The Interface between Self-assembling Erythropoietin Receptor Transmembrane Segments Corresponds to a Membrane-spanning Leucine Zipper
Open Access
- 1 January 2004
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 279 (5) , 3273-3279
- https://doi.org/10.1074/jbc.m309311200
Abstract
No abstract availableKeywords
This publication has 46 references indexed in Scilit:
- In Vitro Selection of Self‐Interacting Transmembrane Segments‐‐Membrane Proteins Approached from a Different PerspectiveIUBMB Life, 2002
- In Vitro Selection of Membrane-spanning Leucine Zipper Protein-Protein Interaction Motifs Using POSSYCCATPublished by Elsevier ,2001
- Structure of the Transmembrane Dimer Interface of Glycophorin A in Membrane BilayersBiochemistry, 2001
- The Erythropoietin Receptor: Structure, Activation and Intracellular Signal TransductionTrends in Endocrinology & Metabolism, 1999
- The dimerization motif of the glycophorin A transmembrane segment in membranes: Importance of glycine residuesProtein Science, 1998
- Cell Surface Organization of the Erythropoietin Receptor Complex Differs Depending on its Mode of ActivationPublished by Elsevier ,1997
- Dimerisation of the Glycophorin A Transmembrane Segment in Membranes Probed with the ToxR Transcription ActivatorJournal of Molecular Biology, 1996
- Coiled coils: new structures and new functionsTrends in Biochemical Sciences, 1996
- A Leucine Zipper Stabilizes the Pentameric Membrane Domain of Phospholamban and Forms a Coiled-coil Pore StructureJournal of Biological Chemistry, 1996
- Dimerization of Bence Jones Proteins: Linking the Rate of Transcription from anEscherichia coliPromoter to the Association Constant of REIvBiological Chemistry Hoppe-Seyler, 1994