Results 21 to 30 of about 157,920 (289)

C2 domain membrane penetration by group IVA cytosolic phospholipase A2 induces membrane curvature changes[S]

open access: yesJournal of Lipid Research, 2012
Group IVA cytosolic phospholipase A2 (cPLA2α) is an 85 kDa enzyme that regulates the release of arachidonic acid (AA) from the sn-2 position of membrane phospholipids.
Katherine E. Ward   +3 more
doaj   +1 more source

Role of the plant-specific calcium-binding C2-DOMAIN ABSCISIC ACID-RELATED (CAR) protein family in environmental signaling

open access: yesEuropean Journal of Cell Biology, 2023
Many signaling processes rely on information decoding at the plasma membrane, and membrane-associated proteins and their complexes are fundamental for regulating this process.
Mingming Cui   +2 more
doaj   +1 more source

Solution structure of the inner DysF domain of myoferlin and implications for limb girdle muscular dystrophy type 2b [PDF]

open access: yes, 2008
Mutations in the protein dysferlin, a member of the ferlin family, lead to limb girdle muscular dystrophy type 2B and Myoshi myopathy. The ferlins are large proteins characterised by multiple C2 domains and a single C-terminal membrane-spanning helix ...
Geddes, Stella M.   +8 more
core   +1 more source

Lipid binding domains: more than simple lipid effectors

open access: yesJournal of Lipid Research, 2009
The spatial and temporal regulation of lipid molecules in cell membranes is a hallmark of cellular signaling and membrane trafficking events. Lipid-mediated targeting provides for strict control and versatility, because cell membranes harbor a large ...
Robert V. Stahelin
doaj   +1 more source

Biochemical and functional studies of a novel complement inhibitor, CRIT, with its interaction partners [PDF]

open access: yes, 2005
Complement C2 receptor trispanning (CRIT), a three transmembrane receptor, was first discovered on the surface of the parasite Schistosoma haematobium and formerly termed Schistosoma trispanning orphan receptor (Sh-TOR). This receptor acts as decoy C2-
Hui, Kwok-Min
core   +1 more source

Substitutions at position 263 within the von Willebrand factor type A domain determine the functionality of complement C2 protein

open access: yesFrontiers in Immunology, 2022
The complement system is one of the first defense lines protecting from invading pathogens. However, it may turn offensive to the body’s own cells and tissues when deregulated by the presence of rare genetic variants that impair physiological regulation ...
Alicja Kuźniewska   +12 more
doaj   +1 more source

μ-calpain binds to lipid bilayers via the exposed hydrophobic surface of its Ca2+-activated conformation [PDF]

open access: yes, 2006
μ- and m-calpain are cysteine proteases requiring micro- and millimolar Ca2+ concentrations for their activation in vitro. Among other mechanisms, interaction of calpains with membrane phospholipids has been proposed to facilitate their activation by ...
Machleidt, Werner   +5 more
core   +1 more source

The molecular basis of ceramide-1-phosphate recognition by C2 domains[S]

open access: yesJournal of Lipid Research, 2013
Group IVA cytosolic phospholipase A2 (cPLA2α), which harbors an N-terminal lipid binding C2 domain and a C-terminal lipase domain, produces arachidonic acid from the sn-2 position of zwitterionic lipids such as phosphatidylcholine. The C2 domain has been
Katherine E. Ward   +5 more
doaj   +1 more source

Ferlins and TgDOC2 in Toxoplasma Microneme, Rhoptry and Dense Granule Secretion

open access: yesLife, 2021
The host cell invasion process of apicomplexan parasites like Toxoplasma gondii is facilitated by sequential exocytosis of the microneme, rhoptry and dense granule organelles. Exocytosis is facilitated by a double C2 domain (DOC2) protein family.
Daniel N. A. Tagoe   +5 more
doaj   +1 more source

Crystal structures of the human Dysferlin inner DysF domain [PDF]

open access: yes, 2014
Background: Mutations in dysferlin, the first protein linked with the cell membrane repair mechanism, causes a group of muscular dystrophies called dysferlinopathies.
Cole, Ambrose R.   +9 more
core   +1 more source

Home - About - Disclaimer - Privacy