M
Mats Andersson
Researcher at Karolinska Institutet
Publications - 54
Citations - 3729
Mats Andersson is an academic researcher from Karolinska Institutet. The author has contributed to research in topics: Antimicrobial peptides & Peptide sequence. The author has an hindex of 29, co-authored 54 publications receiving 3550 citations. Previous affiliations of Mats Andersson include Pasteur Institute.
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Deficiency of antibacterial peptides in patients with morbus Kostmann : an observation study
TL;DR: Neutrophils from patients with morbus Kostmann were deficient in cathelin-LL-37 and had reduced concentrations of a-defensins HNP1-3 and no cathelins could be detected in plasma and saliva from patients.
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NK-lysin, a novel effector peptide of cytotoxic T and NK cells. Structure and cDNA cloning of the porcine form, induction by interleukin 2, antibacterial and antitumour activity.
Mats Andersson,H. Gunne,Birgitta Agerberth,A. Boman,Tomas Bergman,Rannar Sillard,Hans Jörnvall,V. Mutt,Berit Olsson,Hans Wigzell +9 more
TL;DR: It is suggested that NK‐lysin is a new effector molecule of cytotoxic T and NK cells, and exhibits 33% identity with a putative human preproprotein, NKG5, of unknown function but derived from a cDNA clone of activated NK cells.
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Secreted enteric antimicrobial activity localises to the mucus surface layer
Ulf Meyer-Hoffert,Mathias W. Hornef,Birgitta Henriques-Normark,Lars-Göran Axelsson,Tore Midtvedt,Katrin Pütsep,Mats Andersson +6 more
TL;DR: Findings show that secreted antimicrobial peptides are retained by the surface-overlaying mucus and thereby provide a combined physical and antibacterial barrier to prevent bacterial attachment and invasion.
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Saposin fold revealed by the NMR structure of NK-lysin
TL;DR: NK-lysin is the first representative of a family of sequence related proteins--saposins, surfactant-associated protein B, pore forming amoeba proteins, and domains of acid sphingomyelinase, acyloxyacylhydrolase and plant aspartic proteinases--for which a structure has been determined.
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An amphipathic helical motif common to tumourolytic polypeptide NK-lysin and pulmonary surfactant polypeptide SP-B.
TL;DR: It is concluded that the conformations of NK‐lysin and SP‐B are similar, and strictly conserved structural features with implications for helix topology and lipid interactions are observed.