Loss of ECRG4 expression decreases neutrophil mobilization from bone marrow reserves. by Katie D. Pool (20141584)

Subjects:

Biases in larger populations. by Sander W. Keemink (21253563)

“…<p>(<b>A</b>) Maximum absolute bias vs the number of neurons in the population for the Bayesian decoder. …”

The distribution of <i>Giardia duodenalis</i> assemblages in domestic and wild populations of nonhuman mammalian species with a larger number of isolates. by Kareem Hatam-Nahavandi (7384790)

<b>Supporting data for manuscript</b> "<b>Voluntary locomotion induces an early and remote hemodynamic decrease in the large cerebral veins</b>" by Kira Shaw (18796168)

The introduction of mutualisms into assembled communities increases their connectance and complexity while decreasing their richness. by Gui Araujo (22170819)

“…When they stop being introduced in further assembly events (i.e. introduced species do not carry any mutualistic interactions), their proportion slowly decreases with successive invasions. (B) Even though higher proportions of mutualism promote higher richness, introducing this type of interaction into already assembled large communities promotes a sudden drop in richness, while stopping mutualism promotes a slight boost in richness increase. …”

<b>Nest mass in forest tits </b><b><i>Paridae</i></b><b> </b><b>increases with elevation and decreasing body mass, promoting reproductive success</b> by Clara Wild (19246606)

Domain organization of human αB-crystallin protein. by Aref Baharvand (21713886)

Chaperone activity and cytoprotective effects of the αB-crystallin proteins. by Aref Baharvand (21713886)

Chemical, thermal, and proteolytic stability of αB-crystallin proteins. by Aref Baharvand (21713886)

Thermodynamic parameters of αB-crystallin protein samples determined through DSC analysis. by Aref Baharvand (21713886)

Supporting data for the paper "<b>The physiological cost of being hot: high thermal stress and disturbance decrease energy reserves in dragonflies in the wild</b>" by Alex Córdoba-Aguilar (10011050)

Temperature-dependent hydrophobic surface exposure of the αB-crystallin proteins assessed by ANS fluorescence. by Aref Baharvand (21713886)

Fluorescence analysis of wild-type and p.R163C αB-crystallin proteins. by Aref Baharvand (21713886)

Altered structure and function of human αB-crystallin due to the p.R163C mutation. by Aref Baharvand (21713886)

“…This mutant protein tends to form larger oligomers than its wild-type counterpart. Although it exhibits decreased chemical and thermal stability, it demonstrates greater proteolytic stability and shows an increased tendency for fibrillation under thermochemical stress conditions. …”

Spectroscopic characterization of wild-type and p.R163C αB-crystallin: CD, FTIR and Raman analysis. by Aref Baharvand (21713886)

Average contact force and percentage of strong contact force under different conditions: (a) different particle shapes, (b) different particle sizes. by Yongfeng Zhu (7361045)

Gene mapping, mass spectrometry, and purification of the wild-type and p.R163C mutant of human αB-crystallin. by Aref Baharvand (21713886)

The percentage composition of secondary structure elements in wild-type and mutant αB-crystallin, as determined by CD, FTIR, and Raman spectroscopy. by Aref Baharvand (21713886)

The normal force between two particles with different equivalent diameters for P3: (a) hertznormal contact force; (b) normal viscous contact force. by Yongfeng Zhu (7361045)

Structural dynamics of wild-type and p.R163C mutant αB-crystallin dimers: insights from molecular simulations. by Aref Baharvand (21713886)