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The crystal structure of pertussis toxin
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title
The crystal structure of pertussis toxin
(English)
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main subject
crystal structure
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author name string
P E Stein
series ordinal
1
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A Boodhoo
series ordinal
2
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G D Armstrong
series ordinal
3
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S A Cockle
series ordinal
4
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M H Klein
series ordinal
5
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R J Read
series ordinal
6
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language of work or name
English
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publication date
15 January 1994
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published in
Structure
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volume
2
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issue
1
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page(s)
45-57
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cites work
Crystal structure of a cholera toxin-related heat-labile enterotoxin from E. coli.
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Crystal structure of the cell-binding B oligomer of verotoxin-1 from E. coli
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Structure of exotoxin A of Pseudomonas aeruginosa at 3.0-Angstrom resolution
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The crystal structure of diphtheria toxin
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Subunit structure of islet-activating protein, pertussis toxin, in conformity with the A-B model
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Cloning and sequencing of the pertussis toxin genes: operon structure and gene duplication
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Pertussis toxin gene: nucleotide sequence and genetic organization
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Binding of pertussis toxin to eucaryotic cells and glycoproteins
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Stimulation of the thiol-dependent ADP-ribosyltransferase and NAD glycohydrolase activities of Bordetella pertussis toxin by adenine nucleotides, phospholipids, and detergents
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Separation and characterization of two distinct hemagglutinins contained in purified leukocytosis-promoting factor from Bordetella pertussis
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Characterization of Two Adhesins of Bordetella pertussis for Human Ciliated Respiratory-Epithelial Cells
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'Pertussis vaccine encephalopathy': it is time to recognize it as the myth that it is.
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Pertussis vaccine and injury to the brain
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Neurological complications of pertussis inoculation
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Pertussis toxin S1 mutant with reduced enzyme activity and a conserved protective epitope
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Subunit S1 of pertussis toxin: mapping of the regions essential for ADP-ribosyltransferase activity
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Site-specific alterations in the B oligomer that affect receptor-binding activities and mitogenicity of pertussis toxin
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Preliminary X-ray crystallographic analysis of holotoxin from Bordetella pertussis
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Refined structure of Escherichia coli heat-labile enterotoxin, a close relative of cholera toxin
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ADP-ribosyltransferase mutations in the catalytic S-1 subunit of pertussis toxin
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Identification of an active-site residue in subunit S1 of pertussis toxin by photocrosslinking to NAD
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Identification of amino acid residues essential for the enzymatic activities of pertussis toxin
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The detection and classification of membrane-spanning proteins.
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Comparison of the B-pentamers of heat-labile enterotoxin and verotoxin-1: two structures with remarkable similarity and dissimilarity.
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Protein-chemical analysis of pertussis toxin reveals homology between the subunits S2 and S3, between S1 and the A chains of enterotoxins of Vibrio cholerae and Escherichia coli and identifies S2 as the haptoglobin-binding subunit
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Identifiers
DOI
10.1016/S0969-2126(00)00007-1
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
547970
OpenCitations bibliographic resource ID
547970
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
547970
PubMed publication ID
8075982
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
547970
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