scholarly journals Hydrophosphorylation of aliphatic alkynes catalyzed by CuNPs/ZnO for the synthesis of vinyl phosphonates. A DFT study on the reaction mechanism

RSC Advances ◽  
2017 ◽  
Vol 7 (30) ◽  
pp. 18707-18713 ◽  
Author(s):  
Leandro Fortunato ◽  
Yanina Moglie ◽  
Viviana Dorn ◽  
Gabriel Radivoy
Keyword(s):  
Reaction Mechanism ◽  
Essential Role ◽  
Catalyst Support ◽  
Dft Study ◽  
Vinyl Phosphonates

A DFT study on the reaction mechanism for the synthesis of vinyl phosphonates catalyzed by CuNPs/ZnO. Essential role of the solvent and the catalyst support.

Theoretical investigation on the hydrogen evolution reaction mechanism at MoS2 heterostructures: the essential role of the 1T/2H phase interface

2020 ◽  
Vol 10 (2) ◽  
pp. 458-465 ◽  
Author(s):  
Tian Zhang ◽  
Houyu Zhu ◽  
Chen Guo ◽  
Shoufu Cao ◽  
Chi-Man Lawrence Wu ◽  
...  
Keyword(s):  
Reaction Mechanism ◽  
Dft Calculations ◽  
Hydrogen Evolution ◽  
Theoretical Investigation ◽  
Hydrogen Evolution Reaction ◽  
Basal Plane ◽  
Essential Role ◽  
Phase Interface

DFT calculations have been performed to study the HER mechanism at 1T/2H MoS2 heterostructures. The HER activity along the 1T/2H phase interface is comparable with those at the Mo-edge of 2H MoS2 and the basal plane of 1T MoS2.

A DFT study on NHC-catalyzed intramolecular aldehyde–ketone crossed-benzoin reaction: mechanism, regioselectivity, stereoselectivity, and role of NHC

2016 ◽  
Vol 14 (27) ◽  
pp. 6577-6590 ◽  
Author(s):  
Wei Zhang ◽  
Yang Wang ◽  
Donghui Wei ◽  
Mingsheng Tang ◽  
Xinju Zhu
Keyword(s):  
Reaction Mechanism ◽  
Computational Study ◽  
Dft Method ◽  
Dft Study

A computational study on NHC-catalyzed intramolecular aldehyde–ketone crossed-benzoin reaction has been performed using a DFT method.

Essential role of Sharpin in TNFα dependent NFκB activation in primary hepatocytes

2012 ◽  
Vol 50 (01) ◽  
Author(s):  
N Lange ◽  
S Sieber ◽  
A Erhardt ◽  
G Sass ◽  
HJ Kreienkamp ◽  
...  
Keyword(s):  
Essential Role ◽  
Primary Hepatocytes

Different Abilities of Thrombin Receptor Activating Peptide and Thrombin to Induce Platelet Calcium Rise and Full Release Reaction

1995 ◽  
Vol 74 (05) ◽  
pp. 1323-1328 ◽  
Author(s):  
Dominique Lasne ◽  
José Donato ◽  
Hervé Falet ◽  
Francine Rendu
Keyword(s):  
Essential Role ◽  
Calcium Influx ◽  
Dense Granule ◽  
Receptor Interaction ◽  
Thrombin Receptor ◽  
Release Reaction ◽  
External Calcium ◽  
Maximum Rise ◽  
Granule Release

SummarySynthetic peptides (TRAP or Thrombin Receptor Activating Peptide) corresponding to at least the first five aminoacids of the new N-terminal tail generated after thrombin proteolysis of its receptor are effective to mimic thrombin. We have studied two different TRAPs (SFLLR, and SFLLRN) in their effectiveness to induce the different platelet responses in comparison with thrombin. Using Indo-1/AM- labelled platelets, the maximum rise in cytoplasmic ionized calcium was lower with TRAPs than with thrombin. At threshold concentrations allowing maximal aggregation (50 μM SFLLR, 5 μM SFLLRN and 1 nM thrombin) the TRAPs-induced release reaction was about the same level as with thrombin, except when external calcium was removed by addition of 1 mM EDTA. In these conditions, the dense granule release induced by TRAPs was reduced by over 60%, that of lysosome release by 75%, compared to only 15% of reduction in the presence of thrombin. Thus calcium influx was more important for TRAPs-induced release than for thrombin-induced release. At strong concentrations giving maximal aggregation and release in the absence of secondary mediators (by pretreatment with ADP scavengers plus aspirin), SFLLRN mobilized less calcium, with a fast return towards the basal level and induced smaller lysosome release than did thrombin. The results further demonstrate the essential role of external calcium in triggering sustained and full platelet responses, and emphasize the major difference between TRAP and thrombin in mobilizing [Ca2+]j. Thus, apart from the proteolysis of the seven transmembrane receptor, another thrombin binding site or thrombin receptor interaction is required to obtain full and complete responses.

Collagen-Induced Platelet Aggregation: -Evidence Against the Essential Role of Platelet Adenosine Diphosphate

1979 ◽  
Vol 42 (04) ◽  
pp. 1193-1206 ◽  
Author(s):  
Barbara Nunn
Keyword(s):  
Platelet Aggregation ◽  
Time Course ◽  
Essential Role ◽  
Atp Release ◽  
Adenosine Diphosphate ◽  
Human Platelets ◽  
High Doses ◽  
Induced Aggregation

SummaryThe hypothesis that platelet ADP is responsible for collagen-induced aggregation has been re-examined. It was found that the concentration of ADP obtaining in human PRP at the onset of aggregation was not sufficient to account for that aggregation. Furthermore, the time-course of collagen-induced release in human PRP was the same as that in sheep PRP where ADP does not cause release. These findings are not consistent with claims that ADP alone perpetuates a collagen-initiated release-aggregation-release sequence. The effects of high doses of collagen, which released 4-5 μM ADP, were not inhibited by 500 pM adenosine, a concentration that greatly reduced the effect of 300 μM ADP. Collagen caused aggregation in ADP-refractory PRP and in platelet suspensions unresponsive to 1 mM ADP. Thus human platelets can aggregate in response to collagen under circumstances in which they cannot respond to ADP. Apyrase inhibited aggregation and ATP release in platelet suspensions but not in human PRP. Evidence is presented that the means currently used to examine the role of ADP in aggregation require investigation.

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