Spatio-temporal invariants of the time reversal operator

2010 ◽  
Vol 127 (5) ◽  
pp. 2904-2912 ◽  
Author(s):  
Jean-Luc Robert ◽  
Mathias Fink
Author(s):  
Mathias Fink

Time-reversal invariance can be exploited in wave physics to control wave propagation in complex media. Because time and space play a similar role in wave propagation, time-reversed waves can be obtained by manipulating spatial boundaries or by manipulating time boundaries. The two dual approaches will be discussed in this paper. The first approach uses ‘time-reversal mirrors’ with a wave manipulation along a spatial boundary sampled by a finite number of antennas. Related to this method, the role of the spatio-temporal degrees of freedom of the wavefield will be emphasized. In a second approach, waves are manipulated from a time boundary and we show that ‘instantaneous time mirrors’, mimicking the Loschmidt point of view, simultaneously acting in the entire space at once can also radiate time-reversed waves.


2001 ◽  
Vol 109 (5) ◽  
pp. 2397-2397
Author(s):  
Mickael Tanter ◽  
Jean‐Francois Aubry ◽  
Jean‐Louis Thomas ◽  
Mathias Fink

2020 ◽  
Vol 29 (12) ◽  
pp. 125017
Author(s):  
Mazières Valentin ◽  
Romain Pascaud ◽  
Olivier Pascal ◽  
Richard Clergereaux ◽  
Luc Stafford ◽  
...  

2006 ◽  
Vol 120 (5) ◽  
pp. 3140-3140
Author(s):  
Jean‐Luc Robert ◽  
Mathias Fink

2004 ◽  
Vol 116 (3) ◽  
pp. 1348-1350 ◽  
Author(s):  
D. H. Chambers ◽  
J. V. Candy ◽  
S. K. Lehman ◽  
J. S. Kallman ◽  
A. J. Poggio ◽  
...  

2005 ◽  
Vol 41 ◽  
pp. 15-30 ◽  
Author(s):  
Helen C. Ardley ◽  
Philip A. Robinson

The selectivity of the ubiquitin–26 S proteasome system (UPS) for a particular substrate protein relies on the interaction between a ubiquitin-conjugating enzyme (E2, of which a cell contains relatively few) and a ubiquitin–protein ligase (E3, of which there are possibly hundreds). Post-translational modifications of the protein substrate, such as phosphorylation or hydroxylation, are often required prior to its selection. In this way, the precise spatio-temporal targeting and degradation of a given substrate can be achieved. The E3s are a large, diverse group of proteins, characterized by one of several defining motifs. These include a HECT (homologous to E6-associated protein C-terminus), RING (really interesting new gene) or U-box (a modified RING motif without the full complement of Zn2+-binding ligands) domain. Whereas HECT E3s have a direct role in catalysis during ubiquitination, RING and U-box E3s facilitate protein ubiquitination. These latter two E3 types act as adaptor-like molecules. They bring an E2 and a substrate into sufficiently close proximity to promote the substrate's ubiquitination. Although many RING-type E3s, such as MDM2 (murine double minute clone 2 oncoprotein) and c-Cbl, can apparently act alone, others are found as components of much larger multi-protein complexes, such as the anaphase-promoting complex. Taken together, these multifaceted properties and interactions enable E3s to provide a powerful, and specific, mechanism for protein clearance within all cells of eukaryotic organisms. The importance of E3s is highlighted by the number of normal cellular processes they regulate, and the number of diseases associated with their loss of function or inappropriate targeting.


2019 ◽  
Vol 47 (6) ◽  
pp. 1733-1747 ◽  
Author(s):  
Christina Klausen ◽  
Fabian Kaiser ◽  
Birthe Stüven ◽  
Jan N. Hansen ◽  
Dagmar Wachten

The second messenger 3′,5′-cyclic nucleoside adenosine monophosphate (cAMP) plays a key role in signal transduction across prokaryotes and eukaryotes. Cyclic AMP signaling is compartmentalized into microdomains to fulfil specific functions. To define the function of cAMP within these microdomains, signaling needs to be analyzed with spatio-temporal precision. To this end, optogenetic approaches and genetically encoded fluorescent biosensors are particularly well suited. Synthesis and hydrolysis of cAMP can be directly manipulated by photoactivated adenylyl cyclases (PACs) and light-regulated phosphodiesterases (PDEs), respectively. In addition, many biosensors have been designed to spatially and temporarily resolve cAMP dynamics in the cell. This review provides an overview about optogenetic tools and biosensors to shed light on the subcellular organization of cAMP signaling.


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