Staff profile

BSc: 1985 Leeds University Genetics

PhD: 1989 Liverpool Polytechnic and University of California at Davis Biophysics

Postdoc: 1988-1995 Paterson Institute for Cancer Research Manchester

Staff Scientist 1995-1997 Paterson Institute for Cancer Research Manchester

Team Leader 1997-2002 Paterson Institute for Cancer Research Manchester

Lecturer and Head of Electron Microscopy 2002-2010 Durham University School of Biological and Biomedical Sciences

Senior Lecturer/Associate professor and Head of Electron Microscopy 2010-2022 Biosciences

Professor and Head of Electron Microscopy 2022-present

• Microscopy
• Nuclear envelope Structure and Function
• Transmission electron microscopy
• Ultra high resolution field emission scanning electron microscopy

• 2011: Invited speaker at SEB annual meeting in Glasgow:
• 2011: Invited speaker Royal Microscopical Society Botanical Microscopy Meeting in Wageningen, The Netherlands:
• 2011: Seminar Speaker Edinburgh University Biological Sciences:
• 2011: PhD External Examiner Dundee University:
• 2011: Invitation to organise session at SEB Annual Meeting in Glasgow:
• 2010: Talk at Durham EM Workshop, Durham:
• 2010: Talk at Royal Microscopical Society Microsciences Meeting, London:
• 2009: Talk at Nuclear Transport meeting, Banff, Canada:
• 2000: Invitations to contribute several book chapters:

Chapter in book

• Immunoelectron Microscopy of Cryofixed Freeze-Substituted Yeast
  
  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 (pp. 243-258). Humana Press. https://doi.org/10.1007/978-1-4939-6352-2_15
• Immunogold Labeling for Scanning Electron Microscopy
  
  Goldberg, M. W., & Fišerová, J. (2016). Immunogold Labeling for Scanning Electron Microscopy. In High-Resolution Imaging of Cellular Proteins. https://doi.org/10.1007/978-1-4939-6352-2_20
• High-Resolution Scanning Electron Microscopy and Immuno-Gold Labeling of the Nuclear Lamina and Nuclear Pore Complex
  
  Goldberg, M. W. (2016). High-Resolution Scanning Electron Microscopy and Immuno-Gold Labeling of the Nuclear Lamina and Nuclear Pore Complex. In The Nuclear Envelope. https://doi.org/10.1007/978-1-4939-3530-7_27
• Imaging Yeast NPCs: From Classical Electron Microscopy to Immuno-SEM
  
  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 (pp. 59-79). Elsevier/Academic Press. https://doi.org/10.1016/b978-0-12-417160-2.00003-5
• Imaging plant nuclei and membrane-associated cytoskeleton by field emission scanning electron microscopy.
  
  Fišerová, J., & Goldberg, M. (2013). Imaging plant nuclei and membrane-associated cytoskeleton by field emission scanning electron microscopy. In Plant Cell Morphogenesis (pp. 171-181). https://doi.org/10.1007/978-1-62703-643-6_14

Journal Article

• Inhibition of PDIs Downregulates Core LINC Complex Proteins, Promoting the Invasiveness of MDA-MB-231 Breast Cancer Cells in Confined Spaces In Vitro
  
  Young, N., Gui, Z., Mustafa, S., Papa, K., Jessop, E., Ruddell, E., Bevington, L., Quinlan, R. A., Benham, A. M., Goldberg, M. W., Obara, B., & 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
• The major inducible small heat shock protein HSP20-3 in the tardigrade Ramazzottius varieornatus forms filament-like structures and is an active chaperone.
  
  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
• Culturing Keratinocytes on Biomimetic Substrates Facilitates Improved Epidermal Assembly In Vitro
  
  Hunter-Featherstone, E., Young, N., Chamberlain, K., Cubillas, P., Hulette, B., Wei, X., Tiesman, J. P., Bascom, C. C., Benham, A. M., Goldberg, M. W., Saretzki, G., & Karakesisoglou, I. (2021). Culturing Keratinocytes on Biomimetic Substrates Facilitates Improved Epidermal Assembly In Vitro. Cells, 10(5). https://doi.org/10.3390/cells10051177
• STING nuclear partners contribute to innate immune signaling responses
  
