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European Journal of Biochemistry|May 1, 1992
The distribution of charged amino acids in mitochondrial inner-membrane proteins suggests different modes of membrane integration for nuclearly and mitochondrially encoded proteinsY Gavel, G von HeijneProtein Engineering|April 1, 1990
Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: implications for protein engineeringY Gavel, G von HeijneProtein Engineering|October 1, 1990
Cleavage-site motifs in mitochondrial targeting peptidesY Gavel, G von HeijneEuropean Journal of Biochemistry|July 1, 1988
Topogenic signals in integral membrane proteinsG von Heijne, Y GavelFEBS Letters|February 26, 1990
A conserved cleavage-site motif in chloroplast transit peptidesY Gavel, G von HeijneFEBS Letters|August 1, 1988
Mitochondrial targeting sequences. Why 'non-amphiphilic' peptides may still be amphiphilicY Gavel, L Nilsson, G von HeijneThe Biochemical Journal|April 15, 1991
Amino acid distributions around O-linked glycosylation sitesI B Wilson, Y Gavel, G von HeijneFEBS Letters|April 22, 1991
The 'positive-inside rule' applies to thylakoid membrane proteinsY Gavel, J Steppuhn, R Herrmann, et al.European Journal of Biochemistry|June 1, 1983
Patterns of amino acids near signal-sequence cleavage sitesG von HeijneMolecular Microbiology|April 1, 1997
Getting greasy: how transmembrane polypeptide segments integrate into the lipid bilayerG von HeijnePageof 16