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Facilitated transport and diffusion take distinct spatial routes through the nuclear pore complex (2010)
Journal Article
Fiserova, J., Richards, S., Wente, S., & Goldberg, M. (2010). Facilitated transport and diffusion take distinct spatial routes through the nuclear pore complex. Journal of Cell Science, 123(16), 2773-2780. https://doi.org/10.1242/jcs.070730

Transport across the nuclear envelope is regulated by nuclear pore complexes (NPCs). Much is understood about the factors that shuttle and control the movement of cargos through the NPC, but less has been resolved about the translocation process itse... Read More about Facilitated transport and diffusion take distinct spatial routes through the nuclear pore complex.

Cell-specific and lamin-dependent targeting of novel transmembrane proteins in the nuclear envelope (2010)
Journal Article
Malik, P., Korfali, N., Srsen, V., Lazou, V., Batrakou, D., Zuleger, N., …Schirmer, E. (2010). Cell-specific and lamin-dependent targeting of novel transmembrane proteins in the nuclear envelope. Cellular and Molecular Life Sciences, 67(8), 1353-1369. https://doi.org/10.1007/s00018-010-0257-2

Nuclear envelope complexity is expanding with respect to identification of protein components. Here we test the validity of proteomics results that identified 67 novel predicted nuclear envelope transmembrane proteins (NETs) from liver by directly co... Read More about Cell-specific and lamin-dependent targeting of novel transmembrane proteins in the nuclear envelope.

Generation of cell-free extracts of Xenopus eggs and demembranated sperm chromatin for the assembly and isolation of in vitro-formed nuclei for Western blotting and scanning electron microscopy (SEM). (2007)
Journal Article
Allen, T., Rutherford, S., Murray, S., Sanderson, H., Gardiner, F., Kiseleva, E., …Drummond, S. (2007). Generation of cell-free extracts of Xenopus eggs and demembranated sperm chromatin for the assembly and isolation of in vitro-formed nuclei for Western blotting and scanning electron microscopy (SEM). Nature Protocols, 2, 1173-1179

A protocol for isolation and visualization of yeast. (2007)
Journal Article
Kiseleva, E., Allen, T., Rutherford, S., Murray, S., Morozova, K., Gardiner, F., …Drummond, S. (2007). A protocol for isolation and visualization of yeast. Nature Protocols, 2(8), 1943-1953

A protocol for isolating Xenopus oocyte nuclear envelope for visualization and characterization by scanning electron microscopy (SEM) or transmission electron microscopy (TEM). (2007)
Journal Article
Allen, T., Rutherford, S., Murray, S., Sanderson, H., Gardiner, F., Kiseleva, E., …Drummond, S. (2007). A protocol for isolating Xenopus oocyte nuclear envelope for visualization and characterization by scanning electron microscopy (SEM) or transmission electron microscopy (TEM). Nature Protocols, 2, 1166-1172

Reticulon 4a/NogoA locates to regions of high membrane curvature and may have a role in nuclear envelope growth (2007)
Journal Article
Kiseleva, E., Morozova, K., Voeltz, G., Allen, T., & Goldberg, M. (2007). Reticulon 4a/NogoA locates to regions of high membrane curvature and may have a role in nuclear envelope growth. Journal of Structural Biology, 160(2), 224-235. https://doi.org/10.1016/j.jsb.2007.08.005

Reticulon 4a (Rtn4a) is a membrane protein that shapes tubules of the endoplasmic reticulum (ER). The ER is attached to the nuclear envelope (NE) during interphase and has a role in post mitotic/meiotic NE reassembly. We speculated that Rtn4a has a r... Read More about Reticulon 4a/NogoA locates to regions of high membrane curvature and may have a role in nuclear envelope growth.

FGF-2 Release from the Lens Capsule by MMP-2 Maintains Lens Epithelial Cell Viability (2007)
Journal Article
Tholozan, F., Gribbon, C., Li, Z., Goldberg, M., Prescott, A., McKie, N., & Quinlan, R. (2007). FGF-2 Release from the Lens Capsule by MMP-2 Maintains Lens Epithelial Cell Viability. Molecular Biology of the Cell, 18(11), 4222-4231. https://doi.org/10.1091/mbc.e06-05-0416

The lens is an avascular tissue, separated from the aqueous and vitreous humors by its own extracellular matrix, the lens capsule. Here we demonstrate that the lens capsule is a source of essential survival factors for lens epithelial cells. Primary... Read More about FGF-2 Release from the Lens Capsule by MMP-2 Maintains Lens Epithelial Cell Viability.

Nuclear membrane disassembly and rupture (2007)
Journal Article
Cotter, L., Allen, T. D., Kiseleva, E., & Goldberg, M. W. (2007). Nuclear membrane disassembly and rupture. Journal of Molecular Biology, 369(3), 683-695. https://doi.org/10.1016/j.jmb.2007.03.051

The nuclear envelope consists of two membranes traversed by nuclear pore complexes. The outer membrane is continuous with the endoplasmic reticulum. At mitosis nuclear pore complexes are dismantled and membranes disperse. The mechanism of dispersal i... Read More about Nuclear membrane disassembly and rupture.

Periplakin-dependent re-organisation of keratin cytoskeleton and loss of collective migration in Keratin 8 down-regulated epithelial sheets (2006)
Journal Article
Long, H. A., Boczonadi, V., McInroy, L., Goldberg, M., & Maatta, A. (2006). Periplakin-dependent re-organisation of keratin cytoskeleton and loss of collective migration in Keratin 8 down-regulated epithelial sheets. Journal of Cell Science, 119(24), 5147-5159. https://doi.org/10.1242/jcs.03304

Collective migration of epithelial sheets requires maintenance of cell-cell junctions and co-ordination of the movement of the migrating front. We have investigated the role of keratin intermediate filaments and periplakin, a cytoskeletal linker prot... Read More about Periplakin-dependent re-organisation of keratin cytoskeleton and loss of collective migration in Keratin 8 down-regulated epithelial sheets.

Yeast nuclear pore complexes have a cytoplasmic ring and internal filaments (2004)
Journal Article
Kiseleva, E., Allen, T., Rutherford, S., Bucci, M., Wente, S., & Goldberg, M. (2004). Yeast nuclear pore complexes have a cytoplasmic ring and internal filaments. Journal of Structural Biology, 145(3), 272-288. https://doi.org/10.1016/j.jsb.2003.11.010

The nuclear pore complex (NPC) controls transport of macromolecules across the nuclear envelope. It is large and complex but appears to consist of only 30 different proteins despite its mass of >60 MDa. Vertebrate NPC structure has been analyzed by s... Read More about Yeast nuclear pore complexes have a cytoplasmic ring and internal filaments.