(Q40562324)

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Proteomics computational analyses suggest that hepatitis C virus E1 and pestivirus E2 envelope glycoproteins are truncated class II fusion proteins

scientific article published on March 2003

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scholarly article

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Europe PubMed Central

PubMed publication ID

21 September 2017

Proteomics computational analyses suggest that hepatitis C virus E1 and pestivirus E2 envelope glycoproteins are truncated class II fusion proteins (English)

1 reference

Europe PubMed Central

PubMed publication ID

21 September 2017

computational biology

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based on heuristic

inferred from title

Hepatitis C virus

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based on heuristic

inferred from title

Robert F. Garry

1

object named as

Robert F Garry

1 reference

Europe PubMed Central

PubMed publication ID

21 September 2017

2

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Srikanta Dash

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Europe PubMed Central

PubMed publication ID

21 September 2017

language of work or name

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publication date

1 March 2003

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Europe PubMed Central

PubMed publication ID

21 September 2017

1 reference

Europe PubMed Central

PubMed publication ID

21 September 2017

307

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Europe PubMed Central

PubMed publication ID

21 September 2017

2

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Europe PubMed Central

PubMed publication ID

21 September 2017

255-265

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Europe PubMed Central

PubMed publication ID

21 September 2017

Secondary structure prediction: combination of three different methods.

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A spring-loaded mechanism for the conformational change of influenza hemagglutinin

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Core structure of gp41 from the HIV envelope glycoprotein

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Analysis of the C-terminal membrane anchor domains of hepatitis C virus glycoproteins E1 and E2: toward a topological model

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Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins

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Monoclonal Antibodies That Bind to Domain III of Dengue Virus E Glycoprotein Are the Most Efficient Blockers of Virus Adsorption to Vero Cells

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Detection of a fusion peptide sequence in the transmembrane protein of human immunodeficiency virus

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Similar structural models of the transmembrane proteins of Ebola and avian sarcoma viruses

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A general model for the transmembrane proteins of HIV and other retroviruses

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E2-p7 region of the bovine viral diarrhea virus polyprotein: processing and functional studies

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Inhibition of pestivirus infection in cell culture by envelope proteins E(rns) and E2 of classical swine fever virus: E(rns) and E2 interact with different receptors

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Structure of dengue virus: implications for flavivirus organization, maturation, and fusion

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Translocation activity of C-terminal domain of pestivirus Erns and ribotoxin L3 loop

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The Fusion glycoprotein shell of Semliki Forest virus: an icosahedral assembly primed for fusogenic activation at endosomal pH

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Core structure of the envelope glycoprotein GP2 from Ebola virus at 1.9-A resolution

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Attenuation of tick-borne encephalitis virus by structure-based site-specific mutagenesis of a putative flavivirus receptor binding site

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Improved tools for biological sequence comparison

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Characterization of a putative cellular receptor for HIV-1 transmembrane glycoprotein using synthetic peptides

1 reference

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The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution

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Characterization of the equilibrium between the native and fusion-inactive conformation of rabies virus glycoprotein indicates that the fusion complex is made of several trimers

1 reference

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Identification of common molecular subsequences

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Membrane interface-interacting sequences within the ectodomain of the human immunodeficiency virus type 1 envelope glycoprotein: putative role during viral fusion

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Variable and hypervariable domains are found in the regions of HCV corresponding to the flavivirus envelope and NS1 proteins and the pestivirus envelope glycoproteins

1 reference

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Crystal structure of the Ebola virus membrane fusion subunit, GP2, from the envelope glycoprotein ectodomain

1 reference

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

1 reference

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

1 reference

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Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution

1 reference

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Identifiers

10.1016/S0042-6822(02)00065-X

1 reference

Europe PubMed Central

PubMed publication ID

21 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

21 September 2017

ResearchGate publication ID

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