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Coiled-Coil Domain

Known as: Coiled-Coil, 4-3 Hydrophobic Repeat, Left-Handed Twist 
A domain that stabilizes alpha helices in proteins through a very efficient burial of hydrophobic side chains so that polar water molecules do not… 
National Institutes of Health

Papers overview

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Review
2013
Review
2013
The NF-κB family of transcription factors has an essential role in inflammation and innate immunity. Furthermore, NF-κB is… 
Review
2004
Review
2004
The coiled coil is a common structural motif, formed by approximately 3 ± 5% of all amino acids in proteins. Typically, it… 
Review
2000
Review
2000
Hemagglutinin (HA) is the receptor-binding and membrane fusion glycoprotein of influenza virus and the target for infectivity… 
Highly Cited
1999
Highly Cited
1999
The process of autophagy, or bulk degradation of cellular proteins through an autophagosomic-lysosomal pathway, is important in… 
Highly Cited
1999
Highly Cited
1999
Stimuli-sensitive polymer hydrogels, which swell or shrink in response to changes in the environmental conditions, have been… 
Highly Cited
1997
Highly Cited
1997
Fusion of viral and cellular membranes by the envelope glyco-protein gp120/gp41 effects entry of HIV-1 into the cell. The… 
Highly Cited
1991
Highly Cited
1991
The probability that a residue in a protein is part of a coiled-coil structure was assessed by comparison of its flanking… 
Highly Cited
1991
Highly Cited
1991
Recent studies suggest that one or more genes on chromosome 5q21 are important for the development of colorectal cancers… 
Highly Cited
1990
Highly Cited
1990
The macrophage scavenger receptor is a trimeric membrane glycoprotein with unusual ligand-binding properties which has been… 
Highly Cited
1981
Highly Cited
1981
The haemagglutinin glycoprotein of influenza virus is a trimer comprising two structurally distinct regions: a triple-stranded…