Martin W. Goldberg
Durham University
108 Papers
891 Citations
Martin W. Goldberg is an academic researcher from Durham University. The author has contributed to research in topics: Nuclear pore & Lamin. The author has an hindex of 38, co-authored 105 publications. Previous affiliations of Martin W. Goldberg include Johns Hopkins University School of Medicine & Karolinska Institutet.
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Papers
The nuclear pore complex : three-dimensional surface structure revealed by field emission, in-lens scanning electron microscopy, with underlying structure uncovered by proteolysis
TL;DR: It is determined that the nucleoplasmic filaments that make up the baskets are attached to the outer periphery of the coaxial ring at a position between each of its subunits, consistent with the exclusion limit previously found for NPC-transported molecules.
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RNP export is mediated by structural reorganization of the nuclear pore basket.
Elena Kiseleva,Elena Kiseleva,Martin W. Goldberg,Martin W. Goldberg,Bertil Daneholt,Bertil Daneholt,Terence D Allen,Terence D Allen +7 more
TL;DR: A cyclic rearrangement of the basket structure is reported in relation to the translocation of a specific messenger RNP of exceptional size, the Balbiani ring RNP particles in the salivary gland cells in Chironomus.
102
Xenopus lamin B3 has a direct role in the assembly of a replication competent nucleus: evidence from cell-free egg extracts
Martin W. Goldberg,Hazel E. Jenkins,Terry Allen,William G.F. Whitfield,Christopher J. Hutchison +4 more
TL;DR: Xenopus egg extracts which assemble replication competent nuclei in vitro were depleted of lamin B3 using monoclonal antibody L6 5D5 linked to paramagnetic beads and failed to initiate semi-conservative DNA replication, it seems likely that the inability of lamination-depleted extracts to assemble a replication competent nucleus is a direct consequence of a failure to assembling a lamina.
Nuclear envelope assembly in Xenopus extracts visualized by scanning EM reveals a transport-dependent 'envelope smoothing' event
TL;DR: The pathway of nuclear envelope assembly in Xenopus egg extracts using field emission in-lens scanning electron microscopy was analyzed and a change in nuclear envelope morphology termed 'envelope smoothing' occurred 5-15 minutes after enclosure, suggesting that 'smoothing' required active nuclear transport.
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Temporal Differences in the Appearance of NEP-B78 and an LBR-like Protein during Xenopus Nuclear Envelope Reassembly Reflect the Ordered Recruitment of Functionally Discrete Vesicle Types
Sheona P Drummond,Paul Ko Ferrigno,Carol E. Lyon,Jackie Murphy,Martin W. Goldberg,Terence D Allen,Carl Smythe,Christopher J. Hutchison +7 more
TL;DR: It is shown unequivocally that, in the cell-free system, two functionally and biochemically distinct vesicles types are necessary for NE assembly and that NEP-B78 defines a vesicle population involved in the earliest events of reassembly in this system.