T. Greenwell

Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection.

T. Matthews, C. McDanal, C. Wild, 1994, Proceedings of the National Academy of Sciences of the United States of America.

A synthetic peptide from HIV-1 gp41 is a potent inhibitor of virus-mediated cell-cell fusion.

T. Matthews, C. Wild, T. Greenwell, 1993, AIDS research and human retroviruses.

The inhibitory activity of an HIV type 1 peptide correlates with its ability to interact with a leucine zipper structure.

T. Matthews, C. Wild, T. Greenwell, 1995, AIDS research and human retroviruses.

Mitochondrial inhibition in rat retinal cell cultures as a model of metabolic compromise: mechanisms of injury and neuroprotection.

R. Casson, G. Chidlow, J. Wood, 2012, Investigative ophthalmology & visual science.

Propensity for a leucine zipper-like domain of human immunodeficiency virus type 1 gp41 to form oligomers correlates with a role in virus-induced fusion rather than assembly of the glycoprotein complex.

T. Oas, E. Hunter, T. Matthews, 1994, Proceedings of the National Academy of Sciences of the United States of America.

Biophysical characterization of recombinant proteins expressing the leucine zipper-like domain of the human immunodeficiency virus type 1 transmembrane protein gp41

T. Matthews, D. Shugars, C. Wild, 1996, Journal of virology.