Deciphering the Structure and Function of Nuclear Pores Using Single-Molecule Fluorescence Approaches
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- 作者：Siegfried M. Musser1 ; smusser@tamhsc.edu" class="auth_mail" title="E-mail the corresponding author ; David Grü ; nwald2 ; David.Grunwald@umassmed.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：CRLB ; Cramé ; r&ndash ; Rao lower bound ; dSTORM ; direct stochastic optical reconstruction microscopy ; EMCCD ; electron-multiplying CCD ; GSD ; ground state depletion ; NPC ; nuclear pore complex ; NE ; nuclear envelope ; SMF ; single-molecule fluorescence ; SPEED ; single-point edge-excitation subdiffraction ; Nup ; nucleoporin ; NTR ; nuclear transport receptor ; NLS ; nuclear localization signal ; PSF ; point spread function ; QD ; quantum dots ; smFRET ; single-molecule fluorescence resonance energy transfer ; WGA
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：22 May 2016
- 年：2016
- 卷：428
- 期：10
- 页码：2091-2119
- 全文大小：2656 K
文摘
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Nuclear pores mediate macromolecular exchange between the nucleus and cytoplasm.
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A network of intrinsically disordered polypeptides forms the permeability barrier.
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Single-molecule fluorescence approaches have enabled biophysical characterization.
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Transport complex assembly and disassembly occur in vestibules at the pore exits.
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Future single-molecule studies are needed to resolve numerous outstanding problems.