<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Menon, Sneha</style></author><author><style face="normal" font="default" size="100%">Sengupta, Neelanjana</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%"> Influence of crowding and surfaces on protein amyloidogenesis: A thermo-kinetic perspective </style></title><secondary-title><style face="normal" font="default" size="100%">Biochimica ET Biophysica Acta-Proteins and Proteomics</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2019</style></year><pub-dates><date><style  face="normal" font="default" size="100%">OCT</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">1867</style></volume><pages><style face="normal" font="default" size="100%">941-953</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;&lt;span class=&quot;hitHilite&quot;&gt;The&lt;/span&gt; last few decades have irreversibly implicated protein self-assembly and aggregation leading to amyloid fibril formation &lt;span class=&quot;hitHilite&quot;&gt;in&lt;/span&gt; proteopathies that include several neurodegenerative diseases. Emerging studies recognize &lt;span class=&quot;hitHilite&quot;&gt;the&lt;/span&gt; importance &lt;span class=&quot;hitHilite&quot;&gt;of&lt;/span&gt; eliciting &lt;span class=&quot;hitHilite&quot;&gt;the&lt;/span&gt; pathways leading to protein aggregation &lt;span class=&quot;hitHilite&quot;&gt;in&lt;/span&gt; &lt;span class=&quot;hitHilite&quot;&gt;the&lt;/span&gt; context &lt;span class=&quot;hitHilite&quot;&gt;of&lt;/span&gt; &lt;span class=&quot;hitHilite&quot;&gt;the&lt;/span&gt; crowded intracellular environment rather than &lt;span class=&quot;hitHilite&quot;&gt;in&lt;/span&gt; conventional &lt;span class=&quot;hitHilite&quot;&gt;in&lt;/span&gt; vitro conditions. It is found that crowded environments &lt;span class=&quot;hitHilite&quot;&gt;can&lt;/span&gt; have acceleratory as well as inhibitory effects on protein aggregation, depending on &lt;span class=&quot;hitHilite&quot;&gt;the&lt;/span&gt; interplay &lt;span class=&quot;hitHilite&quot;&gt;of&lt;/span&gt; underlying factors on &lt;span class=&quot;hitHilite&quot;&gt;the&lt;/span&gt; crucial &lt;span class=&quot;hitHilite&quot;&gt;rate&lt;/span&gt; limiting steps. &lt;span class=&quot;hitHilite&quot;&gt;The&lt;/span&gt; aggregation mechanism and transient species formed along &lt;span class=&quot;hitHilite&quot;&gt;the&lt;/span&gt; pathway are further altered when they interface with natural and artificial surfaces &lt;span class=&quot;hitHilite&quot;&gt;in&lt;/span&gt; &lt;span class=&quot;hitHilite&quot;&gt;the&lt;/span&gt; cellular milieu. An increasing number &lt;span class=&quot;hitHilite&quot;&gt;of&lt;/span&gt; studies probe &lt;span class=&quot;hitHilite&quot;&gt;the&lt;/span&gt; autocatalytic nature &lt;span class=&quot;hitHilite&quot;&gt;of&lt;/span&gt; amyloid surfaces as well as membrane bilayer effects on amyloidogenesis. Moreover, exposure to modern nanosurfaces via nanomedicines and other sources potentially invokes beneficial or deleterious biological response that needs rigorous investigation. Mounting evidences indicate that nanoparticles &lt;span class=&quot;hitHilite&quot;&gt;can&lt;/span&gt; either promote or impede amyloid aggregation, spurring efforts to tune their interactions for developing effective anti-amyloid strategies. Mechanistic &lt;span class=&quot;hitHilite&quot;&gt;insights&lt;/span&gt; into nanoparticle mediated aggregation pathways are therefore crucial for engineering anti-amyloid nanoparticle strategies that are biocompatible and sustainable. This review is a compilation &lt;span class=&quot;hitHilite&quot;&gt;of&lt;/span&gt; studies that contribute to &lt;span class=&quot;hitHilite&quot;&gt;the&lt;/span&gt; current understanding &lt;span class=&quot;hitHilite&quot;&gt;of&lt;/span&gt; &lt;span class=&quot;hitHilite&quot;&gt;the&lt;/span&gt; altering effects &lt;span class=&quot;hitHilite&quot;&gt;of&lt;/span&gt; molecular crowding as well as natural and artificial surfaces on protein amyloidogenesis.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">10</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;Foreign&lt;/p&gt;
</style></custom3><custom4><style face="normal" font="default" size="100%">&lt;p&gt;&lt;span class=&quot;tooltip&quot;&gt;2.540&lt;/span&gt;&lt;br /&gt;
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