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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Philip R. Dormitzer

Department of Pediatrics

Harvard Medical School

and the Laboratory of Molecular Medicine

Children's Hospital

USA

[email]@*.harvard.edu

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Affiliations

Department of Pediatrics, Harvard Medical School, and the Laboratory of Molecular Medicine, Children's Hospital, USA. 2004
Laboratory of Molecular Medicine, Enders 673, Children's Hospital, 320 Longwood Avenue, USA. 2000 - 2002

References

Structural rearrangements in the membrane penetration protein of a non-enveloped virus. Dormitzer, P.R., Nason, E.B., Prasad, B.V., Harrison, S.C. Nature (2004) [Pubmed]
The rhesus rotavirus VP4 sialic acid binding domain has a galectin fold with a novel carbohydrate binding site. Dormitzer, P.R., Sun, Z.Y., Wagner, G., Harrison, S.C. EMBO J. (2002) [Pubmed]
Specificity and affinity of sialic acid binding by the rhesus rotavirus VP8* core. Dormitzer, P.R., Sun, Z.Y., Blixt, O., Paulson, J.C., Wagner, G., Harrison, S.C. J. Virol. (2002) [Pubmed]
Proteolysis of monomeric recombinant rotavirus VP4 yields an oligomeric VP5* core. Dormitzer, P.R., Greenberg, H.B., Harrison, S.C. J. Virol. (2001) [Pubmed]
Purified recombinant rotavirus VP7 forms soluble, calcium-dependent trimers. Dormitzer, P.R., Greenberg, H.B., Harrison, S.C. Virology (2000) [Pubmed]