MedChemExpress mapk inhibitors 175
Mapk Inhibitors 175, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/mapk inhibitors 175/product/MedChemExpress
Average 96 stars, based on 1 article reviews

mapk inhibitors 175 - by Bioz Stars, 2026-05

96/100 stars

Buy from Supplier

rabbit anti rabgef1 (Novus Biologicals)

Novus Biologicals rabbit anti rabgef1
$( A ) HeLa cells transiently expressing mChery-Parkin and GFP-mRABGEF1 were treated with DMSO or valinomycin for 3 hr followed by immunostaining. The magnified pictures were shown in the right. Bars, 10 μm. ( B ) Total cell lysates of ( A ) were analyzed by immunoblotting. Anti-GFP antibody was used for the GFP-mRABGEF1 detection. * and # denote ubiquitinated forms and truncated forms, respectively. ( C ) Quantification of <t>RABGEF1</t> recruitment to damaged mitochondria in ( A ). None, partial and complete denote that GFP-mRABGEF1 signals were overlapped with no, some of, and all mitochondria, respectively. ( D ) Recombinant ubiquitin (Ub) pre-treated with or without GST-TcPINK1 was subjected to pull-down assay with GST-mRABGEF1. W and E indicate wash and eluted fractions, respectively. 10%, 10% of input. ( E ) Percentages of the amount of ubiquitin in the eluted fraction in ( D ) were shown. The error bars represent mean ±SE from three independent experiments. ( F ) K48-linked and K63-linked Ub chains pre-treated with or without GST-TcPINK1 were subjected to pull-down assay with GST-mRABGEF1. ( G ) Interactions between GST-mRABGEF1 (WT or Y26A/A58D) and ubiquitin or phosphorylated ubiquitin were measured by ITC. N, stoichiometry of binding. 10.7554/eLife.31326.028 Figure 8—source data 1. Quantification of RABGEF1 recruitment to damaged mitochondria during mitophagy. 10.7554/eLife.31326.029 Figure 8—source data 2. Binding affinities of recombinant GST-mRABGEF1 with ubiquitin or phosphorylated ubiquitin. 10.7554/eLife.31326.030 Figure 8—source data 3. Binding affinities of recombinant GST-mRABGEF1 with ubiquitin or phosphorylated ubiquitin.$
Rabbit Anti Rabgef1, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/rabbit anti rabgef1/product/Novus Biologicals
Average 90 stars, based on 1 article reviews

rabbit anti rabgef1 - by Bioz Stars, 2026-05

90/100 stars

Buy from Supplier

c terminus eif3g (Novus Biologicals)

Novus Biologicals c terminus eif3g

(A) Experimental strategy for puromycin labeling experiment. (B) WB images of Shank2, Syngap, GluR1, CamKIIβ-1, <t>eIF3g,</t> and actin in synaptoneurosomes prepared from KIF5C OE- or eGFP-expressing primary HP neurons treated with puromycin. (C) Shank2, Syngap, GluR1, CamKIIβ-1, and eIF3g expression levels normalized to actin in synaptoneurosomes prepared from KIF5C OE or eGFP neurons treated with puromycin. (D) Experimental strategy for detecting newly synthesized proteins in KIF5C OE neurons by proximity labeling assay (PLA). (E) Confocal images showing proximity labeling respectively for eIF3G, GluR1, and CamKIIβ-1 in KIF5C OE-GFP- or eGFP-expressing primary HP neurons treated with puromycin. Newly synthesized proteins are shown in red. (F–H) Quantification of normalized positive puncta counts in labeled dendrites. (I–K) Quantification of normalized positive puncta counts in labeled soma. (L) Experimental strategy. (M) WB images of pS6K (T-389), S6K, pS6 (S235/236), S6, pCREB (S133), CREB, eIF3g, Kinesin, and actin. Primary neurons transduced with eGFP control and KIF5C OE-expressing lentiviruses. Cells lysed at DIV 16 and subjected to immunoblotting. (N) Normalized pS6K to S6K, pS6 to S6, pCREB to CREB, eIF3g to actin, and KIF5C to actin in total lysate of KIF5C OE- or eGFP-expressing neurons. (O) Experimental plan for EIF3G KD and KIF5C OE in same neuron for confocal live imaging. (P) Confocal projection images showing changes in spine, digitally enlarged image in inset. (Q and R) Quantitative analyses of image data shown in (P) completed by selecting dendrites with length of 100 μm. Bar graphs show change in spine density or morphology. Changes compared between neurons in control and KIF5C OE groups. Unpaired, two-tailed Student’s t test or one-way ANOVA followed by Tukey’s or Dunnett’s post hoc test. Error bars represent SEM. *p < 0.05, *p < 0.005, and ***p < 0.0005. Scale bar: 1, 2, or 20 μm.

