Intrinsic Toxin-Derived Peptides Destabilize and Inactivate Clostridium difficile TcdB.

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Cell-penetrating peptides derived from Clostridium difficile TcdB2 and a related large clostridial toxin.The Conserved Cys-2232 in Toxin B Modulates Receptor Binding

P2860

Q49790754-5385FEA7-EB6E-45A7-9B4E-1F4BE33563C8 Q58707992-83F871FB-6DBE-40F3-99EB-6880DDB3C082

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Intrinsic Toxin-Derived Peptides Destabilize and Inactivate Clostridium difficile TcdB.

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http://www.wikidata.org/entity/Q38682995

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2017 nî lūn-bûn

@nan

2017年の論文

@ja

2017年論文

@yue

2017年論文

@zh-hant

2017年論文

@zh-hk

2017年論文

@zh-mo

2017年論文

@zh-tw

2017年论文

@wuu

2017年论文

@zh

2017年论文

@zh-cn

name

Intrinsic Toxin-Derived Peptides Destabilize and Inactivate Clostridium difficile TcdB.

@en

type

Item

label

Intrinsic Toxin-Derived Peptides Destabilize and Inactivate Clostridium difficile TcdB.

@en

prefLabel

Intrinsic Toxin-Derived Peptides Destabilize and Inactivate Clostridium difficile TcdB.

@en

P1476

Intrinsic Toxin-Derived Peptides Destabilize and Inactivate Clostridium difficile TcdB

@en

P2093

Jimmy D Ballard

http://www.w3.org/2001/XMLSchema#string

Jonathan J Hunt

http://www.w3.org/2001/XMLSchema#string

Sarah J Bland

http://www.w3.org/2001/XMLSchema#string

P2860

Defining an allosteric circuit in the cysteine protease domain of Clostridium difficile toxins

Structural Determinants of Clostridium difficile Toxin A Glucosyltransferase Activity

Simple bioconjugate chemistry serves great clinical advances: albumin as a versatile platform for diagnosis and precision therapy

Structural organization of the functional domains of Clostridium difficile toxins A and B

Designing a polyvalent inhibitor of anthrax toxin.

Peptide inhibitors targeting Clostridium difficile toxins A and B.

Frizzled proteins are colonic epithelial receptors for C. difficile toxin B.

Four distinct structural domains in Clostridium difficile toxin B visualized using SAXS.

Crystal structure of receptor-binding C-terminal repeats from Clostridium difficile toxin A.

Translocation domain mutations affecting cellular toxicity identify the Clostridium difficile toxin B pore.

P31

scholarly article

P356

10.1128/MBIO.00503-17

http://www.w3.org/2001/XMLSchema#string

P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P50

Jason L Larabee

P577

2017-05-16T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

28512094

http://www.w3.org/2001/XMLSchema#string

P921

Clostridium difficile

P932

5433098

http://www.w3.org/2001/XMLSchema#string

Intrinsic Toxin-Derived Peptides Destabilize and Inactivate Clostridium difficile TcdB.

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P2860

P2860

Intrinsic Toxin-Derived Peptides Destabilize and Inactivate Clostridium difficile TcdB.

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prefLabel

P1433

P1476

P2093

P2860

P31

P356

P433

P478

P50

P577

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P31

P356

P433

P478

P50

P577

P698

P921

P932