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Professor Martin Goldberg's Outputs (93)

Inhibition of PDIs Downregulates Core LINC Complex Proteins, Promoting the Invasiveness of MDA-MB-231 Breast Cancer Cells in Confined Spaces In Vitro (2024)
Journal Article
Young, N., Gui, Z., Mustafa, S., Papa, K., Jessop, E., Ruddell, E., …Karakesisoglou, I. (2024). Inhibition of PDIs Downregulates Core LINC Complex Proteins, Promoting the Invasiveness of MDA-MB-231 Breast Cancer Cells in Confined Spaces In Vitro. Cells, 13(11), Article 906. https://doi.org/10.3390/cells13110906

Eukaryotic cells tether the nucleoskeleton to the cytoskeleton via a conserved molecular bridge, called the LINC complex. The core of the LINC complex comprises SUN-domain and KASH-domain proteins that directly associate within the nuclear envelope l... Read More about Inhibition of PDIs Downregulates Core LINC Complex Proteins, Promoting the Invasiveness of MDA-MB-231 Breast Cancer Cells in Confined Spaces In Vitro.

The major inducible small heat shock protein HSP20-3 in the tardigrade Ramazzottius varieornatus forms filament-like structures and is an active chaperone. (2023)
Journal Article
Al-Ansari, M., Fitzsimons, T., Wei, W., Goldberg, M. W., Kunieda, T., & Quinlan, R. A. (2024). The major inducible small heat shock protein HSP20-3 in the tardigrade Ramazzottius varieornatus forms filament-like structures and is an active chaperone. Cell Stress and Chaperones, 29(1), 51-65. https://doi.org/10.1016/j.cstres.2023.12.001

The tardigrade Ramazzottius varieornatus has remarkable resilience to a range of environmental stresses. In this study, we have characterised two members of the small heat shock protein (sHSP) family in R. varieornatus, HSP20-3 and HSP20-6. These are... Read More about The major inducible small heat shock protein HSP20-3 in the tardigrade Ramazzottius varieornatus forms filament-like structures and is an active chaperone..

STING nuclear partners contribute to innate immune signaling responses (2021)
Journal Article
Dixon, C. R., Malik, P., de las Heras, J. I., Saiz-Ros, N., de Lima Alves, F., Tingey, M., …Schirmer, E. C. (2021). STING nuclear partners contribute to innate immune signaling responses. iScience, 24(9), https://doi.org/10.1016/j.isci.2021.103055

STimulator of INterferon Genes (STING) is an adaptor for cytoplasmic DNA sensing by cGAMP/cGAS that helps trigger innate immune responses (IIRs). Although STING is mostly localized in the ER, we find a separate inner nuclear membrane pool of STING th... Read More about STING nuclear partners contribute to innate immune signaling responses.

Culturing Keratinocytes on Biomimetic Substrates Facilitates Improved Epidermal Assembly In Vitro (2021)
Journal Article
Hunter-Featherstone, E., Young, N., Chamberlain, K., Cubillas, P., Hulette, B., Wei, X., …Karakesisoglou, I. (2021). Culturing Keratinocytes on Biomimetic Substrates Facilitates Improved Epidermal Assembly In Vitro. Cells, 10(5), https://doi.org/10.3390/cells10051177

Mechanotransduction is defined as the ability of cells to sense mechanical stimuli from their surroundings and translate them into biochemical signals. Epidermal keratinocytes respond to mechanical cues by altering their proliferation, migration, and... Read More about Culturing Keratinocytes on Biomimetic Substrates Facilitates Improved Epidermal Assembly In Vitro.

