In Vivo Detection of Hetero-association of Glycophorin-A and Its Mutants within the Membrane
Open Access
- 1 August 2001
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 276 (33) , 31229-31232
- https://doi.org/10.1074/jbc.m101889200
Abstract
No abstract availableKeywords
This publication has 42 references indexed in Scilit:
- Helix 4 of the Bacillus thuringiensis Cry1Aa Toxin Lines the Lumen of the Ion ChannelJournal of Biological Chemistry, 1999
- The structure and organization within the membrane of the helices composing the pore-forming domain of Bacillus thuringiensis δ-endotoxin are consistent with an “umbrella-like” structure of the poreProceedings of the National Academy of Sciences, 1998
- Refolding of Bacteriorhodopsin from Expressed Polypeptide FragmentsJournal of Biological Chemistry, 1998
- Dimerization of the Synaptic Vesicle Protein Synaptobrevin (Vesicle‐Associated Membrane Protein) II Depends on Specific Residues within the Transmembrane SegmentEuropean Journal of Biochemistry, 1997
- Dimerisation of the Glycophorin A Transmembrane Segment in Membranes Probed with the ToxR Transcription ActivatorJournal of Molecular Biology, 1996
- Molecular recognition between membrane-spanning polypeptidesTrends in Biochemical Sciences, 1995
- The Assembly and Organization of the α5 and α7 Helices from the Pore-forming Domain of Bacillusthuringiensis δ-EndotoxinJournal of Biological Chemistry, 1995
- Glycophorin A Helical Transmembrane Domains Dimerize in Phospholipid Bilayers: A Resonance Energy Transfer StudyBiochemistry, 1994
- Bacteriorhodopsin can be refolded from two independently stable transmembrane helixes and the complementary five-helix fragmentBiochemistry, 1992
- Organization and stability of a polytopic membrane protein: deletion analysis of the lactose permease of Escherichia coli.Proceedings of the National Academy of Sciences, 1991