How proteins produce cellular membrane curvature
By J. Zimmerberg, Michael M. Kozlov. Nature reviews. Molecular cell biology, 2006
1,271 citations recorded by the source corpus.
Subfields: Cell Biology, Molecular Biology, Physiology
View Paper: https://www.semanticscholar.org/paper/1800aff4efbcb9900bf1b42022d0ff75ea493d4e
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Citations in the corpus
- Membrane recognition by phospholipid-binding domains (2008, background): “In principle, any phospholipid-binding domain that penetrates the membrane surface (and there are many) will increase the surface area of the leaflet into which it inserts and thus promote membrane curvatur”
- The Fluid-Mosaic Model of Membrane Structure: still relevant to understanding the structure, function and dynamics of biological membranes after more than 40 years. (2014, background): “Cell membrane lipid asymmetry may also guide membrane curvature and other aspects of membrane structure [59,69,73,74,87,88].”
- Membrane curvature at a glance (2015, background): “…phosphates (PtdIns) confers an inverted conical shape to the lipids, thereby favoring the bending of the membrane into a positive curvature, bending the monolayer away from the headgroups (reviewed in Chernomordik and Kozlov, 2003; Di Paolo and De Camilli, 2006; Zimmerberg and Kozlov, 2006).”
- Advances in Planar Lipid Bilayers and Liposomes (2011, methodology): “Although we explicitly use type I and type II spectrin filaments as the origin of the curvature, the model also applies when the curvature is induced by membrane proteins other than spectrin, such as curved integral proteins [13,39].”
- Microvesicles: mediators of extracellular communication during cancer progression (2010, background): “Third, contractile proteins can conceivably add tensile or contractile forces to one leaflet of the membrane, creating a structural asymmetry that would lead to bending (Huttner and Zimmerberg, 2001; Zimmerberg and Kozlov, 2006).”
- Modification of intracellular membrane structures for virus replication (2008, background): “Curvature can also be induced by peripheral association of scaffolding proteins, such as coat proteins (reviewed in REFs 2, [78] [79] [80] (FIG.”