scispace - formally typeset
A

Anders Håkansson

Researcher at Lund University

Publications -  382
Citations -  10201

Anders Håkansson is an academic researcher from Lund University. The author has contributed to research in topics: Population & Medicine. The author has an hindex of 51, co-authored 330 publications receiving 8776 citations. Previous affiliations of Anders Håkansson include University at Buffalo & State University of New York System.

Papers
More filters
Journal ArticleDOI

Apoptosis induced by a human milk protein

TL;DR: It is raised the possibility that milk contributes to mucosal immunity not only by furnishing antimicrobial molecules but also by policing the function of lymphocytes and epithelium by investigating the effect of human milk on bacterial adherence to a human lung cancer cell line.
Journal ArticleDOI

Conversion of alpha-lactalbumin to a protein inducing apoptosis.

TL;DR: It is proposed that this single amino acid polypeptide chain may perform vastly different biological functions depending on its folding state and the in vivo environment.
Journal ArticleDOI

Interkingdom Signaling Induces Streptococcus pneumoniae Biofilm Dispersion and Transition from Asymptomatic Colonization to Disease

TL;DR: It is shown that infection with influenza A virus and treatment with the resulting host signals induce the release of bacteria from biofilms in a newly developed biofilm model on live epithelial cells both in vitro and during in vivo colonization.
Journal ArticleDOI

A prospective cohort study on breast-feeding and otitis media in Swedish infants

TL;DR: The effect of breast-feeding on the frequency of acute otitis media was analyzed and the AOM frequency was significantly lower in the breast-fed than in the non-breast-fed children in each age group (P < 0.05).
Journal ArticleDOI

Molecular characterization of alpha-lactalbumin folding variants that induce apoptosis in tumor cells.

TL;DR: A protein complex in human milk that induces apoptosis in tumor cells but spares healthy cells is characterized and oligomerization appears to conserve α-lactalbumin in a state with molten globule-like properties at physiological conditions.