scholarly journals Cover Picture: Mechanistic Origin of the Vibrational Coherence Accompanying the Photoreaction of Biomimetic Molecular Switches (Chem. Eur. J. 48/2012)

2012 ◽  
Vol 18 (48) ◽  
pp. 15209-15209
Author(s):  
Jérémie Léonard ◽  
Igor Schapiro ◽  
Julien Briand ◽  
Stefania Fusi ◽  
Riccardo Rossi Paccani ◽  
...  
Keyword(s):  
Molecular Switches ◽  
Vibrational Coherence

scholarly journals Vibrational coherence and quantum yield of retinal-chromophore-inspired molecular switches

2020 ◽  
Vol 221 ◽  
pp. 299-321 ◽  
Author(s):  
Moussa Gueye ◽  
Marco Paolino ◽  
Etienne Gindensperger ◽  
Stefan Haacke ◽  
Massimo Olivucci ◽  
...  
Keyword(s):  
Quantum Yield ◽  
Transient Absorption ◽  
Molecular Switches ◽  
Systematic Investigation ◽  
Vibrational Coherence ◽  
Retinal Chromophore ◽  
Molecular Framework

UV-Vis transient absorption (TA) spectroscopy is used to carry out a systematic investigation of the ultrafast CC double photoisomerization dynamics and quantum yield of each isomer of a set of six chromophores based on the same retinal-inspired, indanylidene pyrrolinium (IP) molecular framework.

Mechanistic Origin of the Vibrational Coherence Accompanying the Photoreaction of Biomimetic Molecular Switches

2012 ◽  
Vol 18 (48) ◽  
pp. 15296-15304 ◽  
Author(s):  
Jérémie Léonard ◽  
Igor Schapiro ◽  
Julien Briand ◽  
Stefania Fusi ◽  
Riccardo Rossi Paccani ◽  
...  
Keyword(s):  
Molecular Switches ◽  
Vibrational Coherence

Protein tyrosine phosphatases: molecular switches in metabolism and diabetes

2015 ◽  
Vol 26 (1) ◽  
pp. 30-39 ◽  
Author(s):  
Esteban N. Gurzov ◽  
William J. Stanley ◽  
Thomas C. Brodnicki ◽  
Helen E. Thomas
Keyword(s):  
Protein Tyrosine Phosphatases ◽  
Molecular Switches ◽  
Tyrosine Phosphatases ◽  
Protein Tyrosine

Metal ions doped into merocyanine form of coumarin derivatives: nonlinear optical molecular switches

2019 ◽  
Vol 25 (8) ◽  
Author(s):  
Ali Muhammad Arif ◽  
Afifa Yousaf ◽  
Rong-Lin Zhong ◽  
Mansoor Akhtar ◽  
Shabbir Muhammad ◽  
...  
Keyword(s):  
Metal Ions ◽  
Nonlinear Optical ◽  
Molecular Switches ◽  
Merocyanine Form ◽  
Coumarin Derivatives

scholarly journals Pore-forming Esx proteins mediate toxin secretion by Mycobacterium tuberculosis

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Uday Tak ◽  
Terje Dokland ◽  
Michael Niederweis
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Pore Formation ◽  
Molecular Switches ◽  
Water Soluble ◽  
Host Cells ◽  
Solvent Exposure ◽  
Membrane Channel ◽  
Toxin Secretion ◽  
Outer Membrane Channel ◽  
Membrane Spanning

AbstractMycobacterium tuberculosis secretes the tuberculosis necrotizing toxin (TNT) to kill host cells. Here, we show that the WXG100 proteins EsxE and EsxF are essential for TNT secretion. EsxE and EsxF form a water-soluble heterodimer (EsxEF) that assembles into oligomers and long filaments, binds to membranes, and forms stable membrane-spanning channels. Electron microscopy of EsxEF reveals mainly pentameric structures with a central pore. Mutations of both WXG motifs and of a GXW motif do not affect dimerization, but abolish pore formation, membrane deformation and TNT secretion. The WXG/GXW mutants are locked in conformations with altered thermostability and solvent exposure, indicating that the WXG/GXW motifs are molecular switches controlling membrane interaction and pore formation. EsxF is accessible on the bacterial cell surface, suggesting that EsxEF form an outer membrane channel for toxin export. Thus, our study reveals a protein secretion mechanism in bacteria that relies on pore formation by small WXG proteins.

scholarly journals PAK and other Rho-associated kinases – effectors with surprisingly diverse mechanisms of regulation

2005 ◽  
Vol 386 (2) ◽  
pp. 201-214 ◽  
Author(s):  
Zhou-shen ZHAO ◽  
Ed MANSER
Keyword(s):  
Rho Gtpases ◽  
Cell Biology ◽  
Rho Gtpase ◽  
Rho Kinase ◽  
Molecular Switches ◽  
Eukaryotic Cell ◽  
Effector Proteins ◽  
Downstream Effector ◽  
P21 Activated Kinase ◽  
Do So

The Rho GTPases are a family of molecular switches that are critical regulators of signal transduction pathways in eukaryotic cells. They are known principally for their role in regulating the cytoskeleton, and do so by recruiting a variety of downstream effector proteins. Kinases form an important class of Rho effector, and part of the biological complexity brought about by switching on a single GTPase results from downstream phosphorylation cascades. Here we focus on our current understanding of the way in which different Rho-associated serine/threonine kinases, denoted PAK (p21-activated kinase), MLK (mixed-lineage kinase), ROK (Rho-kinase), MRCK (myotonin-related Cdc42-binding kinase), CRIK (citron kinase) and PKN (protein kinase novel), interact with and are regulated by their partner GTPases. All of these kinases have in common an ability to dimerize, and in most cases interact with a variety of other proteins that are important for their function. A diversity of known structures underpin the Rho GTPase–kinase interaction, but only in the case of PAK do we have a good molecular understanding of kinase regulation. The ability of Rho GTPases to co-ordinate spatial and temporal phosphorylation events explains in part their prominent role in eukaryotic cell biology.

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