Understanding variability in ethanol teratogenicity

Eberhart, Johann K.; Harris, R. Adron

doi:10.1073/pnas.1302650110

Cited by 4 publications

(4 citation statements)

References 30 publications

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“…In the absence of an external energy source to promote OMP sorting away from the plasma membrane and towards the outer membrane, the only chemical potentials available as driving forces are the OMP folding stabilities and/or the uOMP-chaperone binding free energies [9]. The thermodynamic pull in this sorting hypothesis originates from the observations of unusually high OMP folding stabilities, DG Fold .…”

Section: Sorting Across the Periplasm And Folding Intomentioning

confidence: 99%

“…The thermodynamic pull in this sorting hypothesis originates from the observations of unusually high OMP folding stabilities, DG Fold . OmpLA, PagP and OmpW all have free energies of folding into large unilamellar vesicles (LUVs) in the range 218 to 232 kcal mol 21 [9,10]. These are very large values, and an interesting thought experiment can be constructed to consider their magnitudes: if an Avogadro's number of OMPs possessing the stability of OmpLA (232 kcal mol 21 ) could be envisioned to exist within a Gram-negative bacterium, at equilibrium fewer than 100 of these molecules would be unfolded.…”

Section: Sorting Across the Periplasm And Folding Intomentioning

confidence: 99%

“…The differences between these values and the OMP folding free energies are at least 10 kcal mol 21 , a value that is a thermodynamic potential easily large enough to drive uOMPs into their native conformations. [9]. All numbers in this schematic are standard state free energies measured in vitro reported in kcal mol 21 .…”

Section: Sorting Across the Periplasm And Folding Intomentioning

confidence: 99%

“…Schematic of known thermodynamic parameters for periplasmic folding of outer membrane proteins. Modified from Moon et al[9]. All numbers in this schematic are standard state free energies measured in vitro reported in kcal mol21 .…”

mentioning

confidence: 99%

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A combined kinetic push and thermodynamic pull as driving forces for outer membrane protein sorting and folding in bacteria

Fleming

2015

Phil. Trans. R. Soc. B

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One contribution of 12 to a theme issue 'The bacterial cell envelope'. In vitro folding studies of outer membrane beta-barrels have been invaluable in revealing the lipid effects on folding rates and efficiencies as well as folding free energies. Here, the biophysical results are summarized, and these kinetic and thermodynamic findings are considered in terms of the requirements for folding in the context of the cellular environment. Because the periplasm lacks an external energy source the only driving forces for sorting and folding available within this compartment are binding or folding free energies and their associated rates. These values define functions for periplasmic chaperones and suggest a biophysical mechanism for the BAM complex.

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Section: Sorting Across the Periplasm And Folding Intomentioning

confidence: 99%

Section: Sorting Across the Periplasm And Folding Intomentioning

confidence: 99%

Section: Sorting Across the Periplasm And Folding Intomentioning

confidence: 99%

mentioning

confidence: 99%

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A combined kinetic push and thermodynamic pull as driving forces for outer membrane protein sorting and folding in bacteria

Fleming

2015

Phil. Trans. R. Soc. B

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A Fragment of Adhesion Molecule L1 Binds to Nuclear Receptors to Regulate Synaptic Plasticity and Motor Coordination

et al. 2018

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Proteolytic cleavage of the neuronal isoform of the murine cell adhesion molecule L1, triggered by stimulation of the cognate L1-dependent signaling pathways, results in the generation and nuclear import of an L1 fragment that contains the intracellular domain, the transmembrane domain, and part of the extracellular domain. Here, we show that the LXXLL and FXXLF motifs in the extracellular and transmembrane domain of this L1 fragment mediate the interaction with the nuclear estrogen receptors α (ERα) and β (ERβ), peroxisome proliferator-activated receptor γ (PPARγ), and retinoid X receptor β (RXRβ). Mutations of the LXXLL motif in the transmembrane domain and of the FXXLF motif in the extracellular domain disturb the interaction of the L1 fragment with these nuclear receptors and, when introduced by viral transduction into mouse embryos in utero, result in impaired motor coordination, learning and memory, as well as synaptic connectivity in the cerebellum, in adulthood. These impairments are similar to those observed in the L1-deficient mouse. Our findings suggest that the interplay of nuclear L1 and distinct nuclear receptors is associated with synaptic contact formation and plasticity.

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Intra-laboratory validated human cell-based in vitro vasculogenesis/angiogenesis test with serum-free medium

Toimela

Huttala

Sabell

et al. 2017

Reproductive Toxicology

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Understanding variability in ethanol teratogenicity

Cited by 4 publications

References 30 publications

A combined kinetic push and thermodynamic pull as driving forces for outer membrane protein sorting and folding in bacteria

A combined kinetic push and thermodynamic pull as driving forces for outer membrane protein sorting and folding in bacteria

A Fragment of Adhesion Molecule L1 Binds to Nuclear Receptors to Regulate Synaptic Plasticity and Motor Coordination

Intra-laboratory validated human cell-based in vitro vasculogenesis/angiogenesis test with serum-free medium

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