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- W1567414127 abstract "The nuclear pore complex (NPC), controlling the exchange of matter and information between cell nucleus and cytoplasm, is an amazing structure having a total mass of approximately 125 MDa, measuring approximately 120 nm in diameter and 70 nm in length and being composed of presumably more than 100 different polypeptides, many occurring in multiple copies. Up to now, only about 10% of the estimated more than 100 different proteins of the metazoan NPC have been identified, characterized, and mapped to the NPC. However, further nucleoporins are being identified at a high rate. To understand their tasks within the NPC, it is crucial to find out about their location within the NPC and their association with the numerous substructures of the NPC, such as cytoplasmic and karyoplasmic rings, spokes, central granules, and cytoplasmic and karyoplasmic filaments. A frequently used and successful method for localizing nucleoporins to the NPC is immunogold electron microscopy. The principle of the method is to raise antibodies against specific nucleoporins; to react permeabilized cells, isolated nuclei, or histological sections with these primary antibodies; and to visualize the subcellular binding sites of the antibodies by electron microscopy." @default.
- W1567414127 created "2016-06-24" @default.
- W1567414127 creator A5046365242 @default.
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- W1567414127 date "1997-01-01" @default.
- W1567414127 modified "2023-09-27" @default.
- W1567414127 title "Chapter 13 Mapping Proteins to Nuclear Pore Complexes by Immunogold Electron Microscopy" @default.
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- W1567414127 doi "https://doi.org/10.1016/s0091-679x(08)60883-3" @default.
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