Vibrio cholerae hemolysin: The β-trefoil domain is required for folding to the native conformation

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Vibrio cholerae hemolysin: The β-trefoil domain is required for folding to the native conformation

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2016 nî lūn-bûn

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2016年の論文

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2016年論文

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2016年論文

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2016年論文

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2016年論文

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2016年論文

@zh-tw

2016年论文

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2016年论文

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2016年论文

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Vibrio cholerae hemolysin: The ...... ing to the native conformation

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Vibrio cholerae hemolysin: The ...... ing to the native conformation

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prefLabel

Vibrio cholerae hemolysin: The ...... ing to the native conformation

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P1476

Vibrio cholerae hemolysin: The ...... ing to the native conformation

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P2093

Amarshi Mukherjee

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Kalyan K Banerjee

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Nabendu S Chatterjee

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Sreerupa Ganguly

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P2860

Crystal structure of the Vibrio cholerae cytolysin heptamer reveals common features among disparate pore-forming toxins

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Vibrio cholerae Cytolysin Recognizes the Heptasaccharide Core of Complex N-Glycans with Nanomolar Affinity

Glycan Specificity of the Vibrio vulnificus Hemolysin Lectin Outlines Evolutionary History of Membrane Targeting by a Toxin Family

A novel mode of carbohydrate recognition in jacalin, a Moraceae plant lectin with a beta-prism fold

Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore

The nature of the accessible and buried surfaces in proteins

Three-dimensional structure of different functional forms of the Vibrio cholerae hemolysin oligomer: a cryo-electron microscopic study

Phase separation of integral membrane proteins in Triton X-114 solution

A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples

P304

242-248

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P31

scholarly article

P356

10.1016/J.BBREP.2016.09.009

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P478

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

P577

2016-09-22T00:00:00Z

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P698

28955962

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P921

Vibrio cholerae

P932

5614477

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