Tryptophan at the transmembrane–cytosolic junction modulates thrombopoietin receptor dimerization and activation
Dimerization of single-pass membrane receptors is essential for activation. In the human thrombopoietin receptor (TpoR), a unique amphipathic RWQFP motif separates the transmembrane (TM) and intracellular domains. Using a combination of mutagenesis, spectroscopy, and biochemical assays, we show that...
محفوظ في:
المؤلفون الرئيسيون: | Jean‐Philippe Defour, Miki Itaya, Vitalina Gryshkova, Ian Brett, C. Pecquet, Takeshi Sato, Steven O. Smith, Stefan N. Constantinescu |
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التنسيق: | Artigo |
اللغة: | الإنجليزية |
منشور في: |
2013
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الوصول للمادة أونلاين: | https://doi.org/10.1073/pnas.1211560110 https://www.pnas.org/content/pnas/110/7/2540.full.pdf |
الوسوم: |
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مواد مشابهة
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Tryptophan at the transmembrane–cytosolic junction modulates thrombopoietin receptor dimerization and activation
حسب: Defour, Jean-Philippe, وآخرون
منشور في: (2013) -
Orientation-specific signalling by thrombopoietin receptor dimers
حسب: Staerk, Judith, وآخرون
منشور في: (2011) -
Orientation-specific signalling by thrombopoietin receptor dimers
حسب: Judith Staerk, وآخرون
منشور في: (2011) -
The Thrombopoietin Receptor: Structural Basis of Traffic and Activation by Ligand, Mutations, Agonists, and Mutated Calreticulin
حسب: Varghese, Leila N., وآخرون
منشور في: (2017) -
The Thrombopoietin Receptor: Structural Basis of Traffic and Activation by Ligand, Mutations, Agonists, and Mutated Calreticulin
حسب: Leila N. Varghese, وآخرون
منشور في: (2017)