The site of action for the Bcl-2 family is mostly on the outer mitochondrial membrane.

They also reduce the mitochondrial membrane potential in mammalian cells.

Apo2.7 is a protein confined to the mitochondrial membrane.

It is primarily driven by the mitochondrial membrane potential.

P450scc is associated with the inner mitochondrial membrane, facing the interior (matrix).

Further more it helps to stabilise mitochondrial membrane potential.

It can also work to restore cardiolipin levels in the inner mitochondrial membrane.

BKCa++ is found in the inner mitochondrial membrane of cardiomyocytes.

This occurs in the inner mitochondrial membrane by coupling the two reactions together.

The protein is normally located on the outer surface of the inner mitochondrial membrane.

Whether Hyal-2 causes mitochondrial membrane damage is unknown.

The outer mitochondrial membrane is made up of two essential proteins, Tom40 and Sam50.

Its permeability to mitochondrial membranes makes it particularly useful.

These are particles of 9 nm diameter that pepper the inner mitochondrial membrane.

Interestingly, disturbing this process leads to Ras2 accumulation at the mitochondrial membrane, a behavior that was not observed before.

K1.3 has been reported to be expressed in the inner mitochondrial membrane in lymphocytes.

PE produced in the mitochondrial membrane is also transported throughout the cell to other membranes for use.

It has also been localized in the inner mitochondrial membrane as part of the malate-aspartate shuttle.

Upon induction of apoptosis, it was found to tightly associate with mitochondrial membranes.

This enzyme is required since fatty acids cannot cross the mitochondrial membranes without assistance.

This causes the cristae to pinch off forcing the inner mitochondrial membrane inside out.

ANT is the most plentiful protein in the inner mitochondrial membrane.

The inner mitochondrial membrane contains proteins with five types of functions:

The protein localizes to the outer mitochondrial membrane.

MitoK were first identified in 1991 by single-channel recordings of the inner mitochondrial membrane.