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his-rhoa  (Cytoskeleton Inc)
90
Cytoskeleton Inc his-rhoa
( a ) mDia1 C-t (blue symbols) or Bni1 (FH1FH2)p (orange open diamond) converted G-actin/G-actin catch bonds (gray diamond, data presented in cited ref. ) to slip-only bonds, in the force range measured ( b ) mDia1 N-t inhibited the mDia1 C-t-induced conversion of G-actin/G-actin catch-slip bonds to slip-only bonds, restoring the catch-slip phenotype. ( c ) His <t>RhoA</t> charged <t>with</t> <t>GTPγS</t> (red square), but not GDP (red open triangles), relieved the inhibitory effect of mDia1 N-t on mDia1 C-t. ( d ) G-actin/F-actin catch-slip bonds (gray square, data presented in cited ref. ) were converted to slip-only bonds by 5 nM mDia1 C-t (blue diamond), the effect of which was exacerbated by 2 μM Tmod3 (open up triangle) but diminished by 10 nM CapZ (open down triangle). ( e ) mDia1 C-t-induced conversion from G-actin/F-actin catch-slip bonds to slip-only bonds was inhibited by simultaneous treatment with mDia1 N-t. ( f ) The inhibitory effect mDia1 N-t on mDia1 C-t was relieved by His RhoA charged with GTPγS. Each point represents the mean ± 95% confidence interval (C.I.) of >30 measurements. The confidence interval is calculated as the standard error multiplied by the t statistic from the t table, assuming a t -distribution with a degree of freedom of sample size minus 1. The semilog plots of survival frequency versus lifetime for the G-actin/G-actin interaction with 5 nM mDia1 C-t, G-actin/F-actin interaction with 5 nM mDia1 C-t and 2 μM Tmod3 were shown in the .
His Rhoa, supplied by Cytoskeleton Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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his-rhoa - by Bioz Stars, 2026-03
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( a ) mDia1 C-t (blue symbols) or Bni1 (FH1FH2)p (orange open diamond) converted G-actin/G-actin catch bonds (gray diamond, data presented in cited ref. ) to slip-only bonds, in the force range measured ( b ) mDia1 N-t inhibited the mDia1 C-t-induced conversion of G-actin/G-actin catch-slip bonds to slip-only bonds, restoring the catch-slip phenotype. ( c ) His RhoA charged with GTPγS (red square), but not GDP (red open triangles), relieved the inhibitory effect of mDia1 N-t on mDia1 C-t. ( d ) G-actin/F-actin catch-slip bonds (gray square, data presented in cited ref. ) were converted to slip-only bonds by 5 nM mDia1 C-t (blue diamond), the effect of which was exacerbated by 2 μM Tmod3 (open up triangle) but diminished by 10 nM CapZ (open down triangle). ( e ) mDia1 C-t-induced conversion from G-actin/F-actin catch-slip bonds to slip-only bonds was inhibited by simultaneous treatment with mDia1 N-t. ( f ) The inhibitory effect mDia1 N-t on mDia1 C-t was relieved by His RhoA charged with GTPγS. Each point represents the mean ± 95% confidence interval (C.I.) of >30 measurements. The confidence interval is calculated as the standard error multiplied by the t statistic from the t table, assuming a t -distribution with a degree of freedom of sample size minus 1. The semilog plots of survival frequency versus lifetime for the G-actin/G-actin interaction with 5 nM mDia1 C-t, G-actin/F-actin interaction with 5 nM mDia1 C-t and 2 μM Tmod3 were shown in the .

Journal: Scientific Reports

Article Title: Regulation of actin catch-slip bonds with a RhoA-formin module

doi: 10.1038/srep35058

Figure Lengend Snippet: ( a ) mDia1 C-t (blue symbols) or Bni1 (FH1FH2)p (orange open diamond) converted G-actin/G-actin catch bonds (gray diamond, data presented in cited ref. ) to slip-only bonds, in the force range measured ( b ) mDia1 N-t inhibited the mDia1 C-t-induced conversion of G-actin/G-actin catch-slip bonds to slip-only bonds, restoring the catch-slip phenotype. ( c ) His RhoA charged with GTPγS (red square), but not GDP (red open triangles), relieved the inhibitory effect of mDia1 N-t on mDia1 C-t. ( d ) G-actin/F-actin catch-slip bonds (gray square, data presented in cited ref. ) were converted to slip-only bonds by 5 nM mDia1 C-t (blue diamond), the effect of which was exacerbated by 2 μM Tmod3 (open up triangle) but diminished by 10 nM CapZ (open down triangle). ( e ) mDia1 C-t-induced conversion from G-actin/F-actin catch-slip bonds to slip-only bonds was inhibited by simultaneous treatment with mDia1 N-t. ( f ) The inhibitory effect mDia1 N-t on mDia1 C-t was relieved by His RhoA charged with GTPγS. Each point represents the mean ± 95% confidence interval (C.I.) of >30 measurements. The confidence interval is calculated as the standard error multiplied by the t statistic from the t table, assuming a t -distribution with a degree of freedom of sample size minus 1. The semilog plots of survival frequency versus lifetime for the G-actin/G-actin interaction with 5 nM mDia1 C-t, G-actin/F-actin interaction with 5 nM mDia1 C-t and 2 μM Tmod3 were shown in the .

Article Snippet: His-RhoA (Cytoskeleton) was charged with GTPγS (Cytoskeleton) or GDP (Roche, Nutley, NJ) as described previously .

Techniques:

Actin cytoskeleton dynamics are regulated by forces (blue arrows). They are also regulated by GTPases, contributing an important framework for biochemical signal transduction (red arrows). Force regulates actin dynamics by a catch-slip mechanism (yellow circle); and this biophysical regulation is modulated by biochemical signaling through RhoA and formin (gray dashed arrows). RhoA-formin module can serve as a switch shifting the force dependence of actin dynamics between catch bond (with inactivated RhoA or formin) and slip bond (with activated RhoA and formin). It may contribute a crosstalk between mechanotransduction and signal transduction pathways, which control various cell functions.

Journal: Scientific Reports

Article Title: Regulation of actin catch-slip bonds with a RhoA-formin module

doi: 10.1038/srep35058

Figure Lengend Snippet: Actin cytoskeleton dynamics are regulated by forces (blue arrows). They are also regulated by GTPases, contributing an important framework for biochemical signal transduction (red arrows). Force regulates actin dynamics by a catch-slip mechanism (yellow circle); and this biophysical regulation is modulated by biochemical signaling through RhoA and formin (gray dashed arrows). RhoA-formin module can serve as a switch shifting the force dependence of actin dynamics between catch bond (with inactivated RhoA or formin) and slip bond (with activated RhoA and formin). It may contribute a crosstalk between mechanotransduction and signal transduction pathways, which control various cell functions.

Article Snippet: His-RhoA (Cytoskeleton) was charged with GTPγS (Cytoskeleton) or GDP (Roche, Nutley, NJ) as described previously .

Techniques: Transduction

Evidence supporting the biological significance of actin catch-slip bonds.

Journal: Scientific Reports

Article Title: Regulation of actin catch-slip bonds with a RhoA-formin module

doi: 10.1038/srep35058

Figure Lengend Snippet: Evidence supporting the biological significance of actin catch-slip bonds.

Article Snippet: His-RhoA (Cytoskeleton) was charged with GTPγS (Cytoskeleton) or GDP (Roche, Nutley, NJ) as described previously .

Techniques: Mutagenesis, Activity Assay