Solution Structure, Membrane Interactions, and Protein Binding Partners of the Tetraspanin Sm-TSP-2, a Vaccine Antigen from the Human Blood FlukeSchistosoma mansoni (Q27681356)

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English	Solution Structure, Membrane Interactions, and Protein Binding Partners of the Tetraspanin Sm-TSP-2, a Vaccine Antigen from the Human Blood FlukeSchistosoma mansoni	scientific article

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scholarly article

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Solution Structure, Membrane Interactions, and Protein Binding Partners of the Tetraspanin Sm-TSP-2, a Vaccine Antigen from the Human Blood FlukeSchistosoma mansoni (English)

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Schistosoma mansoni

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protein structure

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solution structure

1 reference

based on heuristic

inferred from title

object named as

Xinying Jia

1

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Mark S. Pearson

object named as

Mark Pearson

5

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object named as

Jason Mulvenna

13

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Geoffrey Gobert

object named as

Geoffrey N Gobert

10

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object named as

Mehdi Mobli

6

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object named as

Norelle L Daly

9

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Malcolm K Jones

object named as

Malcolm K Jones

11

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object named as

David J Craik

12

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author name string

Leigh Schulte

2

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Alex Loukas

3

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Darren Pickering

4

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Alun Jones

7

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Karl J Rosengren

8

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language of work or name

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publication date

7 March 2014

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Journal of Biological Chemistry

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289

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10

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7151-63

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Structural basis of ligand interactions of the large extracellular domain of tetraspanin CD81

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Schistosoma mansoni tegument protein Sm29 is able to induce a Th1-type of immune response and protection against parasite infection

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Tetraspanin functions and associated microdomains

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Suppression of mRNAs encoding tegument tetraspanins from Schistosoma mansoni results in impaired tegument turnover

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Targeting of tetraspanin proteins--potential benefits and strategies

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Protective effect and granuloma down-modulation promoted by RP44 antigen a fructose 1,6 bisphosphate aldolase of Schistosoma mansoni

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Schistosome membrane proteins as vaccines

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