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M. Hochstrasser, “Ubiquitin, Proteasomes, and the Regulation of Intracellular Protein Degradation,” Current Opinion in Cell Biology, Vol. 7, No. 2, 1995, pp. 315-223.
http://dx.doi.org/10.1016/0955-0674(95)80031-X

has been cited by the following article:

• TITLE: Polyubiquitination and Proteasome Signals in Tubulobulbar Complexes of Rat Late Spermatids

  AUTHORS: Manaka Akashi, Sadaki Yokota, Hideaki Fujita

  KEYWORDS: Tubulobulbar Complex; Polyubiquitin Signals; Proteasome; Immunoelectron Microscopy

  JOURNAL NAME: CellBio, Vol.2 No.4, December 4, 2013

  ABSTRACT: To illustrate the involvement of tubulobulbar complexes (TBC) in ubiquitin-proteasome degradation of unnecessary proteins in the head cytoplasm of late spermatids, the localization of polyubiquitin and proteasome was studied by immunofluorescence and immunoelectron microscopy. Polyubiquitin localized to TBC and proteasome subunit α to dense materials surrounding the TBC in the cytoplasm of Sertoli cell enwrapping sickle-shaped spermatid heads. The results suggest that the TBC is a structural device for ubiquin-proteasome degradation of unnecessary proteins in the cytoplasm of spermatid head during rapid reduction of the head cytoplasm and nuclear compaction of late spermatids.