Mobbing in Organisationen. Hintergründe, Ursachen, Bearbeitungsoptionen

Rabl, Tina; Rabl, Sabine

doi:10.1007/978-3-658-32797-2_13

Cited by 2 publications

(2 citation statements)

References 10 publications

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“…[38][39][40] We can only speculate on the mechanisms responsible of the Rabl-like configuration in marsupials as the function of this chromosome pattern still remains a mystery since its initial first cytological description. 41 Although speculative, it is possible that the Rabl configuration is a relic from anaphase-segregating chromosomes. 42 In this case, larger/longer chromosomes would establish a polarized pattern more readily during interphase with size and the heterochromatin distribution favoring a Rabl configuration.…”

Section: Discussionmentioning

confidence: 99%

Principles of 3D chromosome folding and evolutionary genome reshuffling in mammals

et al. 2022

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Section: Discussionmentioning

confidence: 99%

Principles of 3D chromosome folding and evolutionary genome reshuffling in mammals

et al. 2022

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“…Because these are, de facto, distinct proteins, having different ligands, it is conceptually correct to use two distinct FFs and to perform LD simulation started from A using FF B to reproduce the A→B transition occurring upon Ca 2+ binding, and, vice-versa, using FF A for the B→A inverse transition occurring upon Ca 2+ release. A few data are available for the difference in Gibbs free energy between the folded and denatured proteins ranging between ΔG A ~1.5-3.5 32,33 kcal/mole for the A state and ΔG B ~4.5-6.5 kcal/mole for the B state 33 . Energy alignment is not straightforward, however, one might assume the denatured state as reference, and infer that B state is more stable than A of about 2-4 kcal/mole.…”

Section: Molecular Dynamics Of the Open-closed Transition Of Calmodulinmentioning

confidence: 99%

Structural Transition States Explored With Minimalist Coarse Grained Models: Applications to Calmodulin

Delfino

Porozov

Stepanov

et al. 2019

Front. Mol. Biosci.

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Transitions between different conformational states are ubiquitous in proteins, being involved in signaling, catalysis, and other fundamental activities in cells. However, modeling those processes is extremely difficult, due to the need of efficiently exploring a vast conformational space in order to seek for the actual transition path for systems whose complexity is already high in the stable states. Here we report a strategy that simplifies this task attacking the complexity on several sides. We first apply a minimalist coarse-grained model to Calmodulin, based on an empirical force field with a partial structural bias, to explore the transition paths between the apo-closed state and the Ca-bound open state of the protein. We then select representative structures along the trajectory based on a structural clustering algorithm and build a cleaned-up trajectory with them. We finally compare this trajectory with that produced by the online tool MinActionPath, by minimizing the action integral using a harmonic network model, and with that obtained by the PROMPT morphing method, based on an optimal mass transportation-type approach including physical constraints. The comparison is performed both on the structural and energetic level, using the coarse-grained and the atomistic force fields upon reconstruction. Our analysis indicates that this method returns trajectories capable of exploring intermediate states with physical meaning, retaining a very low computational cost, which can allow systematic and extensive exploration of the multi-stable proteins transition pathways.

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Mobbing in Organisationen. Hintergründe, Ursachen, Bearbeitungsoptionen

Cited by 2 publications

References 10 publications

Principles of 3D chromosome folding and evolutionary genome reshuffling in mammals

Principles of 3D chromosome folding and evolutionary genome reshuffling in mammals

Structural Transition States Explored With Minimalist Coarse Grained Models: Applications to Calmodulin

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