  Dixon, C. R., Malik, P., de las Heras, J. I., Saiz-Ros, N., de Lima Alves, F., Tingey, M., Gaunt, E., Richardson, A. C., Kelly, D. A., Goldberg, M. W., Towers, G. J., Yang, W., Rappsilber, J., Digard, P., & 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
• Proteomic mapping by rapamycin-dependent targeting of APEX2 identifies binding partners of VAPB at the inner nuclear membrane
  
  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
• BFSP1 C-terminal domains released by post-translational processing events can alter significantly the calcium regulation of AQP0 water permeability
  
  Tapodi, A., Clemens, D., Uwineza, A., Goldberg, M., Thinon, E., Heal, W., Tate, E., Nemeth-Cahalan, K., Vorontsova, I., Jarrin, M., Hall, J., & 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
• Supramolecular Structures of the Dictyostelium Lamin NE81
  
  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
• Host Vesicle Fusion Protein VAPB Contributes to the Nuclear Egress Stage of Herpes Simplex Virus Type-1 (HSV-1) Replication
  
  Saiz-Ros, N., Czapiewski, R., Epifano, I., Stevenson, A., Swanson, S., Dixon, C., Zamora, D., McElwee, M., Vijayakrishnan, S., Richardson, C., Dong, L., Kelly, D., Pytowski, L., Goldberg, M., Florens, L., Graham, S., & 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 intestinal intermediate filament network responds to and protects against microbial insults and toxins
  
  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
• Farnesyltransferase inhibitor and rapamycin correct aberrant genome organisation and decrease DNA damage respectively, in Hutchinson–Gilford progeria syndrome fibroblasts
  
  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
• Agitation Modules: Flexible Means to Accelerate Automated Freeze Substitution
  
  Reipert, S., Goldammer, H., Richardson, C., Goldberg, M. W., Hawkins, T. J., Hollergschwandtner, E., Kaufmann, W. A., Antreich, S., & Stierhof, Y.-D. (2018). Agitation Modules: Flexible Means to Accelerate Automated Freeze Substitution. Journal of Histochemistry & Cytochemistry, 66(12), 903-921. https://doi.org/10.1369/0022155418786698
• Nuclear pore complex tethers to the cytoskeleton
  
  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
• Repo-Man/PP1 regulates heterochromatin formation in interphase
  
  Castro, I., Budzak, J., Di Giacinto, M. L., Ligammari, L., Gokhan, E., Spanos, C., Moralli, D., Richardson, C., de las Heras, J. I., Salatino, S., Schirmer, E. C., Ullman, K. S., Bickmore, W. A., Green, C., Rappsilber, J., Lamble, S., Goldberg, M. W., Vinciotti, V., & Vagnarelli, P. (2017). Repo-Man/PP1 regulates heterochromatin formation in interphase. Nature Communications, 8, Article 14048. https://doi.org/10.1038/ncomms14048
• Phosphorylation Regulates the Endocytic Function of the Yeast Dynamin-Related Protein Vps1
  
  Smaczynska-de Rooij, I. I., Marklew, C. J., Allwood, E. G., Palmer, S. E., Booth, W. I., Mishra, R., Goldberg, M. W., & 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 Immune Adaptor SLP-76 Binds to SUMO-RANGAP1 at Nuclear Pore Complex Filaments to Regulate Nuclear Import of Transcription Factors in T Cells
  
  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
• Xenopus LAP2β protein knockdown affects location of lamin B and nucleoporins and has effect on assembly of cell nucleus and cell viability
  
  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
• A Charge Swap mutation E461K in the yeast dynamin Vps1 reduces endocytic invagination
  
  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
• A dynamin-actin interaction is required for vesicle scission during endocytosis in yeast
  
  Palmer, S., Smaczynska-de Rooij, I., Marklew, C., Allwood, E., Mishra, R., Johnson, S., Goldberg, M., & 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
• A gradient of matrix-bound FGF-2 and perlecan is available to lens epithelial cells
  
  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
• Entry into the nuclear pore complex is controlled by a cytoplasmic exclusion zone containing dynamic GLFG-repeat nucleoporin domains
  
  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
• Structural Organisation of the Plant Nucleus
  
  Kiseleva, E., Fiserova, J., & Goldberg, M. (2013). Structural Organisation of the Plant Nucleus. Plant Genome Diversity, 2.
• Nucleoskeleton in Plants: The Functional Organization of Filaments in the Nucleus.
  
