Search alternatives:
we decrease » _ decrease (Expand Search), teer decrease (Expand Search), use decreased (Expand Search)
nn decrease » _ decrease (Expand Search), gy decreased (Expand Search), b1 decreased (Expand Search)
a decrease » _ decrease (Expand Search), _ decreased (Expand Search), _ decreases (Expand Search)
we decrease » _ decrease (Expand Search), teer decrease (Expand Search), use decreased (Expand Search)
nn decrease » _ decrease (Expand Search), gy decreased (Expand Search), b1 decreased (Expand Search)
a decrease » _ decrease (Expand Search), _ decreased (Expand Search), _ decreases (Expand Search)
-
18261
-
18262
-
18263
-
18264
Injury-induced cold sensitization in <i>Drosophila</i> larvae involves behavioral shifts that require the TRP channel Brv1
Published 2018“…Under baseline, non-injured conditions larvae primarily produce a CT response to an acute cold (10°C) stimulus, however, we show that cold-evoked responses shift following tissue damage: CT responses decrease, US responses increase and some larvae exhibit a lateral body roll (BR) that is typically only observed in response to high temperature and noxious mechanical stimuli. …”
-
18265
-
18266
-
18267
-
18268
-
18269
-
18270
-
18271
Immunofluorescence of the sst2A receptor in coronal sections through the rat neocortical wall between E14 and P5.
Published 2013“…CP/MZ, cortical plate/marginal zone; CP, cortical plate; MZ, marginal zone; VZ, ventricular zone; I–VI, cortical layers I to VI; WM, white matter. Scale bars: A–A″, B–B″, 50 µm; C–C″, D–D″, E–E″, 100 µm; A″′–E″′,10 µm.…”
-
18272
-
18273
-
18274
Biophysical Characterization Platform Informs Protein Scaffold Evolvability
Published 2019“…Our results support this connection between developability and evolvability by demonstrating a relationship between protein production in the soluble fraction of <i>Escherichia coli</i> and the ability to evolve binding function upon mutation. We further explain the necessity for initial developability by observing a decrease in proteolytic stability of protein mutants that possess binding functionality over nonfunctional mutants. …”
-
18275
-
18276
-
18277
-
18278
-
18279
-
18280