Intramolecular Interaction between Nitroxide Radical and Photoexcited Benzophenone Triplet Linked to Peptide Templates

2003 ◽  
Vol 107 (36) ◽  
pp. 6905-6912 ◽  
Author(s):  
E. Sartori ◽  
A. Toffoletti ◽  
F. Rastrelli ◽  
C. Corvaja ◽  
A. Bettio ◽  
...  
Keyword(s):  
Intramolecular Interaction ◽  
Nitroxide Radical

A Possible Modulation Mechanism of Intramolecular and Intermolecular Interactions for NCAM Polysialylation and Cell Migration

2019 ◽  
Vol 19 (25) ◽  
pp. 2271-2282 ◽  
Author(s):  
Bo Lu ◽  
Xue-Hui Liu ◽  
Si-Ming Liao ◽  
Zhi-Long Lu ◽  
Dong Chen ◽  
...  
Keyword(s):  
Cell Migration ◽  
Intermolecular Interactions ◽  
Mammalian Cells ◽  
Molecular Mechanisms ◽  
Intramolecular Interaction ◽  
Polysialic Acid ◽  
Tumor Cell Migration ◽  
Neural Cell Adhesion ◽  
Polybasic Domains ◽  
Novel Model

Polysialic acid (polySia) is a novel glycan that posttranslationally modifies neural cell adhesion molecules (NCAMs) in mammalian cells. Up-regulation of polySia-NCAM expression or NCAM polysialylation is associated with tumor cell migration and progression in many metastatic cancers and neurocognition. It has been known that two highly homologous mammalian polysialyltransferases (polySTs), ST8Sia II (STX) and ST8Sia IV (PST), can catalyze polysialylation of NCAM, and two polybasic domains, polybasic region (PBR) and polysialyltransferase domain (PSTD) in polySTs play key roles in affecting polyST activity or NCAM polysialylation. However, the molecular mechanisms of NCAM polysialylation and cell migration are still not entirely clear. In this minireview, the recent research results about the intermolecular interactions between the PBR and NCAM, the PSTD and cytidine monophosphate-sialic acid (CMP-Sia), the PSTD and polySia, and as well as the intramolecular interaction between the PBR and the PSTD within the polyST, are summarized. Based on these cooperative interactions, we have built a novel model of NCAM polysialylation and cell migration mechanisms, which may be helpful to design and develop new polysialyltransferase inhibitors.

On possibilities of intramolecular interaction in (2-hydroxyethyl)- and (2-chloroethyl)aryldimethylsilanes

1974 ◽  
Vol 39 (8) ◽  
pp. 2253-2257 ◽  
Author(s):  
D. Šnobl ◽  
J. Vencl ◽  
J. Hetflejš ◽  
V. Chvalovský
Keyword(s):  
Intramolecular Interaction

Multifunctional properties of {CuII2LnIII2} systems involving nitrogen-rich nitronyl nitroxide: single-molecule magnet behavior, luminescence, magnetocaloric effects and heat capacity

2021 ◽  
Author(s):  
Hongdao Li ◽  
Pei Jing ◽  
Jiao Lu ◽  
Lu Xi ◽  
Qi Wang ◽  
...  
Keyword(s):  
Heat Capacity ◽  
Magnetic Properties ◽  
Single Molecule ◽  
Nitroxide Radical ◽  
Nitronyl Nitroxide ◽  
Nitronyl Nitroxide Radical ◽  
Single Molecule Magnet ◽  
Luminescence Behavior ◽  
Multifunctional Properties

A family of 3d–4f heterometallic ring-shaped clusters on the basis of a nitrogen-rich nitronyl nitroxide radical have been obtained, and they feature polyfunctionality including magnetic properties, thermodynamics and luminescence behavior.

One-dimensional magnetism of a linear chain compound containing yttrium(III) and a nitronyl nitroxide radical

1989 ◽  
Vol 28 (16) ◽  
pp. 3230-3234 ◽  
Author(s):  
Cristiano Benelli ◽  
Andrea Caneschi ◽  
Dante Gatteschi ◽  
Luca Pardi ◽  
Paul Rey
Keyword(s):  
Linear Chain ◽  
Nitroxide Radical ◽  
Nitronyl Nitroxide ◽  
Nitronyl Nitroxide Radical ◽  
One Dimensional ◽  
Chain Compound

scholarly journals Autoinhibition of the formin Cappuccino in the absence of canonical autoinhibitory domains

2012 ◽  
Vol 23 (19) ◽  
pp. 3801-3813 ◽  
Author(s):  
Batbileg Bor ◽  
Christina L. Vizcarra ◽  
Martin L. Phillips ◽  
Margot E. Quinlan
Keyword(s):  
Circular Dichroism ◽  
Binding Site ◽  
Actin Polymerization ◽  
Intramolecular Interaction ◽  
Hydrodynamic Analysis ◽  
A Site ◽  
Circular Dichroïsm

Formins are a conserved family of proteins known to enhance actin polymerization. Most formins are regulated by an intramolecular interaction. The Drosophila formin, Cappuccino (Capu), was believed to be an exception. Capu does not contain conserved autoinhibitory domains and can be regulated by a second protein, Spire. We report here that Capu is, in fact, autoinhibited. The N-terminal half of Capu (Capu-NT) potently inhibits nucleation and binding to the barbed end of elongating filaments by the C-terminal half of Capu (Capu-CT). Hydrodynamic analysis indicates that Capu-NT is a dimer, similar to the N-termini of other formins. These data, combined with those from circular dichroism, suggest, however, that it is structurally distinct from previously described formin inhibitory domains. Finally, we find that Capu-NT binds to a site within Capu-CT that overlaps with the Spire-binding site, the Capu-tail. We propose models for the interaction between Spire and Capu in light of the fact that Capu can be regulated by autoinhibition.

Nontrivial intramolecular interaction in ozonation of dimethyl ester of endo,cis-bicyclo[2,2,1]hept-5-en-2,3-dicarbonic acid in diethyl ether

1985 ◽  
Vol 26 (47) ◽  
pp. 5843-5844 ◽  
Author(s):  
Viktor N. Odinokov ◽  
Olga S. Kukovinets ◽  
Leonard M. Khalilov ◽  
Genrikh A. Tolstikov ◽  
Alexander Yu. Kosnikov ◽  
...  
Keyword(s):  
Diethyl Ether ◽  
Intramolecular Interaction ◽  
Dimethyl Ester ◽  
Dicarbonic Acid
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