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","563"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.lastpage","571"],["dc.bibliographiccitation.volume","89"],["dc.contributor.author","Manor, J."],["dc.contributor.author","Khattari, Ziad"],["dc.contributor.author","Salditt, Tim"],["dc.contributor.author","Arkin, I. T."],["dc.date.accessioned","2017-09-07T11:54:24Z"],["dc.date.available","2017-09-07T11:54:24Z"],["dc.date.issued","2005"],["dc.description.abstract","Linear dichroism, the unequal absorption of parallel and perpendicular linear polarized light, is often used to determine the anisotropic ordering of rodlike polymers in a smectic phase, such as helices in a lipid bilayer. It is a measure of two properties of the sample: 1), orientation of the chromophore transition dipole moment (TDM) and 2), disorder. Since it is the orientation of the chromophore TDM that is needed for high resolution structural studies, it is imperative to either deconvolve sample disorder, or at a minimum, estimate its effect upon the calculated TDM orientation. Herein, a rigorous analysis of the effects of disorder is undertaken based on the recently developed Gaussian disorder model implemented in linear dichroism data. The calculation of both the rod tilt and rotational pitch angles as a function of the disorder and dichroism, yield the following conclusions: Disorders smaller than 5 degrees have a vanishingly small effect on the calculated polymer orientation, whereas values smaller than 10 degrees have a negligible effect on the calculated parameters. Disorders larger than 10 degrees have an appreciable effect on the calculated orientational parameters and as such must be estimated before any structural characterization. Finally the theory is tested on the HIV vpu transmembrane domain, employing experimental mosaicity measurements from x-ray reflectivity rocking scans and linear dichroism."],["dc.identifier.doi","10.1529/biophysj.104.058842"],["dc.identifier.gro","3143826"],["dc.identifier.isi","000230114500057"],["dc.identifier.pmid","15834005"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1383"],["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","Disorder influence on linear dichroism analyses of smectic phases"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","45"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","European Biophysics Journal"],["dc.bibliographiccitation.lastpage","55"],["dc.bibliographiccitation.volume","36"],["dc.contributor.author","Khattari, Z."],["dc.contributor.author","Arbely, E."],["dc.contributor.author","Arkin, I. T."],["dc.contributor.author","Salditt, T."],["dc.date.accessioned","2017-09-07T11:49:54Z"],["dc.date.available","2017-09-07T11:49:54Z"],["dc.date.issued","2006"],["dc.description.abstract","We have investigated the effect of the transmembrane domain of three viral ion channel proteins on the lipid bilayer structure by X-ray reflectivity and scattering from oriented planar bilayers. The proteins show a similar effect on the lipid bilayer structural parameters: an increase in the lipid bilayer hydrophobic core, a decrease in the amplitude of the vertical density profile and a systematic change in the ordering of the acyl chains as a function of protein-to-lipid ratio. These results are discussed in a comparative view."],["dc.identifier.doi","10.1007/s00249-006-0099-x"],["dc.identifier.gro","3143578"],["dc.identifier.isi","000241897800005"],["dc.identifier.pmid","17019591"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1107"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0175-7571"],["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","Viral ion channel proteins in model membranes: a comparative study by X-ray reflectivity"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["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"]]