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Basic Characteristics of Mutations
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Mutation Site
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C306G |
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Mutation Site Sentence
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In contrast, all mutants (C53G homodimer, C306G homodimer and C53/306G monomer) were impaired in their ability to reverse the TNF-α-mediated TER decrease of endothelial monolayers (Figure 5). |
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Mutation Level
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Amino acid level |
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Mutation Type
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Nonsynonymous substitution |
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Gene/Protein/Region
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GP |
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Standardized Encoding Gene
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GP
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Genotype/Subtype
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Zaire |
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Viral Reference
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-
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Functional Impact and Mechanisms
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Disease
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Cell line
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Immune
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- |
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Target Gene
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TNF
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Clinical and Epidemiological Correlations
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Clinical Information
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- |
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Treatment
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- |
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Location
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- |
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Literature Information
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PMID
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16977667
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Title
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Structure-function analysis of the soluble glycoprotein, sGP, of Ebola virus
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Author
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Falzarano D,Krokhin O,Wahl-Jensen V,Seebach J,Wolf K,Schnittler HJ,Feldmann H
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Journal
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Chembiochem : a European journal of chemical biology
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Journal Info
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2006 Oct;7(10):1605-11
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Abstract
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In addition to the transmembrane protein, GP(1,2), the Ebola virus glycoprotein gene encodes the soluble glycoproteins sGP and Delta-peptide. Two more soluble proteins, GP(1) and GP(1,2DeltaTM), are generated from GP(1,2) as a result of disulfide-bond instability and proteolytic cleavage, respectively, and are shed from the surface of infected cells. The sGP glycoprotein is secreted as a disulfide-linked homodimer, but there have been conflicting reports on whether it is arranged in a parallel or antiparallel orientation. Off-line HPLC-MALDI-TOF MS (MS/MS) was used to identify the arrangement of all disulfide bonds and simultaneously determine site-specific information regarding N-glycosylation. Our data prove that sGP is a parallel homodimer that contains C53-C53' and C306-C306' disulfide bonds, and although there are six predicted N-linked carbohydrate sites, only five are consistently glycosylated. The disulfide bond arrangement was confirmed by using cysteine to glycine mutations at amino acid positions 53 and 306. The mutants had a reduced ability to rescue the barrier function of TNF-alpha-treated endothelial cells--a function previously reported for sGP. This indicates that these disulfide bonds are critical for the proposed anti-inflammatory function of sGP.
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Sequence Data
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-
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