C Terminus Eif3g, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/c terminus eif3g/product/Novus Biologicals
Average 91 stars, based on 1 article reviews

c terminus eif3g - by Bioz Stars, 2026-05

91/100 stars

Buy from Supplier

Image Search Results

$( A ) HeLa cells transiently expressing mChery-Parkin and GFP-mRABGEF1 were treated with DMSO or valinomycin for 3 hr followed by immunostaining. The magnified pictures were shown in the right. Bars, 10 μm. ( B ) Total cell lysates of ( A ) were analyzed by immunoblotting. Anti-GFP antibody was used for the GFP-mRABGEF1 detection. * and # denote ubiquitinated forms and truncated forms, respectively. ( C ) Quantification of RABGEF1 recruitment to damaged mitochondria in ( A ). None, partial and complete denote that GFP-mRABGEF1 signals were overlapped with no, some of, and all mitochondria, respectively. ( D ) Recombinant ubiquitin (Ub) pre-treated with or without GST-TcPINK1 was subjected to pull-down assay with GST-mRABGEF1. W and E indicate wash and eluted fractions, respectively. 10%, 10% of input. ( E ) Percentages of the amount of ubiquitin in the eluted fraction in ( D ) were shown. The error bars represent mean ±SE from three independent experiments. ( F ) K48-linked and K63-linked Ub chains pre-treated with or without GST-TcPINK1 were subjected to pull-down assay with GST-mRABGEF1. ( G ) Interactions between GST-mRABGEF1 (WT or Y26A/A58D) and ubiquitin or phosphorylated ubiquitin were measured by ITC. N, stoichiometry of binding. 10.7554/eLife.31326.028 Figure 8—source data 1. Quantification of RABGEF1 recruitment to damaged mitochondria during mitophagy. 10.7554/eLife.31326.029 Figure 8—source data 2. Binding affinities of recombinant GST-mRABGEF1 with ubiquitin or phosphorylated ubiquitin. 10.7554/eLife.31326.030 Figure 8—source data 3. Binding affinities of recombinant GST-mRABGEF1 with ubiquitin or phosphorylated ubiquitin.$