  Goldberg, M. (2013). Nucleoskeleton in Plants: The Functional Organization of Filaments in the Nucleus. Annual Plant Reviews, 4, 93-122. https://doi.org/10.1002/9781118472507.ch4
• Nesprin interchain associations control nuclear size.
  
  Lu, W., Schneider, M., Neumann, S., Jaeger, V.-M., Taranum, S., Munck, M., Cartwright, S., Richardson, C., Carthew, J., Noh, K., Goldberg, M., Noegel, A., & 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
• Yeast dynamin Vps1 and amphiphysin Rvs167 function together during endocytosis
  
  Rooij, I. I. S.- de, 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
• Filaments assembly of ectopically expressed Caenorhabditis elegans lamin within Xenopus oocytes
  
  Grossman, E., Dahan, I., Stick, R., Goldberg, M., Gruenbaum, Y., & Medalia, O. (2012). Filaments assembly of ectopically expressed Caenorhabditis elegans lamin within Xenopus oocytes. Journal of Structural Biology, 177(1), 113-118. https://doi.org/10.1016/j.jsb.2011.11.002
• Embryonic and adult isoforms of XLAP2 form microdomains associated with chromatin and the nuclear envelope
  
  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
• System analysis shows distinct mechanisms and common principles of nuclear envelope protein dynamics
  
  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
• Expression of Vps1 I649K a self-assembly defective yeast dynamin, leads to formation of extended endocytic invaginations.
  
  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
• Facilitated transport and diffusion take distinct spatial routes through the nuclear pore complex
  
  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
• Cell-specific and lamin-dependent targeting of novel transmembrane proteins in the nuclear envelope
  
  Malik, P., Korfali, N., Srsen, V., Lazou, V., Batrakou, D., Zuleger, N., Kavanagh, D., Wilkie, G., Goldberg, M., & 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
• Immunoelectron microscopy of cryofixed freeze substituted Saccharomyces cerevisiae.
  
  Fiserova, J., & Goldberg, M. (2010). Immunoelectron microscopy of cryofixed freeze substituted Saccharomyces cerevisiae. Methods Mol Biol., 657, 191-204. https://doi.org/10.1007/978-1-60761-783-9_15
• Oocytes as an experimental system to analyze the ultrastructure of endogenous and ectopically expressed nuclear envelope components.
  
  Stick, R., & Goldberg, M. (2010). Oocytes as an experimental system to analyze the ultrastructure of endogenous and ectopically expressed nuclear envelope components. Methods, 51, 170-176.
• Relationships at the nuclear envelope: lamins and nuclear pore complexes in animals and plants.
  
  Fiserova, J., & Goldberg, M. (2010). Relationships at the nuclear envelope: lamins and nuclear pore complexes in animals and plants. Biochemical Society Transactions, 38, 829-831.
• Immunogold labelling for scanning electron microscopy.
  
  Goldberg, M., & Fiserova, J. (2010). Immunogold labelling for scanning electron microscopy. Methods Mol Biol., 657, 297-313.
• Molecular characterization of Xenopus lamin LIV reveals differences in the lamin composition of sperms in amphibians and mammals.
  
  von Moeller, F., Barendziak, T., Apte, K., Goldberg, M., & Stick, R. (2010). Molecular characterization of Xenopus lamin LIV reveals differences in the lamin composition of sperms in amphibians and mammals. Nucleus, 1, 85-95.
• A role for the dynamin-like protein Vps1 during endocytosis in yeast.
  
  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
• Nuclear envelope and nuclear pore complex structure and organization in tobacco BY-2 cells.
  
  Fiserova, J., Kiseleva, E., & Goldberg, M. (2009). Nuclear envelope and nuclear pore complex structure and organization in tobacco BY-2 cells. Plant Journal, 59(2), 243-255. https://doi.org/10.1111/j.1365-313x.2009.03865.x
• Nucleocytoplasmic transport in yeast: a few roles for many actors.
  
  Fiserova, J., & Goldberg, M. (2009). Nucleocytoplasmic transport in yeast: a few roles for many actors. Biochemical Society Transactions, 38, 273-7. https://doi.org/10.1042/bst0380273
• A new model for nuclear lamina organization.
  