Proteomic mapping by rapamycin-dependent targeting of APEX2 identifies binding partners of VAPB at the inner nuclear membrane (2019)
Journal Article
James, C., Müller, M., Goldberg, M. W., Lenz, C., Urlaub, H., & Kehlenbach, R. H. (2019). Proteomic mapping by rapamycin-dependent targeting of APEX2 identifies binding partners of VAPB at the inner nuclear membrane. Journal of Biological Chemistry, 294(44), 16241-16254. https://doi.org/10.1074/jbc.ra118.007283

Vesicle-associated membrane protein–associated protein B (VAPB) is a tail-anchored protein that is present at several contact sites of the endoplasmic reticulum (ER). We now show by immunoelectron microscopy that VAPB also localizes to the inner nucl... Read More about Proteomic mapping by rapamycin-dependent targeting of APEX2 identifies binding partners of VAPB at the inner nuclear membrane.

BFSP1 C-terminal domains released by post-translational processing events can alter significantly the calcium regulation of AQP0 water permeability (2019)
Journal Article
Tapodi, A., Clemens, D., Uwineza, A., Goldberg, M., Thinon, E., Heal, W., …Quinlan, R. (2019). BFSP1 C-terminal domains released by post-translational processing events can alter significantly the calcium regulation of AQP0 water permeability. Experimental Eye Research, 185, Article 107585. https://doi.org/10.1016/j.exer.2019.02.001

BFSP1 (beaded filament structural protein 1, filensin) is a cytoskeletal protein expressed in the eye lens. It binds AQP0 in vitro and its C-terminal sequences have been suggested to regulate the water channel activity of AQP0. A myristoylated fragme... Read More about BFSP1 C-terminal domains released by post-translational processing events can alter significantly the calcium regulation of AQP0 water permeability.

Supramolecular Structures of the Dictyostelium Lamin NE81 (2019)
Journal Article
Grafe, M., Batsios, P., Meyer, I., Lisin, D., Baumann, O., Goldberg, M., & Gräf, R. (2019). Supramolecular Structures of the Dictyostelium Lamin NE81. Cells, 8(2), Article 162. https://doi.org/10.3390/cells8020162

Nuclear lamins are nucleus-specific intermediate filaments (IF) found at the inner nuclear membrane (INM) of the nuclear envelope (NE). Together with nuclear envelope transmembrane proteins, they form the nuclear lamina and are crucial for gene regul... Read More about Supramolecular Structures of the Dictyostelium Lamin NE81.

Host Vesicle Fusion Protein VAPB Contributes to the Nuclear Egress Stage of Herpes Simplex Virus Type-1 (HSV-1) Replication (2019)
Journal Article
Saiz-Ros, N., Czapiewski, R., Epifano, I., Stevenson, A., Swanson, S., Dixon, C., …Schirmer, E. (2019). Host Vesicle Fusion Protein VAPB Contributes to the Nuclear Egress Stage of Herpes Simplex Virus Type-1 (HSV-1) Replication. Cells, 8(2), Article 120. https://doi.org/10.3390/cells8020120

The primary envelopment/de-envelopment of Herpes viruses during nuclear exit is poorly understood. In Herpes simplex virus type-1 (HSV-1), proteins pUL31 and pUL34 are critical, while pUS3 and some others contribute; however, efficient membrane fusio... Read More about Host Vesicle Fusion Protein VAPB Contributes to the Nuclear Egress Stage of Herpes Simplex Virus Type-1 (HSV-1) Replication.

The intestinal intermediate filament network responds to and protects against microbial insults and toxins (2019)
Journal Article
Geisler, F., Coch, R. A., Richardson, C., Goldberg, M., Denecke, B., Bossinger, O., & Leube, R. E. (2019). The intestinal intermediate filament network responds to and protects against microbial insults and toxins. Development, 146(2), Article dev.169482. https://doi.org/10.1242/dev.169482

The enrichment of intermediate filaments in the apical cytoplasm of intestinal cells is evolutionary conserved forming a sheath that is anchored to apical junctions and positioned below the microvillar brush border suggestive of a protective intracel... Read More about The intestinal intermediate filament network responds to and protects against microbial insults and toxins.

