scispace - formally typeset
J

John-Erik Stig Hansen

Researcher at Hvidovre Hospital

Publications -  73
Citations -  2012

John-Erik Stig Hansen is an academic researcher from Hvidovre Hospital. The author has contributed to research in topics: Virus & Antibody. The author has an hindex of 26, co-authored 73 publications receiving 1985 citations. Previous affiliations of John-Erik Stig Hansen include University of Copenhagen.

Papers
More filters
Journal ArticleDOI

Protein distance constraints predicted by neural networks and probability density functions.

TL;DR: It is shown that distances in proteins are predicted more accurately by neural networks than by probability density functions, and that the accuracy of the predictions can be further increased by using sequence profiles.
Journal ArticleDOI

Autologous HIV-1 neutralizing antibodies: emergence of neutralization-resistant escape virus and subsequent development of escape virus neutralizing antibodies.

TL;DR: The delay in appearance of neutralizing antibodies to the dominant viral strain at any time in the patient and the emergence of neutralization resistant escape virus may be part of the explanation of the apparent failure of the immune system to control HIV infection.
Journal Article

Carbohydrates of human immunodeficiency virus.

TL;DR: If carbohydrate antigens can elicit a neutralizing immune response in vivo, the possibility exists that carbohydrate neoantIGens can be utilized in the construction of a vaccine against AIDS.
Journal ArticleDOI

Resistance to V3-directed neutralization caused by an N-linked oligosaccharide depends on the quaternary structure of the HIV-1 envelope oligomer.

TL;DR: Treatment of virion preparations with detergent exposed the C-terminal D7324 epitope, which is inaccessible on virion-associated gp120 but readily accessible on monomeric, soluble gp120, and the NEA-9205 epitope was readilyaccessible on monomersic gp120 regardless of the presence of the 306N-glycan.
Journal ArticleDOI

Development and characterization of an antibody directed to an alpha-N-acetyl-D-galactosamine glycosylated MUC2 peptide.

TL;DR: The present work presents a useful approach for development of anti-mucin antibodies directed to different glycoforms of individual mucins by using an α-N-acetyl-D-galactosamine glycosylated peptide based on the tandem repeat of the intestinal mucin MUC2 as an immunogen.