Journal: eLife

Article Title: Endosomal Rab cycles regulate Parkin-mediated mitophagy

doi: 10.7554/eLife.31326

Figure Lengend Snippet: ( A ) HeLa cells transiently expressing mChery-Parkin and GFP-mRABGEF1 were treated with DMSO or valinomycin for 3 hr followed by immunostaining. The magnified pictures were shown in the right. Bars, 10 μm. ( B ) Total cell lysates of ( A ) were analyzed by immunoblotting. Anti-GFP antibody was used for the GFP-mRABGEF1 detection. * and # denote ubiquitinated forms and truncated forms, respectively. ( C ) Quantification of RABGEF1 recruitment to damaged mitochondria in ( A ). None, partial and complete denote that GFP-mRABGEF1 signals were overlapped with no, some of, and all mitochondria, respectively. ( D ) Recombinant ubiquitin (Ub) pre-treated with or without GST-TcPINK1 was subjected to pull-down assay with GST-mRABGEF1. W and E indicate wash and eluted fractions, respectively. 10%, 10% of input. ( E ) Percentages of the amount of ubiquitin in the eluted fraction in ( D ) were shown. The error bars represent mean ±SE from three independent experiments. ( F ) K48-linked and K63-linked Ub chains pre-treated with or without GST-TcPINK1 were subjected to pull-down assay with GST-mRABGEF1. ( G ) Interactions between GST-mRABGEF1 (WT or Y26A/A58D) and ubiquitin or phosphorylated ubiquitin were measured by ITC. N, stoichiometry of binding. 10.7554/eLife.31326.028 Figure 8—source data 1. Quantification of RABGEF1 recruitment to damaged mitochondria during mitophagy. 10.7554/eLife.31326.029 Figure 8—source data 2. Binding affinities of recombinant GST-mRABGEF1 with ubiquitin or phosphorylated ubiquitin. 10.7554/eLife.31326.030 Figure 8—source data 3. Binding affinities of recombinant GST-mRABGEF1 with ubiquitin or phosphorylated ubiquitin.

Article Snippet: The following antibodies were used for immunoblotting: rabbit anti-GFP (ab6556; Abcam, Cambridge, MA), mouse anti-MFN2 (ab56889; Abcam), rabbit anti-TOMM20 (sc-11415; Santa Cruz Biotechnology, Dallas, TX), rabbit anti-LC3B (L7543; Sigma, St. Louis, MO), mouse anti-MT-CO2 (ab110258; Abcam), mouse anti-Actin (MAB1501R; Millipore, Bedford, MA), mouse anti-RAB7 (ab50533; Abcam), rabbit anti- RABGEF1 (NBP1-49938; NOVUS BIOLOGICALS, Littleron, CO), mouse anti-CCZ1 (sc-514290; Santa Cruz Biotechnology), mouse anti-ubiquitin (sc-8017; Santa Cruz Biotechnology), and rabbit anti-S65 phosphorylated ubiquitin (described previously [ ]).

Techniques: Expressing, Immunostaining, Western Blot, Recombinant, Ubiquitin Proteomics, Pull Down Assay, Binding Assay

( A ) The indicated cells were treated with DMSO or valinomycin for 3 hr followed by immunostaining. Bars, 10 μm. Graphs for quantification of RABGEF1 recruitment to mitochondria were shown below the images. None, partial and complete denote that GFP-mRABGEF1 signals were overlapped with no, some of, and all mitochondria, respectively. The error bars represent mean ±SE and over 100 cells were counted in each of three separate wells. ( B ) WT and TBC1D15/17 DKO HCT116 cells stably expressing mCherry-Parkin and GFP-mRABGEF1 were treated with DMSO or valinomycin for 3 hr. GFP-mRABGEF1 signals were enhanced by immunostaining with anti-GFP antibody. Bars, 10 μm. ( C ) Total cell lysates in ( B ) were analyzed by immunoblotting. * and # denote ubiquitinated forms and truncated forms, respectively. 10.7554/eLife.31326.031 Figure 8—figure supplement 1—source data 1. This excel file contains quantification of RABGEF1 (WT and Y26A/A58D mutant) recruitment to mitochondria in HCT116 (WT and TBC1D15/17 DKO) cells.