  Goldberg, M., Fiserova, J., Huttenlauch, I., & Stick, R. (2008). A new model for nuclear lamina organization. Biochemical Society Transactions, 36, 1339-43. https://doi.org/10.1042/bst0361339
• Growth and Assembly in Xenopus Oocytes and Egg Extracts is Mediated by Distinct Populations of Membranes
  
  Salpingidou, G., Rzepecki, R., Kiseleva, E., Lyon, 4C., Lane, B., Fusiek, K., Golebiewska, A., Drummond, S., Allen JA., T. D., Goldberg, M. W., & Hutchison, C. J. (2008). Growth and Assembly in Xenopus Oocytes and Egg Extracts is Mediated by Distinct Populations of Membranes. Journal of Cell Science, 121, 706-716.
• Filaments made from A- and B-type lamins differ in structure and organization
  
  Goldberg, M., Huttenlauch, I., Hutchison, C., & Stick, R. (2008). Filaments made from A- and B-type lamins differ in structure and organization. Journal of Cell Science, 121(2), 215-225. https://doi.org/10.1242/jcs.022020
• Scanning electron microscopy of nuclear structure.
  
  Allen, T., Rutherford, S., Murray, S., Drummond, S., Goldberg, M., & Kiseleva, E. (2008). Scanning electron microscopy of nuclear structure. Methods Cell Biol, 88, 389-409.
• Immunolabeling for scanning electron microscopy (SEM) and field emission SEM.
  
  Goldberg, M. (2008). Immunolabeling for scanning electron microscopy (SEM) and field emission SEM. Methods Cell Biol, 88, 109-30.
• Reticulon 4a/NogoA locates to regions of high membrane curvature and may have a role in nuclear envelope growth
  
  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
• FGF-2 Release from the Lens Capsule by MMP-2 Maintains Lens Epithelial Cell Viability
  
  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
• Nuclear membrane disassembly and rupture
  
  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
• A protocol for isolation and visualization of yeast.
  
  Kiseleva, E., Allen, T., Rutherford, S., Murray, S., Morozova, K., Gardiner, F., Goldberg, M., & Drummond, S. (2007). A protocol for isolation and visualization of yeast. Nature Protocols, 2(8), 1943-1953.
• 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).
  
  Allen, T., Rutherford, S., Murray, S., Sanderson, H., Gardiner, F., Kiseleva, E., Goldberg, M., & 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 isolating Xenopus oocyte nuclear envelope for visualization and characterization by scanning electron microscopy (SEM) or transmission electron microscopy (TEM).
  
  Allen, T., Rutherford, S., Murray, S., Sanderson, H., Gardiner, F., Kiseleva, E., Goldberg, M., & 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.
• Visualization of the nucleus and nuclear envelope in situ by SEM in tissue culture cells.
  
  Allen, T., Rutherford, S., Murray, S., Gardiner, F., Kiseleva, E., Goldberg, M., & Drummond, S. (2007). Visualization of the nucleus and nuclear envelope in situ by SEM in tissue culture cells. Nature Protocols, 2, 1180-1184.
• Periplakin-dependent re-organisation of keratin cytoskeleton and loss of collective migration in Keratin 8 down-regulated epithelial sheets
  
  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
• Actin- and protein-4.1-containing filaments link nuclear pore complexesto subnuclear organelles in Xenopus oocyte nuclei
  
  Kiseleva, E., Drummond, S., Goldberg, M., Rutherford, S., Allen, T., & Wilson, K. (2004). Actin- and protein-4.1-containing filaments link nuclear pore complexesto subnuclear organelles in Xenopus oocyte nuclei. Journal of Cell Science, 117(12), 2481-2490.
• Yeast nuclear pore complexes have a cytoplasmic ring and internal filaments
  
  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 cytoplasmic filaments of the nuclear pore complex are dispensiblefor selective nuclear import
  
  Walther, T., Pickersgill, H., Cordes, V., Goldberg, M., Allen, T., Mattaj, I., & Fornerod, M. (2002). The cytoplasmic filaments of the nuclear pore complex are dispensiblefor selective nuclear import. Molecular Biology of the Cell, 13, 381A-382A.
• Concentration of Ran on chromatin induces decondensation, nuclearenvelope formation and nuclear pore complex assembly
  