Agitation Modules: Flexible Means to Accelerate Automated Freeze Substitution (2018)
Journal Article
Reipert, S., Goldammer, H., Richardson, C., Goldberg, M. W., Hawkins, T. J., Hollergschwandtner, E., …Stierhof, Y. (2018). Agitation Modules: Flexible Means to Accelerate Automated Freeze Substitution. Journal of Histochemistry & Cytochemistry, 66(12), 903-921. https://doi.org/10.1369/0022155418786698

For ultrafast fixation of biological samples to avoid artifacts, high-pressure freezing (HPF) followed by freeze substitution (FS) is preferred over chemical fixation at room temperature. After HPF, samples are maintained at low temperature during de... Read More about Agitation Modules: Flexible Means to Accelerate Automated Freeze Substitution.

Farnesyltransferase inhibitor and rapamycin correct aberrant genome organisation and decrease DNA damage respectively, in Hutchinson–Gilford progeria syndrome fibroblasts (2018)
Journal Article
Bikkul, M. U., Clements, C. S., Godwin, L. S., Goldberg, M. W., Kill, I. R., & Bridger, J. M. (2018). Farnesyltransferase inhibitor and rapamycin correct aberrant genome organisation and decrease DNA damage respectively, in Hutchinson–Gilford progeria syndrome fibroblasts. Biogerontology, 19(6), 579-602. https://doi.org/10.1007/s10522-018-9758-4

Hutchinson–Gilford progeria syndrome (HGPS) is a rare and fatal premature ageing disease in children. HGPS is one of several progeroid syndromes caused by mutations in the LMNA gene encoding the nuclear structural proteins lamins A and C. In classic... Read More about Farnesyltransferase inhibitor and rapamycin correct aberrant genome organisation and decrease DNA damage respectively, in Hutchinson–Gilford progeria syndrome fibroblasts.

Nuclear pore complex tethers to the cytoskeleton (2017)
Journal Article
Goldberg, M. W. (2017). Nuclear pore complex tethers to the cytoskeleton. Seminars in Cell and Developmental Biology, 68, 52-58. https://doi.org/10.1016/j.semcdb.2017.06.017

The nuclear envelope is tethered to the cytoskeleton. The best known attachments of all elements of the cytoskeleton are via the so-called LINC complex. However, the nuclear pore complexes, which mediate the transport of soluble and membrane bound mo... Read More about Nuclear pore complex tethers to the cytoskeleton.

Repo-Man/PP1 regulates heterochromatin formation in interphase (2017)
Journal Article
Castro, I., Budzak, J., Di Giacinto, M. L., Ligammari, L., Gokhan, E., Spanos, C., …Vagnarelli, P. (2017). Repo-Man/PP1 regulates heterochromatin formation in interphase. Nature Communications, 8, Article 14048. https://doi.org/10.1038/ncomms14048

Repo-Man is a protein phosphatase 1 (PP1) targeting subunit that regulates mitotic progression and chromatin remodelling. After mitosis, Repo-Man/PP1 remains associated with chromatin but its function in interphase is not known. Here we show that Rep... Read More about Repo-Man/PP1 regulates heterochromatin formation in interphase.

Immunoelectron Microscopy of Cryofixed Freeze-Substituted Yeast (2016)
Book Chapter
Fišerová, J., Richardson, C., & Goldberg, M. W. (2016). Immunoelectron Microscopy of Cryofixed Freeze-Substituted Yeast. In S. D. Schwartzbach, O. Skalli, & T. Schikorski (Eds.), High-Resolution Imaging of Cellular Proteins (243-258). Humana Press. https://doi.org/10.1007/978-1-4939-6352-2_15

Immunolabeling electron microscopy is a challenging technique with demands for perfect ultrastructural and antigen preservation. High-pressure freezing offers an excellent way to fix cellular structure. However, its use for immunolabeling has remaine... Read More about Immunoelectron Microscopy of Cryofixed Freeze-Substituted Yeast.