Journal: eLife

Article Title: Endosomal Rab cycles regulate Parkin-mediated mitophagy

doi: 10.7554/eLife.31326

Figure Lengend Snippet: ( A ) The indicated cells were treated with DMSO or valinomycin for 3 hr followed by immunostaining. Bars, 10 μm. Graphs for quantification of RABGEF1 recruitment to mitochondria were shown below the images. None, partial and complete denote that GFP-mRABGEF1 signals were overlapped with no, some of, and all mitochondria, respectively. The error bars represent mean ±SE and over 100 cells were counted in each of three separate wells. ( B ) WT and TBC1D15/17 DKO HCT116 cells stably expressing mCherry-Parkin and GFP-mRABGEF1 were treated with DMSO or valinomycin for 3 hr. GFP-mRABGEF1 signals were enhanced by immunostaining with anti-GFP antibody. Bars, 10 μm. ( C ) Total cell lysates in ( B ) were analyzed by immunoblotting. * and # denote ubiquitinated forms and truncated forms, respectively. 10.7554/eLife.31326.031 Figure 8—figure supplement 1—source data 1. This excel file contains quantification of RABGEF1 (WT and Y26A/A58D mutant) recruitment to mitochondria in HCT116 (WT and TBC1D15/17 DKO) cells.

Techniques: Immunostaining, Stable Transfection, Expressing, Western Blot, Mutagenesis

( A ) GFP-mRABGEF1 was transiently expressed in siRNA-treated HeLa cells. The cells were then treated with valinomycin for 3 hr followed by immunostaining. Bars, 20 μm. ( B ) Quantification of mitochondrial recruitment of GFP-mRABGEF1 in HeLa cells. ( C ) Quantification of mitochondrial recruitment of GFP-mRABGEF1 in HCT116 cells. None, partial and complete denote that GFP-mRABGEF1 signals were overlapped with no, some of, and all mitochondria, respectively. The error bars represent mean ± SE and over 100 cells were counted in each of three separate wells. 10.7554/eLife.31326.032 Figure 8—figure supplement 2—source data 2. Quantification of RABGEF1 recruitment to mitochondria in HeLa cells treated with the indicated siRNA during mitophagy. 10.7554/eLife.31326.033 Figure 8—figure supplement 2—source data 3. Quantification of RABGEF1 recruitment to mitochondria in HCT116 cells treated with the indicated siRNA during mitophagy.

Journal: eLife

Article Title: Endosomal Rab cycles regulate Parkin-mediated mitophagy

doi: 10.7554/eLife.31326

Figure Lengend Snippet: ( A ) GFP-mRABGEF1 was transiently expressed in siRNA-treated HeLa cells. The cells were then treated with valinomycin for 3 hr followed by immunostaining. Bars, 20 μm. ( B ) Quantification of mitochondrial recruitment of GFP-mRABGEF1 in HeLa cells. ( C ) Quantification of mitochondrial recruitment of GFP-mRABGEF1 in HCT116 cells. None, partial and complete denote that GFP-mRABGEF1 signals were overlapped with no, some of, and all mitochondria, respectively. The error bars represent mean ± SE and over 100 cells were counted in each of three separate wells. 10.7554/eLife.31326.032 Figure 8—figure supplement 2—source data 2. Quantification of RABGEF1 recruitment to mitochondria in HeLa cells treated with the indicated siRNA during mitophagy. 10.7554/eLife.31326.033 Figure 8—figure supplement 2—source data 3. Quantification of RABGEF1 recruitment to mitochondria in HCT116 cells treated with the indicated siRNA during mitophagy.

Techniques: Immunostaining

( A ) WT and RABGEF1-mAID HCT116 cells were treated with or without IAA for 16 hr. Total cell lysates were analyzed by immunoblotting. ( B ) Quantification of Parkin recruitment to mitochondria in WT and RABGEF1-mAID HCT116 cells after 3 hr of valinomycin treatment. Partial and complete denote that YFP-Parkin signals were overlapped with some of and all mitochondria, respectively. ( C ) YFP-Parkin stably expressing WT and RABGEF1-mAID HCT116 cells pre-treated with IAA were treated with valinomycin for the indicated times. Total cell lysates were analyzed by immunoblotting. ( D ) WT and RABGEF1-mAID HCT116 cells stably expressing YFP-Parkin and mt-mKeima were treated with IAA for 16 hr followed by DMSO or OAQ for 6 hr and subjected to FACS analysis. Plots are representative of n = 3 experiments. ( E ) Quantification of mitophagy in ( D ). Error bars represent mean ±SE of three independent experiments. Statistical differences were determined by student’s t-test. *p<0.05. 10.7554/eLife.31326.035 Figure 9—source data 1. Quantification of YFP-Parkin recruitment to mitochondria in RABGEF1-mAID HCT116 and the corresponding WT cells during mitophagy. 10.7554/eLife.31326.036 Figure 9—source data 2. Quantification of mitophagy using mt-mKeima and FACS analysis.

