Sequence Context Strongly Modulates Association of Polar Residues in Transmembrane Helices
- 1 August 2003
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 331 (1) , 255-262
- https://doi.org/10.1016/s0022-2836(03)00714-9
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- Motifs of serine and threonine can drive association of transmembrane helicesJournal of Molecular Biology, 2002
- Polar Residues in Membrane Domains of Proteins: Molecular Basis for Helix−Helix Association in a Mutant CFTR Transmembrane SegmentBiochemistry, 2002
- The Single Transmembrane Domains of ErbB Receptors Self-associate in Cell MembranesJournal of Biological Chemistry, 2002
- Interhelical hydrogen bonds in the CFTR membrane domain.Nature Structural & Molecular Biology, 2001
- Polar residues drive association of polyleucine transmembrane helicesProceedings of the National Academy of Sciences, 2001
- Polar side chains drive the association of model transmembrane peptidesProceedings of the National Academy of Sciences, 2001
- Phosphothreonine recognition comes into focus.Nature Structural & Molecular Biology, 2000
- Asparagine-mediated self-association of a model transmembrane helixNature Structural & Molecular Biology, 2000
- Membrane protein folding and oligomerization: the two-stage modelBiochemistry, 1990
- Multiple independent activations of the neu oncogene by a point mutation altering the transmembrane domain of p185Cell, 1986