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Virginia Ann Lightner

Virginia Ann Lightner

· Medical Assistant Professor in the Department of Dermatology

Duke University · Dermatology

Active 1980–2025

h-index34
Citations2.9k
Papers43
Funding$442k

Academic metrics are sourced from OpenAlex and public funding records; values may differ from Google Scholar.

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About

Virginia Ann Lightner is a Medical Assistant Professor in the Department of Dermatology at Duke University. She is based at the Duke Department of Dermatology located at 11081 Forest Pines Drive, Suite 110, Raleigh, NC 27614. Her professional role involves clinical and academic responsibilities within the department, contributing to education and research in dermatology. Further details about her specific research focus, background, or key contributions are not provided on the page.

Research topics

  • Biology
  • Chemistry
  • Pathology
  • Biochemistry
  • Cell biology

Selected publications

  • Tenascin/hexabrachion in human skin: biochemical identification and localization by light and electron microscopy.

    The Journal of Cell Biology · 1989-06-01 · 150 citations

    articleOpen access1st authorCorresponding

    Tenascin/hexabrachion is a large glycoprotein of the extracellular matrix. Previous reports have demonstrated that tenascin is associated with epithelial-mesenchymal interfaces during embryogenesis and is prominent in the matrix of many tumors. However, the distribution of tenascin is more restricted in adult tissues. We have found tenascin to be present in normal human skin in a distribution distinct from other matrix proteins. Immunohistochemical studies showed staining of the papillary dermis…

    PublisherOA PDFDOI

  • Hexabrachion Protein (Tenascin, Cytotactin, Brachionectin) in Connective Tissues, Embryonic Brain, and Tumors

    Advances in molecular and cell biology · 1988-01-01 · 124 citations

    articleSenior author
    PublisherDOI

  • Binding of hexabrachion (tenascin) to the extracellular matrix and substratum and its effect on cell adhesion

    Journal of Cell Science · 1990-02-01 · 110 citations

    article1st authorCorresponding

    Hexabrachion is a large glycoprotein of the extracellular matrix (ECM) that is prominent in embryogenesis, wound healing and tumorigenesis. Because of the role of extracellular matrix proteins in the regulation of cell differentiation and migration, the interaction of hexabrachion with cells as well as with other components of the ECM is of great interest. Early reports suggested that hexabrachion does not bind to fibronectin or gelatin but does bind to chondroitin sulfate proteoglycans. However…

    PublisherDOI

  • The DNA sequences encoding plsB and dgk loci of Escherichia coli.

    Journal of Biological Chemistry · 1983-09-01 · 105 citations

    articleOpen access1st authorCorresponding

    We have determined the sequence of a 3865-base pair DNA segment from Escherichia coli containing plsB, the structural gene for the sn-glycerol-3-phosphate acyltransferase, and the dgk locus, believed to encode diglyceride kinase. The 806-amino acid sequence encoded within the longest open reading frame is in agreement with NH2-terminal sequences of the sn-glycerol-3-phosphate acyltransferase (Green, P., Vanaman, T. C., Modrich, P., and Bell, R. M. (1983) J. Biol. Chem. 258, 10862-10866), indicat…

    PublisherDOI

  • Membrane phospholipid synthesis in Escherichia coli. Cloning of a structural gene (plsB) of the sn-glycerol-3-phosphate acyl/transferase.

    Journal of Biological Chemistry · 1980-10-01 · 95 citations

    articleOpen access1st authorCorresponding

    Si+ hybrid ColE1 plasmids of the Clarke-Carbon collection (Clarke, C., and Carbon, J. (1976) Cell 9, 91-99) which eliminate the sn-glycerol 3-phosphate growth requirement of a mutant of Escherichia coli with a Km defect in sn-glycerol-3-phosphate acyltransferase (plsB) were identified. Marked overproduction of a plasmid-encoded sn-glycerol-3-phosphate acyltransferase with a wild type Km in a host plsB- background indicates that the hybrid plasmids carry a structural gene for this enzyme. In addi…

    PublisherDOI

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