Journal: eLife

Article Title: Endosomal Rab cycles regulate Parkin-mediated mitophagy

doi: 10.7554/eLife.31326

Figure Lengend Snippet: ( A ) WT and RABGEF1-mAID HCT116 cells were treated with or without IAA for 16 hr. Total cell lysates were analyzed by immunoblotting. ( B ) Quantification of Parkin recruitment to mitochondria in WT and RABGEF1-mAID HCT116 cells after 3 hr of valinomycin treatment. Partial and complete denote that YFP-Parkin signals were overlapped with some of and all mitochondria, respectively. ( C ) YFP-Parkin stably expressing WT and RABGEF1-mAID HCT116 cells pre-treated with IAA were treated with valinomycin for the indicated times. Total cell lysates were analyzed by immunoblotting. ( D ) WT and RABGEF1-mAID HCT116 cells stably expressing YFP-Parkin and mt-mKeima were treated with IAA for 16 hr followed by DMSO or OAQ for 6 hr and subjected to FACS analysis. Plots are representative of n = 3 experiments. ( E ) Quantification of mitophagy in ( D ). Error bars represent mean ±SE of three independent experiments. Statistical differences were determined by student’s t-test. *p<0.05. 10.7554/eLife.31326.035 Figure 9—source data 1. Quantification of YFP-Parkin recruitment to mitochondria in RABGEF1-mAID HCT116 and the corresponding WT cells during mitophagy. 10.7554/eLife.31326.036 Figure 9—source data 2. Quantification of mitophagy using mt-mKeima and FACS analysis.

Techniques: Western Blot, Stable Transfection, Expressing

Journal: eLife

Article Title: Endosomal Rab cycles regulate Parkin-mediated mitophagy

doi: 10.7554/eLife.31326

Figure Lengend Snippet:

Techniques: Sequencing, Ubiquitin Proteomics, Protease Inhibitor, Western Blot, Recombinant, Software, Microscopy

(A) Experimental strategy for puromycin labeling experiment. (B) WB images of Shank2, Syngap, GluR1, CamKIIβ-1, eIF3g, and actin in synaptoneurosomes prepared from KIF5C OE- or eGFP-expressing primary HP neurons treated with puromycin. (C) Shank2, Syngap, GluR1, CamKIIβ-1, and eIF3g expression levels normalized to actin in synaptoneurosomes prepared from KIF5C OE or eGFP neurons treated with puromycin. (D) Experimental strategy for detecting newly synthesized proteins in KIF5C OE neurons by proximity labeling assay (PLA). (E) Confocal images showing proximity labeling respectively for eIF3G, GluR1, and CamKIIβ-1 in KIF5C OE-GFP- or eGFP-expressing primary HP neurons treated with puromycin. Newly synthesized proteins are shown in red. (F–H) Quantification of normalized positive puncta counts in labeled dendrites. (I–K) Quantification of normalized positive puncta counts in labeled soma. (L) Experimental strategy. (M) WB images of pS6K (T-389), S6K, pS6 (S235/236), S6, pCREB (S133), CREB, eIF3g, Kinesin, and actin. Primary neurons transduced with eGFP control and KIF5C OE-expressing lentiviruses. Cells lysed at DIV 16 and subjected to immunoblotting. (N) Normalized pS6K to S6K, pS6 to S6, pCREB to CREB, eIF3g to actin, and KIF5C to actin in total lysate of KIF5C OE- or eGFP-expressing neurons. (O) Experimental plan for EIF3G KD and KIF5C OE in same neuron for confocal live imaging. (P) Confocal projection images showing changes in spine, digitally enlarged image in inset. (Q and R) Quantitative analyses of image data shown in (P) completed by selecting dendrites with length of 100 μm. Bar graphs show change in spine density or morphology. Changes compared between neurons in control and KIF5C OE groups. Unpaired, two-tailed Student’s t test or one-way ANOVA followed by Tukey’s or Dunnett’s post hoc test. Error bars represent SEM. *p < 0.05, *p < 0.005, and ***p < 0.0005. Scale bar: 1, 2, or 20 μm.

