There are several proteins associated with the inner nuclear membrane.

Samp1, is an inner nuclear membrane protein in mammals.

The regulatory functions of inner nuclear membrane proteins strongly suggest this possibility.

SUN proteins are thought to localize to the inner nuclear membrane.

Required for retaining emerin at the inner nuclear membrane.

Lamin A/C is required for samp1 presence at the inner nuclear membrane.

In general, the nucleus is centrally located and the nucleolus is often associated with the inner nuclear membrane.

Samp1 is homologous to the S. Pombe inner nuclear membrane protein Ima1.

The wide array of diseases involving lamins and their associated inner nuclear membrane proteins are collectively called laminopathies.

The first postulates that disruptions of the inner nuclear membrane affect heterochromatin scaffolding and thereby gene expression.

Man1, an inner nuclear membrane protein, regulates vascular remodeling by modulating transforming growth factor beta signaling.

TMEM43 may have an important role in maintaining nuclear envelope structure by organizing protein complexes at the inner nuclear membrane.

The nuclear lamina consist of a two-dimensional matrix of proteins located next to the inner nuclear membrane.

It has been proposed that chromatin-binding/modifying proteins embedded within the inner nuclear membrane may be central in determining the identity of newly differentiated cells.

The nuclear membrane consists of two lipid bilayers-the inner nuclear membrane, and the outer nuclear membrane.

DNA viruses, such as herpesvirus replicate and assemble in the cell nucleus, and exit by budding through the inner nuclear membrane.

In this model, proteins diffuse freely from the ER to the inner nuclear membrane, where association with nuclear lamina or chromatin immobilizes them.

Causes nuclear envelope breakdown by phosphorylating the lamins that form an intermediate filament-type network (nuclear lamina) underlying the inner nuclear membrane.

In metazoan cells, the inner nuclear membrane contains proteins of the nuclear lamina, a protein meshwork underlying the nuclear envelope and providing structural support.

Emerin, together with MAN1, is a LEM domain-containing integral protein of the inner nuclear membrane in vertebrates.

The virus genome replicates and is packaged up within the nucleus, this new nucleocapsid then buds from the inner nuclear membrane and so gains its primary envelope.

They are attached to the nuclear envelope membrane via farnesyl anchors and interaction with inner nuclear membrane proteins such as lamin B receptor and emerin.

The outer membrane is also constant with the inner nuclear membrane since the two layers are fused together at numerous tiny holes called nuclear pores that perforate the nuclear envelope.

Inner nuclear membrane (INM) proteins are proteins that are embedded in or associated with the inner membrane of the nuclear envelope (NE).

At present there is no evidence for IP 3 Rs on the inner nuclear membrane, so the function of any InsP 3 that might be generated in the nucleus remains a problem.