-
giving H2O.
Retinylidene is the
divalent group formed by
removing the
oxygen atom from retinal, and so
opsins have been
called retinylidene proteins. Opsins...
- When an
opsin binds retinal to form a holoprotein, it is
referred to as
Retinylidene protein. However, the
distinction is
often ignored, and
opsin may refer...
-
Retinylidene proteins, or
rhodopsins in a
broad sense, are
proteins that use
retinal as a chromop**** for
light reception. They are the
molecular basis...
-
strong light leads to
formation of
toxic cationic bis-pyridinium salt, N-
retinylidene-N-retinyl-ethanolamine (A2E),
which causes dry and wet age-related macular...
- pRhodopsin)
belongs to the
family of
bacterial transmembrane rhodopsins (
retinylidene proteins). In 1971, the
first microbial transmembrane rhodopsin - Bacteriorhodopsin...
- chromop****,
typically retinal. When
bound to retinal,
opsins become retinylidene proteins, but are
usually still called opsins regardless. Most prominently...
- ac****ulation
leads to
formation of
toxic cationic bis-pyridinium salt, N-
retinylidene-N-retinyl-ethanolamine (A2E),
which causes human dry and wet age-related...
-
flavoproteins and
retinylidene proteins (rhodopsins).
Flavoproteins are
characterized by
containing flavin molecules as chromop****s,
whereas retinylidene proteins...
-
Channelrhodopsins are a
subfamily of
retinylidene proteins (rhodopsins) that
function as light-gated ion channels. They
serve as
sensory photoreceptors...
- base with a
conserved lysine residue, and
interaction of
light with the
retinylidene group causes signal transduction in
color vision (See
visual cycle for...