Journal: Cell reports

Article Title: Molecular motor protein KIF5C mediates structural plasticity and long-term memory by constraining local translation

doi: 10.1016/j.celrep.2021.109369

Figure Lengend Snippet: (A) Experimental strategy for puromycin labeling experiment. (B) WB images of Shank2, Syngap, GluR1, CamKIIβ-1, eIF3g, and actin in synaptoneurosomes prepared from KIF5C OE- or eGFP-expressing primary HP neurons treated with puromycin. (C) Shank2, Syngap, GluR1, CamKIIβ-1, and eIF3g expression levels normalized to actin in synaptoneurosomes prepared from KIF5C OE or eGFP neurons treated with puromycin. (D) Experimental strategy for detecting newly synthesized proteins in KIF5C OE neurons by proximity labeling assay (PLA). (E) Confocal images showing proximity labeling respectively for eIF3G, GluR1, and CamKIIβ-1 in KIF5C OE-GFP- or eGFP-expressing primary HP neurons treated with puromycin. Newly synthesized proteins are shown in red. (F–H) Quantification of normalized positive puncta counts in labeled dendrites. (I–K) Quantification of normalized positive puncta counts in labeled soma. (L) Experimental strategy. (M) WB images of pS6K (T-389), S6K, pS6 (S235/236), S6, pCREB (S133), CREB, eIF3g, Kinesin, and actin. Primary neurons transduced with eGFP control and KIF5C OE-expressing lentiviruses. Cells lysed at DIV 16 and subjected to immunoblotting. (N) Normalized pS6K to S6K, pS6 to S6, pCREB to CREB, eIF3g to actin, and KIF5C to actin in total lysate of KIF5C OE- or eGFP-expressing neurons. (O) Experimental plan for EIF3G KD and KIF5C OE in same neuron for confocal live imaging. (P) Confocal projection images showing changes in spine, digitally enlarged image in inset. (Q and R) Quantitative analyses of image data shown in (P) completed by selecting dendrites with length of 100 μm. Bar graphs show change in spine density or morphology. Changes compared between neurons in control and KIF5C OE groups. Unpaired, two-tailed Student’s t test or one-way ANOVA followed by Tukey’s or Dunnett’s post hoc test. Error bars represent SEM. *p < 0.05, *p < 0.005, and ***p < 0.0005. Scale bar: 1, 2, or 20 μm.

Article Snippet: After 2 more rounds of PBS washing, and blocking in 5% horse serum in 0.1% Triton X-100 PBS, neurons were then incubated with mouse anti-puromyin antibody (1:2000, Sigma, MABE342) and one of rabbit antibody for C terminus eIF3g (1:1000, Novus Biologicals, NB100–93298), GluR1 (1:1000, CST, 13185), or CamKIIβ-1 (1:1000, Sigma, 13–9800) overnight.

