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Production of OVA.TBhsp70 fusion proteins using TBhsp70 segments. (A) Functional and structural domains of TBhsp70 based on crystal structures of the ATPase domain of bovine hsp70 (reference 38) and the peptide-binding domain of E. coli DnaK (reference 39). The full-length TBhsp70 was separated into four segments, I, II, III, and IV. The full-length TBhsp70 and each segment were fused to the COOH terminus of OVA to make OVA.TBhsp70 fusion proteins. The numbers beneath each segment refer to the aa positions in TBhsp70. (B) Purification of OVA.TBhsp70 fusion proteins. Purity was assessed using SDS-PAGE and visualized with Coomassie blue. Each lane was loaded with â¼4 μg of protein. The numbers at left represent molecular weight markers (in kD). Correlation between volume of resection calculated with ImageJ and actual measured weights of the resection specimens (n = 15, Pearsonâs test) Relationship between baseline muscle oxygen consumption and change in muscle oxygen consumption. x axis: baseline muscle oxygen consumption (NIR VO2; arbitrary units); y axis: difference in NIR VO2 after and before transfusion (ÎNIR VO2; arbitrary units). NIR VO2 was calculated as the product of the inverse value of the thenar tissue oxygen saturation (StO2) desaturation slope and the mean tissue hemoglobin index over the first minute of arterial occlusion. r2 = 0.48; P = 0.0015. ILK phosphorylates affixin in vitro. (A) Kinase activity of wild-type ILK and its point mutants overexpressed in COS-7 cells. Flag-tagged ILK or its mutants were overexpressed and immunoprecipitated from COS-7 cell lysates with monoclonal anti-Flag antibody. Kinase activities of the resultant immunocomplexes were examined using MBP as a substrate. Top, autoradiography showing 32P incorporation into MBP; bottom, Western blot analysis of the precipitated Flag-tagged ILK or its mutants using polyclonal anti-Flag antibody. (B) Full-length and COOH-terminal half of ss-affixin are phosphorylated by ILK in vitro. Recombinant full-length and COOH-terminal half of ss-affixin (RP2) were used as substrates to estimate the kinase activity of the ILK immunocomplexes prepared as described in A.
Principle of the assay. In the presence of a bona fide quadruplex ligand, duplex formation is inhibited in the F22â+â37Q system (quadruplex prone, A) and thus fluorescence of the F22 is high (not quenched) whereas duplex formation is unperturbed on the mutated system (F22mâ+â37Qm32, non-quadruplex prone, B) and thus F22m fluorescence is low (quenched). Schematic diagram showing the effect of coengagement of FcεRI with FcγRIIB. Coaggregation of FcεRI with FcγRIIB inhibits degranulation but not the induction of Bim and A1. Proposed mechanism by which PRL may affect CPT1 enzyme activity in breast cancer cells. PRL signaling may alter CPT1 enzyme activity in two distinct manners, with potential cross-talk. In 1), PRL mediates its effect through LKB1, resulting in activation of the AMPK pathway via phosphorylation of AMPKα at Thr172 (pAMPKα) and inactivation of ACC (pACC), culminating in increased CPT1 enzyme activity. In 2), PRL either directly, or indirectly through the activation of AMPK, induces PPARα to increase CPT1A expression, resulting in changes at both the mRNA and protein levels, thereby increasing CPT1 enzyme activity. Dashed arrows and ?s indicate components of the pathway(s) that remain to be conclusively established. Concentration-response relationship of the effect of SNP on endothelium-denuded carotid arteries that were freshly isolated (â), cultured for 3 days (â) and 7 days (â²). Sodium nitroprusside (SNP) was cumulatively added after PE-induced contraction had reached a steady state. The difference between steady state precontraction and basal tension was considered one hundred percent. Results are expressed as mean ± S.E. (n = 15). Growth dependence of Fas2 KO strain on different exogenous fatty acids in YPD.Different amounts of myristic (14â¶0), palmitic (16â¶0), stearic (18â¶0), oleic (18â¶1) acids, and T80 (Tween 80) were added to YPD broth. Yeast growth was determined by cell density after 48 hours at 30°C. The results were the mean of two independent experiments.
The molecular structure of the title molecule, with the atom-numbering scheme. Displacement ellipsoids are drawn at the 30% probability level. The molecular structure of (I), showing 50% probability displacement ellipsoids and the atom numbering scheme. Dual pathways for disulfide bond reduction in the cytoplasm of E. coli. Dual pathways for disulfide bond reduction in the cytoplasm of E. coli. On the knockout of both pathways the reduction of disulfide bonds is inhibited, but there is no active system to catalyze their formation. Model of P. aeruginosa activation of insulin-like signaling.PA14 infection causes an insulin agonist-mediated activation of DAF-2, which likely involves expression of ins-7. Upon DAF-2 activation, several serine-threonine kinases phorphorylate DAF-16, causing the transcription factor to be retained in the cytoplasm and inhibiting its transcriptional-regulatory activity. Consequently, DAF-2âregulated gene expression is affected, causing the downregulation of immune defense genes such as lys-7 and thn-2. Germline signaling and heat shock regulate DAF-16 in parallel to the effect of PA14 and DAF-2 activity. DAF-2 and DAF-16 may function in a network with other signaling components to affect the expression of DAF-2-regulated genes including spp-1. ORTEP plot of 1 with 30% probability ellipsoid.
In vivo [32P]-GTP binding to live, intact Tetrahymena showed saturable, high-affinity binding to surface receptors in both control and deadapted cells but this binding was virtually lost in adapted cells. (A) The amount of [32P]-GTP bound to cells increased in a concentration-dependent manner in both control (open squares) and de-adapted (closed circles) cells but adapted cells (closed triangles) showed no measurable binding at any concentration tested. Each point represents the mean ± SD of three experiments. (B) Scatchard analysis showed that the apparent KD of control cells (open squares) and de-adapted cells (closed circles) were identical while the Bmax values were comparable. Adapted cells showed far less binding (closed triangles). (From Kuruvilla et al. [36].) Crossing scheme used to assess role of RMR1 in establishing Muk-based silencing of MuDR. Western analysis of m144 expression in RMA-m144 and RMA-S-m144 transfectants. (A) Parental lymphoma cell lines (lanes 1 and 2) compared with RMA-m144 and RMA-S-m144 transfectants (lanes 3 and 4) when probed with anti-m144 15C6 mAb. The m144 protein migrated broadly at â¼57â63 kD. (B) Tunicamycin treatment (1 μg/ml overnight) reduced the m144 migrating species to one band at â¼45â47 kD. Proteins were separated by SDS-PAGE and detected by Western analysis as described in Materials and Methods. The positions of the protein standards are shown in kD. These profiles were representative of at least three independent RMA-m144 and RMA-S-m144 clones. Molecular structure of (I) with the atomic numbering scheme. Displacement ellipsoids are drawn at the 50% probability level (Brandenburg, 2001).
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