Dominant negative Hif-2α decreases bacterial burden via an iNOS dependent mechanism. by Philip M. Elks (324793)

PRRSV enters MARC-145 cells via macropinocytosis and rottlerin blocks the macropinocytosis by decreasing actin polymerization. by Yeonglim Kang (21395261)

Protein degradation via the ubiquitin proteasome activity decreases with age and castration tends to increase the activity of this system. by Arik Davidyan (10450896)

Everolimus decreased EC inflammation via lowered IL-1β and IL-6 expression in ECs. by Zsolt Fejes (844136)

Gender category beliefs (GCB) as a function of participant sex and other demographic variables. by Mostafa Salari Rad (8201484)

Error amplification led to modest increases in participants’ error correction gain <i>B</i>, but larger decreases in execution and planning noise variance, <i>σ</i>_<i>EX</i>² and <i>σ</i>_<i>PL</i>², respectively. by Christopher J. Hasson (357863)

Multi-Cilia Cell Hyperplasia Is Due to Mib-Mediated Jagged2a Signaling Pathway via Notch1a and Notch3 Receptors by Ming Ma (43147)

“…<i>jagged2a</i>-<i>sp</i> MO-injected embryos analyzed with the same primers at the same timepoints (lanes 3 and 7) show a larger amplicon of 708 bp caused by a nonsplicing intron 1, which encodes a premature stop codon. …”

Extraction efficiency of a larger volume of specimen, 400 μl specimen input Cp and 200 μl specimen input Cp. by Ana Cabrera (266933)

Points represent regions where the cluster coefficient was significantly larger in HC compared to MCI, at sparsity level of 0.15. by Therese M. Gilligan (7460906)

A Model for MST1-mediated protection in liver fibrosis caused by <i>Schistosoma japonicum</i> infection. by Jianyang Li (461703)

Subjects:

Comparison of the decrease of CFU in CSF and blood between treatment groups within the first 6 h after treatment. by Luca G. Valente (12463057)

The MHC-I decrease mediated by <i>Ba</i> RNA is not due to a loss of cell viability. by Agustina Serafino (7379969)

Image_5_TRAPS mutations in Tnfrsf1a decrease the responsiveness to TNFα via reduced cell surface expression of TNFR1.tif by Takahiko Akagi (13138338)

“…The TNFR1 levels were increased in whole-cell lysates of TRAPS mutant macrophages, whereas the cell surface expression of TNFR1 was significantly decreased in TRAPS mutant macrophages. Taken together, TRAPS mutations did not augment the inflammatory responses to TNFα and LPS; instead, they suppressed the response to TNFα via decreased cell surface expression of TNFR1. …”

Image_1_TRAPS mutations in Tnfrsf1a decrease the responsiveness to TNFα via reduced cell surface expression of TNFR1.tif by Takahiko Akagi (13138338)

“…The TNFR1 levels were increased in whole-cell lysates of TRAPS mutant macrophages, whereas the cell surface expression of TNFR1 was significantly decreased in TRAPS mutant macrophages. Taken together, TRAPS mutations did not augment the inflammatory responses to TNFα and LPS; instead, they suppressed the response to TNFα via decreased cell surface expression of TNFR1. …”

Image_4_TRAPS mutations in Tnfrsf1a decrease the responsiveness to TNFα via reduced cell surface expression of TNFR1.tif by Takahiko Akagi (13138338)

“…The TNFR1 levels were increased in whole-cell lysates of TRAPS mutant macrophages, whereas the cell surface expression of TNFR1 was significantly decreased in TRAPS mutant macrophages. Taken together, TRAPS mutations did not augment the inflammatory responses to TNFα and LPS; instead, they suppressed the response to TNFα via decreased cell surface expression of TNFR1. …”

Image_7_TRAPS mutations in Tnfrsf1a decrease the responsiveness to TNFα via reduced cell surface expression of TNFR1.tif by Takahiko Akagi (13138338)

“…The TNFR1 levels were increased in whole-cell lysates of TRAPS mutant macrophages, whereas the cell surface expression of TNFR1 was significantly decreased in TRAPS mutant macrophages. Taken together, TRAPS mutations did not augment the inflammatory responses to TNFα and LPS; instead, they suppressed the response to TNFα via decreased cell surface expression of TNFR1. …”

Image_3_TRAPS mutations in Tnfrsf1a decrease the responsiveness to TNFα via reduced cell surface expression of TNFR1.tif by Takahiko Akagi (13138338)

“…The TNFR1 levels were increased in whole-cell lysates of TRAPS mutant macrophages, whereas the cell surface expression of TNFR1 was significantly decreased in TRAPS mutant macrophages. Taken together, TRAPS mutations did not augment the inflammatory responses to TNFα and LPS; instead, they suppressed the response to TNFα via decreased cell surface expression of TNFR1. …”

Image_6_TRAPS mutations in Tnfrsf1a decrease the responsiveness to TNFα via reduced cell surface expression of TNFR1.tif by Takahiko Akagi (13138338)

“…The TNFR1 levels were increased in whole-cell lysates of TRAPS mutant macrophages, whereas the cell surface expression of TNFR1 was significantly decreased in TRAPS mutant macrophages. Taken together, TRAPS mutations did not augment the inflammatory responses to TNFα and LPS; instead, they suppressed the response to TNFα via decreased cell surface expression of TNFR1. …”

Image_2_TRAPS mutations in Tnfrsf1a decrease the responsiveness to TNFα via reduced cell surface expression of TNFR1.tif by Takahiko Akagi (13138338)

“…The TNFR1 levels were increased in whole-cell lysates of TRAPS mutant macrophages, whereas the cell surface expression of TNFR1 was significantly decreased in TRAPS mutant macrophages. Taken together, TRAPS mutations did not augment the inflammatory responses to TNFα and LPS; instead, they suppressed the response to TNFα via decreased cell surface expression of TNFR1. …”

Image_1_Phosphodiesterase PDE4D Is Decreased in Frontal Cortex of Aged Rats and Positively Correlated With Working Memory Performance and Inversely Correlated With PKA Phosphorylat... by Shannon N. Leslie (9571943)

“…Therefore, it is important to understand the role of PDE4D in brain regions particularly vulnerable to disease such as the frontal association cortex (FC), where cAMP signaling can impair working memory via opening of potassium channels. We found that PDE4D protein level was decreased in the FC of both moderately and extremely aged rats, and that PDE4D level was correlated with performance on a FC-dependent working memory task. …”