Quantitative and spatio-temporal features of protein aggregation in Escherichia coli and consequences on protein quality control and cellular ageing. - Wikidata - wikimedia - TriplyDB

Quantitative and spatio-temporal features of protein aggregation in Escherichia coli and consequences on protein quality control and cellular ageing.

Quantitative and spatio-temporal features of protein aggregation in Escherichia coli and consequences on protein quality control and cellular ageing.

http://www.wikidata.org/entity/Q30493630

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Localization of protein aggregation in Escherichia coli is governed by diffusion and nucleoid macromolecular crowding effect Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae Robust growth of Escherichia coli.Mechanism to control the cell lysis and the cell survival strategy in stationary phase under heat stress Genetic Manipulation of Glycogen Allocation Affects Replicative Lifespan in E. coli An essential nonredundant role for mycobacterial DnaK in native protein folding Fusion of protein aggregates facilitates asymmetric damage segregation Cytoplasmic dynein is required for the spatial organization of protein aggregates in filamentous fungi RepA-WH1, the agent of an amyloid proteinopathy in bacteria, builds oligomeric pores through lipid vesicles.Mycobacterium tuberculosis proteins involved in mycolic acid synthesis and transport localize dynamically to the old growing pole and septum Some Like It Hot: Heat Resistance of Escherichia coli in Food On the Spatial Organization of mRNA, Plasmids, and Ribosomes in a Bacterial Host Overexpressing Membrane Proteins Stabilization of homoserine-O-succinyltransferase (MetA) decreases the frequency of persisters in Escherichia coli under stressful conditions Protein recovery from inclusion bodies of Escherichia coli using mild solubilization process.Overproduced Brucella abortus PdhS-mCherry forms soluble aggregates in Escherichia coli, partially associating with mobile foci of IbpA-YFP.Segregation of molecules at cell division reveals native protein localization.The Protein Chaperone ClpX Targets Native and Non-native Aggregated Substrates for Remodeling, Disassembly, and Degradation with ClpP Chromosome driven spatial patterning of proteins in bacteria Phenotypic plasticity and effects of selection on cell division symmetry in Escherichia coli.Aging, mortality, and the fast growth trade-off of Schizosaccharomyces pombe.Cellular strategies of protein quality control.Vital dye reaction and granule localization in periplasm of Escherichia coli Global analysis of protein aggregation in yeast during physiological conditions and arsenite stress.Protein aggregation caused by aminoglycoside action is prevented by a hydrogen peroxide scavenger.Critique of the use of fluorescence-based reporters in Escherichia coli as a screening tool for the identification of peptide inhibitors of Aβ42 aggregation.The formation of persister cells in stationary-phase cultures of Escherichia coli is associated with the aggregation of endogenous proteins Repair rather than segregation of damage is the optimal unicellular aging strategy Cytoplasmic dynamics reveals two modes of nucleoid-dependent mobility Non-equilibrium polar localization of proteins in bacterial cells Localization of GroEL determined by in vivo incorporation of a fluorescent amino acid.Protein aggregation in E. coli : short term and long term effects of nutrient density.Pole age affects cell size and the timing of cell division in Methylobacterium extorquens AM1.Overexpressed Arabidopsis Annexin4 accumulates in inclusion body-like structures.Dynamical Localization of DivL and PleC in the Asymmetric Division Cycle of Caulobacter crescentus: A Theoretical Investigation of Alternative Models.Operational Principles for the Dynamics of the In Vitro ParA-ParB System Periplasmic Acid Stress Increases Cell Division Asymmetry (Polar Aging) of Escherichia coli.Gene location and DNA density determine transcription factor distributions in Escherichia coli.Surfing biological surfaces: exploiting the nucleoid for partition and transport in bacteria Hsp33 controls elongation factor-Tu stability and allows Escherichia coli growth in the absence of the major DnaK and trigger factor chaperones Fluorescence Turn-On Folding Sensor To Monitor Proteome Stress in Live Cells.

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Quantitative and spatio-temporal features of protein aggregation in Escherichia coli and consequences on protein quality control and cellular ageing.

http://www.wikidata.org/entity/Q30493630

description

2010 nî lūn-bûn

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2010 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2010 թվականի հունվարին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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Quantitative and spatio-tempor ...... y control and cellular ageing.

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Quantitative and spatio-tempor ...... y control and cellular ageing.

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Quantitative and spatio-tempor ...... y control and cellular ageing.

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Quantitative and spatio-tempor ...... y control and cellular ageing.

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Quantitative and spatio-tempor ...... y control and cellular ageing.

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The EMBO Journal

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Quantitative and spatio-tempor ...... y control and cellular ageing.

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Anja Seybert

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Juliane Winkler

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Lars König

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Matthias Weiss

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Sabine Pruggnaller

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Uta Haselmann

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P2860

Aging and death in an organism that reproduces by morphologically symmetric division

The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress

Misfolded proteins partition between two distinct quality control compartments

Polarised asymmetric inheritance of accumulated protein damage in higher eukaryotes

Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins.

HSP104 required for induced thermotolerance.

Molecular chaperones in the cytosol: from nascent chain to folded protein

Culture medium for enterobacteria

Asymmetric segregation of protein aggregates is associated with cellular aging and rejuvenation.

Tsr-GFP accumulates linearly with time at cell poles, and can be used to differentiate 'old' versus 'new' poles, in Escherichia coli.

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910-923

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10.1038/EMBOJ.2009.412

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5

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29

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Achilleas S Frangakis

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2010-01-21T00:00:00Z

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41112105

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20094032

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quality control

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2837176

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