about
Preprotein-controlled catalysis in the helicase motor of SecAStructure of dimeric SecA, the Escherichia coli preprotein translocase motorStructural Basis for Signal-Sequence Recognition by the Translocase Motor SecA as Determined by NMRStructural Instability Tuning as a Regulatory Mechanism in Protein-Protein InteractionsStructural Basis for Protein Antiaggregation Activity of the Trigger Factor ChaperoneCross-talk between catalytic and regulatory elements in a DEAD motor domain is essential for SecA function.Using nanoelectrospray ion mobility spectrometry (GEMMA) to determine the size and relative molecular mass of proteins and protein assemblies: a comparison with MALLS and QELS.Quantitative analysis of energy transfer between fluorescent proteins in CFP-GBP-YFP and its response to Ca2+.Cloning, purification and characterization of a functional anthracycline glycosyltransferase.Following the leader: bacterial protein export through the Sec pathway.Bacterial protein translocase: a unique molecular machine with an army of substrates.Proteome-wide subcellular topologies of E. coli polypeptides database (STEPdb).Fast and reliable strain characterization of Streptomyces lividans through micro-scale cultivation.The Escherichia coli peripheral inner membrane proteome.Assembly of the translocase motor onto the preprotein-conducting channel.Recognition and targeting mechanisms by chaperones in flagellum assembly and operationSecA: a tale of two protomers.Breaking on through to the other side: protein export through the bacterial Sec system.Antibiotic targeting of the bacterial secretory pathway.SecA-mediated targeting and translocation of secretory proteins.Comparative proteomic analysis of hypertrophic chondrocytes in osteoarthritis.Type III Secretion: Building and Operating a Remarkable Nanomachine.MatureP: prediction of secreted proteins with exclusive information from their mature regions.Proteome Changes during Transition from Human Embryonic to Vascular Progenitor Cells.Protein folding in the cell envelope of Escherichia coli.Analysis of Translocation-Competent Secretory Proteins by HDX-MS.Quantitative Proteomics of the E. coli Membranome.Protein export through the bacterial Sec pathway.Xilmass: A New Approach toward the Identification of Cross-Linked Peptides.Helicase Motif III in SecA is essential for coupling preprotein binding to translocation ATPase.Rapid label-free quantitative analysis of the E. coli BL21(DE3) inner membrane proteome.Identification of small-molecule inhibitors against SecA by structure-based virtual ligand screening.Complete genome sequence of Streptomyces lividans TK24.Double hexameric ring assembly of the type III protein translocase ATPase HrcN.Bacterial preprotein translocase: mechanism and conformational dynamics of a processive enzyme.Dynamics and ligand-induced conformational changes in human prolyl oligopeptidase analyzed by hydrogen/deuterium exchange mass spectrometryType III protein translocase: HrcN is a peripheral ATPase that is activated by oligomerization.Identification of the preprotein binding domain of SecA.Preprotein mature domains contain translocase targeting signals that are essential for secretion.NS5A mutations predict biochemical but not virological response to interferon-alpha treatment of sporadic hepatitis C virus infection in European patients.
P50
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P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Anastassios Economou
@ast
Anastassios Economou
@en
Anastassios Economou
@es
Anastassios Economou
@nl
type
label
Anastassios Economou
@ast
Anastassios Economou
@en
Anastassios Economou
@es
Anastassios Economou
@nl
altLabel
Tassos Economou
@en
prefLabel
Anastassios Economou
@ast
Anastassios Economou
@en
Anastassios Economou
@es
Anastassios Economou
@nl
P1053
P-8292-2017
P106
P1153
7006124323
P21
P2798
P31
P3829
P496
0000-0002-1770-507X