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Wolfgang Dillmann

Biographic Data

ID5209160
NAMEWolfgang Dillmann
GIVEN NAMESWolfgang
FAMILY NAMEDillmann
SIGNATUREDILLMANN W
AFFILIATIONSUniversity of California San Diego
ORCID0000-0003-0361-6946
VERIFIEDYes
TOTAL WORKS1
TOTAL CITATIONS5
WORKS AS AUTHOR1
WORKS AS EDITOR0
FIRST PUBLICATION YEAR2001
LATEST PUBLICATION YEAR2001
H-INDEX1
  • Proteomic comparison of human and great ape blood plasma reveals conserved glycosylation and differences in thyroid hormone metabolism

    Open Access•Pascal Gagneux, Bob Amess et al.•ARTICLE•American Journal of Physical…•2001•Cited by: 5•References: 76

    Most blood plasma proteins are glycosylated. These glycoproteins typically carry sialic acid‐bearing sugar chains, which can modify the observed molecular weights and isoelectric points of those proteins during electrophoretic analyses. To explore changes in protein expression and glycosylation that occurred during great ape and human evolution, we subjected multiple blood plasma samples from all these species to high‐resolution proteomic analysi…

  • Proteomic comparison of human and great ape blood plasma reveals conserved glycosylation and differences in thyroid hormone metabolism

    Open Access•Pascal Gagneux, Bob Amess et al.•ARTICLE•American Journal of Physical…•2001•Cited by: 5•References: 76

    Most blood plasma proteins are glycosylated. These glycoproteins typically carry sialic acid‐bearing sugar chains, which can modify the observed molecular weights and isoelectric points of those proteins during electrophoretic analyses. To explore changes in protein expression and glycosylation that occurred during great ape and human evolution, we subjected multiple blood plasma samples from all these species to high‐resolution proteomic analysi…

  • Proteomic comparison of human and great ape blood plasma reveals conserved glycosylation and differences in thyroid hormone metabolism

    Open Access•Pascal Gagneux, Bob Amess et al.•ARTICLE•American Journal of Physical…•2001•Cited by: 5•References: 76

    Most blood plasma proteins are glycosylated. These glycoproteins typically carry sialic acid‐bearing sugar chains, which can modify the observed molecular weights and isoelectric points of those proteins during electrophoretic analyses. To explore changes in protein expression and glycosylation that occurred during great ape and human evolution, we subjected multiple blood plasma samples from all these species to high‐resolution proteomic analysi…

Biochemistry (1 work) · Biochemistry (1 work) · Biology (1 work) · Blood proteins (1 work) · Cellular transport and secretion (1 work) · Central nervous system (1 work) · Cerebrospinal fluid (1 work) · Choroid plexus (1 work) · Endocrinology (1 work) · Endocrinology (1 work)

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