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ProteasomKomplex

Proteasome Komplex

The proteasome complex is a large, multimeric enzyme complex found in eukaryotic cells that is responsible for the degradation of ubiquitinated proteins. The complex consists of multiple subunits, which are arranged in a spherical shape. Each subunit within the complex is composed of different types of proteolytic active sites, allowing the proteasome to degrade a wide range of protein substrates.

The proteasome complex is involved in a variety of cellular processes including protein quality control, cell

The proteasome complex can be categorized into two main types: the 20S proteasome and the 26S proteasome.

Abnormal proteasome function has been implicated in various diseases, including cancer, neurodegenerative disorders, and autoimmune diseases.

Further research is ongoing to elucidate the mechanisms underlying proteasome function and dysfunction.

cycle
regulation,
and
apoptosis.
It
is
also
involved
in
the
degradation
of
misfolded
proteins,
which
is
essential
for
maintaining
cellular
homeostasis.
In
addition,
the
proteasome
complex
plays
a
crucial
role
in
the
regulation
of
cellular
stress
responses,
including
the
response
to
oxidative
stress
and
heat
shock.
The
20S
proteasome
is
a
smaller,
non-activated
form
of
the
complex,
whereas
the
26S
proteasome
is
a
larger,
activated
form
that
is
capable
of
degrading
protein
substrates.
The
26S
proteasome
consists
of
the
20S
proteasome
and
two
regulatory
particles
that
recognize
and
bind
to
ubiquitinated
proteins.
The
proteasome
complex
has
been
the
target
of
therapeutic
interventions,
including
the
development
of
proteasome
inhibitors,
which
have
shown
promise
in
the
treatment
of
these
diseases.