  Zhang, C., Goldberg, M., Moore, W., Allen, T., & Clarke, P. (2002). Concentration of Ran on chromatin induces decondensation, nuclearenvelope formation and nuclear pore complex assembly. European Journal of Cell Biology, 81(11), 623-633. https://doi.org/10.1078/0171-9335-00288
• The cytoplasmic filaments of the nuclear pore complex are dispensable for selective nuclear protein import
  
  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
• Steps of nuclear pore complex disassembly and reassembly during mitosisin early Drosophila embryos
  
  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 nucleoporin Nup153 is required for nuclear pore basket formation, nuclear pore complex anchoring and import of a subset of nuclear proteins
  
  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. EMBO Journal, 20(20), 5703-5714. https://doi.org/10.1093/emboj/20.20.5703
• Structural modifications of nuclear pure complexes associated withtransport.
  
  Allen, T., Kiseleva, E., Rutherford, S., Bagley, S., Clarke, P., & Goldberg, M. (2000). Structural modifications of nuclear pure complexes associated withtransport. Molecular Biology of the Cell, 11, 152A-153A.
• The nuclear pore complex
  
  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
  
  Goldberg, M., Rutherford, S., Hughes, M., Cotter, L., Bagley, S., Kiseleva, E., Allen, T., & Clarke, P. (2000). Ran alters nuclear pore complex conformation. Journal of Molecular Biology, 300(3), 519-529.
• The nuclear pore complex: mediator of translocation between nucleus andcytoplasm
  
  Allen, T., Cronshaw, J., Bagley, S., Kiseleva, E., & Goldberg, M. (2000). The nuclear pore complex: mediator of translocation between nucleus andcytoplasm. Journal of Cell Science, 113(10), 1651-1659.
• The nuclear pore complex: Structure, function, and dynamics
  
  Kiseleva, E., Goldberg, M., Cronshaw, J., & Allen, T. (2000). The nuclear pore complex: Structure, function, and dynamics. Critical Reviews in Eukaryotic Gene Expression, 10(1), 101-112.
• Structural effects of Ran on the nuclear pore complex
  
  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.
• Nuclear-pore-complex dynamics and transport in higher eukaryotes
  
  Goldberg, M., Cronshaw, J., Kiseleva, E., & Allen, T. (1999). Nuclear-pore-complex dynamics and transport in higher eukaryotes. Protoplasma, 209(3-4), 144-156.
• Nuclear envelope and nuclear pore assembly: analysis of assemblyintermediates by electron microscopy
  
  Gant, T., Goldberg, M., & Allen, T. (1998). Nuclear envelope and nuclear pore assembly: analysis of assemblyintermediates by electron microscopy. Current Opinion in Cell Biology, 10(3), 409-415.
• TPEN, a Zn2+/Fe2+ chelator with low affinity for Ca2+, inhibits laminassembly, destabilizes nuclear architecture and may independentlyprotect nuclei from apoptosis in vitro
  
  Shumaker, D., Vann, L., Goldberg, M., Allen, T., & Wilson, K. (1998). TPEN, a Zn2+/Fe2+ chelator with low affinity for Ca2+, inhibits laminassembly, destabilizes nuclear architecture and may independentlyprotect nuclei from apoptosis in vitro. Cell Calcium, 23(2-3), 151-164.
• Active nuclear pore complexes in Chironomus: visualization oftransporter configurations related to mRNP export
  
  Kiseleva, E., Goldberg, M., Allen, T., & Akey, C. (1998). Active nuclear pore complexes in Chironomus: visualization oftransporter configurations related to mRNP export. Journal of Cell Science, 111, 223-236.
• Three-dimensional surface structure analysis of the nucleus
  
  Allen, T., Rutherford, S., Bennion, G., Wiese, C., Riepert, S., Kiseleva, E., & Goldberg, M. (1998). Three-dimensional surface structure analysis of the nucleus. Methods in Cell Biology, 53, 125-138.
• Xenopus Ran-binding protein 1: molecular interactions and effects onnuclear assembly in Xenopus egg extracts
  
  Nicolas, F., Zhang, C., Hughes, M., Goldberg, M., Watton, S., & Clarke, P. (1997). Xenopus Ran-binding protein 1: molecular interactions and effects onnuclear assembly in Xenopus egg extracts. Journal of Cell Science, 110, 3019-3030.
• Macromolecular substructure in nuclear pore complexes by in-lensfield-emission scanning electron microscopy
  
