Conformational instability governed by disulfide bonds partitions the dominant from subdominant helper T-cell responses specific for HIV-1 envelope glycoprotein gp120. (Q41078346)

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English	Conformational instability governed by disulfide bonds partitions the dominant from subdominant helper T-cell responses specific for HIV-1 envelope glycoprotein gp120.	scientific article

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scholarly article

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Europe PubMed Central

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26 September 2017

Conformational instability governed by disulfide bonds partitions the dominant from subdominant helper T-cell responses specific for HIV-1 envelope glycoprotein gp120. (English)

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Europe PubMed Central

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26 September 2017

Samuel J Landry

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Samuel J Landry

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Hong-Nam P Nguyen

1

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Europe PubMed Central

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26 September 2017

N Kalaya Steede

2

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26 September 2017

James E Robinson

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26 September 2017

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2 May 2015

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Europe PubMed Central

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26 September 2017

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Europe PubMed Central

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26 September 2017

33

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Europe PubMed Central

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26 September 2017

25

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Europe PubMed Central

PMC publication ID

26 September 2017

2887-2896

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Europe PubMed Central

PMC publication ID

26 September 2017

T cell receptor cross-reactivity between similar foreign and self peptides influences naive cell population size and autoimmunity

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Only five of 10 strictly conserved disulfide bonds are essential for folding and eight for function of the HIV-1 envelope glycoprotein

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26 September 2017

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