2009
The Effect of Hydrophilic Substitutions and Anionic Lipids upon the Transverse Positioning of the Transmembrane Helix of the ErbB2 (neu) Protein Incorporated into Model Membrane Vesicles
Shahidullah K, Krishnakumar SS, London E. The Effect of Hydrophilic Substitutions and Anionic Lipids upon the Transverse Positioning of the Transmembrane Helix of the ErbB2 (neu) Protein Incorporated into Model Membrane Vesicles. Journal Of Molecular Biology 2009, 396: 209-220. PMID: 19931543, PMCID: PMC2821092, DOI: 10.1016/j.jmb.2009.11.037.Peer-Reviewed Original Research
2007
The Control of Transmembrane Helix Transverse Position in Membranes by Hydrophilic Residues
Krishnakumar SS, London E. The Control of Transmembrane Helix Transverse Position in Membranes by Hydrophilic Residues. Journal Of Molecular Biology 2007, 374: 1251-1269. PMID: 17997412, PMCID: PMC2175128, DOI: 10.1016/j.jmb.2007.10.032.Peer-Reviewed Original ResearchEffect of Sequence Hydrophobicity and Bilayer Width upon the Minimum Length Required for the Formation of Transmembrane Helices in Membranes
Krishnakumar SS, London E. Effect of Sequence Hydrophobicity and Bilayer Width upon the Minimum Length Required for the Formation of Transmembrane Helices in Membranes. Journal Of Molecular Biology 2007, 374: 671-687. PMID: 17950311, PMCID: PMC2121326, DOI: 10.1016/j.jmb.2007.09.037.Peer-Reviewed Original ResearchMembrane Topography of the Hydrophobic Anchor Sequence of Poliovirus 3A and 3AB Proteins and the Functional Effect of 3A/3AB Membrane Association upon RNA Replication †
Fujita K, Krishnakumar SS, Franco D, Paul AV, London E, Wimmer E. Membrane Topography of the Hydrophobic Anchor Sequence of Poliovirus 3A and 3AB Proteins and the Functional Effect of 3A/3AB Membrane Association upon RNA Replication †. Biochemistry 2007, 46: 5185-5199. PMID: 17417822, PMCID: PMC2519882, DOI: 10.1021/bi6024758.Peer-Reviewed Original ResearchConceptsModel membrane vesiclesAnchor sequenceHydrophobic anchor sequenceMembrane vesiclesViral protein 3ABFull-length proteinN-terminal boundaryTransmembrane topographyMembrane associationSuppressor mutationsTransmembrane segmentsProtein 3ABRNA polymeraseMembranous vesiclesC-terminusMembrane topographyCytoplasmic surfaceHost cellsRNA replicationPoliovirus RNAHeLa cellsSingle tryptophanProteinUridylylation reactionLipid bilayers
2002
Spatial Relationship between the Prodan Site, Trp-214, and Cys-34 Residues in Human Serum Albumin and Loss of Structure through Incremental Unfolding †
Krishnakumar SS, Panda D. Spatial Relationship between the Prodan Site, Trp-214, and Cys-34 Residues in Human Serum Albumin and Loss of Structure through Incremental Unfolding †. Biochemistry 2002, 41: 7443-7452. PMID: 12044178, DOI: 10.1021/bi025699v.Peer-Reviewed Original Research