Pages that link to "Q54246424"
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The following pages link to Thermodynamic Studies of SHC Phosphotyrosine Interaction Domain Recognition of the NPXpY Motif (Q54246424):
Displaying 17 items.
- Sequence-specific recognition of the internalization motif of the Alzheimer's amyloid precursor protein by the X11 PTB domain (Q24536014) (← links)
- FRS2 proteins recruit intracellular signaling pathways by binding to diverse targets on fibroblast growth factor and nerve growth factor receptors (Q24554326) (← links)
- Specificity determinants for lipids bound to β-barrel proteins (Q27642466) (← links)
- Mapping signal transduction pathways by phage display. (Q30823093) (← links)
- Spatio-temporal modeling of signaling protein recruitment to EGFR. (Q30982487) (← links)
- Physical modulation of intracellular signaling processes by locational regulation (Q33915376) (← links)
- Dockers at the crossroads (Q34465504) (← links)
- Modular evolution of phosphorylation-based signalling systems (Q36153880) (← links)
- Backbone nuclear relaxation characteristics and calorimetric investigation of the human Grb7-SH2/erbB2 peptide complex (Q36476851) (← links)
- Functional expression of TrkA receptors in hippocampal neurons (Q40994436) (← links)
- Measuring protein-protein interactions. (Q41728329) (← links)
- In vitro binding and phosphorylation of insulin receptor substrate 1 by the insulin receptor. Role of interactions mediated by the phosphotyrosine-binding domain and the pleckstrin-homology domain. (Q52525172) (← links)
- Characterization of binding interactions by isothermal titration calorimetry (Q73025422) (← links)
- Thermodynamic analysis of the interaction between the 0.5beta Fv fragment and the RP135 peptide antigen derived from the V3 loop of HIV-1 gp120 (Q73935005) (← links)
- Phosphotyrosine binding domains of Shc and insulin receptor substrate 1 recognize the NPXpY motif in a thermodynamically distinct manner (Q74485105) (← links)
- The PTB Domain: The Name Doesn't Say It All (Q78168527) (← links)
- Hydrophobic interactions are the driving force for the binding of peptide mimotopes and Staphylococcal protein A to recombinant human IgG1 (Q79821926) (← links)