Phosphorylation Regulates the Endocytic Function of the Yeast Dynamin-Related Protein Vps1 (2015)
Journal Article
Smaczynska-de Rooij, I. I., Marklew, C. J., Allwood, E. G., Palmer, S. E., Booth, W. I., Mishra, R., …Ayscough, K. R. (2016). Phosphorylation Regulates the Endocytic Function of the Yeast Dynamin-Related Protein Vps1. Molecular and Cellular Biology, 36(5), 742-755. https://doi.org/10.1128/mcb.00833-15

The family of dynamin proteins is known to function in many eukaryotic membrane fusion and fission events. The yeast dynamin-related protein Vps1 functions at several stages of membrane trafficking, including Golgi apparatus to endosome and vacuole,... Read More about Phosphorylation Regulates the Endocytic Function of the Yeast Dynamin-Related Protein Vps1.

The Immune Adaptor SLP-76 Binds to SUMO-RANGAP1 at Nuclear Pore Complex Filaments to Regulate Nuclear Import of Transcription Factors in T Cells (2015)
Journal Article
Liu, H., Schneider, H., Recino, A., Richardson, C., Goldberg, M. W., & Rudd, C. E. (2015). The Immune Adaptor SLP-76 Binds to SUMO-RANGAP1 at Nuclear Pore Complex Filaments to Regulate Nuclear Import of Transcription Factors in T Cells. Molecular Cell, 59(5), 840-849. https://doi.org/10.1016/j.molcel.2015.07.015

While immune cell adaptors regulate proximal T cell signaling, direct regulation of the nuclear pore complex (NPC) has not been reported. NPC has cytoplasmic filaments composed of RanGAP1 and RanBP2 with the potential to interact with cytoplasmic med... Read More about The Immune Adaptor SLP-76 Binds to SUMO-RANGAP1 at Nuclear Pore Complex Filaments to Regulate Nuclear Import of Transcription Factors in T Cells.

Xenopus LAP2β protein knockdown affects location of lamin B and nucleoporins and has effect on assembly of cell nucleus and cell viability (2015)
Journal Article
Dubińska-Magiera, M., Chmielewska, M., Kozioł, K., Machowska, M., Hutchison, C. J., Goldberg, M. W., & Rzepecki, R. (2015). Xenopus LAP2β protein knockdown affects location of lamin B and nucleoporins and has effect on assembly of cell nucleus and cell viability. Protoplasma, 253(3), 943-956. https://doi.org/10.1007/s00709-015-0861-y

Xenopus LAP2β protein is the single isoform expressed in XTC cells. The protein localizes on heterochromatin clusters both at the nuclear envelope and inside a cell nucleus. The majority of XLAP2β fraction neither colocalizes with TPX2 protein during... Read More about Xenopus LAP2β protein knockdown affects location of lamin B and nucleoporins and has effect on assembly of cell nucleus and cell viability.

A Charge Swap mutation E461K in the yeast dynamin Vps1 reduces endocytic invagination (2015)
Journal Article
Palmer, S., Smaczynska-de Rooij, I., Marklew, C., Allwood, E., Mishra, R., Goldberg, M., & Ayscough, K. (2015). A Charge Swap mutation E461K in the yeast dynamin Vps1 reduces endocytic invagination. Communicative and Integrative Biology, 8(4), https://doi.org/10.1080/19420889.2015.1051274

Vps1 is the yeast dynamin-like protein that functions during several membrane trafficking events including traffic from Golgi to vacuole, endosomal recycling and endocytosis. Vps1 can also function in peroxisomal fission indicating that its ability t... Read More about A Charge Swap mutation E461K in the yeast dynamin Vps1 reduces endocytic invagination.

