Search alternatives:
point decrease » point increase (Expand Search)
nm decrease » _ decrease (Expand Search), we decrease (Expand Search), gy decreased (Expand Search)
nn decrease » _ decrease (Expand Search), mean decrease (Expand Search), gy decreased (Expand Search)
a decrease » _ decrease (Expand Search), _ decreased (Expand Search), _ decreases (Expand Search)
e point » _ point (Expand Search), 5 point (Expand Search), a point (Expand Search)
point decrease » point increase (Expand Search)
nm decrease » _ decrease (Expand Search), we decrease (Expand Search), gy decreased (Expand Search)
nn decrease » _ decrease (Expand Search), mean decrease (Expand Search), gy decreased (Expand Search)
a decrease » _ decrease (Expand Search), _ decreased (Expand Search), _ decreases (Expand Search)
e point » _ point (Expand Search), 5 point (Expand Search), a point (Expand Search)
-
481
Semiquantitative immunoblotting and immunohistochemistry of the kidney from the acute kidney injury model.
Published 2016“…(b) S100A8/A9 abundance was increased in the CDDP group (220%) versus the control (100%) and VD groups (83%). …”
-
482
-
483
-
484
-
485
-
486
C.<sub>-100~-110</sub> caused a decrease in the promoter activity but the WT sequence of 11bp is neither an E-box nor a MEF2C binding site.
Published 2015“…<sub>-100~-110</sub> (<i>x</i>) demonstrated a decreased luciferase activity for about 30% as compared to each WT counterparts. …”
-
487
-
488
-
489
Analysis of the <sup>1</sup> H–<sup>15</sup>N HSQC spectrum of the RAGE V domain with unlabeled S100A1.
Published 2018“…Cross-peaks displaying significantly decreased intensity are shown in green boxes.</p> <p>(B) Bar graph analysis representing the intensity change (I/I<sub>0</sub>) of cross-peaks of <sup>15</sup>N V domain to <sup>15</sup>N V domain complex with S100A1 versus residue numbers of RAGE V domain (24–128). …”
-
490
Analysis of the <sup>1</sup>H–<sup>15</sup>N HSQC spectra of S100A1 in complex with the unlabeled RAGE V domain.
Published 2018“…</p> <p>(D) Ribbon representing the structure of homo-dimer. The monomers of S100A1 homodimer are colored in green and blue.</p> <p>(E) A monomer of S100A1 and residues that exhibit significantly decreasing cross-peak signals are mapped on the structure in magenta.…”
-
491
-
492
-
493
-
494
<i>Smed-not1(RNAi)</i> animals have increasing numbers of <i>Smed-agat-1</i> transcripts with increased frequency of long poly(A) tails but decreasing numbers of <i>Smed-agat-1</i>...
Published 2013“…<i>Smed-agat-1</i>-positive cells are shown in green, nuclei counterstaining in magenta. Scale bar: 100 µm. (D) PAT assays reflecting the distribution of mRNA poly(A) tail lengths for <i>Smed-agat-1</i> and <i>Smed-nb.21.11e</i>, the housekeeping mRNAs <i>Smed-ef-2</i> and <i>Smed-eif-3</i>, the tissue specific mRNA <i>Smed-mhc</i> and a spiked-in control mRNAs in <i>control(RNAi)</i> (c) and <i>Smed-not1(RNAi)</i> (n) animals 10 and 15 days after RNAi. …”
-
495
The point mutants E559A, E563A and K567A display altered DNA-binding kinetics.
Published 2014“…(B) The percentage of tetrameric-to-total STAT1 complexed to GAS-nonGAS was significantly elevated in the case of glutamic acid point mutants as compared to the wild-type protein. …”
-
496
-
497
-
498
-
499
-
500