Specificity of Arl2/Arl3 signaling is mediated by a ternary Arl3‐effector‐GAP complex
Copyright policy )Specificity of Arl2/Arl3 signaling is mediated by a ternary Arl3‐effector‐GAP complex
MINT‐6602303: ARL2 (uniprotkb:P36404) binds (MI:0407) to HRG4 (uniprotkb:Q13432) by pull down (MI:0096) MINT‐6602333: ARL3 (uniprotkb:P36405) binds (MI:0407) to CoD (uniprotkb:Q9BTW9) by pull down (MI:0096) MINT‐6602347, MINT‐6602369: RP2 (uniprotkb:O75695), ARL3 (uniprotkb:P36405) and HRG4 (uniprotkb:Q13432) physically interact (MI:0218) by fluorescence polarization spectroscopy (MI:0053) MINT‐6602195: PDE delta (uniprotkb:O43924) and ARL2 (uniprotkb:P36404) bind (MI:0407) by fluorescence polarization spectroscopy (MI:0053) MINT‐6602213: BART (uniprotkb:Q8WZ55) and ARL2 (uniprotkb:P36404) bind (MI:0407) by fluorescence polarization spectroscopy (MI:0053) MINT‐6602239: ARL3 (uniprotkb:P36405) and BART (uniprotkb:Q8WZ55) bind (MI:0407) by fluorescence polarization spectroscopy (MI:0053) MINT‐6602322: ARL2 (uniprotkb:P36404) binds (MI:0407) to CoD (uniprotkb:Q9BTW9) by pull down (MI:0096) MINT‐6602258: RP2 (uniprotkb:Q8IWN7) and ARL3 (uniprotkb:P36405) bind (MI:0407) by fluorescence polarization spectroscopy (MI:0053) MINT‐6602233: ARL3 (uniprotkb:P36405) and HRG4 (uniprotkb:Q13432) bind (MI:0407) by fluorescence polarization spectroscopy (MI:0053) MINT‐6602360: HRG4 (uniprotkb:Q13432), ARL3 (uniprotkb:P36405) and RP2 (uniprotkb:O75695) physically interact (MI:0218) by molecular sieving (MI:0071) MINT‐6602297: ARL2 (uniprotkb:P36404) binds (MI:0407) to PDE delta (uniprotkb:O43924) by pull down (MI:0096) MINT‐6602227: ARL3 (uniprotkb:P36405) and PDE delta (uniprotkb:O43924) bind (MI:0407) by fluorescence polarization spectroscopy (MI:0053) MINT‐6602204: HRG4 (uniprotkb:Q13432) and ARL2 (uniprotkb:P36404) bind (MI:0407) by fluorescence polarization spectroscopy (MI:0053)
- Max Planck Society Germany
- Max Planck Institute of Molecular Physiology Germany
Cyclic Nucleotide Phosphodiesterases, Type 6, Photoreceptor, ADP-Ribosylation Factors, Protein Conformation, GTPase-Activating Proteins, Molecular Sequence Data, Intracellular Signaling Peptides and Proteins, Arf, Membrane Proteins, GAP, Signal transduction, Guanosine Diphosphate, GTP-Binding Proteins, Humans, Amino Acid Sequence, Eye Proteins, G proteins, Adaptor Proteins, Signal Transducing, Photoreceptor Cells, Vertebrate, Signal Transduction
Cyclic Nucleotide Phosphodiesterases, Type 6, Photoreceptor, ADP-Ribosylation Factors, Protein Conformation, GTPase-Activating Proteins, Molecular Sequence Data, Intracellular Signaling Peptides and Proteins, Arf, Membrane Proteins, GAP, Signal transduction, Guanosine Diphosphate, GTP-Binding Proteins, Humans, Amino Acid Sequence, Eye Proteins, G proteins, Adaptor Proteins, Signal Transducing, Photoreceptor Cells, Vertebrate, Signal Transduction
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