A dynamin-actin interaction is required for vesicle scission during endocytosis in yeast (2015)
Journal Article
Palmer, S., Smaczynska-de Rooij, I., Marklew, C., Allwood, E., Mishra, R., Johnson, S., …Ayscough, K. (2015). A dynamin-actin interaction is required for vesicle scission during endocytosis in yeast. Current Biology, 25(7), 868-878. https://doi.org/10.1016/j.cub.2015.01.061

Actin is critical for endocytosis in yeast cells, and also in mammalian cells under tension. However, questions remain as to how force generated through actin polymerization is transmitted to the plasma membrane to drive invagination and scission. He... Read More about A dynamin-actin interaction is required for vesicle scission during endocytosis in yeast.

Imaging Yeast NPCs: From Classical Electron Microscopy to Immuno-SEM (2014)
Book Chapter
Kiseleva, E., Richardson, A. C., Fiserova, J., Strunov, A. A., Spink, M. C., Johnson, S. R., & Goldberg, M. W. (2014). Imaging Yeast NPCs: From Classical Electron Microscopy to Immuno-SEM. In Nuclear Pore Complexes and Nucleocytoplasmic Transport - Methods (59-79). Elsevier/Academic Press. https://doi.org/10.1016/b978-0-12-417160-2.00003-5

Electron microscopy (EM) has been used extensively for the study of nuclear transport as well as the structure of the nuclear pore complex (NPC) and nuclear envelope. However, there are specific challenges faced when carrying out EM in one of the mai... Read More about Imaging Yeast NPCs: From Classical Electron Microscopy to Immuno-SEM.

A gradient of matrix-bound FGF-2 and perlecan is available to lens epithelial cells (2014)
Journal Article
Wu, W., Tholozan, F., Goldberg, M., Bowen, L., Wu, J., & Quinlan, R. (2014). A gradient of matrix-bound FGF-2 and perlecan is available to lens epithelial cells. Experimental Eye Research, 120, 10-14. https://doi.org/10.1016/j.exer.2013.12.004

Fibroblast growth factors play a key role in regulating lens epithelial cell proliferation and differentiation via an anteroposterior gradient that exists between the aqueous and vitreous humours. FGF-2 is the most important for lens epithelial cell... Read More about A gradient of matrix-bound FGF-2 and perlecan is available to lens epithelial cells.

Entry into the nuclear pore complex is controlled by a cytoplasmic exclusion zone containing dynamic GLFG-repeat nucleoporin domains (2014)
Journal Article
Fiserova, J., Spink, M., Richards, S., Saunter, C., & Goldberg, M. (2014). Entry into the nuclear pore complex is controlled by a cytoplasmic exclusion zone containing dynamic GLFG-repeat nucleoporin domains. Journal of Cell Science, 127, 124-136. https://doi.org/10.1242/jcs.133272

Nuclear pore complexes (NPCs) mediate nucleocytoplasmic movement. The central channel contains proteins with phenylalanine-glycine (FG) repeats, or variations (GLFG, glycine-leucine-phenylalanine-glycine). These are ‘intrinsically disordered’ and oft... Read More about Entry into the nuclear pore complex is controlled by a cytoplasmic exclusion zone containing dynamic GLFG-repeat nucleoporin domains.

Microscopic visualisation of metabotropic glutamate receptors on the surface of living cells using bifunctional magnetic resonance imaging probes (2013)
Other
Mishra, A., Mishra, R., Gottschalk, S., Pal, R., Sim, N., Engelmann, J., …Parker, D. (2014). Microscopic visualisation of metabotropic glutamate receptors on the surface of living cells using bifunctional magnetic resonance imaging probes

A series of bimodal metabotropic glutamate-receptor targeted MRI contrast agents has been developed and evaluated, based on established competitive metabotropic Glu receptor subtype 5 (mGluR5) antagonists. In order to directly visualize mGluR5 bindin... Read More about Microscopic visualisation of metabotropic glutamate receptors on the surface of living cells using bifunctional magnetic resonance imaging probes.