  Allen, T., Bennion, G., Rutherford, S., Reipert, S., Ramalho, A., Kiseleva, E., & Goldberg, M. (1997). Macromolecular substructure in nuclear pore complexes by in-lensfield-emission scanning electron microscopy. Scanning, 19(6), 403-410.
• Nuclear envelope assembly in Xenopus extracts visualized by scanning EMreveals a transport-dependent 'envelope smoothing' event
  
  Wiese, C., Goldberg, M., Allen, T., & Wilson, K. (1997). Nuclear envelope assembly in Xenopus extracts visualized by scanning EMreveals a transport-dependent ’envelope smoothing’ event. Journal of Cell Science, 110, 1489-1502.
• Three-dimensional visualization of the route of protein import: Therole of nuclear pore complex substructures
  
  Rutherford, S., Goldberg, M., & Allen, T. (1997). Three-dimensional visualization of the route of protein import: Therole of nuclear pore complex substructures. Experimental Cell Research, 232(1), 146-160.
• Dimples, pores, star-rings, and thin rings on growing nuclearenvelopes: Evidence for structural intermediates in nuclear porecomplex assembly
  
  Goldberg, M., Wiese, C., Allen, T., & Wilson, K. (1997). Dimples, pores, star-rings, and thin rings on growing nuclearenvelopes: Evidence for structural intermediates in nuclear porecomplex assembly. Journal of Cell Science, 110, 409-420.
• Nuclear pore complex structure in birds
  
  Goldberg, M., Solovei, I., & Allen, T. (1997). Nuclear pore complex structure in birds. Journal of Structural Biology, 119(3), 284-294. https://doi.org/10.1006/jsbi.1997.3877
• Structural intermediates in nuclear pore complex assembly identified byscanning EM.
  
  Wiese, C., Goldberg, M., Allen, T., & Wilson, K. (1996). Structural intermediates in nuclear pore complex assembly identified byscanning EM. Molecular Biology of the Cell, 7, 544-544.
• Nuclear lamina and nuclear matrix organization in sperm pronucleiassembled in Xenopus egg extract
  
  Zhang, C., Jenkins, H., Goldberg, M., Allen, T., & Hutchison, C. (1996). Nuclear lamina and nuclear matrix organization in sperm pronucleiassembled in Xenopus egg extract. Journal of Cell Science, 109, 2275-2286.
• The nuclear pore complex and lamina: Three-dimensional structures andinteractions determined by field emission in-lens scanning electronmicroscopy
  
  Goldberg, M., & Allen, T. (1996). The nuclear pore complex and lamina: Three-dimensional structures andinteractions determined by field emission in-lens scanning electronmicroscopy. Journal of Molecular Biology, 257(4), 848-865.
• STRUCTURAL AND FUNCTIONAL-ORGANIZATION OF THE NUCLEAR-ENVELOPE
  
  Goldberg, M., & Allen, T. (1995). STRUCTURAL AND FUNCTIONAL-ORGANIZATION OF THE NUCLEAR-ENVELOPE. Current Opinion in Cell Biology, 7(3), 301-309.
• 4 FUNCTIONS AND A FUNERAL - MITOSIS, REPLICATION, TRANSCRIPTION,TRANSPORT AND APOPTOSIS IN THE NUCLEUS
  
  Allen, T., & Goldberg, M. (1995). 4 FUNCTIONS AND A FUNERAL - MITOSIS, REPLICATION, TRANSCRIPTION,TRANSPORT AND APOPTOSIS IN THE NUCLEUS. Trends in Cell Biology, 5(4), 176-178.
• EVIDENCE FOR THE DIRECT INVOLVEMENT OF LAMINS IN THE ASSEMBLY OF AREPLICATION COMPETENT NUCLEUS
  
  Jenkins, H., Whitfield, W., Goldberg, M., Allen, T., & Hutchison, C. (1995). EVIDENCE FOR THE DIRECT INVOLVEMENT OF LAMINS IN THE ASSEMBLY OF AREPLICATION COMPETENT NUCLEUS. Acta Biochimica Polonica, 42(2), 133-143.
• THE NUCLEAR-PORE COMPLEX - 3-DIMENSIONAL SURFACE-STRUCTURE REVEALED BYFIELD-EMISSION, IN-LENS SCANNING ELECTRON-MICROSCOPY, WITH UNDERLYINGSTRUCTURE UNCOVERED BY PROTEOLYSIS
  
