scholarly journals Single Step Hybrid Coating Process to Enhance the Electrosteric Stabilization of Inorganic Particles

Langmuir ◽  
2011 ◽  
Vol 27 (11) ◽  
pp. 6622-6627 ◽  
Author(s):  
Chantal Rufier ◽  
Mathias Reufer ◽  
Hervé Dietsch ◽  
Peter Schurtenberger
RSC Advances ◽  
2020 ◽  
Vol 10 (44) ◽  
pp. 26504-26507
Author(s):  
Darius Rohleder ◽  
Philipp Vana

A green approach: in a single-step coating process a mesoporous silica shell was tailored onto palladium-nanocubes. Along with a PEG-matrix this core–shell-nanocatalyst could be recovered after C–C-coupling reactions and reused without any significant decrease in product yield.


2003 ◽  
Vol 169-170 ◽  
pp. 45-48 ◽  
Author(s):  
Takayasu Sato ◽  
Kenichi Sugai ◽  
Shizuyo Ueda ◽  
Kouji Matsunami ◽  
Manabu Yasuoka

RSC Advances ◽  
2015 ◽  
Vol 5 (127) ◽  
pp. 104792-104797
Author(s):  
Tomoyo Shimogaki ◽  
Hiroki Tokoro ◽  
Minoru Tabuchi ◽  
Naoto Inoue ◽  
Takuji Tsukamoto ◽  
...  

A surface porous nano silica layer is spontaneously formed via a single step bar-coating process for an antireflective hard resin coating.


2006 ◽  
Vol 17 (15) ◽  
pp. 3892-3896 ◽  
Author(s):  
Shinae Jun ◽  
Eunjoo Jang ◽  
Jung Eun Lim
Keyword(s):  

2005 ◽  
Vol 173 (4S) ◽  
pp. 240-240
Author(s):  
Premal J. Desai ◽  
David A. Hadley ◽  
Lincoln J. Maynes ◽  
D. Duane Baldwin

1996 ◽  
Vol 75 (03) ◽  
pp. 497-502 ◽  
Author(s):  
Hadewijch L M Pekelharing ◽  
Henne A Kleinveld ◽  
Pieter F C.C.M Duif ◽  
Bonno N Bouma ◽  
Herman J M van Rijn

SummaryLp(a) is an LDL-like lipoprotein plus an additional apolipoprotein apo(a). Based on the structural homology of apo(a) with plasminogen, it is hypothesized that Lp(a) interferes with fibrinolysis. Extracellular matrix (ECM) produced by human umbilical vein endothelial cells was used to study the effect of Lp(a) and LDL on plasminogen binding and activation. Both lipoproteins were isolated from the same plasma in a single step. Plasminogen bound to ECM via its lysine binding sites. Lp(a) as well as LDL were capable of competing with plasminogen binding. The degree of inhibition was dependent on the lipoprotein donor as well as the ECM donor. When Lp(a) and LDL obtained from one donor were compared, Lp(a) was always a much more potent competitor. The effect of both lipoproteins on plasminogen binding was reflected in their effect on plasminogen activation. It is speculated that Lp(a) interacts with ECM via its LDL-like lipoprotein moiety as well as via its apo(a) moiety.


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