Nesprin interchain associations control nuclear size. (2012)
Journal Article
Lu, W., Schneider, M., Neumann, S., Jaeger, V., Taranum, S., Munck, M., …Karakesisoglou, I. (2012). Nesprin interchain associations control nuclear size. Cellular and Molecular Life Sciences, 69(20), 3493-3509. https://doi.org/10.1007/s00018-012-1034-1

Nesprins-1/-2/-3/-4 are nuclear envelope proteins, which connect nuclei to the cytoskeleton. The largest nesprin-1/-2 isoforms (termed giant) tether F-actin through their N-terminal actin binding domain (ABD). Nesprin-3, however, lacks an ABD and ass... Read More about Nesprin interchain associations control nuclear size..

Yeast dynamin Vps1 and amphiphysin Rvs167 function together during endocytosis (2012)
Journal Article
Rooij, I. I. S., Allwood, E. G., Mishra, R., Booth, W. I., Aghamohammadzadeh, S., Goldberg, M. W., & Ayscough, K. R. (2012). Yeast dynamin Vps1 and amphiphysin Rvs167 function together during endocytosis. Traffic, 13(2), 317-328. https://doi.org/10.1111/j.1600-0854.2011.01311.x

Dynamins are a conserved family of proteins involved in many membrane fusion and fission events. Previously, the dynamin-related protein Vps1 was shown to localize to endocytic sites, and yeast carrying deletions for genes encoding both the BAR domai... Read More about Yeast dynamin Vps1 and amphiphysin Rvs167 function together during endocytosis.

Embryonic and adult isoforms of XLAP2 form microdomains associated with chromatin and the nuclear envelope (2011)
Journal Article
Chmielewska, M., Dubińska-Magiera, M., Sopel, M., Rzepecka, D., Hutchison, C., Goldberg, M., & Rzepecki, R. (2011). Embryonic and adult isoforms of XLAP2 form microdomains associated with chromatin and the nuclear envelope. Cell and Tissue Research, 344(1), 97-110. https://doi.org/10.1007/s00441-011-1129-2

Laminin-associated polypeptide 2 (LAP2) proteins are alternatively spliced products of a single gene; they belong to the LEM domain family and, in mammals, locate to the nuclear envelope (NE) and nuclear lamina. Isoforms lacking the transmembrane dom... Read More about Embryonic and adult isoforms of XLAP2 form microdomains associated with chromatin and the nuclear envelope.

System analysis shows distinct mechanisms and common principles of nuclear envelope protein dynamics (2011)
Journal Article
Zuleger, N., Kelly, D. A., Richardson, A. C., Kerr, A. R., Goldberg, M. W., Goryachev, A. B., & Schirmer, E. C. (2011). System analysis shows distinct mechanisms and common principles of nuclear envelope protein dynamics. Journal of Cell Biology, 193(1), 109-123. https://doi.org/10.1083/jcb.201009068

The nuclear envelope contains >100 transmembrane proteins that continuously exchange with the endoplasmic reticulum and move within the nuclear membranes. To better understand the organization and dynamics of this system, we compared the trafficking... Read More about System analysis shows distinct mechanisms and common principles of nuclear envelope protein dynamics.

Expression of Vps1 I649K a self-assembly defective yeast dynamin, leads to formation of extended endocytic invaginations. (2011)
Journal Article
Mishra, R., Smaczynska-de Rooij, I., Goldberg, M., & Ayscough, K. (2011). Expression of Vps1 I649K a self-assembly defective yeast dynamin, leads to formation of extended endocytic invaginations. Communicative and Integrative Biology, 4(1), 115-117. https://doi.org/10.4161/cib.14206

The dynamin proteins have been associated with the process of endocytosis for many years. Until recently it was considered that yeast dynamin-related proteins did not play a role in endocytosis and the proposed scission function of dynamin was attrib... Read More about Expression of Vps1 I649K a self-assembly defective yeast dynamin, leads to formation of extended endocytic invaginations..

