K. Mårdberg

Herpes simplex virus type 1 glycoprotein C is necessary for efficient infection of chondroitin sulfate-expressing gro2C cells.

T. Bergström, E. Trybala, F. Tufaro, 2002, The Journal of general virology.

Structural and functional features of the polycationic peptide required for inhibition of herpes simplex virus invasion of cells.

J. Glorioso, B. Svennerholm, S. Olofsson, 2004, Antiviral research.

The role of a single N-linked glycosylation site for a functional epitope of herpes simplex virus type 1 envelope glycoprotein gC.

S. Olofsson, T. Bergström, J. Leckner, 1999, Glycobiology.

Mutation of nucleotide 1,762 in the core promoter region during hepatitis B e seroconversion and its relation to liver damage in hepatitis B e antigen carriers

G. Norkrans, M. Lindh, A. Dhillon, 1998, Journal of medical virology.

Early steps in O-linked glycosylation and clustered O-linked glycans of herpes simplex virus type 1 glycoprotein C: effects on glycoprotein properties.

S. Olofsson, T. Bergström, H. Clausen, 2000, Glycobiology.

Basic amino acids as modulators of an O-linked glycosylation signal of the herpes simplex virus type 1 glycoprotein gC: functional roles in viral infectivity.

S. Olofsson, T. Bergström, H. Clausen, 2004, Glycobiology.

Human antibodies to herpes simplex virus type 1 glycoprotein C are neutralizing and target the heparan sulfate-binding domain.

K. Bieńkowska-Szewczyk, B. Szewczyk, S. Olofsson, 2010, Virology.

Mutational analysis of the major heparan sulfate-binding domain of herpes simplex virus type 1 glycoprotein C.

J. Glorioso, T. Bergström, E. Trybala, 2001, The Journal of general virology.