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4 hits found for Double-stranded RNA-binding protein Staufen homolog 1 with truncated Staufen-swapping motif (ΔSSM)

SASDWK9 – ...Double-stranded RNA-binding protein Staufen homolog 1 with truncated Staufen-swapping (ΔSSM) motif

Double-stranded RNA-binding protein Staufen homolog 1 (81-577 + Δ454-488) experimental SAS data
Human Double-stranded RNA-binding protein Staufen homolog 1 with truncated Staufen-swapping (ΔSSM) motif Rg histogram
Human Double-stranded RNA-binding protein Staufen homolog 1 with truncated Staufen-swapping (ΔSSM) motif Rg histogram
Human Double-stranded RNA-binding protein Staufen homolog 1 with truncated Staufen-swapping (ΔSSM) motif Rg histogram
Human Double-stranded RNA-binding protein Staufen homolog 1 with truncated Staufen-swapping (ΔSSM) motif Rg histogram
Sample: Double-stranded RNA-binding protein Staufen homolog 1 (81-577 + Δ454-488) , 52 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl, 300 mM NaCl, 3.6 mM β-mercaptoethanol, pH: 7
Experiment: SAXS data collected at ...1000, CEITEC on 2020 Apr 5
Staufen-swapping motif is crucial for Staufen dimerization, structure, and Staufen-mediated mRNA decay. Protein Sci 35(7):e70669 (2026)
Tripepi A, Shakoor H, Zlobina M, Klumpler T, Kubíčková M, Houser J, Klapetek P, Lukavsky PJ
RgGuinier 5.1 nm
Dmax 13.8 nm
VolumePorod 105 nm3

SASDWN9 – ...Double-stranded RNA-binding protein Staufen homolog 1 with truncated RNA-binding domain 2 and truncated Staufen-swapping (ΔSSM) motif

Double-stranded RNA-binding protein Staufen homolog 1 (178-577 + Δ454-488) experimental SAS data
Human Double-stranded RNA-binding protein Staufen homolog 1 with truncated RNA-binding domain 2 and truncated Staufen-swapping (ΔSSM) motif Rg histogram
Sample: Double-stranded RNA-binding protein Staufen homolog 1 (178-577 + Δ454-488) monomer, 41 kDa Homo sapiens protein
Buffer: ...150 mM NaCl, 3.6 mM β-mercaptoethanol, pH: 8
Experiment: SAXS data collected at ...12, PETRA III on ...17
Staufen-swapping motif is crucial for Staufen dimerization, structure, and Staufen-mediated mRNA decay. Protein Sci 35(7):e70669 (2026)
Tripepi A, Shakoor H, Zlobina M, Klumpler T, Kubíčková M, Houser J, Klapetek P, Lukavsky PJ
RgGuinier 4.6 nm
Dmax 16.9 nm
VolumePorod 99 nm3

SASDUV5 – ...Double-stranded RNA-binding protein Staufen homolog 1 with truncated RNA-binding domain 2 and truncated Staufen-swapping (ΔSSM) motif bound to 3'UTR fragment of ADP-ribosylation factor 1

3'UTR fragment of ADP-ribosylation factor 1Double-stranded RNA-binding protein Staufen homolog 1 with truncated RNA-binding domain 2 and truncated Staufen-swapping (ΔSSM) experimental SAS data
CORAL model
Sample: ...1 monomer, 14 kDa Homo sapiens RNA
Double-stranded RNA-binding protein Staufen homolog 1 with truncated RNA-binding domain 2 and truncated Staufen-swapping (ΔSSM) dimer, 81 kDa Homo sapiens protein
Buffer: 50 mM TRIS, 300 mM NaCl, 3.8 mM β-mercaptoethanol, pH: 7
Experiment: SAXS data collected at Rigaku BioSAXS-2000, CEITEC on ...12
...Protein Complexes by Atomic Force Microscopy. Curr Protoc 5(1):e70084 (2025)
Tripepi A, Shakoor H, Klapetek P
RgGuinier 5.5 nm
Dmax 16.1 nm
VolumePorod 139 nm3

SASDWL9 – ...Double-stranded RNA-binding protein Staufen homolog 1 with truncated RNA-binding domain 2 and truncated RNA-binding domain 3 and truncated Staufen-swapping (ΔSSM) motif

Double-stranded RNA-binding protein Staufen homolog 1 (286-577 + Δ454-488) experimental SAS data
Human Double-stranded RNA-binding protein Staufen homolog 1 with truncated RNA-binding domain 2 and truncated RNA-binding domain 3 and truncated Staufen-swapping (ΔSSM) motif Rg histogram
Sample: Double-stranded RNA-binding protein Staufen homolog 1 (286-577 + Δ454-488) monomer, 29 kDa Homo sapiens protein
Buffer: ...150 mM NaCl, 3.6 mM β-mercaptoethanol, pH: 8
Experiment: SAXS data collected at ...12, PETRA III on ...17
Staufen-swapping motif is crucial for Staufen dimerization, structure, and Staufen-mediated mRNA decay. Protein Sci 35(7):e70669 (2026)
Tripepi A, Shakoor H, Zlobina M, Klumpler T, Kubíčková M, Houser J, Klapetek P, Lukavsky PJ
RgGuinier 4.1 nm
Dmax 19.5 nm
VolumePorod 64 nm3