SRP-dependent co-translational targeting and SecA-dependent translocation analyzed as individual steps in the export of a bacterial protein. - Wikidata - wikimedia - TriplyDB

SRP-dependent co-translational targeting and SecA-dependent translocation analyzed as individual steps in the export of a bacterial protein.

SRP-dependent co-translational targeting and SecA-dependent translocation analyzed as individual steps in the export of a bacterial protein.

http://www.wikidata.org/entity/Q40388434

about

Structure of the E. coli protein-conducting channel bound to a translating ribosome Visualization of a polytopic membrane protein during SecY-mediated membrane insertion YidC, an assembly site for polytopic Escherichia coli membrane proteins located in immediate proximity to the SecYE translocon and lipids Evidence for a novel GTPase priming step in the SRP protein targeting pathway.Secretion of LamB-LacZ by the signal recognition particle pathway of Escherichia coli Two-partner secretion of gram-negative bacteria: a single β-barrel protein enables transport across the outer membrane Predominant membrane localization is an essential feature of the bacterial signal recognition particle receptor.Molecular cloning, expression of testicular transcript abundant in germ cells and immunobiological effects of the recombinant protein.Peculiar properties of DsbA in its export across the Escherichia coli cytoplasmic membrane Target-directed proteolysis at the ribosome.Dynamic interaction of the sec translocon with the chaperone PpiD Novel proteomic tools reveal essential roles of SRP and importance of proper membrane protein biogenesis Biogenesis of inner membrane proteins in Escherichia coli.SecA drives transmembrane insertion of RodZ, an unusual single-span membrane protein.Heat shock transcription factor σ32 co-opts the signal recognition particle to regulate protein homeostasis in E. coli.The translational regulatory function of SecM requires the precise timing of membrane targeting.Secretome of obligate intracellular Rickettsia.Signal recognition particle and SecA cooperate during export of secretory proteins with highly hydrophobic signal sequences.Small RNA Transcriptome of the Oral Microbiome during Periodontitis Progression.Promiscuous targeting of polytopic membrane proteins to SecYEG or YidC by the Escherichia coli signal recognition particle.Regulation by a chaperone improves substrate selectivity during cotranslational protein targeting Membrane binding of the bacterial signal recognition particle receptor involves two distinct binding sites Sec-dependent protein translocation across biological membranes: evolutionary conservation of an essential protein transport pathway (review).Oxa1/Alb3/YidC system for insertion of membrane proteins in mitochondria, chloroplasts and bacteria (review).Ligand crowding at a nascent signal sequence.Dissecting structures and functions of SecA-only protein-conducting channels: ATPase, pore structure, ion channel activity, protein translocation, and interaction with SecYEG/SecDF•YajC.Rational design of ultrastable and reversibly photoswitchable fluorescent proteins for super-resolution imaging of the bacterial periplasm.Protein export by the mycobacterial SecA2 system is determined by the preprotein mature domain.Stability of the cbb3-type cytochrome oxidase requires specific CcoQ-CcoP interactions.Mapping polypeptide interactions of the SecA ATPase during translocation.Lipid dependencies, biogenesis and cytoplasmic micellar forms of integral membrane sugar transport proteins of the bacterial phosphotransferase system.The Sec translocon mediated protein transport in prokaryotes and eukaryotes.Separate analysis of twin-arginine translocation (Tat)-specific membrane binding and translocation in Escherichia coli.Role for both DNA and RNA in GTP hydrolysis by the Neisseria gonorrhoeae signal recognition particle receptor Identification of ZipA, a signal recognition particle-dependent protein from Neisseria gonorrhoeae.Capsid protease domain as a tool for assessing protein-domain folding during organelle import of nascent polypeptides in living cells.Electrostatics and Intrinsic Disorder Drive Translocon Binding of the SRP Receptor FtsY.Reconstitution of Sec-dependent membrane protein insertion: nascent FtsQ interacts with YidC in a SecYEG-dependent manner.Visualization of distinct entities of the SecYEG translocon during translocation and integration of bacterial proteins Signal sequence-independent SRP-SR complex formation at the membrane suggests an alternative targeting pathway within the SRP cycle.

P2860

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P2860

SRP-dependent co-translational targeting and SecA-dependent translocation analyzed as individual steps in the export of a bacterial protein.

http://www.wikidata.org/entity/Q40388434

description

2000 nî lūn-bûn

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2000年の論文

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2000年学术文章

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2000年学术文章

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2000年学术文章

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2000年学术文章

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2000年学术文章

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2000年學術文章

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2000年學術文章

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2000年學術文章

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name

SRP-dependent co-translational ...... export of a bacterial protein.

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type

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SRP-dependent co-translational ...... export of a bacterial protein.

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prefLabel

SRP-dependent co-translational ...... export of a bacterial protein.

@en

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The EMBO Journal

P1476

SRP-dependent co-translational ...... export of a bacterial protein.

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P2093

C Neumann-Haefelin

http://www.w3.org/2001/XMLSchema#string

H G Koch

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M Müller

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U Schäfer

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P2860

The E. coli signal recognition particle is required for the insertion of a subset of inner membrane proteins

The structure of multiple polypeptide domains determines the signal recognition particle targeting requirement of Escherichia coli inner membrane proteins.

The translocon: a dynamic gateway at the ER membrane.

A mutant hunt for defects in membrane protein assembly yields mutations affecting the bacterial signal recognition particle and Sec machinery

Differential use of the signal recognition particle translocase targeting pathway for inner membrane protein assembly in Escherichia coli.

Binding of signal recognition particle gives ribosome/nascent chain complexes a competitive advantage in endoplasmic reticulum membrane interaction.

Signal recognition particle-dependent targeting of ribosomes to the rough endoplasmic reticulum in the absence and presence of the nascent polypeptide-associated complex.

Membrane topology analysis of Escherichia coli mannitol permease by using a nested-deletion method to create mtlA-phoA fusions

A site-specific, membrane-dependent cleavage event defines the membrane binding domain of FtsY.

In vitro studies with purified components reveal signal recognition particle (SRP) and SecA/SecB as constituents of two independent protein-targeting pathways of Escherichia coli.

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6419-6426

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23

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19

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305875

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