The positive-inside rule dictates the distribution of charged residues in membrane proteins
the verdict
SUPPORTED
the evidence backs this
confidence 87/100
Multiple studies and foundational rules confirm that the positive-inside rule dictates the asymmetric distribution of charged residues (particularly lysine and arginine) to determine the orientation and topogenesis of membrane proteins.
Evidence for · 8
Lipid-Protein Interactions Drive Membrane Protein Topogenesis in Accordance with the Positive Inside Rule*
2009 · cited by 77
Positively and negatively charged amino acids in extramembrane domains act as determinants of membrane protein orientation.
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More for · 7
Interplay between hydrophobicity and the positive-inside rule in determining membrane-protein topology
2016 · cited by 48
The positive-inside rule orients segments with respect to the membrane and drives insertion.
Topogenesis and cell surface trafficking of GPR34 are facilitated by positive-inside rule that effects through a tri-basic motif in the first intracellular loop.
2016 · cited by 5
A tri-basic motif acts as a topogenic signal dictating transmembrane domain orientation via the positive-inside rule.
Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule.
1992 · cited by 0
Bacterial inner membrane protein topology prediction relies successfully on the positive-inside rule.
Lipid-dependent membrane protein topogenesis.
2009 · cited by 0
Positively charged residues act as retention signals that determine membrane protein topology alongside lipid interactions.
Lipid-Assisted Membrane Protein Folding and Topogenesis.
2019 · cited by 0
The positive-inside rule governs transmembrane protein folding and topogenesis, sometimes extended to a charge balance rule.
Positive charge loading at protein termini is due to membrane protein topology, not a translational ramp.
2014 · cited by 0
N-terminal positive charge loading is explicitly explained by the membrane orientation rules of the positive-inside rule.
On the physical basis for the cis-positive rule describing protein orientation in biological membranes.
1995 · cited by 0
The asymmetry of positively charged residues on membrane sides characterizes hydrophobic intramembrane protein topology.