Selection of rotavirus VP4 cell receptor binding domains for MA104 cells using a phage display library (Q30712112)

26 June 2017

title

Selection of rotavirus VP4 cell receptor binding domains for MA104 cells using a phage display library (English)

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ORCID Public Data File 2021

26 June 2017

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author name string

Jolly CL

series ordinal

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26 June 2017

Huang JA

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26 June 2017

Holmes IH

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26 June 2017

language of work or name

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1 October 2001

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Journal of Virological Methods

26 June 2017

published in

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26 June 2017

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26 June 2017

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26 June 2017

page(s)

41-51

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Identification and partial characterization of a rhesus rotavirus binding glycoprotein on murine enterocytes

26 June 2017

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Temporal correlation between a single amino acid change in the VP4 of a porcine rotavirus and a marked change in pathogenicity

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Sequence analysis of two porcine rotaviruses differing in growth in vitro and in pathogenicity: distinct VP4 sequences and conservation of NS53, VP6 and VP7 genes

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Role of VP3 in human rotavirus internalization after target cell attachment via VP7.

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Comparative sequence analysis of VP4s from five Australian porcine rotaviruses: implication of an apparent new P type

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Functional and structural analysis of the sialic acid-binding domain of rotaviruses

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Some effects of chloramine T induced radioiodination on the physico-chemical properties of oligomeric proteins

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7 January 2021

Rotavirus infection of MA104 cells is inhibited by Ricinus lectin and separately expressed single binding domains.

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Attachment and growth of human rotaviruses RV-3 and S12/85 in Caco-2 cells depend on VP4.

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Rotavirus Antigenicity Is Affected by the Genetic Context and Glycosylation of VP7

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7 January 2021

Genetic mapping indicates that VP4 is the rotavirus cell attachment protein in vitro and in vivo

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7 January 2021

Identification of mutations in the rotavirus protein VP4 that alter sialic-acid-dependent infection

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7 January 2021

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Phage display selection on whole cells yields a peptide specific for melanocortin receptor 1.

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Construction of transforming growth factor alpha (TGF-alpha) phage library and identification of high binders of epidermal growth factor receptor (EGFR) by phage display

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

10.1016/S0166-0934(01)00357-3

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DOI

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26 June 2017

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