Production of catalytically inactive BoNT/A1 holoprotein and comparison with BoNT/A1 subunit vaccines against toxin subtypes A1, A2, and A3. (Q47776201)

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scientific article published on 28 May 2009

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English	Production of catalytically inactive BoNT/A1 holoprotein and comparison with BoNT/A1 subunit vaccines against toxin subtypes A1, A2, and A3.	scientific article published on 28 May 2009

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/19450643

Production of catalytically inactive BoNT/A1 holoprotein and comparison with BoNT/A1 subunit vaccines against toxin subtypes A1, A2, and A3. (English)

1 reference

Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/19450643

author name string

Robert P Webb

1

1 reference

Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/19450643

Theresa J Smith

2

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Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/19450643

Patrick Wright

3

1 reference

Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/19450643

Jennifer Brown

4

1 reference

Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/19450643

Leonard A Smith

5

1 reference

Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/19450643

language of work or name

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publication date

28 May 2009

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Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/19450643

number of pages

8

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Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/19450643

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Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/19450643

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Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/19450643

4490-4497

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Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/19450643

Sequence homology and structural analysis of the clostridial neurotoxins

1 reference

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A structural perspective of the sequence variability within botulinum neurotoxin subtypes A1-A4.

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Genetic diversity among Botulinum Neurotoxin-producing clostridial strains

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Re-engineering the target specificity of Clostridial neurotoxins - a route to novel therapeutics

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Protection with recombinant Clostridium botulinum C1 and D binding domain subunit (Hc) vaccines against C and D neurotoxins

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Expression, purification, and efficacy of the type A botulinum neurotoxin catalytic domain fused to two translocation domain variants

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7 January 2021

Design of methanol Feed control in Pichia pastoris fermentations based upon a growth model

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Proteolysis of synthetic peptides by type A botulinum neurotoxin

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Hypersensitivity reactions associated with botulinal antitoxin

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Production and purification of the heavy-chain fragment C of botulinum neurotoxin, serotype B, expressed in the methylotrophic yeast Pichia pastoris

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7 January 2021

Purification and scale-up of a recombinant heavy chain fragment C of botulinum neurotoxin serotype E in Pichia pastoris GS115.

1 reference

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7 January 2021

Fermentation, Purification, and Efficacy of a Recombinant Vaccine Candidate against Botulinum Neurotoxin Type F from Pichia pastoris

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7 January 2021

Recombinant holotoxoid vaccine against botulism

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Characterization of the antibody response to the receptor binding domain of botulinum neurotoxin serotypes A and E.

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The complete amino acid sequence of the Clostridium botulinum type A neurotoxin, deduced by nucleotide sequence analysis of the encoding gene

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Botulinum neurotoxin A selectively cleaves the synaptic protein SNAP-25

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Expression and Purification of the Light Chain of Botulinum Neurotoxin A: A Single Mutation Abolishes Its Cleavage of SNAP-25 and Neurotoxicity after Reconstitution with the Heavy Chain

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7 January 2021

Light chain of botulinum A neurotoxin expressed as an inclusion body from a synthetic gene is catalytically and functionally active

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7 January 2021

N-terminal helix reorients in recombinant C-fragment of Clostridium botulinum type B

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Purification, potency, and efficacy of the botulinum neurotoxin type A binding domain from Pichia pastoris as a recombinant vaccine candidate.

1 reference

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7 January 2021

Identifiers

10.1016/J.VACCINE.2009.05.030

1 reference

Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/19450643

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

5 February 2018

http://europepmc.org/abstract/MED/19450643

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