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    Chapter 35 Effector Translocation Assay: Differential Solubilization
  37. Altmetric Badge
    Chapter 36 Quantitative Determination of Anti-bacterial Activity During Bacterial Co-culture
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    Chapter 37 Erratum to: Bacterial Filamentous Appendages Investigated by Solid-State NMR Spectroscopy
Attention for Chapter 4: Defining Lipoprotein Localisation by Fluorescence Microscopy
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Chapter title
Defining Lipoprotein Localisation by Fluorescence Microscopy
Chapter number 4
Book title
Bacterial Protein Secretion Systems
Published in
Methods in molecular biology, July 2017
DOI 10.1007/978-1-4939-7033-9_4
Pubmed ID
28667602
Book ISBNs
978-1-4939-7031-5, 978-1-4939-7033-9
Authors

Casabona, Maria Guillermina, Robert-Genthon, Mylène, Grunwald, Didier, Attrée, Ina, Maria Guillermina Casabona, Mylène Robert-Genthon, Didier Grunwald, Ina Attrée

Editors

Laure Journet, Eric Cascales

Abstract

In recent years it has become evident that lipoproteins play crucial roles in the assembly of bacterial envelope-embedded nanomachineries and in the processes of protein export/secretion. In this chapter we describe a method to determine their precise localisation, for example inner versus outer membrane, in Gram-negative bacteria using human opportunistic pathogen Pseudomonas aeruginosa as a model. A fusion protein between a given putative lipoprotein and the red fluorescent protein mCherry must be created and expressed in a strain expressing cytoplasmic green fluorescent protein (GFP). Then the peripheral localisation of the fusion protein in the cell can be examined by treating cells with lysozyme to create spheroplasts and monitoring fluorescence under a confocal microscope. Mutants in the signal peptide can be engineered to study the association with the membrane and efficiency of transport. This protocol can be adapted to monitor lipoprotein localisation in other Gram-negative bacteria.

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X Demographics

X Demographics

The data shown below were collected from the profiles of 3 X users who shared this research output. Click here to find out more about how the information was compiled.
 Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 8 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 8 100%

Demographic breakdown

Readers by professional status Count As %
Researcher 2 25%
Unspecified 1 13%
Other 1 13%
Student > Bachelor 1 13%
Student > Doctoral Student 1 13%
Other 2 25%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 7 88%
Unspecified 1 13%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 2. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 03 July 2017.
All research outputs
#13,976,488
of 22,865,319 outputs
Outputs from Methods in molecular biology
#3,936
of 13,127 outputs
Outputs of similar age
#168,260
of 313,601 outputs
Outputs of similar age from Methods in molecular biology
#55
of 268 outputs
Altmetric has tracked 22,865,319 research outputs across all sources so far. This one is in the 37th percentile – i.e., 37% of other outputs scored the same or lower than it.
So far Altmetric has tracked 13,127 research outputs from this source. They receive a mean Attention Score of 3.4. This one has gotten more attention than average, scoring higher than 68% of its peers.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 313,601 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 44th percentile – i.e., 44% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 268 others from the same source and published within six weeks on either side of this one. This one has done well, scoring higher than 77% of its contemporaries.

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