A role for the dynamin-like protein Vps1 during endocytosis in yeast. (2010)
Journal Article
Smaczynska-de Rooij, I., Allwood, E., Aghamohammadzadeh, S., Hettema, E., Goldberg, M., & Ayscough, K. (2010). A role for the dynamin-like protein Vps1 during endocytosis in yeast. Journal of Cell Science, 123(20), 3496-3506. https://doi.org/10.1242/%26%238203%3Bjcs.070508

Dynamins are a conserved family of proteins involved in membrane fusion and fission. Although mammalian dynamins are known to be involved in several membrane-trafficking events, the role of dynamin-1 in endocytosis is the best-characterised role of t... Read More about A role for the dynamin-like protein Vps1 during endocytosis in yeast..

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.

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

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

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.

The cytoplasmic filaments of the nuclear pore complex are dispensable for selective nuclear protein import (2002)
Journal Article
Walther, T., Pickersgill, H., Cordes, V., Goldberg, M., Allen, T., Mattaj, I., & Fornerod, M. (2002). The cytoplasmic filaments of the nuclear pore complex are dispensable for selective nuclear protein import. Journal of Cell Biology, 158(1), 63-77. https://doi.org/10.1083/jcb.200202088

The nuclear pore complex (NPC) mediates bidirectional macromolecular traffic between the nucleus and cytoplasm in eukaryotic cells. Eight filaments project from the NPC into the cytoplasm and are proposed to function in nuclear import. We investigate... Read More about The cytoplasmic filaments of the nuclear pore complex are dispensable for selective nuclear protein import.

The nucleoporin Nup153 is required for nuclear pore basket formation, nuclear pore complex anchoring and import of a subset of nuclear proteins (2001)
Journal Article
Walther, T., Fornerod, M., Pickersgill, H., Goldberg, M., Allen, T., & Mattaj, I. (2001). The nucleoporin Nup153 is required for nuclear pore basket formation, nuclear pore complex anchoring and import of a subset of nuclear proteins. The EMBO Journal, 20(20), 5703-5714. https://doi.org/10.1093/emboj/20.20.5703

The nuclear pore complex (NPC) is a large proteinaceous structure through which bidirectional transport of macromolecules across the nuclear envelope (NE) takes place. Nup153 is a peripheral NPC component that has been implicated in protein and RNP t... Read More about The nucleoporin Nup153 is required for nuclear pore basket formation, nuclear pore complex anchoring and import of a subset of nuclear proteins.

Steps of nuclear pore complex disassembly and reassembly during mitosisin early Drosophila embryos (2001)
Journal Article
Kiseleva, E., Rutherford, S., Cotter, L., Allen, T., & Goldberg, M. (2001). Steps of nuclear pore complex disassembly and reassembly during mitosisin early Drosophila embryos. Journal of Cell Science, 114(20), 3607-3618

The mechanisms of nuclear pore complex (NPC) assembly and disassembly during mitosis in vivo are not well defined. To address this and to identify the steps of the NPC disassembly and assembly, we investigated Drosophila embryo nuclear structure at t... Read More about Steps of nuclear pore complex disassembly and reassembly during mitosisin early Drosophila embryos.

The nuclear pore complex (2000)
Journal Article
Bagley, S., Goldberg, M., Cronshaw, J., Rutherford, S., & Allen, T. (2000). The nuclear pore complex. Journal of Cell Science, 113(22), 3885-3886

Ran alters nuclear pore complex conformation (2000)
Journal Article
Goldberg, M., Rutherford, S., Hughes, M., Cotter, L., Bagley, S., Kiseleva, E., …Clarke, P. (2000). Ran alters nuclear pore complex conformation. Journal of Molecular Biology, 300(3), 519-529

Structural effects of Ran on the nuclear pore complex (1999)
Journal Article
Goldberg, M., Rutherford, S., Cotter, L., Kiseleva, E., Allen, T., & Clarke, P. (1999). Structural effects of Ran on the nuclear pore complex. Molecular Biology of the Cell, 10, 435A-435A