Khattari, Ziad

[["dc.bibliographiccitation.firstpage","769"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Molecular Biology"],["dc.bibliographiccitation.lastpage","779"],["dc.bibliographiccitation.volume","341"],["dc.contributor.author","Arbely, E"],["dc.contributor.author","Khattari, Ziad"],["dc.contributor.author","Brotons, Guillaume"],["dc.contributor.author","Akkawi, M"],["dc.contributor.author","Salditt, Tim"],["dc.contributor.author","Arkin, I. T."],["dc.date.accessioned","2017-09-07T11:43:16Z"],["dc.date.available","2017-09-07T11:43:16Z"],["dc.date.issued","2004"],["dc.description.abstract","The agent responsible for the recent severe acute respiratory syndrome (SARS) outbreak is a previously unidentified coronavirus. While there is a wealth of epidemiological studies, little if any molecular characterization of SARS coronavirus (SCoV) proteins has been carried out. Here we describe the molecular characterization of SCoV E protein, a critical component of the virus responsible for virion envelope morphogenesis. We conclusively show that SCoV E protein contains an unusually short, palindromic transmembrane helical hairpin around a previously unidentified pseudo-center of symmetry, a structural feature which seems to be unique to SCoV The hairpin deforms lipid bilayers by way of increasing their curvature, providing for the first time a molecular explanation of E protein's pivotal role in viral budding. The molecular understanding of this critical component of SCoV may represent the beginning of a concerted effort aimed at inhibiting its function, and consequently, viral infectivity. (C) 2004 Elsevier Ltd. All rights reserved."],["dc.identifier.doi","10.1016/j.jmb.2004.06.044"],["dc.identifier.gro","3143955"],["dc.identifier.isi","000223240200010"],["dc.identifier.pmid","15288785"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1526"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0022-2836"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Salditt (Structure of Biomolecular Assemblies and X-Ray Physics)"],["dc.subject.gro","membrane biophysics"],["dc.title","A highly unusual palindromic transmembrane helical hairpin formed by SARS coronavirus E protein"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","34"],["dc.bibliographiccitation.issue","1-2"],["dc.bibliographiccitation.lastpage","38"],["dc.bibliographiccitation.volume","357"],["dc.contributor.author","Khattari, Ziad"],["dc.contributor.author","Brotons, Guillaume"],["dc.contributor.author","Arbely, E"],["dc.contributor.author","Arkin, I. T."],["dc.contributor.author","Metzger, T. H."],["dc.contributor.author","Salditt, Tim"],["dc.date.accessioned","2017-09-07T11:54:32Z"],["dc.date.available","2017-09-07T11:54:32Z"],["dc.date.issued","2005"],["dc.description.abstract","We report on an anomalous X-ray reflectivity study to locate a labelled residue of a membrane protein with respect to the lipid bilayer. From such experiments, important constraints on the protein or peptide conformation can be derived. Specifically, our aim is to localize an iodine-labelled phenylalanine in the SARS E protein, incorporated in DMPC phospholipid bilayers, which are deposited in the form of thick multilamellar stacks on silicon surfaces. Here, we discuss the experimental aspects and the difficulties associated with the Fourier synthesis analysis that gives the electron density profile of the membranes. (C) 2004 Elsevier B.V. All rights reserved."],["dc.identifier.doi","10.1016/j.physb.2004.11.015"],["dc.identifier.gro","3143885"],["dc.identifier.isi","000227309100008"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1448"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Elsevier Science Bv"],["dc.publisher.place","Amsterdam"],["dc.relation.eissn","1873-2135"],["dc.relation.eventlocation","Bad Honnef, GERMANY"],["dc.relation.ispartof","Physica B: Condensed Matter"],["dc.relation.issn","0921-4526"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Salditt (Structure of Biomolecular Assemblies and X-Ray Physics)"],["dc.subject.gro","x-ray scattering"],["dc.subject.gro","membrane biophysics"],["dc.title","SARS E protein in phospholipid bilayers: an anomalous X-ray reflectivity study"],["dc.type","conference_paper"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2038"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.lastpage","2050"],["dc.bibliographiccitation.volume","90"],["dc.contributor.author","Khattari, Ziad"],["dc.contributor.author","Brotons, Guillaume"],["dc.contributor.author","Akkawi, M."],["dc.contributor.author","Arbely, E"],["dc.contributor.author","Arkin, I. T."],["dc.contributor.author","Salditt, Tim"],["dc.date.accessioned","2017-09-07T11:53:20Z"],["dc.date.available","2017-09-07T11:53:20Z"],["dc.date.issued","2006"],["dc.description.abstract","We investigated the structure of the hydrophobic domain of the severe acute respiratory syndrome E protein in model lipid membranes by x-ray reflectivity and x-ray scattering. In particular, we used x-ray reflectivity to study the location of an iodine-labeled residue within the lipid bilayer. The label imposes spatial constraints on the protein topology. Experimental data taken as a function of protein/lipid ratioP/L and different swelling states support the hairpin conformation of severe acute respiratory syndrome E protein reported previously. Changes in the bilayer thickness and acyl-chain ordering are presented as a function of P/L, and discussed in view of different structural models."],["dc.identifier.doi","10.1529/biophysj.105.072892"],["dc.identifier.gro","3143728"],["dc.identifier.isi","000235709500017"],["dc.identifier.pmid","16361349"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1274"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0006-3495"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Salditt (Structure of Biomolecular Assemblies and X-Ray Physics)"],["dc.subject.gro","x-ray scattering"],["dc.subject.gro","membrane biophysics"],["dc.title","SARS coronavirus E protein in phospholipid bilayers: An X-ray study"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]