  Goldberg, M., & Allen, T. (1993). THE NUCLEAR-PORE COMPLEX - 3-DIMENSIONAL SURFACE-STRUCTURE REVEALED BYFIELD-EMISSION, IN-LENS SCANNING ELECTRON-MICROSCOPY, WITH UNDERLYINGSTRUCTURE UNCOVERED BY PROTEOLYSIS. Journal of Cell Science, 106, 261-274.
• HIGH-RESOLUTION SCANNING ELECTRON-MICROSCOPY OF THE NUCLEAR-ENVELOPE -DEMONSTRATION OF A NEW, REGULAR, FIBROUS LATTICE ATTACHED TO THEBASKETS OF THE NUCLEOPLASMIC FACE OF THE NUCLEAR-PORES
  
  Goldberg, M., & Allen, T. (1992). HIGH-RESOLUTION SCANNING ELECTRON-MICROSCOPY OF THE NUCLEAR-ENVELOPE -DEMONSTRATION OF A NEW, REGULAR, FIBROUS LATTICE ATTACHED TO THEBASKETS OF THE NUCLEOPLASMIC FACE OF THE NUCLEAR-PORES. Journal of Cell Biology, 119(6), 1429-1440.
• THE USE OF FIELD-EMISSION IN-LENS SCANNING ELECTRON-MICROSCOPY TO STUDYTHE STEPS OF ASSEMBLY OF THE NUCLEAR-ENVELOPE INVITRO
  
  Goldberg, M., Blow, J., & Allen, T. (1992). THE USE OF FIELD-EMISSION IN-LENS SCANNING ELECTRON-MICROSCOPY TO STUDYTHE STEPS OF ASSEMBLY OF THE NUCLEAR-ENVELOPE INVITRO. Journal of Structural Biology, 108(3), 257-268. https://doi.org/10.1016/1047-8477%2892%2990026-7
• ATP DEPENDENT HISTONE PHOSPHORYLATION AND NUCLEOSOME ASSEMBLY IN AHUMAN CELL-FREE-EXTRACT
  
  Banerjee, S., Bennion, G., Goldberg, M., & Allen, T. (1991). ATP DEPENDENT HISTONE PHOSPHORYLATION AND NUCLEOSOME ASSEMBLY IN AHUMAN CELL-FREE-EXTRACT. Nucleic Acids Research, 19(21), 5999-6006.
• NEUTRON AND X-RAY SCATTER STUDIES OF THE HISTONE OCTAMER AND AMINO ANDCARBOXYL DOMAIN TRIMMED OCTAMERS
  
  Wood, M., Yau, P., Imai, B., Goldberg, M., Lambert, S., Fowler, A., Baldwin, J., Godfrey, J., Moudrianakis, E., Koch, M., Ibel, K., May, R., & Bradbury, E. (1991). NEUTRON AND X-RAY SCATTER STUDIES OF THE HISTONE OCTAMER AND AMINO ANDCARBOXYL DOMAIN TRIMMED OCTAMERS. Journal of Biological Chemistry, 266(9), 5696-5702.
• THE USE OF IN LENS FIELD-EMISSION SCANNING ELECTRON-MICROSCOPY FORSTUDIES OF THE ORGANIZATION OF INTERPHASE NUCLEAR CHROMATIN ANDNUCLEAR-PORE FORMATION
  
  Allen, T., Goldberg, M., & Blow, J. (n.d.). THE USE OF IN LENS FIELD-EMISSION SCANNING ELECTRON-MICROSCOPY FORSTUDIES OF THE ORGANIZATION OF INTERPHASE NUCLEAR CHROMATIN ANDNUCLEAR-PORE FORMATION. Institute of Physics Conference Series., 98, 663-666.

Other (Print)

• Microscopic visualisation of metabotropic glutamate receptors on the surface of living cells using bifunctional magnetic resonance imaging probes
  
  Mishra, A., Mishra, R., Gottschalk, S., Pal, R., Sim, N., Engelmann, J., Goldberg, M., & Parker, D. (2014). Microscopic visualisation of metabotropic glutamate receptors on the surface of living cells using bifunctional magnetic resonance imaging probes (pp. 128-137). ACS chemical neuroscience.