<p>(A) ProteoStat-stained amyloid fibrils at different time points following agitation (100 μg/ml, red) were mixed with eGFP-labeled HIV-1 virions (green, R5 strains) for 3 h, and the samples were imaged using fluorescence confocal microscopy. The scale bar is 5 μm. (B) ProteoStat-stained amyloid fibrils at different time points following agitation (200 μg/ml, red) were added to eGFP-labeled HIV-1 virions (green, R5 strains), and the mixtures were added to GHOST (3) Hi-5 cells (blue). The effects of fibril presence on the binding of HIV-1 virions to target cells were assessed using fluorescence confocal microscopy. The scale bar is 10 μm.</p
Naturally occurring fragments of the abundant semen proteins prostatic acid phosphatase (PAP) and se...
<p>Fibril formation of PAP248-286 was promoted by agitation in the presence of polyanions (30 µg/ml)...
<p>(A) Images of empty vector-transfected HeLa cells infected with fluorescently labeled HIV-2. The ...
<p>Fibrils were generated by incubating 3 mg/ml PAP248-286 in the presence or absence of EP2 (100 μg...
<p>(A) PAP248-286 amyloid fibrils enhanced HIV-1 infection. Under agitation at 37°C, PAP248-286 slow...
PAP248-286 is a 39-residue fragment (residues 248 to 286) derived from protease cleavage of prostati...
PAP248-286 is a 39-residue fragment (residues 248 to 286) derived from protease cleavage of prostati...
<p>(A) EP2 promoted PAP248-286 amyloid fibril formation (3 mg/ml) in a concentration-dependent manne...
Semen is a major vehicle for HIV transmission. Prostatic acid phosphatase (PAP) fragments, such as P...
AbstractPAP248–286 is a 39-residue fragment (residues 248 to 286) derived from protease cleavage of ...
<p>PAP248-286 (3 mg/ml) was agitated to allow fibril formation in the presence or absence of EP2 (10...
Amyloid fibrils are a form of highly ordered, β-sheet protein structure found in many sites in the b...
Amyloidogenic peptides present in human semen self-assemble into positively charged fibrils that mar...
Human Immunodeficiency Virus (HIV) affects millions of individuals worldwide. The primary mode of tr...
Despite its discovery over 30 years ago, human immunodeficiency virus (HIV) continues to threaten pu...
Naturally occurring fragments of the abundant semen proteins prostatic acid phosphatase (PAP) and se...
<p>Fibril formation of PAP248-286 was promoted by agitation in the presence of polyanions (30 µg/ml)...
<p>(A) Images of empty vector-transfected HeLa cells infected with fluorescently labeled HIV-2. The ...
<p>Fibrils were generated by incubating 3 mg/ml PAP248-286 in the presence or absence of EP2 (100 μg...
<p>(A) PAP248-286 amyloid fibrils enhanced HIV-1 infection. Under agitation at 37°C, PAP248-286 slow...
PAP248-286 is a 39-residue fragment (residues 248 to 286) derived from protease cleavage of prostati...
PAP248-286 is a 39-residue fragment (residues 248 to 286) derived from protease cleavage of prostati...
<p>(A) EP2 promoted PAP248-286 amyloid fibril formation (3 mg/ml) in a concentration-dependent manne...
Semen is a major vehicle for HIV transmission. Prostatic acid phosphatase (PAP) fragments, such as P...
AbstractPAP248–286 is a 39-residue fragment (residues 248 to 286) derived from protease cleavage of ...
<p>PAP248-286 (3 mg/ml) was agitated to allow fibril formation in the presence or absence of EP2 (10...
Amyloid fibrils are a form of highly ordered, β-sheet protein structure found in many sites in the b...
Amyloidogenic peptides present in human semen self-assemble into positively charged fibrils that mar...
Human Immunodeficiency Virus (HIV) affects millions of individuals worldwide. The primary mode of tr...
Despite its discovery over 30 years ago, human immunodeficiency virus (HIV) continues to threaten pu...
Naturally occurring fragments of the abundant semen proteins prostatic acid phosphatase (PAP) and se...
<p>Fibril formation of PAP248-286 was promoted by agitation in the presence of polyanions (30 µg/ml)...
<p>(A) Images of empty vector-transfected HeLa cells infected with fluorescently labeled HIV-2. The ...