scholarly journals Artificial transmembrane signal transduction mediated by dynamic covalent chemistry

2021 ◽  
Author(s):  
Carlo Bravin ◽  
Nol Duindam ◽  
Christopher A. Hunter
Keyword(s):  
Signal Transduction ◽  
Dynamic Covalent Chemistry ◽  
Michael Acceptor ◽  
Reversible Formation ◽  
Covalent Adducts

Reversible formation of covalent adducts between a thiol and a membrane-anchored Michael acceptor has been used to control the activation of a caged enzyme encapsulated inside vesicles.

scholarly journals Template effects of vesicles in dynamic covalent chemistry

2020 ◽  
Vol 11 (34) ◽  
pp. 9122-9125 ◽  
Author(s):  
Carlo Bravin ◽  
Christopher A. Hunter
Keyword(s):  
Lipid Bilayers ◽  
Product Distribution ◽  
Dynamic Covalent Chemistry ◽  
Michael Adducts ◽  
Michael Acceptor

Vesicle lipid bilayers have been employed as templates to modulate the product distribution in a dynamic covalent library of Michael adducts formed by mixing a Michael acceptor with thiols.

Ultrastructural aspects of olfactory signal transduction and its development

1994 ◽  
Vol 52 ◽  
pp. 142-143
Author(s):  
Bert Ph. M. Menco
Keyword(s):  
Signal Transduction ◽  
Olfactory Receptor ◽  
Receptor Cell ◽  
Freeze Substitution ◽  
Luminal Surface ◽  
Tissue Sections ◽  
Olfactory Receptor Cells ◽  
Receptor Cells ◽  
Olfactory Signal ◽  
Odor Molecule

Vertebrate olfactory receptor cells are specialized neurons that have numerous long tapering cilia. The distal parts of these cilia line the interface between the external odorous environment and the luminal surface of the olfactory epithelium. The length and number of these cilia results in a large surface area that presumably increases the chance that an odor molecule will meet a receptor cell. Advanced methods of cryoprepration and immuno-gold labeling were particularly useful to preserve the delicate ultrastructural and immunocytochemical features of olfactory cilia required for localization of molecules involved in olfactory signal-transduction. We subjected olfactory tissues to freeze-substitution in acetone (unfixed tissues) or methanol (fixed tissues) followed by low temperature embedding in Lowicryl K11M for that purpose. Tissue sections were immunoreacted with several antibodies against proteins that are presumably important in olfactory signal-transduction.

Signal-regulated oxidation of proteins via MICAL

2020 ◽  
Vol 48 (2) ◽  
pp. 613-620
Author(s):  
Clara Ortegón Salas ◽  
Katharina Schneider ◽  
Christopher Horst Lillig ◽  
Manuela Gellert
Keyword(s):  
Signal Transduction ◽  
Hydrogen Peroxide ◽  
Cell Death ◽  
Redox Regulation ◽  
Signal Transduction Pathways ◽  
Cellular Functions ◽  
Intracellular Signals ◽  
Amino Acid Side Chains ◽  
Specific Receptors ◽  
Sulfur Containing

Processing of and responding to various signals is an essential cellular function that influences survival, homeostasis, development, and cell death. Extra- or intracellular signals are perceived via specific receptors and transduced in a particular signalling pathway that results in a precise response. Reversible post-translational redox modifications of cysteinyl and methionyl residues have been characterised in countless signal transduction pathways. Due to the low reactivity of most sulfur-containing amino acid side chains with hydrogen peroxide, for instance, and also to ensure specificity, redox signalling requires catalysis, just like phosphorylation signalling requires kinases and phosphatases. While reducing enzymes of both cysteinyl- and methionyl-derivates have been characterised in great detail before, the discovery and characterisation of MICAL proteins evinced the first examples of specific oxidases in signal transduction. This article provides an overview of the functions of MICAL proteins in the redox regulation of cellular functions.

Specificity of receptor-mediated signal transduction by E. coli type its heat-labile toxin

2001 ◽  
Vol 120 (5) ◽  
pp. A700-A700
Author(s):  
S WIMERMACKIN ◽  
R HOLMES ◽  
A WOLF ◽  
W LENCER ◽  
M JOBLING
Keyword(s):  
Signal Transduction ◽  
E Coli ◽  
Heat Labile

149: The Effect of Denervation on Signal Transduction Mechanisms of M2 and M3 Mediated Bladder Contractile Response

2005 ◽  
Vol 173 (4S) ◽  
pp. 40-40
Author(s):  
Leo R. Doumanian ◽  
Alan S. Braverman ◽  
Amitt S. Tibb ◽  
Michael R. Ruggieri
Keyword(s):  
Signal Transduction ◽  
Contractile Response ◽  
Transduction Mechanisms

1447: Neurotrophic Signal Transduction in Major Pelvic Ganglia

2004 ◽  
Vol 171 (4S) ◽  
pp. 381-381
Author(s):  
Guiting Lin ◽  
Ching-Shwun Lin ◽  
Tom F. Lue ◽  
San Francisco
Keyword(s):  
Signal Transduction ◽  
Pelvic Ganglia
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