Analysis of Development Edited by Prof Benjamin H Willier, Prof Paul A Weiss and Prof Viktor Hamburger Pp xii + 735 (Philadelphia and London: W B Saunders Company, 1955) 105s

Mechanisms of Development

Histone and chromatin cross-talk.

https://mcb.berkeley.edu/courses/mcb230/WEB/PAPERS/mistelli.pdf

Beyond the sequence : Cellular organization of genome function

/pdf/heterochromatin-revisited-nat-rev-genet-1s49kjmsfl.pdf

Heterochromatin revisited. Nat Rev Genet

As the sole site of nucleocytoplasmic transport, the nuclear pore complex (NPC) has a vital cellular role. Nonetheless, much remains to be learned about many fundamental aspects of NPC function. To further understand the structure and function of the mammalian NPC, we have completed a proteomic analysis to identify and classify all of its protein components. We used mass spectrometry to identify all proteins present in a biochemically purified NPC fraction. Based on previous characterization, sequence homology, and subcellular localization, 29 of these proteins were classified as nucleoporins, and a further 18 were classified as NPC-associated proteins. Among the 29 nucleoporins were six previously undiscovered nucleoporins and a novel family of WD repeat nucleoporins. One of these WD repeat nucleoporins is ALADIN, the gene mutated in triple-A (or Allgrove) syndrome. Our analysis defines the proteome of the mammalian NPC for the first time and paves the way for a more detailed characterization of NPC structure and function.

/pdf/proteomic-analysis-of-the-mammalian-nuclear-pore-complex-2afvmqsc2k.pdf

Proteomic analysis of the mammalian nuclear pore complex

https://www.cell.com/cell/pdf/S0092-8674(02)00756-0.pdf

Ghislaine Arib

Papers

Chromatin Boundaries in Budding Yeast: The Nuclear Pore Connection

Nup-PI: the nucleopore-promoter interaction of genes in yeast.

Following the intracellular localization of the iab-8ncRNA of the bithorax complex using the MS2-MCP-GFP system.