Disulfide Reduction in CD4 Domain 1 or 2 Is Essential for Interaction with HIV Glycoprotein 120 (gp120), which Impairs Thioredoxin-driven CD4 Dimerization

Thioredoxin-1 and protein disulfide isomerase catalyze the reduction of similar disulfides in HIV gp120

(2012) Kathrin Reiser et al.   INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY

Cell-type specific requirements for thiol/disulfide exchange during HIV-1 entry and infection

(2012) Tzanko S Stantchev et al.   Retrovirology

Design and Characterization of Stabilized Derivatives of Human CD4D12 and CD4D1

(2011) Piyali Saha et al.   BIOCHEMISTRY

Stabilization of HIV-1 gp120-CD4 Receptor Complex through Targeted Interchain Disulfide Exchange

(2010) Nichole Cerutti et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Reduced Monomeric CD4 Is the Preferred Receptor for HIV

(2010) Lisa J. Matthias et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

DichroCalc--circular and linear dichroism online

(2009) B. M. Bulheller et al.   BIOINFORMATICS

Human glutaredoxin-1 catalyzes the reduction of HIV-1 gp120 and CD4 disulfides and its inhibition reduces HIV-1 replication

(2008) Joeri Auwerx et al.   INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY