<p>(A) PAP248-286 amyloid fibrils enhanced HIV-1 infection. Under agitation at 37°C, PAP248-286 slowly (~ 24 h) formed amyloid fibrils, which enhanced HIV-1 infection. (B) EP2 promoted the formation of PAP248-286 amyloid fibrils. Without agitation, EP2 rapidly (~ 1 min) self-assembled into nanofibers. These nanofibers accelerated (~ 4 h) the formation of amyloid fibrils, which enhanced HIV-1 infection.</p
<p>PAP248-286 (3 mg/ml) was agitated to allow fibril formation in the presence or absence of EP2 (10...
Amyloid fibrils are cross-beta-sheet-rich protein/peptide fibrils that are typically associated with...
Despite its discovery over 30 years ago, human immunodeficiency virus (HIV) continues to threaten pu...
Semen is a major vehicle for HIV transmission. Prostatic acid phosphatase (PAP) fragments, such as P...
<p>Fibrils were generated by incubating 3 mg/ml PAP248-286 in the presence or absence of EP2 (100 μg...
<p>(A) ProteoStat-stained amyloid fibrils at different time points following agitation (100 μg/ml, r...
Background Semen is a major vehicle for HIV transmission. Prostatic acid phosphatase (PAP) frag-ment...
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...
This dissertation focuses on targeting amyloid aggregates as a means to inhibit disease transmission...
AbstractPAP248–286 is a 39-residue fragment (residues 248 to 286) derived from protease cleavage of ...
<p>(A) EP2 promoted PAP248-286 amyloid fibril formation (3 mg/ml) in a concentration-dependent manne...
AbstractSemen-derived enhancer of viral infection (SEVI), an amyloid fibril formed from a cationic p...
Amyloid fibrils are a form of highly ordered, β-sheet protein structure found in many sites in the b...
Human Immunodeficiency Virus (HIV) affects millions of individuals worldwide. The primary mode of tr...
<p>PAP248-286 (3 mg/ml) was agitated to allow fibril formation in the presence or absence of EP2 (10...
Amyloid fibrils are cross-beta-sheet-rich protein/peptide fibrils that are typically associated with...
Despite its discovery over 30 years ago, human immunodeficiency virus (HIV) continues to threaten pu...
Semen is a major vehicle for HIV transmission. Prostatic acid phosphatase (PAP) fragments, such as P...
<p>Fibrils were generated by incubating 3 mg/ml PAP248-286 in the presence or absence of EP2 (100 μg...
<p>(A) ProteoStat-stained amyloid fibrils at different time points following agitation (100 μg/ml, r...
Background Semen is a major vehicle for HIV transmission. Prostatic acid phosphatase (PAP) frag-ment...
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...
This dissertation focuses on targeting amyloid aggregates as a means to inhibit disease transmission...
AbstractPAP248–286 is a 39-residue fragment (residues 248 to 286) derived from protease cleavage of ...
<p>(A) EP2 promoted PAP248-286 amyloid fibril formation (3 mg/ml) in a concentration-dependent manne...
AbstractSemen-derived enhancer of viral infection (SEVI), an amyloid fibril formed from a cationic p...
Amyloid fibrils are a form of highly ordered, β-sheet protein structure found in many sites in the b...
Human Immunodeficiency Virus (HIV) affects millions of individuals worldwide. The primary mode of tr...
<p>PAP248-286 (3 mg/ml) was agitated to allow fibril formation in the presence or absence of EP2 (10...
Amyloid fibrils are cross-beta-sheet-rich protein/peptide fibrils that are typically associated with...
Despite its discovery over 30 years ago, human immunodeficiency virus (HIV) continues to threaten pu...