Receptors and Binding Structures for Clostridium difficile Toxins A and B.

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Expression and (Lacking) Internalization of the Cell Surface Receptors of Clostridioides difficile Toxin B.Novel Chimeric Protein Vaccines Against Infection The Conserved Cys-2232 in Toxin B Modulates Receptor Binding

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Receptors and Binding Structures for Clostridium difficile Toxins A and B.

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http://www.wikidata.org/entity/Q51662356

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2016 nî lūn-bûn

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2016年の論文

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年学术文章

@zh-hans

2016年学术文章

@zh-my

2016年学术文章

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2016年學術文章

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2016年學術文章

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Receptors and Binding Structures for Clostridium difficile Toxins A and B.

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Receptors and Binding Structures for Clostridium difficile Toxins A and B.

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type

Item

label

Receptors and Binding Structures for Clostridium difficile Toxins A and B.

@en

Receptors and Binding Structures for Clostridium difficile Toxins A and B.

@nl

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Receptors and Binding Structures for Clostridium difficile Toxins A and B.

@en

Receptors and Binding Structures for Clostridium difficile Toxins A and B.

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P1476

Receptors and Binding Structures for Clostridium difficile Toxins A and B.

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P2093

Ralf Gerhard

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The repetitive oligopeptide sequences modulate cytopathic potency but are not crucial for cellular uptake of Clostridium difficile toxin A

The membrane-spanning proteoglycan NG2 binds to collagens V and VI through the central nonglobular domain of its core protein

Synergistic action of nectins and cadherins generates the mosaic cellular pattern of the olfactory epithelium

Clostridium difficile Toxin B causes epithelial cell necrosis through an autoprocessing-independent mechanism

Mechanism of Action and Epitopes of Clostridium difficile Toxin B-neutralizing Antibody Bezlotoxumab Revealed by X-ray Crystallography

Theranostic impact of NG2/CSPG4 proteoglycan in cancer

Membrane vesicles as conveyors of immune responses

Annexin V, the regulator of phosphatidylserine-catalyzed inflammation and coagulation during apoptosis.

Expression of recombinant Clostridium difficile toxin A and B in Bacillus megaterium

LRP1 is a receptor for Clostridium perfringens TpeL toxin indicating a two-receptor model of clostridial glycosylating toxins

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79-96

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scholarly article

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10.1007/82_2016_17

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406

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2016-07-06T00:00:00Z

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27380268

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P921

Clostridium difficile

Receptors and Binding Structures for Clostridium difficile Toxins A and B.

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P2860

P2860

Receptors and Binding Structures for Clostridium difficile Toxins A and B.

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P1433

P1476

P2093

P2860

P304

P31

P356

P478

P577

P698

P921

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P478

P577

P698

P921