Techniques: Labeling, Expressing, Synthesized, Transduction, Control, Western Blot, Imaging, Two Tailed Test

(A) Experimental strategy for in vivo manipulation and mouse behavior using lentivirus to overexpress KIF5C . (B) MWM test strategy. (C) Heatmap showing mouse tracking during MWM. (D–I) MWM performance. (D) Time spent in Q1 during probe test. (E) Total visits to Q1 during probe test. (F) Time spent every 30 s in Q1 during probe test. (G) Time spent in Q4 during probe test. (H) Total distance traveled during probe test. (I) Swimming velocity during test. (J) Contextual fear memory test strategy. (K) Contextual freezing responses during test at 24 h after conditioning. (L) Total distance traveled during test at 24 h after conditioning. (M) Mean percentage freezing time-averaged every minute during 5 min test at 24 h after conditioning. (N) Experimental strategy for assessing consolidation, extinction, and recall of contextual fear in CA1 KIF5C OE mice using reduced-intensity foot shocks during training. (O) Extinction training shows significant reduction in percent freezing at 30 min. Control, n = 11; KIF5C -O/E, n = 9. For all statistical analyses, data expressed as means ± SEM (*p < 0.05, **p < 0.05; unpaired, two-tailed Student’s t test). (P) KIF5C functions as critical regulator of structural plasticity associated with LTM, linking transcription, transport, and local translation. KIF5C mediates long-distance transport of RNA substrates for local translation for learning-related synaptic remodeling. EIF3G , regulator of eukaryotic translational initiation, and several key components determining plasticity and function of excitatory synapses such as GLUR1 , SYNGAP , SHANK2 , and CaMKII-β , are transported as RNA cargo of KIF5C .

Journal: Cell reports

Article Title: Molecular motor protein KIF5C mediates structural plasticity and long-term memory by constraining local translation

doi: 10.1016/j.celrep.2021.109369

Figure Lengend Snippet: (A) Experimental strategy for in vivo manipulation and mouse behavior using lentivirus to overexpress KIF5C . (B) MWM test strategy. (C) Heatmap showing mouse tracking during MWM. (D–I) MWM performance. (D) Time spent in Q1 during probe test. (E) Total visits to Q1 during probe test. (F) Time spent every 30 s in Q1 during probe test. (G) Time spent in Q4 during probe test. (H) Total distance traveled during probe test. (I) Swimming velocity during test. (J) Contextual fear memory test strategy. (K) Contextual freezing responses during test at 24 h after conditioning. (L) Total distance traveled during test at 24 h after conditioning. (M) Mean percentage freezing time-averaged every minute during 5 min test at 24 h after conditioning. (N) Experimental strategy for assessing consolidation, extinction, and recall of contextual fear in CA1 KIF5C OE mice using reduced-intensity foot shocks during training. (O) Extinction training shows significant reduction in percent freezing at 30 min. Control, n = 11; KIF5C -O/E, n = 9. For all statistical analyses, data expressed as means ± SEM (*p < 0.05, **p < 0.05; unpaired, two-tailed Student’s t test). (P) KIF5C functions as critical regulator of structural plasticity associated with LTM, linking transcription, transport, and local translation. KIF5C mediates long-distance transport of RNA substrates for local translation for learning-related synaptic remodeling. EIF3G , regulator of eukaryotic translational initiation, and several key components determining plasticity and function of excitatory synapses such as GLUR1 , SYNGAP , SHANK2 , and CaMKII-β , are transported as RNA cargo of KIF5C .

Techniques: In Vivo, Control, Two Tailed Test

Journal: Cell reports

Article Title: Molecular motor protein KIF5C mediates structural plasticity and long-term memory by constraining local translation

doi: 10.1016/j.celrep.2021.109369

Figure Lengend Snippet: KEY RESOURCES TABLE

Techniques: Virus, Recombinant, Cell Culture, Saline, Sterility, Live Cell Imaging, Transfection, Protein Extraction, Protease Inhibitor, Labeling, SYBR Green Assay, Ointment, Adhesive, Gel Extraction, Isolation, TA Cloning, Sequencing, Plasmid Preparation, shRNA, Software, Control

mapk inhibitors 175 Search Results

Image Search Results