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The reovirus cell attachment protein possesses two independently active trimerization domains: Basis of dominant negative effects

Data up to Jan 2025

Published1992
Citations38
References44

Total Citations Per Year

Abstract

References (44)

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Protein σ1 is the reovirus cell attachment protein

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1990 • 131 citations

Molecular structure of the cell-attachment protein of reovirus: correlation of computer-processed electron micrographs with sequence-based predictions

1990 • 118 citations

Sequence of reovirus haemagglutinin predicts a coiled-coil structure

1985 • 117 citations

Glycophorin is the reovirus receptor on human erythrocytes

1987 • 100 citations

Identification of conserved domains in the cell attachment proteins of the three serotypes of reovirus

1990 • 75 citations

Biochemical and biophysical characterization of the reovirus cell attachment protein σ1: Evidence that it is a homotrimer

1991 • 64 citations

High-level synthesis of biologically active reovirus protein σ1 in a mammalian expression vector system

1988 • 62 citations

Studies on reovirus receptors of L cells: Virus binding characteristics and comparison with reovirus receptors of erythrocytes

1984 • 59 citations

Molecular cloning and sequencing of the reovirus (serotype 3) S1 gene which encodes the viral ceil attachment protein σ1

1984 • 56 citations

Analysis of functional domains on reovirus cell attachment protein σ1 using cloned s1 gene deletion mutants

1987 • 55 citations

Consider the coiled coil

1991 • 49 citations

The N-terminal quarter of reovirus cell attachment protein σ1 possesses intrinsic virion-anchoring function

1990 • 45 citations

The cell attachment proteins of type 1 and type 3 reovirus are differentially susceptible to trypsin and chymotrypsin

1989 • 39 citations

Conformational and functional analysis of the C-terminal globular head of the reovirus cell attachment protein

1991 • 38 citations

The N-terminal heptad repeat region of reovirus cell attachment protein σ1 is responsible for σ1 oligomer stability and possesses intrinsic oligomerization function

1991 • 38 citations

The incorporation of reovirus cell attachment protein σ1 into virions requires the N-terminal hydrophobic tail and the adjacent heptad repeat region

1991 • 36 citations

Site-directed mutagenesis of the C-terminal portion of reovirus protein σ1: Evidence for a conformation-dependent receptor binding domain

1992 • 34 citations

Purification and characterization of the reovirus cell attachment protein σ1

1987 • 30 citations

Reovirus protein σ1 translated in vitro, as well as truncated derivatives of it that lack up to two-thirds of its C-terminal portion, exists as two major tetrameric molecular species that differ in electrophoretic mobility

1990 • 30 citations

Biosynthesis of reovirus-specified polypeptides: Ribosome pausing during the translation of reovirus S1 mRNA

1992 • 28 citations

Trimerization of the reovirus cell attachment protein (σI) induces conformational changes in σI necessary for its cell-binding function

1991 • 20 citations

Suppression with a difference

1991 • 20 citations

Identification of the σ1S protein in reovirus serotype 2-infected cells with antibody prepared against a bacterial fusion protein

1989 • 11 citations

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The reovirus cell attachment protein possesses two independently active trimerization… (1992) – Cell | Metascience Observatory Explorer