Spatio-temporal source analysis

1997 ◽  
Vol 103 (1) ◽  
pp. 47
Author(s):  
M Scherq

1998 ◽  
Vol 11 (1) ◽  
pp. 21-28 ◽  
Author(s):  
Ina M. Tarkka ◽  
Luis F. H. Basile

This study was an attempt to replicate recent magnetoencephalographic (MEG) findings on human task-specific CNV sources (Basile et al., Electroencephalography and Clinical Neurophysiology 90, 1994, 157–165) by means of a spatio-temporal electric source localization method (Scherg and von Cramon, Electroencephalography and Clinical Neurophysiology 62, 1985, 32–44; Scherg and von Cramon, Electroencephalography and Clinical Neurophysiology 65, 1986, 344-360; Scherg and Berg, Brain Electric Source Analysis Handbook, Version 2). The previous MEG results showed CNV sources in the prefrontal cortex of the two hemispheres for two tasks used, namely visual pattern recognition and visual spatial recognition tasks. In the right hemisphere, the sources were more anterior and inferior for the spatial recognition task than for the pattern recognition task. In the present study we obtained CNVs in five subjects during two tasks identical to the MEG study. The elicited electric potentials were modeled with four spatio-temporal dipoles for each task, three of which accounted for the visual evoked response and one that accounted for the CNV. For all subjects the dipole explaining the CNV was always localized in the frontal region of the head, however, the dipole obtained during the visual spatial recognition task was more anterior than the one obtained during the pattern recognition task. Thus, task-specific CNV sources were again observed, although the stable model consisted of only one dipole located close to the midline instead of one dipole in each hemisphere. This was a major difference in the CNV sources between the previous MEG and the present electric source analysis results. We discuss the possible basis for the difference between the two methods used to study slow brain activity that is believed to originate from extended cortical patches.



2005 ◽  
Vol 52 (3) ◽  
pp. 414-420 ◽  
Author(s):  
L.J. Waldorp ◽  
H.M. Huizenga ◽  
A. Nehorai ◽  
R.P.P.P. Grasman ◽  
P.C.M. Molenaar


1997 ◽  
Vol 28 ◽  
pp. S191
Author(s):  
Minoru Hoshiyama ◽  
Ryusuke Kakigi ◽  
Sachiko Koyama


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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